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Information on EC 3.6.4.10 - non-chaperonin molecular chaperone ATPase

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EC Tree
IUBMB Comments
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
hsp90, heat shock protein, grp78, hsp60, groel, molecular chaperone, heat shock protein 70, hsc70, heat shock protein 90, hsp40, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 kD heat shock protein
90 kDa heat shock protein
-
-
90-kDa heat shock protein
AAA+ ATPase
-
-
AAA+ ATPase ClpB
-
AAA+ chaperone
AAA+ chaperone ClpB
-
ATP-dependent foldase
-
-
ATPase chaperone
ATPase ClpB
-
-
bATPase
-
-
bona fide chaperone
-
-
chaperone ClpB
-
-
chaperone hsp90
chaperone Hsp90alpha
-
-
chaperone Hsp90beta
-
-
ClpB chaperone
-
-
ClpB disaggregase
-
ClpB2/HSP101
-
-
ClpX heat-shock protein
-
-
disaggregase
-
-
DnaK ATPase
-
-
DnaK chaperone
endoplasmic reticulum chaperone
-
-
ER lumenal hsc70 BiP
-
-
eukaryotic Hsc70 ATPase
Grp78
hATPase
-
-
heat shock cognate 70
-
heat shock cognate protein
heat shock protein
-
-
heat shock protein 70
heat shock protein 90
heat shock protein 90-alpha
-
-
heat shock protein GroEl
-
-
heat shock protein-70
-
heat shock protein-90
-
-
heat-shock cognate protein 70
-
heat-shock protein 70
-
heat-shock protein 90
-
-
Hsc70
Hsp100
Hsp14.0
Hsp19.7
Hsp70 chaperone
Hsp70 chaperone Ssa1
-
-
Hsp70-1
Hsp70-2
Hsp90 molecular chaperone
Hsp90a
-
-
Hsp90alpha
-
-
HSPA1L
-
-
HspA8
-
-
human alphabeta crystallin
-
-
human Hsp70 molecular chaperone
-
-
human stress70c
-
-
inducible heat shock protein 70
-
Kar2
-
ATPase domain of BiP
maize stress70er
-
-
MecB protein
-
-
-
mitochondrial chaperone
-
-
mitochondrial heat shock protein 40
-
-
mitochondrial heat shock protein 70
-
-
mitochondrial heat-shock protein 70
-
-
mitochondrial hsp70
molecular chaperone
molecular chaperone BiP
-
-
molecular chaperone GroEl
-
-
molecular chaperone Hsc70 ATPase
-
-
-
-
mortalin/mtHsp70
-
-
mouse alphabeta crystallin
-
-
mtHSP70
p97-valosin-containing protein
-
-
p97-VCP
-
-
stress70 protein
tomato stress70c
-
-
vacuolar H+-ATPase
-
-
vacuolar membrane ATPase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-polymerizing)
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + ATP
ATP + ADP
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + aggregated alpha-casein
ADP + phosphate + activated alpha-casein
show the reaction diagram
-
-
-
-
?
ATP + H2O + aggregated fructose-1,6-bisphosphate aldolase
ADP + phosphate + activated fructose-1,6-bisphosphate aldolase
show the reaction diagram
ATP + H2O + aggregated glucose-6-phosphate dehydrogenase
ADP + phosphate + activated glucose-6-phosphate dehydrogenase
show the reaction diagram
ATP + H2O + aggregated RepE
ADP + phosphate + activated RepE
show the reaction diagram
-
-
-
-
?
ATP + H2O + fluorescein isothiocyanate tagged-casein
ADP + phosphate + ?
show the reaction diagram
CDP + H2O
?
show the reaction diagram
-
Hsp70
-
-
?
dCDP + H2O
?
show the reaction diagram
-
Hsp70
-
-
?
dGDP + H2O
?
show the reaction diagram
-
Hsp70
-
-
?
dTDP + H2O
?
show the reaction diagram
-
Hsp70
-
-
?
GDP + H2O
?
show the reaction diagram
-
Hsp70
-
-
?
UDP + H2O
?
show the reaction diagram
-
Hsp70
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + ATP
ATP + ADP
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mo6+
-
-
Ni2+
-
Hsp70 activity stimulated by
Rb+
-
activates to half the turnover rate observed with K+
V5+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1aR,2Z,4E,6Z,14R)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylacetyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
-
-
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-6-([[(dimethylamino)acetyl]oxy]imino)-9,11-dihydroxy-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-(methylimino)-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylcarbonyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-6-(hydroxyimino)-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aS,2Z,15R,16aR)-9-chloro-10,12-dihydroxy-15-methyl-1a,15,16,16a-tetrahydro-1H-7,4-(metheno)cyclopropa[h][12,2,3,4]benzoxatriazacyclopentadecin-13(8H)-one
-
-
(1R)-2-(5-chloro-2,4-dihydroxybenzoyl)-N-ethyl-2,3-dihydro-1H-isoindole-1-carboxamide
-
-
(3R,5E,9E,11Z)-13-chloro-7,14,16-trihydroxy-3-methyl-11-[[(piperidin-1-ylacetyl)oxy]imino]-3,4,7,8,11,12-hexahydro-1H-2-benzoxacyclotetradecin-1-one
-
-
(3S)-14,16-dihydroxy-3-methyl-3,4,5,6,9,10,11,12-octahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-amino-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
IPI-493
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[benzyl(ethyl)amino]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-20-chloro-13,19-dihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-9-(carbamoyloxy)-13,20,22-trihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-N-(prop-2-en-1-yl)-2-azabicyclo[16.3.1]docosa-1(22),4,6,10,18,20-hexaen-19-aminium chloride
(4E,6Z,8S,9S,10E,12S,13R,14S,16S,17R)-22-hydroxy-8,13,14,17-tetramethoxy-4,10,12,16,20-pentamethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,8S,9S,10E,12S,13R,14S,16R)-13,20-dihydroxy-8,14-dimethoxy-10,12,16-trimethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(22),4,10,18,20-pentaen-9-yl carbamate
(5-[4-amino-6-[(2-methoxyphenyl)sulfanyl]-1,3,5-triazin-2-yl]-2,4-dichlorophenoxy)acetonitrile
-
-
(5E)-5-[(1-benzyl-1H-indol-3-yl)methylidene]-1-(2-fluorocyclohexyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
(5E,9E,11Z)-13-chloro-14,16-dihydroxy-11-[[(piperidin-1-ylacetyl)oxy]imino]-3,4,7,8,11,12-hexahydro-1H-2-benzoxacyclotetradecin-1-one
-
-
(5Z)-7-[4-fluoro-2-(pyridin-3-yl)phenyl]-5-(hydroxyimino)-4-methyl-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-2-amine
-
-
(7R)-2-amino-7-[5-(6-methoxypyrazin-2-yl)-1,3-thiazol-4-yl]-4-methyl-7,8-dihydropyrido[4,3-d]pyrimidin-5(6H)-one
-
-
1,3-dihydro-2H-isoindol-2-yl[2,4-dihydroxy-5-(propan-2-yl)phenyl]methanone
-
-
1,3-dihydro-2H-isoindol-2-yl[6-hydroxy-3-(3-methylbenzyl)-1H-indazol-5-yl]methanone
-
-
1-(3H-imidazo[4,5-c]pyridin-2-yl)-2,3-dihydro-5H-pyrrolo[2,1-a]isoindol-5-one
-
-
1-(4-aminoquinazolin-6-yl)-3,6,6-trimethyl-1,5,6,7-tetrahydro-4H-indol-4-one
-
-
1-(5-ethyl-2,4-dihydroxyphenyl)-5-(trifluoromethyl)-1,3-dihydro-2H-benzimidazol-2-one
-
-
1-(6-amino-9H-purin-8-yl)-3,6,6-trimethyl-1,5,6,7-tetrahydro-4H-indazol-4-one
-
-
1-[4-(2-[6-amino-8-[(7-bromo-2,3-dihydro-1,4-benzodioxin-6-yl)sulfanyl]-3H-purin-3-yl]ethyl)piperidin-1-yl]-2-hydroxy-2-methylpropan-1-one
-
-
17-(2-dimethylaminoethyl)amino-17-demethoxygeldanamycin
17-(allylamino)-17-demethoxygeldanamycin
-
-
17-allyl-amino-17-demethoxygeldanamycin
-
0.002 mM, 20% inhibition
17-allylamino-17-demethoxygeldanamycin
i.e. tanespimycin, binding kinetics, overview
17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride
-
-
17-dimethylaminoethylamino-17-demethoxygeldanamycin hydrochloride
-
-
2'-methoxy-5-[4-(2-methoxyethyl)-4H-1,2,4-triazol-3-yl]-5'-(propan-2-yl)biphenyl-2,4-diol
-
-
2,4-dihydroxy-5-[5-hydroxy-4-(2-methylphenyl)-4H-1,2,4-triazol-3-yl]-N-methyl-N-pentylbenzamide
-
-
2,4-dihydroxy-5-[5-hydroxy-4-(2-methylphenyl)-4H-1,2,4-triazol-3-yl]-N-methyl-N-[2-(3-methylphenyl)ethyl]benzamide
-
-
2,4-dihydroxy-N-methyl-N-(3-methylbenzyl)-5-[1-(2-methylphenyl)-1H-pyrazol-5-yl]benzamide
-
-
2,5-dichloro-N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]benzenesulfonamide
2-(5-[3-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-5-hydroxy-4H-1,2,4-triazol-4-yl]-1H-indol-1-yl)ethyl dihydrogen phosphate
-
-
2-([3-[2-(dimethylamino)ethoxy]-4-methoxyphenyl]amino)-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indazol-1-yl)benzamide
-
-
2-amino-4-chloro-8-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-5-propyl-7,8-dihydropteridin-6(5H)-one
-
-
2-amino-4-methyl-7-[2-(phenylamino)phenyl]-7,8-dihydroquinazolin-5(6H)-one
-
-
2-amino-4-[2,4-dichloro-5-[3-(pyrrolidin-1-yl)propoxy]phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamide
-
NVP-BEP800/VER-82576
2-amino-6-benzyl-4-(2,4-dichlorophenyl)-5,6-dihydro-7H-pyrrolo[3,4-d]pyrimidin-7-one
-
-
2-amino-6-chloro-9-[(4-iodo-3,5-dimethylpyridin-2-yl)methyl]-7-[2-(1H-pyrrol-1-yl)ethyl]-7,9-dihydro-8H-purin-8-one
-
-
2-amino-N-ethyl-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
-
SNX-7081, weak inhibitor
2-bromo-4-(5-oxo-5,6,7,8-tetrahydronaphthalen-1-yl)benzonitrile
-
-
2-chloro-6-(2,4-dichlorophenyl)-9H-purine
-
-
2-chloro-N-[3-(5-ethyl-2,4-dihydroxyphenyl)-1H-pyrazol-4-yl]benzamide
-
-
2-fluoro-6-(tetrahydro-2H-pyran-4-ylamino)-4-(2,3,6,6-tetramethyl-4-oxo-4,5,6,7-tetrahydro-1H-indol-1-yl)benzamide
-
-
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide
-
-
2-[(6-bromo-1,3-benzodioxol-5-yl)methyl]-1-methyl-5-(propanoylamino)-1H-imidazole-4-carboxamide
-
-
2-[(E)-2-(2-hydroxy-3-methoxyphenyl)ethenyl]-3-(4-methoxycyclohexyl)quinazolin-4(3H)-one
-
-
2-[(E)-2-(2-hydroxy-3-methoxyphenyl)ethenyl]-3-(4-methoxyphenyl)quinazolin-4(3H)-one
2-[2-[(4-methoxy-3,5-dimethyl-3,4-dihydropyridin-2-yl)methyl]-7,8-dihydro-2H-6-thia-1,2,3,5-tetraazaacenaphthylen-7-yl]-N-(5-methyl-1,3-thiazol-2-yl)acetamide
-
-
2-[4-(1-methyl-1H-indol-5-yl)-5-sulfanyl-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)pyridine-3,5-diol
-
-
2-[6-amino-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9H-purin-9-yl]ethyl sulfamate
-
-
2-[6-amino-8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9H-purin-9-yl]-N-hydroxyacetamide
-
-
2-[[4-(2-chloro-5-hydroxy-4-methoxyphenyl)-5-cyano-7H-pyrrolo[2,3-d]pyrimidin-2-yl]sulfanyl]-N,N-dimethylacetamide
-
-
2-[[5-(1,3-benzodioxol-5-yl)-4-phenyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1-phenylethanone
-
-
2-[[6-(dimethylamino)-1,3-benzodioxol-5-yl]sulfanyl]-1-[2-[(2,2-dimethylpropyl)amino]ethyl]-1H-imidazo[4,5-c]pyridin-4-amine
-
CUDC-305
3,6-diamino-5-cyano-4-(4-methoxy-3-[[3-(trifluoromethyl)benzoyl]amino]phenyl)thieno[2,3-b]pyridine-2-carboxamide
-
-
3-(5-chloro-2,4-dihydroxyphenyl)-N-(4-fluorophenyl)-4H-pyrazole-4-carboxamide
-
-
3-(5-chloro-2,4-dihydroxyphenyl)-N-(4-methoxyphenyl)-4H-pyrazole-4-carboxamide
-
-
3-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1H-pyrazole-5-carboxamide
3-(5-chloro-2,4-dihydroxyphenyl)-N-[3-(trifluoromethyl)phenyl]-4H-pyrazole-4-carboxamide
-
-
3-(cyclopentylmethyl)-6-hydroxy-N-methyl-N-[4-(morpholin-4-yl)phenyl]-1H-indazole-5-carboxamide
-
-
3-benzyl-4-fluoro-1H-indazol-6-ol
-
-
3-[(4-hydroxycyclohexyl)amino]-2',3'-dimethoxybiphenyl-4-carbonitrile
-
-
3-[(E)-[2-[(2-amino-6-methylpyrimidin-4-yl)ethynyl]benzylidene]amino]-1,3-oxazolidin-2-one
4-(1,3-benzodioxol-5-yl)-3-(5-ethyl-2,4-dihydroxyphenyl)-1H-pyrazole-5-carboxylic acid
4-(1-phenyl-1H-1,2,3-triazol-4-yl)-6-(propan-2-yl)benzene-1,3-diol
-
-
4-(2,4-dichloro-5-methoxyphenyl)-2,6-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
4-(2,4-dichloro-5-methoxyphenyl)-2-[2-(diethylamino)ethoxy]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
4-(2,4-dichlorophenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
-
-
4-(4-[4-methoxy-3-[methyl(2-methylpropyl)amino]phenyl]-5-sulfanyl-4H-1,2,4-triazol-3-yl)-6-(propan-2-yl)benzene-1,3-diol
-
-
4-(but-2-yn-1-yl)-6-[4-(4-methoxyphenyl)-5-methyl-1,2-oxazol-3-yl]benzene-1,3-diol
-
-
4-([2-carbamoyl-5-[6,6-dimethyl-4-oxo-3-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-indazol-1-yl]phenyl]amino)cyclohexyl glycinate
-
SNX-5422
4-([2-[3,5-bis(trifluoromethyl)phenyl]-4,5-bis(4-methoxyphenyl)-1H-imidazol-1-yl]methyl)benzoic acid
-
inhibits the ATPase activity of Hsc70 by binding to its ATPase domain
4-amino-11,18,20-trimethyl-7-thia-3,5,11,15-tetraazatricyclo[15.3.1.12,6]docosa-1(21),2(22),3,5,17,19-hexaene-10,16-dione
-
-
4-chloro-6-(2,4-dichlorophenyl)pyrimidin-2-amine
-
-
4-chloro-6-(4-[4-[4-(methylsulfonyl)benzyl]piperazin-1-yl]-1H-pyrazol-3-yl)benzene-1,3-diol
4-chloro-6-(5-[[2-(morpholin-4-yl)ethyl]amino]-1,2-benzoxazol-3-yl)benzene-1,3-diol
4-chloro-6-phenylpyrimidin-2-amine
-
-
4-chloro-6-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol
4-chloro-6-[5-(4-ethoxyphenyl)-1,2,3-thiadiazol-4-yl]benzene-1,3-diol
-
-
4-ethyl-6-[4-(1H-imidazol-4-yl)-1H-pyrazol-3-yl]benzene-1,3-diol
4-ethyl-6-[4-(4-methoxynaphthalen-1-yl)-5-sulfanyl-4H-1,2,4-triazol-3-yl]benzene-1,3-diol
-
-
4-ethyl-6-[5-hydroxy-4-(naphthalen-1-yl)-1H-pyrazol-3-yl]benzene-1,3-diol
-
-
4-[2-amino-4-chloro-7-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidin-5-yl]but-3-yn-1-ol
-
-
4-[4-(1,3-benzodioxol-5-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
-
-
4-[4-(1-methyl-1H-indol-5-yl)-5-[(pyridin-3-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
-
-
4-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
4-[4-(2-fluorophenyl)-5-hydroxy-4H-1,2,4-triazol-3-yl]-6-(2-phenylethyl)benzene-1,3-diol
-
-
4-[4-(2-methyl-1,3-thiazol-4-yl)-5-(trifluoromethyl)-1,2-oxazol-3-yl]benzene-1,3-diol
4-[4-(4-benzylpiperazin-1-yl)-1H-pyrazol-3-yl]-6-chlorobenzene-1,3-diol
4-[4-(6-fluoro-1H-benzimidazol-2-yl)-9H-carbazol-9-yl]-2-[(trans-4-hydroxycyclohexyl)amino]benzamide
-
-
4-[4-(diethylamino)phenyl]-5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-1,2-oxazole-3-carboxamide
4-[5-hydroxy-4-(1-methyl-1H-indol-5-yl)-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
-
-
4-[5-hydroxy-4-[4-(morpholin-4-yl)phenyl]-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
-
-
4-[6,6-dimethyl-4-oxo-3-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-indazol-1-yl]-2-[(4-hydroxycyclohexyl)amino]benzamide
-
SNX-2112
5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1,2-oxazole-3-carboxamide
5-(5-ethyl-2,4-dihydroxyphenyl)-1-(naphthalen-1-yl)-1,3-dihydro-2H-imidazol-2-one
-
-
5-amino-1-(5-aminopentyl)-2-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-1H-imidazole-4-carboxamide
-
-
5-amino-1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]-1H-imidazole-4-carboxamide
-
-
5-hydroxy-4-[5-hydroxy-4-[6-(morpholin-4-yl)pyridin-3-yl]-4H-1,2,4-triazol-3-yl]-2-(propan-2-yl)phenyl dihydrogen phosphate
-
-
5-[1-[(6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoyl)(hexyl)amino]-2-[(1E)-butylideneamino]-2-oxoethyl]-2-(carboxymethoxy)benzoic acid
-
-
5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-4-[4-(morpholin-4-yl)phenyl]-1,2-oxazole-3-carboxamide
6-(4-benzylpiperazin-1-yl)-2-chloro-9H-purine
-
-
6-bromo-N-[4-(quinolin-3-yl)-9H-fluoren-9-yl]-1,8a-dihydropyrido[2,3-d]pyrimidine-5-carboxamide
-
-
6-chloro-9-[(3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
-
-
6-chloro-9-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
6-chloro-9-[(5-methoxy-4,6-dimethylpyridin-3-yl)methyl]-9H-purin-2-amine
6-[(2R)-2-[(5-fluoro-2-methoxyphenoxy)methyl]pyrrolidin-1-yl]-9H-purine
-
-
6-[5-[(benzyloxy)carbonyl]-4-(4-cyclohexylphenyl)-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
-
IC50 value about 0.12-0.2 mM
6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
-
IC50 value about 0.12-0.2 mM
7-[2,4-dichloro-6-[2-(1H-pyrazol-1-yl)ethoxy]phenyl][1,3]thiazolo[5,4-d]pyrimidin-5-amine
-
-
8-(2-chloro-3,4,5-trimethoxybenzyl)-2-fluoro-9-(pent-4-yn-1-yl)-9H-purin-6-amine
8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
8-[[5-(diethylamino)pentyl]amino]quinolin-6-ol
-
-
9-butyl-8-(3,4,5-trimethoxybenzyl)-9H-purin-6-amine
9-butyl-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-6-amine
9-[2-(tert-butylamino)ethyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
9-[2-[(2,2-dimethylpropyl)amino]ethyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
9-[3-(tert-butylamino)propyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
alvespimycin
-
-
Apg2
-
at high concentration (0.002 mM), Agp2 inhibits the ATPase activity of the enzyme
-
apoptozole
-
inhibits Hsc70 activity by binding to its ATPase domain
ATI3387
P07900; P08238
competitive inhibitor
cisplatin
-
-
CNF1010
-
-
cyclohexyl 5-[6-amino-8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9H-purin-9-yl]-L-norvalinate
-
-
cycloproparadicicol
deguelin
-
inhibits HSP90 by interacting with its ATP-binding pocket
desmethoxy-geldanamycin
diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
ethyl (4-[3-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-5-sulfanyl-4H-1,2,4-triazol-4-yl]benzyl)carbamate
-
-
ethyl 2-amino-4-(4-bromo-2-chloro-5-methoxyphenyl)-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidine-6-carboxylate
-
-
ethyl 4-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-6-methyl-2-oxo-1,2-dihydropyrimidine-5-carboxylate
-
-
geldanamycin
goniothalamin
Guanidinium chloride
-
approx. 50% uncompetitive inhibition above 0.5 mM
KW-2478
-
-
MDC-3100
P07900; P08238
competitive inhibitor
methyl (2E)-3-[2-amino-4-(1,3-dihydro-2H-isoindol-2-ylcarbonyl)quinazolin-6-yl]prop-2-enoate
-
-
methyl 4-(naphthalen-2-yl)-2-oxo-6-(phenoxymethyl)-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
IC50 value about 0.12 -0.2 mM
Mg2+
-
above 20 mM, approx. 50% inhibition at 100 mM
MPC-3100
-
-
mycograb
-
-
-
N-(4-acetylphenyl)-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
N-(4-acetylphenyl)-3-(5-chloro-2,4-dihydroxyphenyl)-4H-pyrazole-4-carboxamide
-
-
N-benzyl-6-(3-[[(2,6-dichloro-9H-purin-9-yl)acetyl]amino]-8-azabicyclo[3.2.1]oct-8-yl)pyridine-3-carboxamide
-
-
N-butyl-2,4-dihydroxy-5-[(5-hydroxy-1,3-dihydro-2H-isoindol-2-yl)carbonyl]benzamide
-
-
N-ethylmaleimide
-
5 mM, approx. 85% inhibition
N-[2-(dimethylamino)ethyl]-6-[3-[(4-methoxy-2-methylbenzoyl)amino]-8-azabicyclo[3.2.1]oct-8-yl]pyridine-3-carboxamide
-
-
N-[4-(3H-imidazo[4,5-c]pyridin-2-yl)-9H-fluoren-9-yl]quinoline-5-carboxamide
-
-
N-[4-(aminosulfonothioyl)benzyl]-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]thiophene-2-sulfonamide
-
-
NaCl
-
approx. 50% inhibition at 100 mM, approx. 90% inhibition at 600 mM
novobiocin
-
analogs
NVP-AUY922
P07900; P08238
competitive inhibitor
NVPHSP990
-
-
p23 protein
-
pochonin A
pochonin D
radamide
radester
radicicol
retaspimycin
-
IP-504
retaspimycin hydrochloride
P07900; P08238
competitive inhibitor
STA-1474
-
-
STA-9090
-
-
Sti1
-
co-chaperone, almost complete non-competitive inhibition at a 6fold excess of Sti1 in the presence of 80 mM KCL
-
Sti1 protein
-
-
-
tanespimycin
-
-
XL888
-
-
[(2R)-1-(5-chloro-2,4-dihydroxybenzoyl)pyrrolidin-2-yl](1,3-dihydro-2H-isoindol-2-yl)methanone
-
-
[1-(3-bromo-4-cyanophenyl)-2-oxo-2,4,5,6,7,7a-hexahydro-1H-indol-3-yl]acetic acid
-
-
[2,4-dihydroxy-5-(propan-2-yl)phenyl](5-[[methyl(piperidin-1-yl)amino]methyl]-1,3-dihydro-2H-isoindol-2-yl)methanone
-
AT-13387
[4-[(2S)-1-(5-chloro-2,4-dihydroxybenzoyl)pyrrolidin-2-yl]phenyl](3,3-difluoropyrrolidin-1-yl)methanone
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15-deoxyspergualin
activator of Hsp90 ATPase
-
Aha1, 5fold activation of intrinsic ATPase activity
-
aggregated alpha-casein
-
-
-
aggregated glucose-6-phosphate dehydrogenase
-
-
-
aggregated RepE
-
-
-
Aha1
P07900; P08238
potent activator of the ATPase subunit of the enzyme
-
Aha1 protein
-
-
-
Aha1p
-
potent stimulator of the enzyme ATPase activity
-
Apg2
-
at low concentration (0.0004 mM), Agp2 stimulates the ATPase activity of the enzyme
-
apo c
-
cytosolic precursor of cytochrome c
-
Asn-Asp-Leu-Leu-Leu-Thr-Gly
ATP-gammaS
Bacillus subtilis ClpC adaptor protein MecA
-
the refolding activity of SyClpC is enhanced 3fold in presence of Bacillus subtilis ClpC adaptor protein MecA
-
DnaJ
-
EhAha1c
co-chaperone Aha1, i.e. activator of Hsp90 ATPase, lacking a canonical Aha1 N-terminal domain compared to other Aha1 co-chaperones. EhAha1c is capable of binding and stimulating ATPase activity of EhHsp90. The Aha1 protein is characterized by the presence of two domains joined by a small linker, interaction analysis with the enzyme, overview
-
geranylgeraniol
-
presence of peptide NRLLLTG eliminates stimulatory effect
goniothalamin
GroES
-
required for the functioning of the Escherichia coli heat shock protein, also stimulates the reassembly
-
GrpE
-
Hep1
-
Hsp70 escort protein, interacts with mtHsp70 and is crucial for maintaining native mtHsp70 in its functional state, Hep1 is required for the folding of the ATPase domain of mtHsp70. Folding of mtHsp70 is impaired in mitochondria lacking Hep1
-
Hsc20
-
ISCU
-
the iron-sulfur cluster scaffold protein, the ATPase activity of mtHSP70 is accelerated by co-chaperone HSC20 and further accelerated by HSC20 plus scaffold protein ISCU. mtHSP70 binds preferentially to the D-state of ISCU and that HSC20 binds preferentially to the S-state of ISCU, detailed interaction analysis
-
kappa-casein
-
L-cysteine
-
stimulates 2fold
lambdaO
-
-
-
Nonidet P-40
-
-
NRLLLTG
-
peptide binding to the substrate-binding site. Stimulates ATPase activity, eliminates stimulatory effect of geranylgeraniol
poly-L-lysine
tamoxifen
unfolded protein
-
reduced carboxymethylated alpha-lactalbumin, 0.08 mM, 28% stimulation above intrinsic activity
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31
ADP
-
-
0.000019 - 11
ATP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00018 - 1.2
ATP
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
ATP
recombinant enzyme, pH 7.4, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
3-[(E)-[2-[(2-amino-6-methylpyrimidin-4-yl)ethynyl]benzylidene]amino]-1,3-oxazolidin-2-one
-
pH and temperature not specified in the publication
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000546 - 0.115
17-allylamino-17-demethoxygeldanamycin
0.0007
2,5-dichloro-N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]benzenesulfonamide
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.00009
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00074
4-chloro-6-(4-[4-[4-(methylsulfonyl)benzyl]piperazin-1-yl]-1H-pyrazol-3-yl)benzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.001
4-chloro-6-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.0089
4-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.0006
4-[4-(4-benzylpiperazin-1-yl)-1H-pyrazol-3-yl]-6-chlorobenzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.000028
5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1,2-oxazole-3-carboxamide
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.065 - 0.13
5-[1-[(6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoyl)(hexyl)amino]-2-[(1E)-butylideneamino]-2-oxoethyl]-2-(carboxymethoxy)benzoic acid
0.0003
6-chloro-9-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
6-chloro-9-[(5-methoxy-4,6-dimethylpyridin-3-yl)methyl]-9H-purin-2-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0046
8-(2-chloro-3,4,5-trimethoxybenzyl)-2-fluoro-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00028
8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000035
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.001 - 0.002
9-butyl-8-(3,4,5-trimethoxybenzyl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00018
9-butyl-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00014
9-[3-(tert-butylamino)propyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000028
diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000026
-
-
0.00086
purified recombinant enzyme, pH 7.5, 37°C
0.00167
-
purified recombinant enzyme, pH 7.5, 25°C, in absence of activators
0.00283
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.006 mM HSC20
0.0075
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.015 mM ISCU
0.025
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.004 mM HSC20 and 0.015 mM ISCU
0.412
purified recombinant enzyme, pH 7.4, temperature not specified in the publication
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
ATP hydrolysis
7.5 - 8.5
-
-
7.5 - 9
-
stimulated ATPase in presence of 0.5 mM ADP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9
-
no ATPase activity below pH 4.5
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 35
-
the refolding level is 2fold higher at 35°C than at 10°C
25
-
assay at
37 - 45
-
ATP hydrolysis
50 - 55
-
-
55
protein aggregate reactivation assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 45
-
approx. 12fold increase in reaction rate between 10°C and 15°C, approx. 4fold increase in reaction rate between 25°C and 35°C
15 - 37
-
-
25 - 37
-
2fold increase of ATPase activity at 37°C
25 - 70
-
approx. 64% of maximal activity at 40°C, approx. 50% of maximal activity at 65°C
34 - 47
-
about 60% of maximal activity at 34°C and at 47°C
4 - 37
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.97
sequence calculation
5.4
sequence calculation
6
-
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oat, var Ogle
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isoform BiP
-
-
Manually annotated by BRENDA team
chinese hamster
-
-
Manually annotated by BRENDA team
isoform Hsp90a
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
serovar Copenhageni
-
-
Manually annotated by BRENDA team
Leptospira interrogans Fiocruz L1-130
serovar Copenhageni
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
three isoforms of Hsp70
-
-
Manually annotated by BRENDA team
gene PnHSP70
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
tomato
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
Helicobacter pylori (cagA+, vacA+) and Hp (cagA-, vacA-) inhibit expression of HSP70 in gastric carcinoma MKN7 cells independently of the presence or absence of cagA genes
Manually annotated by BRENDA team
-
transcripts that differ slightly in size (2.8 and 2.9 kb) are present in heat-shocked mycelia. ONly the 2.8 kb transcripts are seen in vegetative mycelia and in mycelia undergoing antheridiol-induced differentiation. Two different hsp90 cDNAs are isolated and characterized. Although nearly identical, an additional eight nucleotide sequence is present at the end of the 3'UTP of one of the two cDNAs.Hsp90 transcripts lacking this sequence are present in vegetative mycelia and the levels of these transcripts increase in both heat-shocked and hormone-treated mycelia
Manually annotated by BRENDA team
-
knock-down of mortalin/mtHsp70 causes their growth arrest
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
three pea chloroplastic Hsp70 isoforms, of which two are soluble proteins located in the stroma, and one isoform, termed imsHsp70 isoform, is tightly associated to the outer membrane but not exposed at the outer surface of the chloroplasts
Manually annotated by BRENDA team
-
associated to on the matrix side
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BIP_APLCA
667
0
73698
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_ASHGO
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
674
1
73898
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_ASPAW
672
1
73459
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_ASPKA
672
1
73459
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_ASPNG
672
1
73459
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_BOVIN
655
0
72400
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_CANGA
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
667
1
73330
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_CHICK
652
0
72019
Swiss-Prot
Secretory Pathway (Reliability: 3)
BIP_CORAV
668
1
73564
Swiss-Prot
Secretory Pathway (Reliability: 2)
BIP_CRIGR
654
0
72379
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_DEBHA
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968)
683
1
74585
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_DROME
656
0
72261
Swiss-Prot
Secretory Pathway (Reliability: 2)
HS90A_BOVIN
733
0
84731
Swiss-Prot
other Location (Reliability: 1)
HS90A_CRIGR
733
0
84849
Swiss-Prot
other Location (Reliability: 1)
HS90A_HORSE
733
0
84770
Swiss-Prot
other Location (Reliability: 1)
HS90A_HUMAN
732
0
84660
Swiss-Prot
other Location (Reliability: 1)
HS90A_MACFA
733
0
84789
Swiss-Prot
other Location (Reliability: 1)
HS90A_MOUSE
733
0
84788
Swiss-Prot
other Location (Reliability: 1)
HS90A_PIG
733
0
84775
Swiss-Prot
other Location (Reliability: 1)
HS90A_RABIT
694
0
79733
Swiss-Prot
other Location (Reliability: 1)
HS90A_RAT
733
0
84815
Swiss-Prot
other Location (Reliability: 1)
SPA5L_BOVIN
767
0
82554
Swiss-Prot
other Location (Reliability: 2)
SPA5L_HUMAN
753
0
80710
Swiss-Prot
other Location (Reliability: 2)
SPA5L_MOUSE
747
0
80742
Swiss-Prot
other Location (Reliability: 1)
SPA5L_RAT
747
0
80414
Swiss-Prot
other Location (Reliability: 1)
SPA5L_XENTR
593
0
64731
Swiss-Prot
other Location (Reliability: 2)
SSB2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
613
0
66595
Swiss-Prot
other Location (Reliability: 2)
BIP_YARLI
Yarrowia lipolytica (strain CLIB 122 / E 150)
670
1
73524
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
682
1
74468
Swiss-Prot
Secretory Pathway (Reliability: 1)
SSB1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
613
0
66602
Swiss-Prot
other Location (Reliability: 2)
SSB1_ZYGRC
Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229)
613
0
66730
Swiss-Prot
other Location (Reliability: 2)
BIBH_CAEEL
657
0
72288
Swiss-Prot
Secretory Pathway (Reliability: 3)
HSP7M_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
666
0
72372
Swiss-Prot
Mitochondrion (Reliability: 1)
SSB1_ASHGO
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
613
0
66253
Swiss-Prot
other Location (Reliability: 2)
SSB1_CANAW
Candida albicans (strain WO-1)
613
0
66479
Swiss-Prot
other Location (Reliability: 2)
SSB1_CANGA
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
613
0
66396
Swiss-Prot
other Location (Reliability: 2)
SSB1_CHATD
Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
614
0
67030
Swiss-Prot
other Location (Reliability: 1)
SSB1_KLUDE
613
0
66428
Swiss-Prot
other Location (Reliability: 2)
SSB1_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
613
0
66244
Swiss-Prot
other Location (Reliability: 2)
SSB1_KLUMA
613
0
66087
Swiss-Prot
other Location (Reliability: 2)
SSB1_MAGO7
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
614
0
66666
Swiss-Prot
other Location (Reliability: 1)
SSB1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
613
0
67205
Swiss-Prot
other Location (Reliability: 2)
HSP7C_BOVIN
650
0
71241
Swiss-Prot
other Location (Reliability: 2)
HSP7C_CRIGR
646
0
70805
Swiss-Prot
other Location (Reliability: 2)
HSP7C_HORSE
646
0
70898
Swiss-Prot
other Location (Reliability: 2)
HSP7C_HUMAN
646
0
70898
Swiss-Prot
other Location (Reliability: 2)
HSP7C_MOUSE
646
0
70871
Swiss-Prot
other Location (Reliability: 2)
BIP_ECHGR
651
0
71921
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_ECHMU
649
0
71675
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_HORSE
15
0
1647
Swiss-Prot
other Location (Reliability: 1)
BIP_HUMAN
654
0
72333
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_ICTTR
654
0
72329
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
679
1
74448
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_MESAU
654
0
72379
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_MOUSE
655
0
72422
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
661
1
72332
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_PICAN
665
1
73222
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_PIG
262
0
28912
Swiss-Prot
other Location (Reliability: 2)
BIP_PLAFA
279
0
30657
Swiss-Prot
other Location (Reliability: 2)
BIP_PLAFO
655
0
72776
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_PONAB
654
0
72315
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_RAT
654
0
72347
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
663
1
73227
Swiss-Prot
Secretory Pathway (Reliability: 1)
BIP_XENLA
658
0
72635
Swiss-Prot
Secretory Pathway (Reliability: 1)
HSP7M_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
674
0
72977
Swiss-Prot
Mitochondrion (Reliability: 2)
HSP7Q_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
657
0
72365
Swiss-Prot
Mitochondrion (Reliability: 3)
AFG2H_CAEEL
724
0
79549
Swiss-Prot
other Location (Reliability: 3)
AFG2_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
809
0
88472
Swiss-Prot
Mitochondrion (Reliability: 3)
AFG2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
780
0
84748
Swiss-Prot
Mitochondrion (Reliability: 5)
BIP1_USTMA
Ustilago maydis (strain 521 / FGSC 9021)
660
1
71100
Swiss-Prot
Mitochondrion (Reliability: 2)
HSP77_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
654
0
70628
Swiss-Prot
Mitochondrion (Reliability: 2)
HSP77_YEASX
655
0
70800
Swiss-Prot
Mitochondrion (Reliability: 2)
HSP7C_PONAB
646
0
70868
Swiss-Prot
other Location (Reliability: 2)
HSP7C_RAT
646
0
70871
Swiss-Prot
other Location (Reliability: 2)
SPAT5_HUMAN
893
0
97904
Swiss-Prot
Mitochondrion (Reliability: 3)
SPAT5_MOUSE
893
0
97256
Swiss-Prot
Mitochondrion (Reliability: 5)
A0A8H3YZ47_VENIN
677
1
73627
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6P4L6_9EURO
671
1
73266
TrEMBL
Secretory Pathway (Reliability: 2)
A0A139HXS9_9PEZI
681
1
74586
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2G7G9B5_9EURO
671
1
73368
TrEMBL
Secretory Pathway (Reliability: 2)
J3KIQ8_COCIM
Coccidioides immitis (strain RS)
675
1
73843
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1E3IXY1_9TREE
671
1
73391
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2C5ZCW5_9HYPO
664
1
72890
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3E2HI09_SCYLI
670
1
73132
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CBK9_9BRAD
79
0
8518
TrEMBL
-
A0A507C6A2_9FUNG
1024
0
111496
TrEMBL
other Location (Reliability: 1)
A0A0D2DGP3_9EURO
679
1
74362
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D2A2I2_9PEZI
667
1
73363
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CBK5_9BRAD
79
0
8504
TrEMBL
-
A0A5N7AY01_9EURO
672
1
73448
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2K1QMY3_9PEZI
677
1
74035
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7X380_9HELO
671
1
73315
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M2TFE2_9EURO
675
1
73633
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7D8V666_9TREE
684
1
74741
TrEMBL
Mitochondrion (Reliability: 4)
A0A8H5MS48_9HYPO
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A420IMC5_9PEZI
676
1
73714
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H7B621_9PLEO
675
1
74139
TrEMBL
Secretory Pathway (Reliability: 3)
A0A167ICL8_9HYPO
665
1
72490
TrEMBL
Secretory Pathway (Reliability: 1)
S8DPM8_FOMPI
Fomitopsis pinicola (strain FP-58527)
655
1
71960
TrEMBL
Secretory Pathway (Reliability: 4)
A0A4S9DDR7_AURPU
671
1
73382
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Z1G2G8_9HELO
670
1
73086
TrEMBL
Secretory Pathway (Reliability: 1)
A1DFN8_NEOFI
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181)
672
1
73395
TrEMBL
Secretory Pathway (Reliability: 2)
A0A261Y4L6_9FUNG
661
1
72595
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6C1EB06_SACPS
683
1
74602
TrEMBL
Secretory Pathway (Reliability: 1)
A0A094AVJ9_9PEZI
669
1
73121
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6RF71_9PEZI
681
1
74489
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1Q2YGK0_9ASCO
669
1
73614
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4P9YYV2_9FUNG
665
0
73105
TrEMBL
Secretory Pathway (Reliability: 2)
A0A162ZD69_PHYB8
Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555)
653
0
71819
TrEMBL
Secretory Pathway (Reliability: 1)
G9NMR9_HYPAI
Hypocrea atroviridis (strain ATCC 20476 / IMI 206040)
662
1
72381
TrEMBL
Secretory Pathway (Reliability: 1)
A0A194WX47_9HELO
669
1
73299
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T4B5W7_9HYPO
664
1
72606
TrEMBL
Secretory Pathway (Reliability: 1)
J4G6Z1_9APHY
672
1
73531
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Y2DRH3_9PEZI
664
1
72570
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6JRT3_9PLEO
675
1
74083
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5C3LYJ7_9AGAR
675
1
73293
TrEMBL
Secretory Pathway (Reliability: 3)
C7GSQ6_YEAS2
Saccharomyces cerevisiae (strain JAY291)
682
1
74468
TrEMBL
Secretory Pathway (Reliability: 1)
W1QLJ9_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
665
1
73233
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T2PD92_CORCC
677
1
74218
TrEMBL
Secretory Pathway (Reliability: 4)
A0A6G1GVU2_9PEZI
682
1
74579
TrEMBL
Secretory Pathway (Reliability: 2)
A0A409XS62_PSICY
668
1
73485
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2S7XWA8_BEABA
665
1
72490
TrEMBL
Secretory Pathway (Reliability: 1)
M2QDB6_CERS8
Ceriporiopsis subvermispora (strain B)
677
1
74545
TrEMBL
Mitochondrion (Reliability: 5)
W6XXH4_COCCA
675
1
73855
TrEMBL
Secretory Pathway (Reliability: 4)
A0A084RKZ5_STACH
662
1
72389
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T0AIR9_RHOTO
601
0
65854
TrEMBL
Mitochondrion (Reliability: 4)
A0A1B7TCR0_9ASCO
679
1
75145
TrEMBL
Secretory Pathway (Reliability: 1)
F7W676_SORMK
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
645
1
70661
TrEMBL
Secretory Pathway (Reliability: 1)
K9FZ18_PEND1
Penicillium digitatum (strain Pd1 / CECT 20795)
673
1
73776
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1F8AFC4_9EURO
672
1
73408
TrEMBL
Secretory Pathway (Reliability: 2)
A0A093YS26_9PEZI
670
1
73217
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0U1LPA2_TALIS
673
1
73566
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4LBC0_9HYPO
663
1
72732
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y1W443_9FUNG
655
0
71895
TrEMBL
Secretory Pathway (Reliability: 1)
A0A166B655_9AGAM
672
1
72961
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5NB18_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A316UZZ1_9BASI
700
1
75556
TrEMBL
Mitochondrion (Reliability: 1)
A0A4S9Q6N6_AURPU
671
1
73383
TrEMBL
Secretory Pathway (Reliability: 1)
A0A366Q2V9_VERDA
666
1
72642
TrEMBL
Secretory Pathway (Reliability: 1)
J3NFN7_GAET3
Gaeumannomyces tritici (strain R3-111a-1)
663
1
72153
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3T9S5_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A364LTZ1_ASPFL
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A163L1D0_DIDRA
673
1
74071
TrEMBL
Secretory Pathway (Reliability: 3)
A0A4T0FUQ4_9BASI
654
1
71879
TrEMBL
Secretory Pathway (Reliability: 1)
B0XV51_ASPFC
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)
672
1
73385
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F7ZFL3_9HYPO
666
1
73110
TrEMBL
Secretory Pathway (Reliability: 1)
A7TJ69_VANPO
Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17)
685
1
74895
TrEMBL
Secretory Pathway (Reliability: 1)
A0A194S7K7_RHOGW
Rhodotorula graminis (strain WP1)
662
1
71736
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E4RLK7_9ASCO
679
1
74195
TrEMBL
Secretory Pathway (Reliability: 1)
A0A364N8H1_9PLEO
676
1
73988
TrEMBL
Secretory Pathway (Reliability: 3)
A0A397TVI8_9GLOM
659
1
73035
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6D6P7_ASPPA
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H5D662_9AGAR
683
1
74352
TrEMBL
Mitochondrion (Reliability: 3)
A0A8H7Z1K8_AJECA
676
1
73825
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1G4M772_LACFM
678
1
74267
TrEMBL
Secretory Pathway (Reliability: 1)
A0A177U8U2_9BASI
694
1
75807
TrEMBL
Mitochondrion (Reliability: 3)
A0A8F2VZ00_CANAR
657
0
72156
TrEMBL
Secretory Pathway (Reliability: 5)
A0A284RTV4_ARMOS
675
1
74394
TrEMBL
Mitochondrion (Reliability: 3)
A0A369JBW1_HYPMA
673
1
73160
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0D7BNB4_9AGAR
682
1
75431
TrEMBL
Mitochondrion (Reliability: 3)
A0A5J5F1T1_9PEZI
665
1
72930
TrEMBL
Secretory Pathway (Reliability: 1)
E9EQK1_METRA
Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075)
1099
1
120954
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4S2N6D5_9PEZI
664
1
72645
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6G1NVF1_VERDA
652
1
71090
TrEMBL
Secretory Pathway (Reliability: 1)
W9VFE8_9EURO
687
1
75186
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1B9GVP8_9TREE
680
1
74319
TrEMBL
Mitochondrion (Reliability: 5)
A0A0H2S4Q8_9AGAM
677
1
74313
TrEMBL
Secretory Pathway (Reliability: 4)
A0A6A6SU95_9PLEO
681
1
74904
TrEMBL
Secretory Pathway (Reliability: 3)
A0A6C1DW43_SACPS
682
1
74452
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2U9RAU7_PICKU
671
1
74052
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1U8QVL2_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
674
1
73697
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1B8GWC5_9PEZI
670
1
73137
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H2ZJN7_TRIPA
654
1
71521
TrEMBL
Secretory Pathway (Reliability: 1)
A0A346R8X7_EPICN
686
1
75209
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B8FWB0_9PEZI
669
1
73094
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6ZA01_9EURO
672
1
73406
TrEMBL
Secretory Pathway (Reliability: 2)
A0A179I5H2_CORDF
666
1
72703
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4JEC5_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5H295_9AGAR
674
1
73294
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H3NU05_9EURO
672
1
73435
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0C9YFZ5_9AGAR
672
1
74225
TrEMBL
Mitochondrion (Reliability: 5)
R4XDD6_TAPDE
Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 / NBRC 8474)
660
0
72138
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H7L1Z4_9AGAM
670
1
72797
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0A2JNX9_PENEN
673
1
73788
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7U309_9APHY
676
1
74078
TrEMBL
Secretory Pathway (Reliability: 3)
C4YJ74_CANAW
Candida albicans (strain WO-1)
687
1
74562
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3DD83_ARMGA
675
1
74340
TrEMBL
Mitochondrion (Reliability: 3)
A0A0B4HC13_METGA
Metarhizium guizhouense (strain ARSEF 977)
662
1
72733
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B9HM73_9TREE
680
1
74319
TrEMBL
Mitochondrion (Reliability: 5)
A0A439D7Y6_9PEZI
666
1
73125
TrEMBL
Secretory Pathway (Reliability: 1)
W4K2B1_HETIT
Heterobasidion irregulare (strain TC 32-1)
675
1
73367
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6G1IRP6_9PLEO
674
1
74247
TrEMBL
Secretory Pathway (Reliability: 3)
A0A372R452_9GLOM
656
0
73103
TrEMBL
Secretory Pathway (Reliability: 1)
I1C685_RHIO9
Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880)
660
1
72444
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4V5N863_9PEZI
688
1
75437
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1C7N2F6_9FUNG
658
1
72088
TrEMBL
Secretory Pathway (Reliability: 1)
F2SM79_TRIRC
Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892)
677
1
74137
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5M6C973_9TREE
680
1
73870
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P2H075_ASPFA
Aspergillus flavus (strain ATCC MYA-384 / AF70)
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1X2J109_9FUNG
661
1
72581
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3JMC5_WOLCO
Wolfiporia cocos (strain MD-104)
675
1
73984
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8H4BSK8_MUCCL
659
1
72291
TrEMBL
Secretory Pathway (Reliability: 1)
I1RYL5_GIBZE
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1)
663
1
72506
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5Q7YBA0_CANAR
676
1
74308
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2I1ENE0_9GLOM
652
1
72605
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F8V0S2_9EURO
671
1
73151
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1R1YDP9_9FUNG
666
1
73123
TrEMBL
Secretory Pathway (Reliability: 1)
A0A238FH90_9BASI
713
0
77743
TrEMBL
other Location (Reliability: 3)
A0A8H3EJK0_9LECA
676
1
73654
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2I1GR29_9GLOM
646
1
72374
TrEMBL
Secretory Pathway (Reliability: 1)
W6Z4I2_COCMI
675
1
73857
TrEMBL
Secretory Pathway (Reliability: 4)
A0A6A6HQN4_9PEZI
652
0
71227
TrEMBL
other Location (Reliability: 1)
C5GGS1_AJEDR
Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586)
678
1
73838
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3D8RMF5_9HELO
666
1
72758
TrEMBL
Secretory Pathway (Reliability: 1)
A0A135RPV0_9PEZI
664
1
72587
TrEMBL
Secretory Pathway (Reliability: 1)
A0A319AAB6_ASPLB
Aspergillus lacticoffeatus (strain CBS 101883)
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6KQS3_9PEZI
665
1
72661
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0L6VKS9_9BASI
666
0
72875
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1X6MNR8_9APHY
676
1
73962
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7S8I4W1_FUSPS
663
1
72520
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M7FS35_HORWE
688
1
75337
TrEMBL
Secretory Pathway (Reliability: 5)
A0A165NBA2_9APHY
675
1
73866
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5C3FJG9_PSEA2
689
1
74269
TrEMBL
Mitochondrion (Reliability: 2)
A0A3N4MBQ6_9PEZI
666
1
73397
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1G4J9K6_9SACH
678
1
73803
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1Y2GZ24_9FUNG
564
1
61327
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3BLB0_9AGAR
660
1
72218
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6J8D4A4_MYTCO
681
0
75091
TrEMBL
Mitochondrion (Reliability: 4)
A0A1Y2AI48_9FUNG
654
0
71586
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6J8EZS0_MYTCO
308
0
33988
TrEMBL
other Location (Reliability: 2)
A0A4S8LVY0_DENBC
Dendrothele bispora (strain CBS 962.96)
675
1
73651
TrEMBL
Secretory Pathway (Reliability: 3)
A0A015KGC4_RHIIW
Rhizophagus irregularis (strain DAOM 197198w)
652
1
72627
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CBI2_9BRAD
79
0
8525
TrEMBL
-
C5DMC8_LACTC
Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
678
1
74248
TrEMBL
Secretory Pathway (Reliability: 2)
A0A232M762_9EURO
675
1
73726
TrEMBL
Secretory Pathway (Reliability: 2)
A0A397SQC7_9GLOM
659
1
73032
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6ZX29_9PLEO
677
1
74093
TrEMBL
Secretory Pathway (Reliability: 3)
A0A6A5Q9Q8_AMPQU
676
1
74046
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1B7SBJ4_9ASCO
665
1
73222
TrEMBL
Secretory Pathway (Reliability: 1)
E6ZT14_SPORE
Sporisorium reilianum (strain SRZ2)
689
1
74379
TrEMBL
Mitochondrion (Reliability: 2)
A0A316YP60_9BASI
706
1
76112
TrEMBL
Mitochondrion (Reliability: 2)
A0A8H6SYJ1_9AGAR
848
0
92537
TrEMBL
other Location (Reliability: 2)
A0A4U6X8B1_9PEZI
667
1
72844
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0J6I1W7_COCPO
675
1
73816
TrEMBL
Secretory Pathway (Reliability: 2)
A0A371CX43_9APHY
664
1
73009
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6L045_9LECA
684
1
74738
TrEMBL
Secretory Pathway (Reliability: 1)
J8LM34_SACAR
Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644)
682
1
74536
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P7YDQ5_9PEZI
495
1
54635
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4T0WZV5_9ASCO
678
1
74751
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2K0U1D3_TRIHA
663
1
72503
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B8DBW6_9PEZI
670
1
73038
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E3Q9H5_LIPST
671
1
73380
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6S362_9PLEO
675
1
73982
TrEMBL
Secretory Pathway (Reliability: 4)
A0A7T6XGA8_PENDI
673
1
73776
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1W6S9W9_9HYME
67
0
7641
TrEMBL
other Location (Reliability: 1)
A0A1V6P1M5_PENPO
672
1
73702
TrEMBL
Secretory Pathway (Reliability: 2)
C4QZS3_KOMPG
Komagataella phaffii (strain GS115 / ATCC 20864)
678
1
74214
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4STF5_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A559MJX8_9HELO
671
1
73259
TrEMBL
Secretory Pathway (Reliability: 1)
A0A177D9G3_ALTAL
675
1
74139
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2W1HB60_9PLEO
634
1
69623
TrEMBL
Secretory Pathway (Reliability: 3)
A0A061HDD9_BLUGR
578
1
63285
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6WDW8_9PEZI
673
1
73869
TrEMBL
Secretory Pathway (Reliability: 2)
A0A370PA78_ASPPH
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1R1YF72_9FUNG
666
1
73220
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A5Z6P1_9PLEO
681
1
75194
TrEMBL
Mitochondrion (Reliability: 4)
A0A2R4QHD2_KARMI
140
0
14817
TrEMBL
other Location (Reliability: 3)
A0A8H5WN31_FUSHE
663
1
72505
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0G2ID67_9EURO
709
1
77556
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3L6NLN7_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A177W7B3_BATDL
Batrachochytrium dendrobatidis (strain JEL423)
650
1
70632
TrEMBL
Secretory Pathway (Reliability: 1)
A0A074YQL3_AURSE
Aureobasidium subglaciale (strain EXF-2481)
646
0
70549
TrEMBL
other Location (Reliability: 2)
A0A137QZR8_9AGAR
674
1
73191
TrEMBL
Secretory Pathway (Reliability: 3)
A0A369JWE8_HYPMA
687
1
75161
TrEMBL
Mitochondrion (Reliability: 3)
A0A5B0RK06_PUCGR
737
0
80892
TrEMBL
Mitochondrion (Reliability: 2)
A0A1Q8RLY2_9PEZI
664
1
72487
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2V1AIC6_9ASCO
1336
1
147900
TrEMBL
Secretory Pathway (Reliability: 1)
J6EVL4_TRIAS
Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654)
681
1
74075
TrEMBL
Mitochondrion (Reliability: 4)
A0A395N6G1_9HYPO
663
1
72538
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CBL3_9BRAD
79
0
8504
TrEMBL
-
F9WWJ1_ZYMTI
Zymoseptoria tritici (strain CBS 115943 / IPO323)
659
0
71817
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H4X893_9HYPO
664
1
72653
TrEMBL
Secretory Pathway (Reliability: 1)
K9FFL8_PEND2
Penicillium digitatum (strain PHI26 / CECT 20796)
673
1
73776
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H5BPN7_9AGAR
Tulosesus angulatus
718
1
78493
TrEMBL
Mitochondrion (Reliability: 2)
A0A8H7LV42_9AGAM
660
1
71828
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4P9WIC4_9FUNG
665
0
72376
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y2GNJ7_9FUNG
663
1
72082
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6F1U6_9PEZI
654
0
71288
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2U1JBD1_SMIAN
663
1
72921
TrEMBL
Secretory Pathway (Reliability: 2)
A0A370C5Z0_ASPNG
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A507FK48_9FUNG
660
0
72204
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4R0R8J8_9APHY
681
1
74558
TrEMBL
Secretory Pathway (Reliability: 4)
A0A507E5V4_9FUNG
668
1
72685
TrEMBL
Secretory Pathway (Reliability: 1)
A0A109FDJ5_9BASI
668
0
72841
TrEMBL
Mitochondrion (Reliability: 3)
A0A1Q5TDU4_9EURO
672
1
73341
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1L9TYG4_9EURO
673
1
73855
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0C3C8H3_HEBCY
678
1
74111
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0C2XJB3_HEBCY
676
1
73516
TrEMBL
Secretory Pathway (Reliability: 2)
G0V5E5_NAUCC
Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630)
683
1
74676
TrEMBL
Secretory Pathway (Reliability: 1)
G8YM05_PICSO
Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL Y-12695)
682
1
74273
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3HNQ1_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4T0HNX8_WALIC
654
1
71871
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A5ZWC3_9PLEO
675
1
74102
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0D2D945_9EURO
684
1
74888
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0J0XQ73_9TREE
684
1
75137
TrEMBL
Mitochondrion (Reliability: 4)
A0A5N6WG21_9EURO
672
1
73464
TrEMBL
Secretory Pathway (Reliability: 2)
A0A318YS69_ASPNB
Aspergillus neoniger (strain CBS 115656)
672
1
73431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y1Y404_9FUNG
656
1
71995
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y1YDD2_9FUNG
661
0
72606
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0P1L0Y9_9SACH
679
1
74418
TrEMBL
Secretory Pathway (Reliability: 3)
C4YC34_CLAL4
Clavispora lusitaniae (strain ATCC 42720)
678
1
74152
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6JXQ0_MONLA
670
1
73337
TrEMBL
Secretory Pathway (Reliability: 1)
W9CC31_SCLBF
Sclerotinia borealis (strain F-4128)
670
1
73124
TrEMBL
Secretory Pathway (Reliability: 1)
A0A421DBU2_9EURO
671
1
73160
TrEMBL
Secretory Pathway (Reliability: 2)
A0A427YBK9_9TREE
684
1
74887
TrEMBL
Mitochondrion (Reliability: 5)
A0A0A1V7A6_9HYPO
662
1
72671
TrEMBL
Secretory Pathway (Reliability: 1)
A0A316VU64_9BASI
658
0
71394
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C7MWT6_9SACH
682
1
74487
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1X2IX63_9FUNG
659
1
72349
TrEMBL
Secretory Pathway (Reliability: 1)
A0A077WLJ6_9FUNG
667
1
73502
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6FYS0_PETAA
672
1
73435
TrEMBL
Secretory Pathway (Reliability: 2)
B3LQ77_YEAS1
Saccharomyces cerevisiae (strain RM11-1a)
682
1
74468
TrEMBL
Secretory Pathway (Reliability: 1)
A0A099P3V3_PICKU
671
1
74066
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3FCH4_GIBZA
663
1
72506
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M7HX24_HORWE
688
1
75347
TrEMBL
Secretory Pathway (Reliability: 5)
A0A094DHT9_9PEZI
670
1
73233
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6H1RJ70_9TRYP
Endotrypanum sp
165
0
17941
TrEMBL
Secretory Pathway (Reliability: 5)
A0A428QVA4_9HYPO
663
1
72646
TrEMBL
Secretory Pathway (Reliability: 1)
M1VU60_CLAP2
Claviceps purpurea (strain 20.1)
1498
0
161795
TrEMBL
other Location (Reliability: 1)
A0A8H7NEZ4_BIOOC
584
1
63583
TrEMBL
Secretory Pathway (Reliability: 1)
G9ML11_HYPVG
Hypocrea virens (strain Gv29-8 / FGSC 10586)
663
1
72444
TrEMBL
Secretory Pathway (Reliability: 1)
A0A074WC76_9PEZI
672
1
73628
TrEMBL
Secretory Pathway (Reliability: 2)
A0A367XQ57_9ASCO
686
1
74755
TrEMBL
Secretory Pathway (Reliability: 1)
F4NSA1_BATDJ
Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211)
660
1
71851
TrEMBL
Secretory Pathway (Reliability: 1)
A0A427YIK1_9TREE
679
1
74040
TrEMBL
Mitochondrion (Reliability: 5)
A0A5C3DZM1_9BASI
689
1
74238
TrEMBL
Mitochondrion (Reliability: 2)
A0A1E3HC95_9TREE
674
1
73718
TrEMBL
Secretory Pathway (Reliability: 4)
A0A409WI94_9AGAR
1004
0
110014
TrEMBL
other Location (Reliability: 1)
A0A0F4GJS5_9PEZI
883
0
97620
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V6NNL8_PENDC
671
1
73299
TrEMBL
Secretory Pathway (Reliability: 1)
E9DYG4_METAQ
Metarhizium acridum (strain CQMa 102)
662
1
72733
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2S6CJU2_9PEZI
684
1
74541
TrEMBL
Secretory Pathway (Reliability: 5)
A0A319B5C4_ASPVC
Aspergillus vadensis (strain CBS 113365 / IMI 142717 / IBT 24658)
672
1
73431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2V1AR82_9ASCO
677
1
74100
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G4T022_RHIZD
651
1
71882
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1J9P197_9EURO
678
1
73882
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5N7DT35_9EURO
672
1
73345
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Y2CFK7_9FUNG
665
0
72896
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0A7CBH5_9BRAD
79
0
8518
TrEMBL
-
A0A0C3QKC8_9AGAM
670
1
73082
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7REN3_9FUNG
659
1
72349
TrEMBL
Secretory Pathway (Reliability: 1)
A0A162C1W4_PENCH
673
1
73730
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F2M4U6_SPOSC
671
1
73535
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4T0ISR8_WALIC
654
1
71855
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3G2S230_9BASI
673
1
73418
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7R8A4Y3_ASPKA
500
1
54647
TrEMBL
Secretory Pathway (Reliability: 1)
D5GM11_TUBMM
Tuber melanosporum (strain Mel28)
656
1
71711
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y1YPS5_9FUNG
654
1
72073
TrEMBL
Secretory Pathway (Reliability: 1)
A0A166M7C6_9PEZI
761
1
83277
TrEMBL
other Location (Reliability: 4)
I2JVW4_DEKBR
677
1
74300
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1L9R6P4_ASPWE
673
1
73570
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1V6RW01_9EURO
673
1
73839
TrEMBL
Secretory Pathway (Reliability: 2)
A0A177BZM0_9PLEO
675
1
74081
TrEMBL
Secretory Pathway (Reliability: 4)
A3LN25_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
681
1
73802
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1F5L709_9EURO
673
1
73998
TrEMBL
Secretory Pathway (Reliability: 2)
A0A428UJT7_9HYPO
663
1
72674
TrEMBL
Secretory Pathway (Reliability: 1)
F2RV54_TRIT1
Trichophyton tonsurans (strain CBS 112818)
677
1
74153
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3N4J258_9PEZI
684
1
74998
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6BXC2_9PEZI
664
0
72554
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D1YHM8_9EURO
679
1
74442
TrEMBL
Secretory Pathway (Reliability: 1)
A0A084FYZ1_PSEDA
664
1
72294
TrEMBL
Secretory Pathway (Reliability: 1)
D8J0N3_HERSS
Herbaspirillum seropedicae (strain SmR1)
123
0
13300
TrEMBL
-
A0A4Q4U343_9PEZI
665
1
72827
TrEMBL
Secretory Pathway (Reliability: 1)
P87028_PNECA
655
0
72502
TrEMBL
Secretory Pathway (Reliability: 1)
A0A146F7Z3_ASPKA
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6PYJ4_9EURO
673
1
73384
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1D2JNC6_PARBR
677
1
73876
TrEMBL
Secretory Pathway (Reliability: 1)
B0D8U9_LACBS
Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686)
672
1
73918
TrEMBL
Mitochondrion (Reliability: 5)
A0A0L8VMU8_9SACH
682
1
74468
TrEMBL
Secretory Pathway (Reliability: 1)
T0LT38_COLGC
Colletotrichum gloeosporioides (strain Cg-14)
666
1
72653
TrEMBL
Secretory Pathway (Reliability: 1)
G2QHD4_MYCTT
Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
662
1
72519
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2N1NJJ6_9GLOM
575
1
64515
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D2DK65_9EURO
688
1
75412
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H6SCY9_9AGAR
674
1
72983
TrEMBL
Secretory Pathway (Reliability: 2)
X8JBQ3_9AGAM
665
1
72113
TrEMBL
Secretory Pathway (Reliability: 1)
R7Z1X4_CONA1
Coniosporium apollinis (strain CBS 100218)
677
1
73998
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5C3E2E9_9BASI
689
1
74294
TrEMBL
Mitochondrion (Reliability: 2)
A0A6A6V421_9PLEO
677
1
74126
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H2DU72_ORBOL
673
1
73203
TrEMBL
Secretory Pathway (Reliability: 1)
A0A437AEJ2_9PEZI
672
1
73234
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y3NDL6_PIRSE
Piromyces sp. (strain E2)
663
0
72840
TrEMBL
Secretory Pathway (Reliability: 2)
A0A194UP87_9PEZI
666
1
72917
TrEMBL
Secretory Pathway (Reliability: 1)
G4UYV3_NEUT9
Neurospora tetrasperma (strain FGSC 2509 / P0656)
661
1
72332
TrEMBL
Secretory Pathway (Reliability: 1)
A0A067N792_PLEOS
673
1
73183
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7EMJ3_9FUNG
661
0
73005
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y2FBV5_PROLT
662
1
71737
TrEMBL
Secretory Pathway (Reliability: 1)
K1V9J6_TRIAC
Trichosporon asahii var. asahii (strain CBS 8904)
681
1
74075
TrEMBL
Mitochondrion (Reliability: 4)
A0A370TN82_9HELO
672
1
73726
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1L9VPQ6_ASPGL
672
1
73234
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0M8N9I1_9HYPO
666
1
72954
TrEMBL
Secretory Pathway (Reliability: 1)
G2YSM3_BOTF4
Botryotinia fuckeliana (strain T4)
670
1
73121
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Z1PDQ2_9PEZI
677
1
73915
TrEMBL
Secretory Pathway (Reliability: 1)
C9SSS1_VERA1
Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
666
1
72605
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5BNX0_9AGAR
Tulosesus angulatus
669
1
72691
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H3EBZ5_9AGAM
661
1
71887
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A5TSS2_9PLEO
673
1
73972
TrEMBL
Secretory Pathway (Reliability: 4)
A0A4S9XJ65_AURPU
671
1
73392
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4S9I0R6_AURPU
671
1
73397
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6G1L1B5_9PEZI
690
1
75506
TrEMBL
Mitochondrion (Reliability: 4)
A0A3N4I5X1_ASCIM
653
0
71429
TrEMBL
Secretory Pathway (Reliability: 1)
H2B0M3_KAZAF
Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 / NRRL Y-8276)
718
1
78973
TrEMBL
other Location (Reliability: 4)
A0A8H8A7K1_9ASCO
1278
0
142595
TrEMBL
Mitochondrion (Reliability: 5)
A0A4P9XAZ2_9FUNG
663
0
72200
TrEMBL
Secretory Pathway (Reliability: 1)
A0A015K0B4_RHIIW
Rhizophagus irregularis (strain DAOM 197198w)
413
1
46299
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2C5XBC5_9HYPO
666
1
72569
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2V1BPR3_9HELO
671
1
73362
TrEMBL
Secretory Pathway (Reliability: 1)
A0A346R8X8_EPICN
664
1
72743
TrEMBL
Secretory Pathway (Reliability: 1)
A0A136JI23_9PEZI
664
1
72855
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B9INC9_9TREE
679
1
74261
TrEMBL
Mitochondrion (Reliability: 5)
A0A550C8E4_9AGAR
660
0
71807
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Y2EQ42_9FUNG
662
0
72743
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0G2FQD7_9PEZI
669
1
73208
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H3P6S6_9EURO
671
1
73306
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7J6JQ88_COLFN
Colletotrichum fructicola (strain Nara gc5)
664
1
72465
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Z1JP27_9HELO
670
1
73104
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B2JHD1_PICPA
677
1
74127
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M7MM62_9EURO
675
1
73878
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E3P031_WICAA
Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8)
674
1
73685
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5C3KZB1_9AGAR
693
1
76234
TrEMBL
Mitochondrion (Reliability: 3)
A0A899G2P6_9ASCO
1021
0
113933
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8H4QE84_9HYPO
663
1
72698
TrEMBL
Secretory Pathway (Reliability: 1)
A0A202G9I1_CLALS
678
1
74152
TrEMBL
Secretory Pathway (Reliability: 1)
H6CAK8_EXODN
Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656)
682
1
74693
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2S4PTU4_9PEZI
673
1
73693
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4S3JRW0_9EURO
672
1
73193
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6G1MB71_ORBOL
673
1
73153
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4H6D9_9EURO
672
1
73397
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0I9XPI4_GIBFU
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A179G817_METCM
664
1
72454
TrEMBL
Secretory Pathway (Reliability: 1)
G0W7Y0_NAUDC
Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639)
685
1
74762
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2I1GCC1_9GLOM
652
1
72456
TrEMBL
Secretory Pathway (Reliability: 1)
W9ZNG5_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8E2JBK2_9PEZI
681
1
74378
TrEMBL
Secretory Pathway (Reliability: 2)
A0A854Q2U0_CRYNV
742
2
81380
TrEMBL
Mitochondrion (Reliability: 4)
A0A4Q4R2J2_9PLEO
675
1
74084
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1L9SE54_9EURO
674
1
73790
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4Q4SYI5_9PEZI
665
1
72932
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7D8USD8_9HELO
670
1
73298
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4Y6F8_9HYPO
663
1
72525
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E5RYD7_HANUV
680
1
75197
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4R2U2_9AGAR
682
1
74449
TrEMBL
Mitochondrion (Reliability: 3)
A0A2H1FLZ3_ZYMTR
683
1
74543
TrEMBL
Secretory Pathway (Reliability: 5)
A0A150UZY5_9PEZI
664
0
72891
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6G1KNA8_9PLEO
674
1
73861
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5C3QGW2_9AGAR
673
1
73040
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H4KQX7_9HYPO
664
1
72620
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T6ZET1_TUBBO
656
1
71645
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4BYJ9_YEASX
682
1
74468
TrEMBL
Secretory Pathway (Reliability: 1)
A0A017SF25_9EURO
672
1
73357
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6J8EY72_MYTCO
342
0
37868
TrEMBL
Secretory Pathway (Reliability: 1)
M9LZJ5_PSEA3
Pseudozyma antarctica (strain T-34)
1134
1
121699
TrEMBL
other Location (Reliability: 1)
A0A4V1Y0F0_9PEZI
665
1
72889
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B4FPC4_METAF
Metarhizium anisopliae (strain ARSEF 549)
662
1
72685
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5C3MGN1_9AGAR
680
1
74804
TrEMBL
Mitochondrion (Reliability: 2)
A0A6A6ZL40_9PLEO
667
1
73529
TrEMBL
Secretory Pathway (Reliability: 3)
A0A4U0XV95_9PEZI
691
1
75699
TrEMBL
Secretory Pathway (Reliability: 5)
A0A074RQQ0_9AGAM
667
1
72258
TrEMBL
Secretory Pathway (Reliability: 1)
A0A024S561_HYPJR
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
664
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A5X9A3_9PLEO
681
1
74814
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8J5Q4U3_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A022XQZ0_TRISD
676
1
74024
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C9XWX8_9AGAR
676
1
73427
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0A7CC81_9BRAD
79
0
8518
TrEMBL
-
A6ZPU2_YEAS7
Saccharomyces cerevisiae (strain YJM789)
682
1
74468
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3DTZ9_ARMGA
660
1
72248
TrEMBL
Secretory Pathway (Reliability: 2)
C1GRW7_PARBA
Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01)
677
1
73835
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2S4L7P5_9HYPO
647
1
70879
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1X7RFK7_ZYMTR
683
1
74577
TrEMBL
Mitochondrion (Reliability: 5)
A0A0L0N1Y2_TOLOC
Tolypocladium ophioglossoides (strain CBS 100239)
664
1
72885
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C9SX40_PLICR
666
0
72606
TrEMBL
Secretory Pathway (Reliability: 1)
F8PMM3_SERL3
Serpula lacrymans var. lacrymans (strain S7.3)
672
1
73472
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2C5X6Z5_9PEZI
666
1
72727
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0W4ZBG4_PNEC8
Pneumocystis carinii (strain B80)
655
0
72506
TrEMBL
Secretory Pathway (Reliability: 1)
E2LZB1_MONPE
Moniliophthora perniciosa (strain FA553 / isolate CP02)
612
0
67656
TrEMBL
other Location (Reliability: 2)
A0A7U2ICI6_PHANO
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173)
532
1
58048
TrEMBL
Secretory Pathway (Reliability: 3)
A0A117NPJ3_9EURO
672
1
73716
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0D0WXX2_9TREE
744
1
82095
TrEMBL
Secretory Pathway (Reliability: 4)
A0A4Z1G8Z4_9HELO
670
1
73104
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1G4AR91_9PEZI
664
1
72583
TrEMBL
Secretory Pathway (Reliability: 1)
U9UA52_RHIID
Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
658
1
73035
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0S7DT56_9EURO
671
1
73243
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4Q9NZP2_9APHY
672
1
73644
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0W7VX65_9HYPO
662
1
72331
TrEMBL
Secretory Pathway (Reliability: 1)
W9KDS8_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V6YC82_PENNA
673
1
73857
TrEMBL
Secretory Pathway (Reliability: 2)
A0A067MHA6_9AGAM
662
1
72145
TrEMBL
Secretory Pathway (Reliability: 2)
Q2ULV1_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H4CU00_COLGL
666
1
72623
TrEMBL
Secretory Pathway (Reliability: 1)
Q0CJU4_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
672
1
73416
TrEMBL
Secretory Pathway (Reliability: 2)
G3YCR7_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6GDV4_9PEZI
679
1
74323
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4Q4U2D0_9PEZI
665
1
72962
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Q5Q7Z3_9EURO
673
1
73571
TrEMBL
Secretory Pathway (Reliability: 1)
A0A517LB40_9PEZI
676
1
73544
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E3HCV0_9TREE
531
1
58091
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1M2W4E6_TRAPU
671
1
73456
TrEMBL
Secretory Pathway (Reliability: 3)
C5M618_CANTT
Candida tropicalis (strain ATCC MYA-3404 / T1)
686
1
74636
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6QQR8_9PEZI
678
1
74056
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2B7ZM72_9EURO
675
1
73651
TrEMBL
Secretory Pathway (Reliability: 1)
A0A151GD43_9HYPO
664
1
72662
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4VT53_9HELO
1606
1
174077
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D1ZAY3_EXOME
678
1
74475
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B1R2N6_9AGAM
677
1
73699
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1S7HJ36_9SACH
673
1
73560
TrEMBL
Secretory Pathway (Reliability: 1)
G9FXE9_9PLEO
676
1
74203
TrEMBL
Secretory Pathway (Reliability: 3)
A0A061AQG2_CYBFA
668
1
73099
TrEMBL
Secretory Pathway (Reliability: 1)
A0A177TQ29_9BASI
694
1
75807
TrEMBL
Mitochondrion (Reliability: 3)
A0A2T0FIR7_9ASCO
665
1
72904
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Z5T6P8_HORWE
688
1
75338
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2X0N0Z9_9BASI
655
0
71806
TrEMBL
other Location (Reliability: 4)
A0A015J6X3_RHIIW
Rhizophagus irregularis (strain DAOM 197198w)
658
1
73035
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0H1BC36_9EURO
679
1
74006
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5IC58_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A8NJP4_COPC7
Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
655
1
71892
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0W4ZGR4_PNEJ7
Pneumocystis jirovecii (strain RU7)
691
0
76379
TrEMBL
other Location (Reliability: 5)
V5EVW5_KALBG
Kalmanozyma brasiliensis (strain GHG001)
690
1
74469
TrEMBL
Mitochondrion (Reliability: 2)
B8LYJ0_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
675
1
73584
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1S8VYF4_9FUNG
718
3
78773
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2S5B6V5_9BASI
663
1
72390
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0M9WIR4_9EURO
673
1
73787
TrEMBL
Secretory Pathway (Reliability: 2)
A0A066WE10_TILAU
Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951)
694
1
75387
TrEMBL
Mitochondrion (Reliability: 1)
A0A3M2SB71_9HYPO
663
1
72674
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8E2DN44_9APHY
676
1
74409
TrEMBL
Secretory Pathway (Reliability: 5)
A0A4S4LJG3_9AGAM
653
1
71142
TrEMBL
Secretory Pathway (Reliability: 1)
A0A177F9X8_9EURO
684
1
74878
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2J6QXS4_9HELO
670
1
72995
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y1VNP8_9FUNG
662
0
72725
TrEMBL
Secretory Pathway (Reliability: 2)
A0A428RGJ0_9HYPO
663
1
72674
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396JQ46_MEDTR
349
0
39473
TrEMBL
other Location (Reliability: 5)
A0A8H5EJZ2_FUSOX
403
1
44435
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V8UEM0_9PEZI
664
0
72539
TrEMBL
other Location (Reliability: 4)
O00053_9ASCO
652
1
72346
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F7SXV6_PHARH
661
1
71778
TrEMBL
Secretory Pathway (Reliability: 2)
S8A9Q8_DACHA
Dactylellina haptotyla (strain CBS 200.50)
672
1
73042
TrEMBL
Secretory Pathway (Reliability: 1)
A0A317XSZ0_9BASI
690
1
74457
TrEMBL
Mitochondrion (Reliability: 2)
M2U4D6_COCH5
Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O)
675
1
73923
TrEMBL
Secretory Pathway (Reliability: 4)
A0A316U1F3_9BASI
693
1
75409
TrEMBL
Mitochondrion (Reliability: 2)
A0A2I2FL41_9EURO
671
1
73065
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5TZI4_GIBCI
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A316ZDL6_9BASI
681
1
73507
TrEMBL
Secretory Pathway (Reliability: 1)
A0A229W7Q9_ASPFM
672
1
73385
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7D9GZB7_DEKBR
677
1
74300
TrEMBL
Secretory Pathway (Reliability: 1)
A0A179GCA7_PURLI
664
1
72561
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A5ZEZ3_9PLEO
682
1
74790
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2T4AH05_TRIHA
663
1
72560
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N7AFL1_9EURO
671
1
73313
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8A1MKD4_AJECA
676
1
73843
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N5PU72_9PEZI
664
1
72399
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H7DIC8_9AGAR
668
1
72751
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3A2Z353_9EURO
672
1
73496
TrEMBL
Secretory Pathway (Reliability: 2)
A0A430M2Z5_9HYPO
663
1
72674
TrEMBL
Secretory Pathway (Reliability: 1)
Q9P8E1_PIRSE
Piromyces sp. (strain E2)
348
0
38609
TrEMBL
other Location (Reliability: 1)
A0A421JQF7_9ASCO
1367
1
153200
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D7B0L8_9AGAR
660
0
71607
TrEMBL
Secretory Pathway (Reliability: 1)
A0A094FHU7_9PEZI
670
1
73130
TrEMBL
Secretory Pathway (Reliability: 1)
D4ALR8_ARTBC
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
790
1
86827
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3M7MN74_9EURO
672
1
73801
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D9P6X4_METAN
662
1
72671
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M7FGP2_HORWE
577
1
63125
TrEMBL
Secretory Pathway (Reliability: 5)
A0A6H1RL45_LEIBR
111
0
11851
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8H5Y269_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A166X3D0_9PEZI
750
1
82030
TrEMBL
other Location (Reliability: 3)
A0A0C9MDS9_9FUNG
659
1
72293
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H3BT71_9AGAM
418
1
45625
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1W2TV33_ROSNE
665
1
73023
TrEMBL
Secretory Pathway (Reliability: 1)
A0A168IAC2_CORDF
666
1
72616
TrEMBL
Secretory Pathway (Reliability: 1)
R8BWF8_PHAM7
Phaeoacremonium minimum (strain UCR-PA7)
666
1
72941
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C2S6B6_AMAMK
Amanita muscaria (strain Koide BX008)
673
1
74014
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0A2VVP4_BEABA
665
1
72490
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2V5JI14_9EURO
673
1
73402
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0L0HE34_SPIPD
Spizellomyces punctatus (strain DAOM BR117)
746
1
81480
TrEMBL
Mitochondrion (Reliability: 5)
E4V4P9_ARTGP
Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893)
676
1
73766
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E3NII5_9ASCO
670
1
73672
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6J8BRS7_MYTCO
558
0
63960
TrEMBL
other Location (Reliability: 2)
A0A8H7PY47_9FUNG
664
1
72613
TrEMBL
Secretory Pathway (Reliability: 1)
M2MRK1_BAUPA
Baudoinia panamericana (strain UAMH 10762)
668
0
73024
TrEMBL
Secretory Pathway (Reliability: 1)
N1JD65_BLUG1
Blumeria graminis f. sp. hordei (strain DH14)
653
0
71453
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7R7VXD3_ASPCH
672
1
73259
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Y2IRD5_PYCCO
711
0
77763
TrEMBL
Secretory Pathway (Reliability: 1)
A0A346R8X9_EPICN
664
1
72758
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H3J0D3_9EURO
673
1
73547
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1T3CLQ6_9HYPO
663
1
72560
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0J5PMH5_ASPFM
672
1
73385
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4S4K5Z2_9APHY
Hermanssonia centrifuga
964
0
106341
TrEMBL
other Location (Reliability: 1)
A0A4U0TWU6_9PEZI
Salinomyces thailandica
688
1
75252
TrEMBL
Secretory Pathway (Reliability: 4)
M3JFH1_CANMX
Candida maltosa (strain Xu316)
687
1
74535
TrEMBL
Secretory Pathway (Reliability: 1)
L2FLM9_COLFN
Colletotrichum fructicola (strain Nara gc5)
668
1
72940
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8E0QI58_9EURO
672
1
73454
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H8NJY6_9AGAM
662
1
72136
TrEMBL
Secretory Pathway (Reliability: 2)
Q56D08_PICPA
678
1
74214
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H7J7S0_9PLEO
672
1
73944
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H5F460_9AGAR
685
1
74883
TrEMBL
Mitochondrion (Reliability: 2)
A0A061AMC0_RHOTO
663
1
71941
TrEMBL
Secretory Pathway (Reliability: 1)
B9WAG1_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
685
1
74369
TrEMBL
Secretory Pathway (Reliability: 1)
A0A395I935_ASPHC
Aspergillus homomorphus (strain CBS 101889)
673
1
73400
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5C3MQS7_9AGAM
669
1
73420
TrEMBL
Secretory Pathway (Reliability: 2)
A0A059JA14_TRIIM
Trichophyton interdigitale (strain MR816)
611
0
67164
TrEMBL
other Location (Reliability: 2)
A0A7H9HX36_9SACH
681
1
74416
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P5HMJ7_9PEZI
665
1
72823
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6F5S8_9EURO
671
1
73375
TrEMBL
Secretory Pathway (Reliability: 2)
A0A060S7E6_PYCCI
1043
1
114556
TrEMBL
Secretory Pathway (Reliability: 3)
H8WXM9_CANO9
Candida orthopsilosis (strain 90-125)
683
1
74431
TrEMBL
Secretory Pathway (Reliability: 1)
M7SAS9_EUTLA
Eutypa lata (strain UCR-EL1)
666
1
72850
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7C8IUR7_9PEZI
634
1
69605
TrEMBL
Secretory Pathway (Reliability: 1)
A0A094HCL8_9PEZI
669
1
73064
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1X0QQG2_RHIZD
660
1
72778
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q4MAG0_9PLEO
675
1
74018
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2N0Q7Y0_9GLOM
658
1
73035
TrEMBL
Secretory Pathway (Reliability: 1)
N4XAW2_COCH4
Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T)
675
1
73923
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0C3FS01_PILCF
Piloderma croceum (strain F 1598)
663
0
72197
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8G1VMA0_9EURO
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1L7WI73_9HELO
671
1
73441
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T5M7B9_9EURO
671
1
73151
TrEMBL
Secretory Pathway (Reliability: 2)
G7XAE1_ASPKW
Aspergillus kawachii (strain NBRC 4308)
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5Q4BVU2_9PEZI
664
1
72565
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2J5HMI4_9EURO
653
1
71053
TrEMBL
Secretory Pathway (Reliability: 1)
A0A367KWN2_RHIST
659
1
72236
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6V8QMN0_9HYPO
662
1
72415
TrEMBL
Secretory Pathway (Reliability: 1)
A0A553I600_9PEZI
666
1
73165
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B9I8L7_9TREE
679
1
74164
TrEMBL
Secretory Pathway (Reliability: 5)
R9P7F2_PSEHS
Pseudozyma hubeiensis (strain SY62)
690
1
74314
TrEMBL
Mitochondrion (Reliability: 2)
C8ZBH9_YEAS8
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
682
1
74452
TrEMBL
Secretory Pathway (Reliability: 1)
A0A164QCR3_9AGAM
674
1
73617
TrEMBL
Secretory Pathway (Reliability: 5)
A0A443I6R8_BYSSP
669
1
73062
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E3JH55_9TREE
671
1
73306
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1B9FZY8_9TREE
679
1
74076
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2S4VUS8_9BASI
682
0
75270
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2V5HBB1_ASPV1
Aspergillus violaceofuscus (strain CBS 115571)
673
1
73432
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1S9RG19_PENBI
672
1
73429
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H6TL76_MYCCL
672
1
72789
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H3CVQ8_9AGAM
659
1
71829
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H2XKH1_9AGAM
665
1
72113
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7H9AWC1_ZYGMR
681
1
74677
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D2ABL3_9EURO
685
1
74967
TrEMBL
Secretory Pathway (Reliability: 3)
A0A4S9E910_AURPU
671
1
73395
TrEMBL
Secretory Pathway (Reliability: 1)
K2RDV3_MACPH
Macrophomina phaseolina (strain MS6)
672
1
73592
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0A7CBG8_9BRAD
79
0
8518
TrEMBL
-
A0A2I0RU78_9PEZI
672
1
73245
TrEMBL
Secretory Pathway (Reliability: 5)
S3CZS4_GLAL2
Glarea lozoyensis (strain ATCC 20868 / MF5171)
672
1
73523
TrEMBL
Secretory Pathway (Reliability: 1)
R0K559_SETT2
Setosphaeria turcica (strain 28A)
674
1
73861
TrEMBL
Secretory Pathway (Reliability: 4)
N1QKS6_SPHMS
Sphaerulina musiva (strain SO2202)
684
1
74450
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8H3XYM7_ASPTU
672
1
73431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A395SYR1_9HYPO
663
1
72479
TrEMBL
Secretory Pathway (Reliability: 1)
E3QX97_COLGM
Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212)
664
1
72671
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C9ZIH3_9AGAM
654
1
71439
TrEMBL
Secretory Pathway (Reliability: 1)
A0A167KHU8_METRR
Metarhizium rileyi (strain RCEF 4871)
668
1
73230
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D2LJB2_HYPSF
Hypholoma sublateritium (strain FD-334 SS-4)
696
1
75659
TrEMBL
Mitochondrion (Reliability: 4)
A0A317V7N1_9EURO
643
1
70431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y2EVC7_9FUNG
662
0
72759
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1E1M2H5_RHYSE
671
1
73198
TrEMBL
Secretory Pathway (Reliability: 1)
Q2GS48_CHAGB
Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970)
661
1
72265
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6AK21_9HELO
670
1
73092
TrEMBL
Secretory Pathway (Reliability: 1)
W7EPZ9_COCVI
675
1
73855
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0B7FKV5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
660
1
71767
TrEMBL
Secretory Pathway (Reliability: 1)
G1XSH8_ARTOA
Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
672
1
73021
TrEMBL
Secretory Pathway (Reliability: 1)
A0A433QW80_9FUNG
635
0
69904
TrEMBL
Secretory Pathway (Reliability: 5)
A2QW80_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C9W302_9AGAM
678
1
73993
TrEMBL
Secretory Pathway (Reliability: 5)
A0A6G1FVN0_9PEZI
688
1
75299
TrEMBL
Mitochondrion (Reliability: 2)
A0A8H5XH30_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
C7Z550_FUSV7
Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4)
656
0
71926
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E3B2I5_9EURO
671
1
73022
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6P8B3S9_MAGGR
665
1
72436
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8J8WKD9_9EURO
672
1
73369
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1X2H8F5_SYNRA
625
0
68703
TrEMBL
other Location (Reliability: 1)
T5AQC8_OPHSC
Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243)
667
1
73124
TrEMBL
Secretory Pathway (Reliability: 1)
C5DQE5_ZYGRC
Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229)
673
1
73549
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H8RNP6_9HELO
670
1
73246
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H2W496_9HELO
668
1
73075
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0M9VQC0_9BASI
670
1
72929
TrEMBL
Secretory Pathway (Reliability: 1)
I3RV96_DUNSA
696
0
79589
TrEMBL
other Location (Reliability: 4)
A0A0A7CBV3_9BRAD
79
0
8504
TrEMBL
-
A0A4Y9Z9J3_9AGAM
658
1
71686
TrEMBL
Secretory Pathway (Reliability: 1)
M5FXW7_DACPD
Dacryopinax primogenitus (strain DJM 731)
671
1
73721
TrEMBL
Secretory Pathway (Reliability: 3)
A0A420H8F9_9PEZI
632
0
69223
TrEMBL
other Location (Reliability: 4)
A0A6A5UMU0_9PLEO
676
1
74355
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5M8PWI2_9LECA
674
1
73598
TrEMBL
Secretory Pathway (Reliability: 1)
A0A165KVL8_EXIGL
680
1
74314
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2X0M4V3_9BASI
677
0
73790
TrEMBL
other Location (Reliability: 2)
A0A8H6I8Z0_9AGAR
Tulosesus angulatus
627
1
68843
TrEMBL
Mitochondrion (Reliability: 2)
A0A1Y2UGN6_9PEZI
664
1
72835
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3D8SGX0_9HELO
666
1
72795
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5LR27_9AGAR
694
1
75900
TrEMBL
Secretory Pathway (Reliability: 5)
A0A6A4I927_9AGAR
703
1
77669
TrEMBL
Mitochondrion (Reliability: 2)
A0A0J8QP36_COCIT
499
1
54635
TrEMBL
Secretory Pathway (Reliability: 2)
W7LS95_GIBM7
Gibberella moniliformis (strain M3125 / FGSC 7600)
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5ZYG0_ASPBU
672
1
73449
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3N4L203_9PEZI
665
1
72680
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H7PUA2_MORIS
665
1
72867
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6UDX9_9PEZI
680
1
74383
TrEMBL
Secretory Pathway (Reliability: 3)
V2XBC3_MONRO
Moniliophthora roreri (strain MCA 2997)
810
2
89662
TrEMBL
Mitochondrion (Reliability: 4)
A0A1Y2I3Y1_9FUNG
681
1
74172
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A7BZE1_9PEZI
664
1
72597
TrEMBL
Secretory Pathway (Reliability: 1)
A0A319DTK2_9EURO
672
1
73270
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6N4I3_9PEZI
665
1
72661
TrEMBL
Secretory Pathway (Reliability: 1)
A6RA17_AJECN
Ajellomyces capsulatus (strain NAm1 / WU24)
677
1
74319
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8J5C345_9ASCO
671
1
73587
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Y9ZXA4_9AGAM
655
1
71119
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0S6XF77_BLOB1
Fungal sp. (strain No.11243)
677
1
74061
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1E1KA60_9HELO
671
1
73198
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y2B7A7_9TREE
676
1
74106
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8H8RPH0_9HELO
671
1
73210
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E4TR60_PACTA
662
1
72501
TrEMBL
Secretory Pathway (Reliability: 1)
F9FL45_FUSOF
Fusarium oxysporum (strain Fo5176)
663
1
72593
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4U0V804_9PEZI
688
1
75474
TrEMBL
Mitochondrion (Reliability: 5)
A0A6A6HWJ2_9PLEO
678
1
74619
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8J2T748_ZYGB2
Zygosaccharomyces bailii (strain CLIB 213 / ATCC 58445 / CBS 680 / BCRC 21525 / NBRC 1098 / NCYC 1416 / NRRL Y-2227)
673
1
73560
TrEMBL
Secretory Pathway (Reliability: 1)
A0A060T8H6_BLAAD
664
1
72605
TrEMBL
Secretory Pathway (Reliability: 1)
A0A292PSZ9_9PEZI
666
1
72845
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2U3EM60_PURLI
1093
1
120887
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E4STI2_9ASCO
671
1
73969
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1R0GT76_9FUNG
674
0
73935
TrEMBL
Secretory Pathway (Reliability: 1)
B2ART7_PODAN
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
663
1
72334
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1L7V6T4_FUSPR
Fusarium proliferatum (strain ET1)
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5RXK0_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4LSI1_9HYPO
667
1
73124
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CCM3_9BRAD
79
0
8518
TrEMBL
-
A0A4S4L704_9AGAM
682
1
74600
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0A7CCM6_9BRAD
79
0
8518
TrEMBL
-
A0A2N1MPQ0_9GLOM
658
1
73075
TrEMBL
Secretory Pathway (Reliability: 1)
A0A175WAG9_9PEZI
665
1
72343
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0L1J4W2_ASPNO
672
1
73389
TrEMBL
Secretory Pathway (Reliability: 2)
A0A225XER9_CRYNV
742
2
81406
TrEMBL
Mitochondrion (Reliability: 4)
A0A0K1W3I4_9METZ
483
0
53147
TrEMBL
other Location (Reliability: 1)
A0A7C8L6M1_TALMA
675
1
73568
TrEMBL
Secretory Pathway (Reliability: 1)
A0A074XNR6_AURPU
671
1
73354
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B7N6U8_9FUNG
653
1
71809
TrEMBL
Secretory Pathway (Reliability: 1)
A0A177A3A4_9PEZI
669
1
73063
TrEMBL
Secretory Pathway (Reliability: 1)
J5JYV0_BEAB2
Beauveria bassiana (strain ARSEF 2860)
665
1
72504
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A5W2U1_9PLEO
679
1
74564
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0A7CBV5_9BRAD
78
0
8386
TrEMBL
-
A0A8H3I8Y9_9LECA
670
1
73213
TrEMBL
Secretory Pathway (Reliability: 1)
V5I0Q7_BYSSN
Byssochlamys spectabilis (strain No. 5 / NBRC 109023)
669
1
73054
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0L6W8M4_9AGAR
668
1
72439
TrEMBL
Secretory Pathway (Reliability: 3)
H0GIK3_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
682
1
74449
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1G4KM33_9SACH
680
1
74277
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3M6ZL34_HORWE
678
1
74181
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1U7LVJ9_NEOID
Neolecta irregularis (strain DAH-3)
657
0
71533
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6S6VQI5_9PLEO
676
1
74215
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H3HSY2_9AGAM
661
1
71906
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F8UU55_9EURO
670
1
72836
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9I5L6_9LAMI
1081
0
119654
TrEMBL
other Location (Reliability: 5)
A0A0A7CBL7_9BRAD
79
0
8525
TrEMBL
-
A0A8H5D3E8_9AGAR
675
1
73719
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5N7ESN9_9EURO
671
1
73313
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Y6L8K1_ZYMTR
683
1
74543
TrEMBL
Secretory Pathway (Reliability: 5)
A0A507FK91_9FUNG
658
0
72045
TrEMBL
Secretory Pathway (Reliability: 1)
B6Q4C4_TALMQ
Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
675
1
73568
TrEMBL
Secretory Pathway (Reliability: 1)
A7U5U5_MAGOR
656
0
71546
TrEMBL
Secretory Pathway (Reliability: 1)
A0A163MV25_ABSGL
737
1
81224
TrEMBL
Mitochondrion (Reliability: 5)
A0A2I2GRV0_9EURO
671
1
73145
TrEMBL
Secretory Pathway (Reliability: 1)
A0A834RL02_9PLEO
628
1
68638
TrEMBL
Secretory Pathway (Reliability: 3)
H0EWA5_GLAL7
Glarea lozoyensis (strain ATCC 74030 / MF5533)
672
1
73523
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CC78_9BRAD
79
0
8518
TrEMBL
-
A0A5N5WUN2_9EURO
672
1
73364
TrEMBL
Secretory Pathway (Reliability: 2)
A0A093YFC0_9PEZI
670
1
73233
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D0VIC6_CRYGA
696
1
76464
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1L9PAT1_ASPVE
671
1
73781
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q4P6H0_9PLEO
675
1
74067
TrEMBL
Secretory Pathway (Reliability: 3)
A0A179UFL9_BLAGS
Blastomyces gilchristii (strain SLH14081)
678
1
73838
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8I2YMT6_9AGAM
1831
2
196868
TrEMBL
other Location (Reliability: 2)
A0A6A6E8C3_9PEZI
670
1
74454
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0K3C4V2_RHOTO
658
1
71482
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1A6A2L4_9TREE
679
1
74234
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1M3TW15_ASPLC
Aspergillus luchuensis (strain CBS 106.47)
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T4C583_TRILO
664
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178BZM0_9EURO
685
1
74932
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7D5Z356_9HYPO
662
1
72715
TrEMBL
Secretory Pathway (Reliability: 1)
H1VJE3_COLHI
Colletotrichum higginsianum (strain IMI 349063)
647
0
70667
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1J9Q125_9EURO
678
1
73849
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6PM20_9PEZI
665
0
72694
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C3SDU8_PHLGI
679
1
74690
TrEMBL
Secretory Pathway (Reliability: 5)
W3WVM2_PESFW
Pestalotiopsis fici (strain W106-1 / CGMCC3.15140)
667
1
73170
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4S9F6N6_AURPU
692
1
75663
TrEMBL
other Location (Reliability: 4)
B8N4E9_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A365N7D7_GIBIN
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
E9CWZ3_COCPS
Coccidioides posadasii (strain RMSCC 757 / Silveira)
675
1
73843
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5B0SID7_PUCGR
669
0
73197
TrEMBL
Secretory Pathway (Reliability: 5)
A0A075AYJ3_ROZAC
Rozella allomycis (strain CSF55)
650
0
71272
TrEMBL
Secretory Pathway (Reliability: 2)
U1HTX7_ENDPU
Endocarpon pusillum (strain Z07020 / HMAS-L-300199)
674
1
73715
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0E9NAR8_SAICN
Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748 / NRRL Y-17804)
691
1
75725
TrEMBL
other Location (Reliability: 3)
A0A8H4S1T8_9EURO
673
1
73801
TrEMBL
Secretory Pathway (Reliability: 2)
A0A165DMS1_9APHY
676
1
74233
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8G1S1E4_9EURO
673
1
73402
TrEMBL
Secretory Pathway (Reliability: 2)
N1QAQ1_PSEFD
Pseudocercospora fijiensis (strain CIRAD86)
682
1
74767
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1B8CQ34_9PEZI
670
1
73093
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A5K6H0_9PLEO
675
1
73949
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2A9NNJ7_9AGAR
659
1
72167
TrEMBL
Secretory Pathway (Reliability: 1)
L7QJJ0_SALEU
696
0
79761
TrEMBL
other Location (Reliability: 5)
A0A4V3XI99_9APHY
678
1
74528
TrEMBL
Secretory Pathway (Reliability: 4)
E4ZXX2_LEPMJ
Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
674
1
73768
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2H0ZKS1_CANAR
676
1
74308
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y1X8R1_9FUNG
663
0
72996
TrEMBL
Secretory Pathway (Reliability: 2)
K5WQK0_PHACS
Phanerochaete carnosa (strain HHB-10118-sp)
675
1
74375
TrEMBL
Secretory Pathway (Reliability: 4)
A0A409YF38_9AGAR
674
1
73400
TrEMBL
Secretory Pathway (Reliability: 4)
Q4WHP9_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
672
1
73385
TrEMBL
Secretory Pathway (Reliability: 2)
A0A317SFB2_9PEZI
672
1
73442
TrEMBL
Secretory Pathway (Reliability: 1)
A5DUX8_LODEL
Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239)
687
1
74684
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7S9KLK3_EPIFF
Epichloe festucae (strain Fl1)
1304
1
142754
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M7EUN9_HORWE
678
1
74167
TrEMBL
Secretory Pathway (Reliability: 1)
E3K4X4_PUCGT
Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
669
0
73197
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1B8AH18_FUSPO
663
1
72612
TrEMBL
Secretory Pathway (Reliability: 1)
A0A022VYV4_TRIRU
677
1
74137
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D2J4M5_9EURO
678
1
74382
TrEMBL
Secretory Pathway (Reliability: 1)
J7S8H7_KAZNA
Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3)
683
1
74414
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0G2E0Q1_9EURO
1290
1
142020
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7T4T3_9HELO
671
1
73390
TrEMBL
Secretory Pathway (Reliability: 1)
G0RPK6_HYPJQ
Hypocrea jecorina (strain QM6a)
664
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6GSQ7_FUSOX
663
1
72593
TrEMBL
Secretory Pathway (Reliability: 1)
A0A163JMB1_ABSGL
659
1
72207
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A1TKQ5_9HYPO
664
1
72495
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0G4KGF7_9PEZI
666
1
72642
TrEMBL
Secretory Pathway (Reliability: 1)
F0XBZ3_GROCL
Grosmannia clavigera (strain kw1407 / UAMH 11150)
663
1
72475
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V6RNS8_9EURO
673
1
73801
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6A7B247_9PLEO
497
1
54492
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2G8SKY8_9APHY
667
1
73504
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1X7R563_9SACH
682
1
74515
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4ZKL7_FUSAU
663
1
72506
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6NPQ3_9PEZI
665
1
72661
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5B0E9_9AGAR
674
1
73237
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H4J666_9PEZI
672
1
73729
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Y2WKB6_9PEZI
664
1
72619
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6TT92_9EURO
672
1
73128
TrEMBL
Secretory Pathway (Reliability: 2)
A0A059J900_TRIIM
Trichophyton interdigitale (strain MR816)
677
1
74139
TrEMBL
Secretory Pathway (Reliability: 1)
A0A395RGZ5_FUSSP
663
1
72506
TrEMBL
Secretory Pathway (Reliability: 1)
A0A068SH58_9FUNG
667
1
73325
TrEMBL
Secretory Pathway (Reliability: 1)
C5FQB8_ARTOC
Arthroderma otae (strain ATCC MYA-4605 / CBS 113480)
675
1
73913
TrEMBL
Secretory Pathway (Reliability: 2)
A0A168BLX5_CORFA
Cordyceps fumosorosea (strain ARSEF 2679)
667
1
72794
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E5R238_9ASCO
692
1
76334
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1K0GKM6_9BASI
696
1
74820
TrEMBL
Mitochondrion (Reliability: 2)
A0A0F7RSC2_9BASI
689
1
74553
TrEMBL
Mitochondrion (Reliability: 3)
A0A559LDX7_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
X0MF53_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4U0VPJ6_9BASI
1013
0
112145
TrEMBL
Mitochondrion (Reliability: 3)
A0A1Y2ERW4_9BASI
660
1
72017
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0P7AR35_9HYPO
665
1
72466
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C2JBE1_9PEZI
664
1
72769
TrEMBL
Secretory Pathway (Reliability: 2)
W2RVL0_9EURO
673
1
73595
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5S2X3_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178Z703_9EURO
685
1
75022
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5N6SV17_ASPPS
671
1
73327
TrEMBL
Secretory Pathway (Reliability: 2)
A0A284RI62_ARMOS
629
0
68879
TrEMBL
other Location (Reliability: 4)
A0A0A7CBH9_9BRAD
79
0
8518
TrEMBL
-
I3RV97_DUNSA
692
0
79145
TrEMBL
other Location (Reliability: 4)
A0A7C8I3V9_9PLEO
678
1
74411
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H7XPJ9_PSICU
676
1
73534
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H7XPJ9_PSICU
Psychedelic mushroom
676
1
73534
TrEMBL
Secretory Pathway (Reliability: 3)
A0A875RPT7_EENNA
679
1
74830
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2S4VEC9_9BASI
639
0
70031
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2S4UJS3_9BASI
667
0
73681
TrEMBL
Secretory Pathway (Reliability: 5)
A0A094ESM0_9PEZI
670
1
73130
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5Q5M2_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
M7X6H4_RHOT1
Rhodosporidium toruloides (strain NP11)
663
1
71941
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Z1KR51_9HELO
670
1
73117
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4P9ZV63_9FUNG
631
0
68873
TrEMBL
other Location (Reliability: 1)
A0A8H3C3R0_9AGAM
659
1
71707
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6UM21_9EURO
671
1
73326
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6A5RFJ3_9PLEO
674
1
74106
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8A3PLH0_9HELO
671
1
73323
TrEMBL
Secretory Pathway (Reliability: 1)
Q5BBL8_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
674
1
73697
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4Q4SM17_9PLEO
675
1
74105
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2V1DWX0_9PLEO
647
0
71068
TrEMBL
other Location (Reliability: 1)
A0A0D0XF94_9TREE
696
1
76500
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2B7XKK2_9EURO
676
1
73768
TrEMBL
Secretory Pathway (Reliability: 2)
A0A317VC64_9EURO
672
1
73303
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7H8QXB3_9EURO
672
1
73499
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0P1BFB0_9BASI
681
1
73737
TrEMBL
Mitochondrion (Reliability: 3)
A0A0N0NM54_9EURO
699
1
76967
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A2L6C3_PENIT
673
1
73764
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1S8BGR6_9PEZI
747
1
81643
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1E4TB56_9ASCO
664
1
72410
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4V1IVY4_9FUNG
672
0
73589
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V8UFH9_9PEZI
690
1
75589
TrEMBL
Mitochondrion (Reliability: 5)
A0A6G1IAL1_9PEZI
678
0
73759
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T2ZY85_9PEZI
666
1
72769
TrEMBL
Secretory Pathway (Reliability: 1)
A0A423VLU6_9PEZI
666
1
72916
TrEMBL
Secretory Pathway (Reliability: 1)
A0A428QEF1_9HYPO
663
1
72674
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T9ZD48_9FUNG
842
1
92875
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B7NEK6_9AGAM
659
1
71911
TrEMBL
Secretory Pathway (Reliability: 1)
C5PGZ0_COCP7
Coccidioides posadasii (strain C735)
675
1
73785
TrEMBL
Secretory Pathway (Reliability: 2)
A0A318ZFC9_9EURO
672
1
73381
TrEMBL
Secretory Pathway (Reliability: 2)
A0A094E0G5_9PEZI
670
1
73137
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5RKZ3_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7U2ICE1_PHANO
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173)
673
1
73788
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0C9UDA1_SPHS4
Sphaerobolus stellatus (strain SS14)
693
1
76190
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0V1PR87_9ASCO
682
1
74378
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C4DZ87_MAGP6
Magnaporthiopsis poae (strain ATCC 64411 / 73-15)
663
1
72129
TrEMBL
Secretory Pathway (Reliability: 1)
Q9UWE3_ASPOZ
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A068J4B7_KARVE
611
0
67231
TrEMBL
other Location (Reliability: 2)
A0A0D2XQC1_FUSO4
Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936)
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
N4UXU9_COLOR
Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422)
667
1
72954
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Z1HHX5_9HELO
670
1
73104
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2L2SX50_9HYPO
663
1
72612
TrEMBL
Secretory Pathway (Reliability: 1)
A0A397GS70_9EURO
672
1
73303
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2I1EVN1_9GLOM
621
1
69747
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CBH2_9BRAD
79
0
8518
TrEMBL
-
W9XG78_9EURO
687
1
75033
TrEMBL
Secretory Pathway (Reliability: 3)
A0A139IDJ4_9PEZI
723
1
79389
TrEMBL
Mitochondrion (Reliability: 5)
A0A1E4SJM0_9ASCO
681
1
73765
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Q3E3S1_LENED
676
1
73726
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1D8PG96_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
687
1
74562
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4T0VU73_9PEZI
657
0
71727
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B7NMC1_9EURO
610
0
66648
TrEMBL
other Location (Reliability: 1)
A0A8H3F9F0_9LECA
726
1
79353
TrEMBL
Secretory Pathway (Reliability: 2)
M7U2N0_BOTF1
Botryotinia fuckeliana (strain BcDW1)
670
1
73121
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4P9ZIB2_9ASCO
682
1
74700
TrEMBL
Secretory Pathway (Reliability: 1)
A0A218Z0P8_9HELO
670
1
73340
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0M9EY05_FUSLA
663
1
72492
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1L9V1X6_ASPBC
Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946)
672
1
73431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T9YV17_9FUNG
663
1
72921
TrEMBL
Secretory Pathway (Reliability: 2)
F8NLD2_SERL9
Serpula lacrymans var. lacrymans (strain S7.9)
672
1
73472
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1X2G838_9FUNG
641
0
70577
TrEMBL
other Location (Reliability: 1)
A0A1E1KFV5_9HELO
671
1
73208
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178ER49_TRIRU
677
1
74137
TrEMBL
Secretory Pathway (Reliability: 1)
N1P0X7_YEASC
Saccharomyces cerevisiae (strain CEN.PK113-7D)
682
1
74468
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4ZKV6_9HYPO
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D2KIH5_9EURO
685
1
74932
TrEMBL
Secretory Pathway (Reliability: 3)
A0A6H1RIF2_9TRYP
Leishmania sp
66
0
7016
TrEMBL
Secretory Pathway (Reliability: 4)
A0A165SBZ6_9AGAM
671
1
73611
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H3AJN3_9AGAM
659
1
71666
TrEMBL
Secretory Pathway (Reliability: 1)
A0A077QYT6_9BASI
689
1
74144
TrEMBL
Mitochondrion (Reliability: 2)
A0A8F2RIM0_9ASCO
676
1
74089
TrEMBL
Secretory Pathway (Reliability: 1)
A0A067T2G1_GALM3
Galerina marginata (strain CBS 339.88)
676
1
73405
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0A8L3S7_9SACH
678
1
74220
TrEMBL
Secretory Pathway (Reliability: 1)
A0A507FPD6_9FUNG
2101
0
231986
TrEMBL
other Location (Reliability: 4)
A0A6J8EW09_MYTCO
680
0
75393
TrEMBL
other Location (Reliability: 2)
A0A0C3DBX2_9AGAM
677
1
73846
TrEMBL
Secretory Pathway (Reliability: 3)
B6H0S5_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
673
1
73730
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4P7MV61_MAGOR
664
1
72349
TrEMBL
Secretory Pathway (Reliability: 1)
C0S072_PARBP
Paracoccidioides brasiliensis (strain Pb03)
677
1
73876
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4R8QRP6_9PEZI
664
1
72636
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6XRW2_9PLEO
673
1
73608
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1E3I9Q3_9TREE
677
1
74199
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0A7CCN6_9BRAD
78
0
8451
TrEMBL
-
A0A1E3IML7_9TREE
677
1
74226
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8H5HEI1_9AGAR
659
1
72143
TrEMBL
Secretory Pathway (Reliability: 3)
A0A6A6ET27_9PEZI
681
1
74687
TrEMBL
Secretory Pathway (Reliability: 3)
A0A511KAA3_RHOTO
656
1
71494
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q4YQ99_9PEZI
665
1
72860
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y2LTD3_EPING
773
1
84831
TrEMBL
other Location (Reliability: 2)
A0A1L9N0Q2_ASPTC
Aspergillus tubingensis (strain CBS 134.48)
672
1
73431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A395NIZ7_TRIAR
663
1
72446
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0W0FHK0_9AGAR
677
1
73767
TrEMBL
Secretory Pathway (Reliability: 5)
A0A4R8TR36_9PEZI
664
1
72606
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Z0YLY8_9PEZI
666
1
73241
TrEMBL
Secretory Pathway (Reliability: 1)
C4JGG9_UNCRE
Uncinocarpus reesii (strain UAMH 1704)
674
1
73564
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0A1NIY7_RHIZD
660
1
72738
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V1SZK1_9FUNG
666
1
73111
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2Z6QIR5_9GLOM
659
1
73022
TrEMBL
Secretory Pathway (Reliability: 1)
A0A180GG57_PUCT1
Puccinia triticina (isolate 1-1 / race 1 (BBBD))
660
0
72296
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2N5URC3_9BASI
669
0
73235
TrEMBL
Secretory Pathway (Reliability: 5)
U4LQ17_PYROM
Pyronema omphalodes (strain CBS 100304)
664
1
72719
TrEMBL
Secretory Pathway (Reliability: 1)
A0A194VYR5_9PEZI
666
1
72860
TrEMBL
Secretory Pathway (Reliability: 1)
A0A074XJ30_9PEZI
646
0
70393
TrEMBL
other Location (Reliability: 2)
A0A2N0RGU0_9GLOM
621
1
69933
TrEMBL
Secretory Pathway (Reliability: 1)
A0A367YMW5_9ASCO
686
1
74711
TrEMBL
Secretory Pathway (Reliability: 1)
S9R983_SCHOY
Schizosaccharomyces octosporus (strain yFS286)
660
1
73094
TrEMBL
Secretory Pathway (Reliability: 1)
N4UV24_FUSC1
Fusarium oxysporum f. sp. cubense (strain race 1)
645
1
70700
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0J6XY52_COCIT
675
1
73843
TrEMBL
Secretory Pathway (Reliability: 2)
A0A067XS28_KARVE
247
0
27473
TrEMBL
other Location (Reliability: 5)
A0A8H3XIV3_GIGMA
659
1
72945
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V6TSR2_9EURO
673
1
73784
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2T3ZDN8_9HYPO
662
1
72429
TrEMBL
Secretory Pathway (Reliability: 1)
S8B581_PENO1
Penicillium oxalicum (strain 114-2 / CGMCC 5302)
672
1
73378
TrEMBL
Secretory Pathway (Reliability: 2)
A0A165G5D4_9BASI
670
1
73346
TrEMBL
Secretory Pathway (Reliability: 3)
A0A545A3I7_9PEZI
672
1
73374
TrEMBL
Secretory Pathway (Reliability: 1)
A0A420HGS6_9PEZI
632
0
69199
TrEMBL
other Location (Reliability: 3)
A0A384K0D3_BOTFB
Botryotinia fuckeliana (strain B05.10)
670
1
73121
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B8DTK6_9PEZI
668
1
72966
TrEMBL
Secretory Pathway (Reliability: 1)
A0A812DCY0_SEPPH
714
0
79919
TrEMBL
Mitochondrion (Reliability: 4)
A0A5C2TTE3_9APHY
676
1
74138
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1G4JDC4_9SACH
681
1
74415
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0L0T7V3_ALLM3
Allomyces macrogynus (strain ATCC 38327)
680
1
74061
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q2D842_9AGAR
650
0
71918
TrEMBL
other Location (Reliability: 2)
A0A1Y2A4S2_9PLEO
683
1
74804
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5P2U7D6_KLULC
679
1
74448
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B8F1G5_9PEZI
670
1
73107
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4C2E3I9_9SACH
673
1
73637
TrEMBL
Secretory Pathway (Reliability: 1)
D6RLN6_COPC7
Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
727
1
79739
TrEMBL
Mitochondrion (Reliability: 3)
A0A8J5BVN6_9ASCO
670
1
73561
TrEMBL
Secretory Pathway (Reliability: 1)
M2SQA7_COCSN
Cochliobolus sativus (strain ND90Pr / ATCC 201652)
675
1
73869
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8G0LGJ2_9HYPO
663
1
72560
TrEMBL
Secretory Pathway (Reliability: 1)
V2WVN8_MONRO
Moniliophthora roreri (strain MCA 2997)
677
1
73695
TrEMBL
Secretory Pathway (Reliability: 5)
A0A178EAY6_9PLEO
676
1
74230
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H5M9D6_9AGAR
1499
7
166595
TrEMBL
Mitochondrion (Reliability: 2)
A0A0F8B5F9_CERFI
666
1
72727
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y1UGM2_9TREE
679
1
74193
TrEMBL
Secretory Pathway (Reliability: 4)
A0A7G3ZJ01_9SACH
681
1
74418
TrEMBL
Secretory Pathway (Reliability: 2)
I2G6Y4_USTH4
Ustilago hordei (strain Uh4875-4)
696
1
74809
TrEMBL
Mitochondrion (Reliability: 2)
F4RMF9_MELLP
Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7)
670
0
73016
TrEMBL
Secretory Pathway (Reliability: 4)
A0A421JFB0_9ASCO
677
1
74005
TrEMBL
Secretory Pathway (Reliability: 1)
A0A197K8M1_9FUNG
665
0
72349
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E5R8P0_9ASCO
680
1
75152
TrEMBL
Secretory Pathway (Reliability: 2)
A0A396GU25_MEDTR
89
0
10632
TrEMBL
other Location (Reliability: 2)
W9ZEM9_9EURO
678
1
74320
TrEMBL
Secretory Pathway (Reliability: 1)
A0A372R247_9GLOM
658
1
73045
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3N2PNZ4_9PEZI
663
1
72257
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8E2JWM2_9PEZI
647
0
70906
TrEMBL
other Location (Reliability: 1)
A0A0D0DHT5_9AGAM
661
0
72117
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1B7YC11_COLHI
Colletotrichum higginsianum (strain IMI 349063)
664
1
72546
TrEMBL
Secretory Pathway (Reliability: 1)
L7JAP8_MAGOP
Magnaporthe oryzae (strain P131)
664
1
72367
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0W0FWL7_9AGAR
699
1
76833
TrEMBL
Mitochondrion (Reliability: 4)
A0A367LSL9_9HYPO
1487
0
161770
TrEMBL
other Location (Reliability: 1)
A0A2K3Q9K5_9HYPO
665
1
72850
TrEMBL
Secretory Pathway (Reliability: 1)
G4MKA5_MAGO7
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
664
1
72367
TrEMBL
Secretory Pathway (Reliability: 1)
L8G135_PSED2
Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21)
669
1
73063
TrEMBL
Secretory Pathway (Reliability: 1)
L7HXE1_MAGOY
Magnaporthe oryzae (strain Y34)
664
1
72367
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CC77_9BRAD
79
0
8518
TrEMBL
-
A0A0H5C094_CYBJN
Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 / NRRL Y-1542)
673
1
73441
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7C8K5L2_ORBOL
673
1
73189
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4T0TBC8_9BASI
654
1
71867
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H8JA06_9AGAM
662
1
72136
TrEMBL
Secretory Pathway (Reliability: 2)
A0A072P303_9EURO
679
1
74575
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Y7SKS1_9AGAR
669
1
72355
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2N3NGL6_9PEZI
664
1
72466
TrEMBL
Secretory Pathway (Reliability: 1)
A0A319ER48_ASPSB
Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362)
672
1
73569
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1L0CRW8_9ASCO
679
1
75071
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q4U9H3_9PEZI
665
1
72793
TrEMBL
Secretory Pathway (Reliability: 1)
A0A447C9Y5_PODCO
663
1
72334
TrEMBL
Secretory Pathway (Reliability: 2)
G0S916_CHATD
Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
664
1
72732
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6NM66_9PEZI
677
1
74427
TrEMBL
Secretory Pathway (Reliability: 2)
B6JWL3_SCHJY
Schizosaccharomyces japonicus (strain yFS275 / FY16936)
661
1
73059
TrEMBL
Secretory Pathway (Reliability: 1)
S2J7C3_MUCC1
Mucor circinelloides f. circinelloides (strain 1006PhL)
659
1
72321
TrEMBL
Secretory Pathway (Reliability: 1)
A0A448YIC3_BRENA
677
1
74462
TrEMBL
Secretory Pathway (Reliability: 1)
A8Q4X6_MALGO
Malassezia globosa (strain ATCC MYA-4612 / CBS 7966)
667
0
72624
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1G4K2W1_9SACH
678
1
74535
TrEMBL
Secretory Pathway (Reliability: 2)
A0A178AJP9_9PLEO
676
1
73993
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0A7CC87_9BRAD
79
0
8525
TrEMBL
-
A0A135S402_9PEZI
664
1
72587
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F7VFH4_PENBI
672
1
73411
TrEMBL
Secretory Pathway (Reliability: 2)
A0A146IN94_MYCCL
676
1
72954
TrEMBL
Secretory Pathway (Reliability: 2)
A0A383V2H4_BLUHO
669
1
73185
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5M3MC92_CONPW
Coniophora puteana (strain RWD-64-598)
674
1
73754
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H6W3P8_MYCCL
542
1
59150
TrEMBL
Mitochondrion (Reliability: 4)
A0A8H3BB66_9AGAM
661
1
71884
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H2XZ05_9AGAM
660
1
71801
TrEMBL
Secretory Pathway (Reliability: 1)
A0A084QHZ8_STAC4
Stachybotrys chlorohalonata (strain IBT 40285)
662
1
72360
TrEMBL
Secretory Pathway (Reliability: 1)
D8PZZ5_SCHCM
Schizophyllum commune (strain H4-8 / FGSC 9210)
670
1
72840
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2I1CL83_ASPN1
Aspergillus novofumigatus (strain IBT 16806)
672
1
73453
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H6FEV6_9LECA
684
1
74752
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1C1CJ06_9EURO
687
1
75246
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1E3PKT7_9ASCO
665
1
73094
TrEMBL
Secretory Pathway (Reliability: 1)
G8YB62_PICSO
Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL Y-12695)
682
1
74349
TrEMBL
Secretory Pathway (Reliability: 1)
A0A167D4D5_9ASCO
677
1
73950
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7S8D820_FUSCU
663
1
72506
TrEMBL
Secretory Pathway (Reliability: 1)
A0A366S5Y8_9HYPO
663
1
72538
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1S1W4I8_9PEZI
664
1
72666
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CBK3_9BRAD
79
0
8518
TrEMBL
-
J9VW24_CRYNH
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
679
1
74465
TrEMBL
Secretory Pathway (Reliability: 4)
Q5K6Z5_CRYNJ
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
679
1
74524
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0L8RGL5_SACEU
683
1
74602
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F4Z857_9PEZI
665
1
72474
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5C3NZH6_9APHY
672
1
73473
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0G4PD87_PENCA
673
1
73815
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1A0H7U1_9ASCO
678
1
73632
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F9X826_TRIHA
663
1
72546
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2N1L8S7_TRIHA
663
1
72560
TrEMBL
Secretory Pathway (Reliability: 1)
A0A093ZNV6_9PEZI
1607
0
173854
TrEMBL
other Location (Reliability: 1)
A0A286U7U0_9AGAM
677
1
74008
TrEMBL
Secretory Pathway (Reliability: 4)
G2X5L1_VERDV
Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
666
1
72656
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2A9P588_9HYPO
665
1
73130
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1E3QII5_9ASCO
651
0
70780
TrEMBL
other Location (Reliability: 1)
A0A165FM10_XYLHT
Xylona heveae (strain CBS 132557 / TC161)
675
1
73721
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4Q7JXN9_METCM
622
0
68063
TrEMBL
other Location (Reliability: 5)
A0A2D3VCT1_9PEZI
684
1
74789
TrEMBL
Secretory Pathway (Reliability: 5)
A0A6S6WPA7_9PLEO
676
1
74215
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1L0D5Z5_9ASCO
680
1
74354
TrEMBL
Secretory Pathway (Reliability: 1)
A0A063BLC5_USTVR
665
1
72661
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6Y1M2_9PEZI
679
1
74206
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5C5FQ28_9BASI
685
1
73891
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0L0VU72_9BASI
661
0
72483
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0D0C7K2_9AGAR
676
1
73640
TrEMBL
Secretory Pathway (Reliability: 5)
A0A137P2F9_CONC2
Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
655
0
72259
TrEMBL
Secretory Pathway (Reliability: 1)
G3JHM3_CORMM
Cordyceps militaris (strain CM01)
665
1
72470
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H8D9B9_9ASCO
684
1
74564
TrEMBL
Secretory Pathway (Reliability: 1)
A0A168JJN0_MUCCL
659
1
72291
TrEMBL
Secretory Pathway (Reliability: 1)
S7Q8K7_GLOTA
Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617)
673
1
73727
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0B7K7L9_BIOOC
667
1
72407
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0U1V1W7_KARMI
445
0
47568
TrEMBL
other Location (Reliability: 3)
K0KHM2_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
672
1
73361
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H8CYG2_9EURO
Histoplasma ohiense
676
1
73811
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B1PAX3_UNCNE
673
1
73721
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6J964_9EURO
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
K1WW58_MARBU
Marssonina brunnea f. sp. multigermtubi (strain MB_m1)
671
1
73319
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C3B4G4_9AGAM
653
0
70866
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N5NGE8_9PEZI
664
1
72372
TrEMBL
Secretory Pathway (Reliability: 1)
I4YD25_WALMC
Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66)
654
1
71867
TrEMBL
Secretory Pathway (Reliability: 1)
A0A068J3X2_KARVE
608
0
67365
TrEMBL
other Location (Reliability: 1)
A0A068J3Q5_KARVE
213
0
24187
TrEMBL
other Location (Reliability: 1)
A0A510P4H8_CANAR
1329
1
147942
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2I1D0B9_9EURO
670
1
72976
TrEMBL
Secretory Pathway (Reliability: 1)
S9VXF4_SCHCR
Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691)
661
1
73139
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8J1YQH5_9TREE
678
1
74089
TrEMBL
Secretory Pathway (Reliability: 4)
A0A6J3M7H2_9PEZI
654
0
71207
TrEMBL
other Location (Reliability: 3)
A0A8H5Z5W9_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A167ZY63_9PEZI
666
1
73054
TrEMBL
Secretory Pathway (Reliability: 2)
A0A135V1I0_9PEZI
664
1
72477
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1L9X1L4_ASPA1
Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094)
673
1
73402
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H4QHX1_9AGAR
676
1
73405
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1Q3A8B8_ZYGRO
673
1
73549
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4S9S1D1_AURPU
671
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3F3QA80_9EURO
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
K3VXR0_FUSPC
Fusarium pseudograminearum (strain CS3096)
663
1
72520
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4S8R6F7_9HELO
670
1
73104
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3S4F364_9PEZI
663
1
72585
TrEMBL
Secretory Pathway (Reliability: 1)
R9XCR2_ASHAC
679
1
74418
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0L0S448_ALLM3
Allomyces macrogynus (strain ATCC 38327)
680
1
74145
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2H4S7B3_CORMI
661
1
72091
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q2DIK3_9AGAR
671
1
72918
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7RHJ2_9FUNG
656
1
71845
TrEMBL
Secretory Pathway (Reliability: 1)
A0A094JW92_9PEZI
669
1
72965
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P7YYL0_9ASCO
1336
1
148124
TrEMBL
Secretory Pathway (Reliability: 1)
G4TLJ8_SERID
Serendipita indica (strain DSM 11827)
654
0
71203
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B0DZU7_NEUCS
661
1
72332
TrEMBL
Secretory Pathway (Reliability: 1)
A0A177UXX3_9BASI
701
1
76116
TrEMBL
Mitochondrion (Reliability: 2)
A0A1P8YXV6_PASFU
663
0
72321
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q4WGM0_9PEZI
665
1
72948
TrEMBL
Secretory Pathway (Reliability: 1)
R9AL06_WALI9
Wallemia ichthyophaga (strain EXF-994 / CBS 113033)
654
1
71841
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M0W8C9_9EURO
672
1
73724
TrEMBL
Secretory Pathway (Reliability: 1)
G8C145_TETPH
Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5)
681
1
74140
TrEMBL
Secretory Pathway (Reliability: 1)
A0A369GRK6_9HYPO
1484
0
161351
TrEMBL
other Location (Reliability: 1)
A0A2J8DJA6_VERDA
666
1
72656
TrEMBL
Secretory Pathway (Reliability: 1)
A0A059J945_TRIIM
Trichophyton interdigitale (strain MR816)
699
1
76924
TrEMBL
Secretory Pathway (Reliability: 1)
A1XM68_BLAEM
533
1
58015
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8B8UU53_SACPA
682
1
74501
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5C3KHW5_9AGAR
673
1
73249
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8J2J1F1_FUSEQ
663
1
72538
TrEMBL
Secretory Pathway (Reliability: 1)
U7PW24_SPOS1
Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183)
664
1
72755
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1D8NIB8_YARLL
670
1
73524
TrEMBL
Secretory Pathway (Reliability: 1)
W3VHV9_PSEA5
Pseudozyma aphidis (strain ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318 / NBRC 10182 / NRRL Y-7954 / St-0401)
1070
1
114986
TrEMBL
other Location (Reliability: 1)
F8MXP0_NEUT8
Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657)
661
1
72332
TrEMBL
Secretory Pathway (Reliability: 1)
W0TAL8_KLUMD
Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
679
1
74362
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0G2FGZ7_9PEZI
664
1
72636
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5M3Z4V0_ASPTE
672
1
73402
TrEMBL
Secretory Pathway (Reliability: 2)
F0UU32_AJEC8
Ajellomyces capsulatus (strain H88)
676
1
73811
TrEMBL
Secretory Pathway (Reliability: 1)
U5HCC9_USTV1
Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064)
662
1
71895
TrEMBL
Secretory Pathway (Reliability: 1)
B0D7M5_LACBS
Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686)
676
1
73407
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2K0WTT6_GIBNY
663
1
72607
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2N1JDA1_9BASI
669
1
73258
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2J6TRR6_9HELO
672
1
73486
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5C2SCA5_9APHY
653
0
71507
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D7APZ8_9AGAR
664
1
73596
TrEMBL
Mitochondrion (Reliability: 4)
A0A8H2VG40_9SACH
683
1
74585
TrEMBL
Secretory Pathway (Reliability: 1)
A0A067XTQ5_KARVE
211
0
23817
TrEMBL
other Location (Reliability: 1)
A0A409VB70_9AGAR
672
1
73956
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8H7BXR6_AGABI
675
1
73489
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7S920_9FUNG
660
1
72603
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H7Y4U4_PSICU
679
1
74769
TrEMBL
Secretory Pathway (Reliability: 3)
A0A4Z1HME0_9HELO
662
1
72411
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5M9J7U5_MONFR
650
1
71036
TrEMBL
Secretory Pathway (Reliability: 1)
V9D122_9EURO
687
1
75246
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3M7IAE2_HORWE
688
1
75319
TrEMBL
Secretory Pathway (Reliability: 5)
A0A010QA29_9PEZI
664
1
72560
TrEMBL
Secretory Pathway (Reliability: 1)
G8ZVI6_TORDC
Torulaspora delbrueckii (strain ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866)
673
1
73563
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3D8S3Y2_9EURO
674
1
73709
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H6HPK9_9AGAR
Tulosesus angulatus
669
1
72650
TrEMBL
Secretory Pathway (Reliability: 1)
A0A066WXV8_COLSU
664
1
72807
TrEMBL
Secretory Pathway (Reliability: 1)
A0A066WXV8_COLSU
Sorghum anthracnose fungus
664
1
72807
TrEMBL
Secretory Pathway (Reliability: 1)
A0A507R1R5_MONPU
676
1
73928
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5C2TYX1_9APHY
653
0
71507
TrEMBL
Secretory Pathway (Reliability: 1)
I2H386_TETBL
Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 / UCD 77-7)
684
1
74988
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6I7Q3_9EURO
672
1
73375
TrEMBL
Secretory Pathway (Reliability: 2)
C1G8H6_PARBD
Paracoccidioides brasiliensis (strain Pb18)
677
1
73876
TrEMBL
Secretory Pathway (Reliability: 1)
F5HE90_CRYNB
Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
744
2
81965
TrEMBL
Mitochondrion (Reliability: 2)
A0A093VL07_TALMA
675
1
73567
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CC83_9BRAD
78
0
8451
TrEMBL
-
A0A094DU94_9PEZI
669
1
73062
TrEMBL
Secretory Pathway (Reliability: 1)
A0A139ACR8_GONPJ
Gonapodya prolifera (strain JEL478)
666
1
72953
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6A6AXQ4_9PEZI
673
1
73717
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7AGD1_9EURO
674
1
73741
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N5QJ42_9AGAM
661
1
71910
TrEMBL
Secretory Pathway (Reliability: 2)
A0A166A4B0_9AGAM
674
1
73617
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2T4GD46_FUSCU
659
1
72125
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4S4KHG4_9APHY
Hermanssonia centrifuga
613
0
67630
TrEMBL
other Location (Reliability: 2)
A0A2G5BDB2_COERN
Coemansia reversa (strain ATCC 12441 / NRRL 1564)
666
1
73584
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C4F2G0_PUCT1
Puccinia triticina (isolate 1-1 / race 1 (BBBD))
646
0
70759
TrEMBL
Secretory Pathway (Reliability: 1)
A0A420YLF4_9PEZI
663
1
72411
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1D9Q0W0_SCLS1
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1)
668
1
73059
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q1BQV5_TREME
682
1
74381
TrEMBL
Secretory Pathway (Reliability: 5)
A0A371CTV1_9APHY
672
1
73507
TrEMBL
Secretory Pathway (Reliability: 3)
A0A423VMC1_9PEZI
658
0
71964
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B4IEQ3_METMF
Metarhizium majus (strain ARSEF 297)
662
1
72668
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4U7BAC6_9PEZI
679
1
74333
TrEMBL
Secretory Pathway (Reliability: 2)
A0A364L8A9_9EURO
673
1
73503
TrEMBL
Secretory Pathway (Reliability: 1)
A0A067PL27_9AGAM
676
1
74029
TrEMBL
Secretory Pathway (Reliability: 4)
A0A167HNG2_CALVF
Calocera viscosa (strain TUFC12733)
669
1
73458
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2N8U7K9_9BASI
689
1
74441
TrEMBL
Mitochondrion (Reliability: 2)
U9USX0_RHIID
Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
652
1
72627
TrEMBL
Secretory Pathway (Reliability: 1)
A0A366Q0L4_GIBMO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3F3RTB3_ASPNG
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M7IWW2_HORWE
688
1
75338
TrEMBL
Secretory Pathway (Reliability: 5)
A0A507D2S2_9FUNG
674
0
73470
TrEMBL
Secretory Pathway (Reliability: 2)
X0JP11_FUSC4
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
E3RVA0_PYRTT
Pyrenophora teres f. teres (strain 0-1)
676
1
74215
TrEMBL
Secretory Pathway (Reliability: 3)
K5WZI1_AGABU
Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC 10392)
675
1
73475
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5C2SKW9_9APHY
676
1
74023
TrEMBL
Secretory Pathway (Reliability: 2)
W6MM85_9ASCO
672
1
73110
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5L8S8_9HYPO
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7C8PCE0_ORBOL
673
1
73233
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7C8RAI4_ORBOL
612
0
66747
TrEMBL
other Location (Reliability: 1)
G2WGY4_YEASK
Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557)
682
1
74452
TrEMBL
Secretory Pathway (Reliability: 1)
W9IL64_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
L0PFV0_PNEJ8
Pneumocystis jirovecii (strain SE8)
639
1
70756
TrEMBL
Secretory Pathway (Reliability: 2)
A0A166T1H4_9AGAM
667
1
72681
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5C6G5M9_9HYPO
665
1
72935
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2T3B5Z6_AMORE
606
0
66379
TrEMBL
other Location (Reliability: 1)
A0A1Y2WZD6_9PEZI
664
1
72856
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V6Q3G3_9EURO
673
1
73925
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5E8C4F6_9ASCO
670
1
73828
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q4X8V3_9PEZI
665
1
72923
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1W5D1H2_9LECA
674
1
73625
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Q2ZTU1_ZYGRO
673
1
73549
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CBV9_9BRAD
78
0
8451
TrEMBL
-
A0A2G5ICV9_CERBT
684
1
74542
TrEMBL
Secretory Pathway (Reliability: 5)
A0A4T0AAI2_AURPU
692
1
75677
TrEMBL
other Location (Reliability: 4)
A0A4T0EJR9_AURPU
692
1
75675
TrEMBL
other Location (Reliability: 4)
A0A420HPF2_9PEZI
Erysiphe neolycopersici
672
1
73699
TrEMBL
Secretory Pathway (Reliability: 2)
A0A094F1G6_9PEZI
669
1
72938
TrEMBL
Secretory Pathway (Reliability: 1)
A0A067T5X6_GALM3
Galerina marginata (strain CBS 339.88)
678
1
74399
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2H3CPU8_9AGAR
675
1
74323
TrEMBL
Mitochondrion (Reliability: 3)
A0A507EQZ8_9FUNG
664
1
72415
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6J8EYF1_MYTCO
828
0
92338
TrEMBL
other Location (Reliability: 2)
A0A6J8EW57_MYTCO
270
0
30115
TrEMBL
other Location (Reliability: 2)
A0A1Z5TGH0_HORWE
688
1
75319
TrEMBL
Secretory Pathway (Reliability: 5)
F5H9D5_CRYNB
Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
798
2
88118
TrEMBL
Mitochondrion (Reliability: 2)
A0A2P4QAN5_RHIID
Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
597
1
67334
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1V6V9C4_9EURO
673
1
73827
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7DMV2_PLEOS
673
1
73157
TrEMBL
Secretory Pathway (Reliability: 2)
G7E7S0_MIXOS
Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970)
689
1
74595
TrEMBL
Mitochondrion (Reliability: 3)
A0A6H0Y5X2_9PEZI
678
1
74401
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1R3RWV2_ASPC5
Aspergillus carbonarius (strain ITEM 5010)
672
1
73511
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Y7QJT0_9AGAM
669
0
72750
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Y9YT78_9APHY
675
1
74109
TrEMBL
Secretory Pathway (Reliability: 4)
W9PY29_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
Q5K6Z6_CRYNJ
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
733
1
80677
TrEMBL
Secretory Pathway (Reliability: 3)
A0A059J8W5_TRIIM
Trichophyton interdigitale (strain MR816)
633
0
69949
TrEMBL
other Location (Reliability: 2)
R1EY42_BOTPV
Botryosphaeria parva (strain UCR-NP2)
670
1
73320
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H5Q5R1_GIBSU
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A1CEK9_ASPCL
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
673
1
73389
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3M9YLH0_9PEZI
666
1
72592
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7R7XFX3_9EURO
673
1
73899
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D1YK40_9EURO
679
1
74293
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0X8HWL2_9SACH
685
1
74670
TrEMBL
Secretory Pathway (Reliability: 1)
A0A423VJC5_9PEZI
666
1
72736
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5J6SH86_9HELO
670
1
73090
TrEMBL
Secretory Pathway (Reliability: 1)
M5E4B4_MALS4
Malassezia sympodialis (strain ATCC 42132)
672
1
73467
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H3BH27_9AGAM
660
1
71814
TrEMBL
Secretory Pathway (Reliability: 1)
W7HSY1_9PEZI
684
1
74297
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H4UIS3_9HYPO
665
1
72702
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2B7Z2R9_9EURO
676
1
73824
TrEMBL
Secretory Pathway (Reliability: 2)
G8JXH1_ERECY
Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582)
689
1
74906
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2J6PP97_9HELO
670
1
73029
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2B7Y0N4_9EURO
676
1
73758
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4U7KQ83_9BASI
689
1
74497
TrEMBL
Mitochondrion (Reliability: 2)
A0A8H4FXM7_9ASCO
677
1
74100
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C3B9Z0_9AGAM
669
1
73507
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0A7CCM9_9BRAD
79
0
8518
TrEMBL
-
A0A317W932_ASPEC
Aspergillus eucalypticola (strain CBS 122712 / IBT 29274)
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
A0A871RKX4_DEKBR
677
1
74286
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3M7NM66_9EURO
673
1
73702
TrEMBL
Secretory Pathway (Reliability: 1)
A0A086SYT5_ACRC1
Acremonium chrysogenum (strain ATCC 11550 / CBS 779.69 / DSM 880 / IAM 14645 / JCM 23072 / IMI 49137)
667
1
72964
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6BYW3_CANAX
672
1
73241
TrEMBL
Secretory Pathway (Reliability: 1)
A0A100IJA2_ASPNG
672
1
73431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0U5G793_ASPCI
674
1
73649
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6A5SE49_9PLEO
674
1
73790
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8H3WBM2_9PEZI
664
1
72536
TrEMBL
Secretory Pathway (Reliability: 1)
A0A507AZI4_9PEZI
Thyridium curvatum
667
1
72473
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H7ING1_9AGAM
640
1
69627
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1J9RUB3_9PEZI
669
1
73108
TrEMBL
Secretory Pathway (Reliability: 2)
G2QXK9_THETT
Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126)
663
1
72585
TrEMBL
Secretory Pathway (Reliability: 1)
S0DPR1_GIBF5
Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831)
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
F2T234_AJEDA
Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68)
678
1
73838
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5E3WXY3_9AGAM
672
1
72926
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H3YDE6_9TREE
665
1
73182
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0S1S8F8_9PROT
Novacetimonas cocois
268
0
28790
TrEMBL
-
U9UPW7_RHIID
Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
383
0
42931
TrEMBL
other Location (Reliability: 2)
A0A0D2N7U1_HYPSF
Hypholoma sublateritium (strain FD-334 SS-4)
677
1
73633
TrEMBL
Mitochondrion (Reliability: 5)
A0A8J2MWP5_9PLEO
675
1
74141
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2T9Y4S9_9FUNG
655
0
72117
TrEMBL
other Location (Reliability: 1)
A0A4R8REP7_COLTR
664
1
72636
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Z1EXJ7_9HELO
670
1
73104
TrEMBL
Secretory Pathway (Reliability: 1)
A7EAD4_SCLS1
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1)
668
1
73059
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5N6X636_9EURO
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A397ISF6_9GLOM
660
1
73013
TrEMBL
Secretory Pathway (Reliability: 1)
A0A401KMH7_ASPAW
672
1
73459
TrEMBL
Secretory Pathway (Reliability: 1)
C0NS16_AJECG
Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
676
1
73825
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Y2TUM3_9PEZI
664
1
72853
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5C3PXS1_9APHY
664
1
73061
TrEMBL
Secretory Pathway (Reliability: 1)
A0A397HPX8_9EURO
671
1
73180
TrEMBL
Secretory Pathway (Reliability: 2)
A0A168CJA4_9HYPO
665
1
72515
TrEMBL
Secretory Pathway (Reliability: 1)
A0A428V0Q3_9HYPO
999
0
110786
TrEMBL
other Location (Reliability: 5)
A0A1C7MH82_GRIFR
657
1
72157
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0D2FGC7_9EURO
680
1
74322
TrEMBL
Secretory Pathway (Reliability: 1)
E6RG70_CRYGW
Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
744
1
82095
TrEMBL
Secretory Pathway (Reliability: 4)
R7SW21_DICSQ
Dichomitus squalens (strain LYAD-421)
672
1
73670
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5N7CFB9_PETAA
672
1
73433
TrEMBL
Secretory Pathway (Reliability: 2)
A0A135LH73_PENPA
672
1
73620
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0C9UGV3_SPHS4
Sphaerobolus stellatus (strain SS14)
683
1
74593
TrEMBL
Secretory Pathway (Reliability: 4)
A0A545V8S4_9HYPO
665
1
72509
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0C3NXP0_PISTI
482
1
52761
TrEMBL
Secretory Pathway (Reliability: 3)
A0A4S8WXD7_AURPU
691
1
75534
TrEMBL
other Location (Reliability: 5)
A0A3M6WG85_HORWE
688
1
75317
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1V8SXR0_9PEZI
690
1
75619
TrEMBL
Mitochondrion (Reliability: 5)
A0A5C3FBR0_9BASI
703
1
75748
TrEMBL
Mitochondrion (Reliability: 2)
A0A8J5TUM0_FUSOX
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A319CGP0_9EURO
673
1
73356
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2I1FY86_9GLOM
656
1
72799
TrEMBL
Secretory Pathway (Reliability: 1)
A0A395GPD2_9EURO
672
1
73431
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D7A2I4_9AGAR
661
0
71841
TrEMBL
Secretory Pathway (Reliability: 1)
A0A150ASS0_9PEZI
663
1
72370
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Q2W9U5_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4U0XYU0_9PEZI
680
1
74581
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0J9XAK4_GEOCN
667
0
73664
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1J7J6U8_9PEZI
655
0
71578
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B0NEC4_PUCGR
669
0
73197
TrEMBL
Secretory Pathway (Reliability: 5)
W9YPJ8_9EURO
677
1
74194
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4Y8DHM7_9HELO
670
1
73121
TrEMBL
Secretory Pathway (Reliability: 1)
T5BX11_AJEDE
678
1
73838
TrEMBL
Secretory Pathway (Reliability: 2)
X0CJ60_FUSOX
663
1
72577
TrEMBL
Secretory Pathway (Reliability: 1)
X0IIV4_FUSOX
663
1
72593
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4P6XI27_9ASCO
679
1
73625
TrEMBL
Secretory Pathway (Reliability: 1)
A0A165CYX0_EXIGL
672
1
72898
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3M7FAK6_HORWE
688
1
75321
TrEMBL
Mitochondrion (Reliability: 5)
A0A438ND16_EXOME
678
1
74519
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0A7CCN2_9BRAD
78
0
8451
TrEMBL
-
A0A1S7HG52_9SACH
673
1
73551
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4S9IK98_AURPU
692
1
75695
TrEMBL
other Location (Reliability: 4)
A0A4S9M472_AURPU
722
1
78800
TrEMBL
Secretory Pathway (Reliability: 3)
A0A084AZJ1_STACB
Stachybotrys chartarum (strain CBS 109288 / IBT 7711)
662
1
72389
TrEMBL
Secretory Pathway (Reliability: 1)
D4D5D5_TRIVH
Trichophyton verrucosum (strain HKI 0517)
696
1
76273
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D2G3X3_XYLBA
687
1
75052
TrEMBL
Secretory Pathway (Reliability: 3)
A0A4Q2D005_9AGAR
671
1
72934
TrEMBL
Secretory Pathway (Reliability: 2)
H2AVB9_KAZAF
Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 / NRRL Y-8276)
681
1
74588
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2C5ZNX9_9HYPO
666
1
72632
TrEMBL
Secretory Pathway (Reliability: 1)
A0A642VEB6_9ASCO
613
0
67139
TrEMBL
other Location (Reliability: 2)
A0A5M9KXT2_9PLEO
582
1
63377
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0G4MVU9_9PEZI
666
1
72643
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178CIH8_9EURO
684
1
74891
TrEMBL
Secretory Pathway (Reliability: 3)
N1Q5A5_DOTSN
Dothistroma septosporum (strain NZE10 / CBS 128990)
683
1
74477
TrEMBL
Secretory Pathway (Reliability: 5)
A0A401GY73_9APHY
678
1
74358
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1D2VB97_9ASCO
697
1
75726
TrEMBL
Secretory Pathway (Reliability: 1)
A0A409VSV7_PSICY
1157
0
126568
TrEMBL
other Location (Reliability: 1)
A0A1Y1WTB9_9FUNG
654
1
72059
TrEMBL
Secretory Pathway (Reliability: 1)
Q9C1C1_9BASI
669
0
72980
TrEMBL
Secretory Pathway (Reliability: 4)
F2PPH0_TRIEC
Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97)
677
1
74153
TrEMBL
Secretory Pathway (Reliability: 1)
G3AYE2_CANTC
Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 / NRRL Y-1498 / VKM Y-70)
681
1
74568
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G8RWI6_9APHY
660
0
72207
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8I2YF61_9AGAM
2124
2
228458
TrEMBL
other Location (Reliability: 3)
A0A0C9YHK1_9AGAM
674
1
73682
TrEMBL
Secretory Pathway (Reliability: 4)
G8BEU5_CANPC
Candida parapsilosis (strain CDC 317 / ATCC MYA-4646)
684
1
74548
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H8RB45_9HELO
671
1
73259
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F4YUB1_TALEM
670
1
73316
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1G4JT89_9SACH
682
1
74544
TrEMBL
Secretory Pathway (Reliability: 4)
A0A094B688_9PEZI
670
1
73032
TrEMBL
Secretory Pathway (Reliability: 1)
I8I8C8_ASPO3
Aspergillus oryzae (strain 3.042)
672
1
73450
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5N5DAB7_9PEZI
671
1
73495
TrEMBL
Secretory Pathway (Reliability: 2)
M7NI55_PNEMU
Pneumocystis murina (strain B123)
656
0
72901
TrEMBL
Secretory Pathway (Reliability: 1)
A0A316V4D9_9BASI
678
1
73283
TrEMBL
Secretory Pathway (Reliability: 1)
W6QK09_PENRF
Penicillium roqueforti (strain FM164)
673
1
73835
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1L7T6U8_FUSMA
663
1
72591
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8H6YQH8_9AGAR
672
1
73871
TrEMBL
Mitochondrion (Reliability: 4)
A0A0A7CBV7_9BRAD
79
0
8518
TrEMBL
-
A0A0L7LXM6_PLAF4
1070
0
122496
TrEMBL
-
A1XQQ5_MIRFO
645
0
70768
TrEMBL
-
A1XQQ6_RIMEX
608
0
67053
TrEMBL
-
D2XNF3_PHYPA
710
0
75492
TrEMBL
-
D2XNF4_PHYPA
707
0
76213
TrEMBL
-
O93240_PAROL
640
0
70609
TrEMBL
-
HSP82_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
709
0
81406
Swiss-Prot
Secretory Pathway (Reliability: 2)
HS701_ARATH
651
0
71358
Swiss-Prot
other Location (Reliability: 2)
HS702_ARATH
653
0
71387
Swiss-Prot
-
GRP75_HUMAN
679
0
73680
Swiss-Prot
-
CLPB_ECOLI
Escherichia coli (strain K12)
857
0
95585
Swiss-Prot
-
Q596W8_RHASR
639
0
70193
TrEMBL
-
Q596W9_RHASR
649
0
71080
TrEMBL
-
Q5KTW9_ENTHI
708
0
81893
TrEMBL
-
CLPX_LEPIC
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
420
0
46562
Swiss-Prot
-
Q8IB03_PLAF7
1070
0
122508
TrEMBL
-
Q8UWM8_XIPMA
637
0
70567
TrEMBL
-
Q8UWM9_XIPMA
639
0
70128
TrEMBL
other Location (Reliability: 1)
Q8UWN0_XIPMA
638
0
70278
TrEMBL
-
Q8YST5_NOSS1
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
839
0
93140
TrEMBL
-
DNAK_TETHA
618
0
66784
Swiss-Prot
other Location (Reliability: 4)
CLPB_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
854
0
96254
Swiss-Prot
-
HTPG_ECOLI
Escherichia coli (strain K12)
624
0
71423
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
-
1 * 70000 + 1 * 60000 + 1 * 44000 + 1 * 42000 + 1 * 36000 + 1 * 16000 + 1 * 13000, SDS-PAGE
16000
-
1 * 70000 + 1 * 60000 + 1 * 44000 + 1 * 42000 + 1 * 36000 + 1 * 16000 + 1 * 13000, SDS-PAGE
180000
P07900; P08238
gel filtration
184000
-
native PAGE
23000
-
1 * 44000 + 1 * 23000, 44-kDa ATP binding domain and 23-kDA COOH-terminal domain
30000
-
1 * 44000 + 1 * 30000
36000
-
1 * 70000 + 1 * 60000 + 1 * 44000 + 1 * 42000 + 1 * 36000 + 1 * 16000 + 1 * 13000, SDS-PAGE
42000
-
1 * 70000 + 1 * 60000 + 1 * 44000 + 1 * 42000 + 1 * 36000 + 1 * 16000 + 1 * 13000, SDS-PAGE
480000
-
N-terminally truncated protein, gel filtration
560000
-
full-length enzyme, gel filtration
570000
-
gel filtration
60000
611000
-
sedimentation equilibrium analysis
64000
-
gel filtration, calnexin, subunit of the multimeric enzyme
66000
-
Hsc66
70100
x * 70100, about, sequence calculation
72820
-
x * 72820, sequence calculation
73500
-
gel filtration
78000
-
grp78/BiP
82990
x * 82990, about, sequence calculation, x * 86000, recombinant His6-tagged enzyme, SDS-PAGE
86000
x * 82990, about, sequence calculation, x * 86000, recombinant His6-tagged enzyme, SDS-PAGE
90000
-
2 * 90000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heptamer
heterohexamer
a ring-shaped ClpB hexamer
hexamer
homodimer
homohexamer
monomer
oligomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the enzyme contains the endoplasmic reticulum-targeting signal sequence with the predicted signal peptide cleavage between Ser23 and Lys24 in PfClpB1
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
44-kDa wild-type Hsc70 ATPase fragment
-
hanging-drop vapour-diffusion method. Crystals of the C-terminal 10 kDa helical lid domain (residues 542–640) from a Caenorhabditis elegans Hsp70 homologue, diffract X-rays to 3.4 A, crystals belong to space group I2(1)2(1)2(1), with unit-cell parameters a = b = 197, c = 200 A
-
crystals of ClpB diffract to 1.95 A
-
crystals of ClpB nucleotide-binding domain 2 diffract to 2.5 A
-
crystals of ClpB nucleotide-binding domain diffract to 1.8 A
-
recombinant ClpX lacking the N-terminal Cys cluster domain, i.e. residues 71-446, hanging drop vapor diffusion at 22°C, reservoir solution contains 100 mM imidazole, pH 8.0, 1 M (NH4)2HPO4 and 200 mM NaCl, to obtain crystals of ClpX complexed with nucleotides, 5 mM ADP or ATPgammaS and MgCl2 are added, crystals diffract to 2.6 A
-
41.9-kDa human Hsp70 ATPase domain
-
atomic resolution analysis of the Hsp90 N-terminal domain binding energy landscape by simulating protein dynamics with binding partners such as ATP, ADP, shepherdin. The activity of the molecular chaperone may be linked to local folding-unfolding transitions and conformational switching of the active site lid upon binding and differences in the underlying protein dynamics as a function of the binding partner
-
Bag2-BNB-Hsc70-nucleotide-binding domain complex
-
cDNa sequence encoding alphabeta crystallin inserted into pET16b, expressed in Escherichia coli Bl21
-
crystal structures of four human Hsp70 isoforms are presented: nucleotide binding domains NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. All four proteins crystallize in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB is observed for the HSPA5-ADP complex. The structures presented support the view that the nucleotide binding domains of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the substrate binding domains and by accessory proteins
-
molecular docking studies with Hsc70 and apoptozole. The 3,5-bis(trifluoromethyl)phenyl group of apoptozole interacts with the binding site of a triphosphate moiety of ATP through polar interactions, and the two 4-methoxy phenyl moieties of apoptozole are located at the adenosine binding site of Hsc70. The CONH2 group of apoptozole can interact with the Glu376 side chain of Hsc70 via a hydrogen-bonding interaction
-
purified recombinant enzyme, X-ray diffraction structure determination and analysis, small angle X-ray scattering, modeling
purified isolated N-terminal domains of ClpB1 bound to GFP, ClpB1-sfGFP, X-ray diffraction structure determination and analysis at 1.8 A resolution
purified isolated N-terminal domains of ClpB1, X-ray diffraction structure determination and analysis at 1.65-2.01 A resolution
crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex, hanging drop vapour diffusion method, with the mother liquid containing 100 mM Tris/HCl, pH 7.0 and 42.5%(w/v) (NH4)2SO4. The crystals belong to the space group of P4(1)2(1)2 with the cell parameters of a = 112.17 A and c = 171.31 A
-
Hsp90, isoform Hsp82
-
nucleotide-binding domain of Hsp70 in complex with Hsp110 (nucleotide exchange factor Sse1p)
-
44-kDa wild-type stress70c ATPase fragment
-
electron cryomicroscopy reconstruction of ATP-activated trap mutant E271A/E668A, along with native ClpB, in complex with ADP or 5'-adenylyl-beta,gamma-imidodiphosphate, or nucleotide-free. Motif 2 of the ClpB domain M is positioned between the D1-large domains of neighboring subunits and could facilitate a concerted, ATP-driven conformational change in the AAA-1 ring. ATP is essential for high-affinity substrate binding to ClpB and cannot be substituted by 5'-adenylyl-beta,gamma-imidodiphosphate
-
44-kDa wild-type stress70er ATPase fragment
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V431F
-
mutant is unable to suppress the thermosensitivity of an Escherichia coli dnak103 deletion strain. Mutant is able to prevent the thermal aggregation of malate dehydrogenase
D526A
-
the DnaK mutant is unable to render a stimulated bichaperone complex with ClpB and doe s not reactivate glucose-6-phosphate dehydrogenase aggregates
E12C
-
C for fluorescent labelling
E12C/C-terminal truncation
-
containing residue 1-496, monomeric
E12C/E34A
-
mutant hydrolyses ATP about 10-times more slowly than wild-type protein, C for fluorescent labelling
E274A/E678A
-
inactive ClpB mutant
E279A/K476C/E678A
site-directed mutagenesis, the mutant shows a reduced number of subunits
E279Q/E678Q
-
ATP-hydrolysis deficient substrate-trapping variant
E34A
-
mutant hydrolyses ATP about 10-times more slowly than wild-type protein
F105W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
F276W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
F603W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
K476C
site-directed mutagenesis, the mutation weakens the dynamic interaction between M-domain and AAA1 ring resulting in M-domain dissociation and persistent, Hsp70-independent derepression of ClpB ATPase activity. Consequently, the ATPase activation by substrate is much stronger than in wild-type ClpB, and mutant ClpB-K476C has increased protein disaggregation activity, linked to its ability to unfold stable domains, an activity not observed for wild-type ClpB. ATP concentrations at half-maximal ATP hydrolysis rates of ClpB-K476C drop to 1.4 mM in the presence of substrate, compared with 4.3 mM for wild-type ClpB in the presence of substrate indicating that only the fully two-step activated state of ClpB reaches high ATPase activity at physiological ATP concentrations, which coincides with decreased cooperativity. Substrate-bound ClpB-K476C structures reveal large displacements of AAA2 pore loops
K70A
-
the DnaK mutant shows impaired ATP hydrolysis activity
T199A
-
the DnaK mutant shows impaired ATP hydrolysis activity
T213N
-
mutation in Walker A motif
T213N/T612N
-
mutations in Walker A motif
T612N
-
mutation in Walker A motif
V210C
-
DnaK (residue 1-655), C used for spin labeling experiments
W462F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
Y251A/K476C
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to wild-type enzyme
Y251A/K476C/Y653A
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to wild-type enzyme
Y251W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
Y653A/K476C
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to wild-type enzyme
Y812/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
A116N
-
reduced affinity to co-chaperone Hop in the presence of ATP analogue AMPPNP
K71E
-
no ATPase activity
T110I
-
wild-type affinity to co-chaperone Hop
E371C
site-directed mutagenesis, the chaperone activity of ClpBE731C is similar to that of the wild-type protein
S433C
site-directed mutagenesis, the chaperone activity of ClpBS433C is similar to that of the wild-type protein
S499C
site-directed mutagenesis, the mutant shows 10-20fold increased ATPase activity, the chaperone activity of mutantt ClpBS499C is 20-25% more efficient than the wild-type
A107N
the mutation increases ATPase activity about 5fold compared to the wild type
A17V
-
nucleotide-binding domain mutant
C63A
-
the ATPase activity displayed by the unmodified ATPase domain Kar2 is fully maintained when Cys63 is replaced with Ala
C63E
-
the mutant shows limited ATPase activity
C63F
-
the mutation leads to loss of ATPase activity. The mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63H
-
the mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63N
-
the mutant shows limited ATPase activity
C63P
-
the mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63V
-
the ATPase activity displayed by the unmodified ATPase domain Kar2 is fully maintained when Cys63 is replaced with Val
C63W
-
the mutation leads to loss of ATPase activity. The mutation leads to loss of ATPase activity. The mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63Y
-
the mutation leads to loss of ATPase activity. The mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
D61C/Q333C
-
C used to label with fluorescent dyes
E285Q
-
impaired hydrolysis of ATP at nucleotide-binding domain 1
E285Q/E687Q
-
impaired hydrolysis of ATP at nucleotide-binding domains 1 and 2
E381K
-
no loss of ATPase activity at the non permissive temperature of 37°C
E687Q
-
impaired hydrolysis of ATP at nucleotide-binding domain 2
K199N
-
missense Sis1 mutant exhibits greatly reduced binding affinity for the Ssa1 lid domain
K202N
-
missense Sis1 mutant exhibits greatly reduced binding affinity for the Ssa1 lid domain
K214N
-
missense Sis1 mutant exhibits greatly reduced binding affinity for the Ssa1 lid domain
K218T
K620T
-
impaired binding and hydrolysis of ATP at nucleotide-binding domain 2
L483W
-
substrate-binding domain mutant
Q385C
-
M domain
R34K
-
nucleotide-binding domain mutant
S25P
-
the mutation of Hsp82p impairs ATPase stimulation by Aha1p. The intrinsic ATPase activity of the mutant is comparable to that of wildtype enzyme
T101I
the mutation substantially reduces ATPase activity
T22F
-
increased ATP hydrolysis rate
E271A/E668A
E271Q/R576C/A821C
site-directed mutagenesis
E271Q/R576C/E668Q/A821C
site-directed mutagenesis
I403A/L406A/L413A/L420A/L432A/I439A/I446A/L449A
-
residues of hydrophobic interactions
I403A/L406A/L413A/L420A/L432A/I439A/I446A/L449A/I459A/L463A/L470A/V473A/I477A/L492A/L497A/L500A/L507A/L511A
-
residues of hydrophobic interactions
I459A/L463A/L470A/V473A/I477A/L492A/L497A/L500A/L507A/L511A
-
residues of hydrophobic interactions
K204A/T205A/R576C/A821C
site-directed mutagenesis
K204A/T205A/R576C/K601A/K602A/A821C
site-directed mutagenesis
K204Q
-
Walker A mutant
K204Q/K601Q
-
Walker A mutant
K601Q
-
Walker A mutant
L406A/L413A/L420A/L432A/I439A/I446A
-
residues of hydrophobic interactions
L406A/L413A/L420A/L432A/I439A/I446A/L463A/L470A/I477A/L492A/L500A/L507A
-
residues of hydrophobic interactions
L413A/L420A/L432A/I439A
-
residues of hydrophobic interactions
L413A/L420A/L432A/I439A/L470A/I477A/L492A/L500A
-
residues of hydrophobic interactions
L463A/L470A/I477A/L492A/L500A/L507A
-
residues of hydrophobic interactions
L470A/I477A/L492A/L500A
-
residues of hydrophobic interactions
Q184C/A390C
site-directed mutagenesis
Q184C/A390C/E668Q
site-directed mutagenesis
Q184C/A390C/K601A/K602A
site-directed mutagenesis
Q184C/A390C/R747A
site-directed mutagenesis
Q184C/E271Q/A390C
site-directed mutagenesis
Q184C/E271Q/A390C/E668Q
site-directed mutagenesis
Q184C/K204A/T205A/A390C
site-directed mutagenesis
Q184C/K204A/T205A/A390C/K601A/K602A
site-directed mutagenesis
Q184C/R322A/A390C
site-directed mutagenesis
R322A/R576C/A821C
site-directed mutagenesis
R576C/A821C
site-directed mutagenesis
R576C/E668Q/A821C
site-directed mutagenesis
R576C/K601A/K602A/A821C
site-directed mutagenesis
R576C/R747A/A821C
site-directed mutagenesis
S783C
-
C used to label specifically by thiol-reactive dyes
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
wild-type Hsp14.0 exhibits only slight dissociation of the oligomers at 50°C
50 - 63
-
no loss of activity after 60 min
59.7
-
melting temperature
60
-
1 h, activity decreases to 19%
65 - 80
-
almost complete loss of activity after 60 min
67
-
melting temperature
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP binding to ClpB stabilizes the enzyme hexamer and ADP dissociates it
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
both wild-type and recombinant proteins
Co-NTA agarose column chromatography and Superdex S200 gel filtration
DEAE-Sephacel, ATP-agarose
-
HisPur cobalt resin column chromatography and Superdex S200 gel filtration
-
HisTrap column chromatography and Superdex S200 gel filtration
-
isolation of the 44-kDa ATPase domain after limited proteolysis
-
Ni-NTA column chromatography
Ni-NTA column chromatography and Superdex S200 gel filtration
nucleotide-binding domain (residue 1-381), 44 kDa
-
Q-Sepharose column chromatography and Sephacryl S-200 gel filtration
recombinant ClpB
-
recombinant ClpX lacking the N-terminal Cys cluster domain, i.e. residues 71-446, Q-Sepharose, Superdex-200
-
recombinant DnaK
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration
recombinant His-tagged SUMO fusion enzyme mtHSP70 from Escherichia coli by nickel affinity chromatography, His-tag and SUMO cleavage and again nickel affinity exchange chromatography for tag removal, followed by gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21 pLysS by nickel affinity chromatograhy
recombinant Hsp104
-
recombinant Hsp90
-
recombinant Hsp90, metal affinity, gel filtration, ion-exchange chromatography
-
recombinant murine BiP, expressed in Escherichia coli
-
recombinant p97-VCP
-
recombinant PfHsp70, nickel-chelating Sepharose affinity chromatography
-
recombinant protein
-
recombinant wild-type and mutant enzymes by gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
recombinant wild-type Hsc7, expressed in Escherichia coli
-
recombinant yHsp90
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from spleen cDNA, DNA and amino acid sequence determination and analysis, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 pLysS, co-expression with His-tagged EhAha1c
DnaK (residue 1-638, residue 1-605, residue 1-388)
-
Escherichia coli-based overexpression system
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain M15
-
expressed in Escherichia coli strain Rosetta(DE3)
-
expression in Escherichia coli
expression of ClpX lacking the N-terminal Cys cluster domain, i.e. residues 71-446 in Escherichia coli
-
expression of GFP-Hsp70 fusion protein in HeLa cells
-
expression of His-tagged PfHsp70 in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
gene coding for ClpX sequenced
-
gene PnHSP70, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant transient expression of GFP-tagged enzyme expression in Arabidopsis thaliana mesophyll protoplast mitochondria, real-time PCR enzyme expression analysis
-
heat-shock cognate protein 70
Hsc 70, Hsc70 nucleotide binding domain (residue 1-381)
-
Hsp104 is expressed as a transgene in a human leukemic T-cell line (PEER). Hsp104 inhibited heat-shock-induced loss of viability in PEER cells, and Hsp104 cooperates with endogenous human Hsp70 and Hsc70 molecular chaperones and their J-domain-containing cochaperones Hdj1 and Hdj2 to produce a functional hybrid bichaperone network capable of refolding aggregated luciferase. Hsp104 shuttles across the nuclear envelope and enhances the chaperoning capacity of both the cytoplasm and nucleoplasm of intact cells
-
Hsp90beta, Hsp90beta-delta, Hsp90 C-terminal domain (residue 546-724), Hsp90beta-MC (residue 546-724)
-
nucleotide-binding domain (residue 1-381), 44 kDa
-
p9/25PCR1 consists of a 2.4-kb cDNA encoding maize pre-stress70er cloned and expressed in Escherichia coli
-
pLeHsc70-2 consists of a 2.1-kb cDNA encoding tomato stress70c cloned into pUC19
-
pT7-mBiP containing the cDNA sequence encoding mature mouse BiP cloned and expressed in Escherichia coli BL21
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), production of folded and soluble recombinant mortalin when co-expressed with the human Hsp70-escort protein 1, but Hsp70 is still likely prone to self-association
recombinant expression of His-tagged enzyme mtHSP70 as N-terminal SUMO fusion protein, lacking the gene sequence coding for N-terminal mitochondrial targeting peptide, in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant wild-type Hsc70, cloned and expressed in Escherichia coli
-
strains carrying plasmid pRLM163 designed for overexpression of a cloned dnaK gene
-
two different hsp90 cDNAs are isolated and characterized. Although nearly identical, an additional eight nucleotide sequence is present at the end of the 3'UTP of one of the two cDNAs
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of PoHsp70 is upregulated in a time-dependent manner by vaccination of flounder with a DNA vaccine, pSia10, that expresses a Streptococcus iniae antigen Sia10
low or high temperature, salinity, drought or PEG treatments as well as UV-B radiation induce up-regulation of PnHSP70 expression levels. The plant hormones abscisic acid and jasmonic acid also up-regulate the expression levels of PnHSP70
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
high-throughput screening method in 96-well plates for ATPase activity of DnaK. Screening of potential inhibitors
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lissin, N.M.; Venyaminov, S.Y.; Girshovich, A.S.
(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL
Nature
348
339-342
1990
Escherichia coli
Manually annotated by BRENDA team
Sadis, S.; Hightower, L.E.
Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange
Biochemistry
31
9406-9412
1992
Bos taurus, Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Blond-Elguindi, S.; Fourie, A.M.; Sambrook, J.F.; Gething, M.J.H.
Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers
J. Biol. Chem.
268
12730-12735
1993
Bos taurus, Cricetulus griseus, Mus musculus
Manually annotated by BRENDA team
Wawrzynow, A.; Wojtkowiak, D.; Marszalek, J.; Banecki, B.; Jonsen, M.; Graves, B.; Georgopoulos, C.; Zylicz, M.
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
EMBO J.
14
1867-1877
1995
Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
O'Brien, M.C.; McKay, D.B.
How potassium affects the activity of the molecular chaperone Hsc70 I. Potassium is required for optimal ATPase activity
J. Biol. Chem.
270
2247-2250
1995
Bos taurus, Escherichia coli
Manually annotated by BRENDA team
Wilbanks, S.M.; McKay, D.B.
How potassium affects the activity of the molecular chaperone Hsc70 II. Potassium binds specifically in the ATPase active site
J. Biol. Chem.
270
2251-2257
1995
Bos taurus
Manually annotated by BRENDA team
Jordan, R.; McMackens, R.
Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
J. Biol. Chem.
270
4563-4569
1995
Escherichia coli
Manually annotated by BRENDA team
Ha, J.H.; McKay, D.B.
Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding
Biochemistry
34
11635-11644
1995
Bos taurus, Escherichia coli
Manually annotated by BRENDA team
Miernyk, J.A.; Hayman, G.T.
ATPase activity and molecular chaperone function of the stress70 proteins
Plant Physiol.
110
419-424
1996
Escherichia coli, Homo sapiens, Solanum lycopersicum, Zea mays
Manually annotated by BRENDA team
Sriram, M.; Osipiuk, J.; Freeman, B.C.; Morimoto, R.I.; Joachimiak, A.
Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
Structure
5
403-414
1997
Bos taurus, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Russell, R.; Jordan, R.; McMacken, R.
Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone
Biochemistry
37
596-607
1998
Bos taurus, Escherichia coli
Manually annotated by BRENDA team
Slepenkov, S.; Witt, S.N.
Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: Evidence that a three-step reaction precedes ATP hydrolysis
Biochemistry
37
1015-1024
1998
Escherichia coli, Solanum lycopersicum, Zea mays
Manually annotated by BRENDA team
Li, X.; Su, R.T.C.; Hsu, H.; Sze, H.
The molecular chaperone calnexin associates with the vacuolar H+-ATPase from oat seedlings
Plant Cell
10
119-130
1998
Arabidopsis thaliana, Avena sativa, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Muchowski, P.J.; Clark, J.I.
ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin
Proc. Natl. Acad. Sci. USA
95
1004-1009
1998
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Hiromura, M.; Yano, M.; Mori, H.; Inoue, M.; Kido, H.
Intrinsic ADP-ATP exchange activity is a novel function of the molecular chaperone, Hsp70
J. Biol. Chem.
273
5435-5438
1998
Bos taurus, Escherichia coli
Manually annotated by BRENDA team
Panaretou, B.; Prodromou, C.; Roe, S.M.; O'Brien, R.; Ladbury, J.E.; Piper, P.W.; Pearl, L.H.
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
EMBO J.
17
4829-4836
1998
Saccharomyces cerevisiae, Escherichia coli, Saccharomyces cerevisiae PP30
Manually annotated by BRENDA team
McClellan, A.J.; Endres, J.B.; Vogel, J.P.; Palazzi, D.; Rose, M.D.; Brodsky, J.L.
Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER
Mol. Biol.
9
3533-3545
1998
Bos taurus, Cricetulus griseus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Brodsky, J.L.
Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin. Modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactions
Biochem. Pharmacol.
57
877-880
1999
Bos taurus, Saccharomyces cerevisiae, Rattus norvegicus
Manually annotated by BRENDA team
Chadli, A.; Ladjimi, M.M.; Baulieu, E.E.; Catelli, M.G.
Heat-induced oligomerization of the molecular chaperone Hsp90
J. Biol. Chem.
274
4133-4239
1999
Escherichia coli, Gallus sp., Neurospora crassa
Manually annotated by BRENDA team
Silberg, J.J.; Vickery, L.E.
Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli
J. Biol. Chem.
275
7779-7786
2000
Escherichia coli
Manually annotated by BRENDA team
Li, J.; Sha, B.
Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1)
Acta Crystallogr. Sect. D
57
909-911
2001
Escherichia coli
Manually annotated by BRENDA team
Li, J.; Sha, B.
Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 nucleotide-binding domain 2 (NBD2)
Acta Crystallogr. Sect. D
58
1030-1031
2002
Escherichia coli
Manually annotated by BRENDA team
Rowlands, M.G.; Newbatt, Y.M.; Prodromou, C.; Pearl, L.H.; Workman, P.; Aherne, W.
High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
Anal. Biochem.
327
176-183
2004
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Sehorn, M.G.; Slepenkov, S.V.; Witt, S.N.
Characterization of two partially unfolded intermediates of the molecular chaperone DnaK at low pH
Biochemistry
41
8499-8507
2002
Escherichia coli
Manually annotated by BRENDA team
Buczynski, G.; Slepenkov, S.V.; Sehorn, M.G.; Witt, S.N.
Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants
J. Biol. Chem.
276
27231-27236
2001
Escherichia coli
Manually annotated by BRENDA team
Richter, K.; Reinstein, J.; Buchner, J.
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle
J. Biol. Chem.
277
44905-44910
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lotz, G.P.; Lin, H.; Harst, A.; Obermann, W.M.
Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
J. Biol. Chem.
278
17228-17235
2003
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Song, C.; Wang, Q.; Li, C.C.
ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
J. Biol. Chem.
278
3648-3655
2003
Homo sapiens
Manually annotated by BRENDA team
Kim, D.Y.; Kim, K.K.
Crystal structure of ClpX molecular chaperone from Helicobacter pylori
J. Biol. Chem.
278
50664-50670
2003
Helicobacter pylori
Manually annotated by BRENDA team
Tupling, A.R.; Gramolini, A.O.; Duhamel, T.A.; Kondo, H.; Asahi, M.; Tsuchiya, S.C.; Borrelli, M.J.; Lepock, J.R.; Otsu, K.; Hori, M.; MacLennan, D.H.; Green, H.J.
HSP70 binds to the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1a) and prevents thermal inactivation
J. Biol. Chem.
279
52382-52389
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Grimminger, V.; Richter, K.; Imhof, A.; Buchner, J.; Walter, S.
The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104
J. Biol. Chem.
279
7378-7383
2004
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zeng, X.C.; Bhasin, S.; Wu, X.; Lee, J.G.; Maffi, S.; Nichols, C.J.; Lee, K.J.; Taylor, J.P.; Greene, L.E.; Eisenberg, E.
Hsp70 dynamics in vivo: effect of heat shock and protein aggregation
J. Cell Sci.
117
4991-5000
2004
Homo sapiens
Manually annotated by BRENDA team
Place, S.P.; Hofmann, G.E.
Temperature interactions of the molecular chaperone Hsc70 from the eurythermal marine goby Gillichthys mirabilis
J. Exp. Biol.
204
2675-2682
2001
Gillichthys mirabilis
Manually annotated by BRENDA team
Groemping, Y.; Klostermeier, D.; Herrmann, C.; Veit, T.; Seidel, R.; Reinstein, J.
Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE
J. Mol. Biol.
305
1173-1183
2001
Thermus thermophilus
Manually annotated by BRENDA team
McLaughlin, S.H.; Ventouras, L.A.; Lobbezoo, B.; Jackson, S.E.
Independent ATPase activity of hsp90 subunits creates a flexible assembly platform
J. Mol. Biol.
344
813-826
2004
Homo sapiens
Manually annotated by BRENDA team
Zhang, Z.; Quick, M.K.; Kanelakis, K.C.; Gijzen, M.; Krishna, P.
Characterization of a plant homolog of hop, a cochaperone of hsp90
Plant Physiol.
131
525-535
2003
Glycine max
Manually annotated by BRENDA team
Matambo, T.S.; Odunuga, O.O.; Boshoff, A.; Blatch, G.L.
Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70
Protein Expr. Purif.
33
214-222
2004
Plasmodium falciparum
Manually annotated by BRENDA team
Boshoff, A.; Hennessy, F.; Blatch, G.L.
The in vivo and in vitro characterization of DnaK from Agrobacterium tumefaciens RUOR
Protein Expr. Purif.
38
161-169
2004
Agrobacterium tumefaciens
Manually annotated by BRENDA team
Li, J.; Sha, B.
Crystal structure of the E. coli Hsp100 ClpB N-terminal domain
Structure
11
323-328
2003
Escherichia coli
Manually annotated by BRENDA team
Worrall, L.; Walkinshaw, M.D.
Crystallization and X-ray data analysis of the 10 kDa C-terminal lid subdomain from Caenorhabditis elegans Hsp70
Acta Crystallogr. Sect. F
62
938-943
2006
Caenorhabditis elegans
Manually annotated by BRENDA team
Sharp, S.; Workman, P.
Inhibitors of the HSP90 molecular chaperone: current status
Adv. Cancer Res.
95
323-348
2006
Homo sapiens
Manually annotated by BRENDA team
Deane, E.E.; Woo, N.Y.
Cloning and characterization of the hsp70 multigene family from silver sea bream: Modulated gene expression between warm and cold temperature acclimation
Biochem. Biophys. Res. Commun.
330
776-783
2005
Rhabdosargus sarba (Q596W8), Rhabdosargus sarba (Q596W9)
Manually annotated by BRENDA team
Wadhwa, R.; Takano, S.; Kaur, K.; Aida, S.; Yaguchi, T.; Kaul, Z.; Hirano, T.; Taira, K.; Kaul, S.C.
Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60
Biochem. J.
391
185-190
2005
Homo sapiens
Manually annotated by BRENDA team
Li, J.; Wu, Y.; Qian, X.; Sha, B.
Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex
Biochem. J.
398
353-360
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mosser, D.D.; Ho, S.; Glover, J.R.
Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling
Biochemistry
43
8107-8115
2004
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chesnokova, L.S.; Witt, S.N.
Switches, catapults, and chaperones: Steady-state kinetic analysis of Hsp70-substrate interactions. [Erratum to document cited in CA143:262085]
Biochemistry
44
13224
2005
Escherichia coli
-
Manually annotated by BRENDA team
Tanaka, N.; Nakao, S.; Chatellier, J.; Tani, Y.; Tada, T.; Kunugi, S.
Effect of the polypeptide binding on the thermodynamic stability of the substrate binding domain of the DnaK chaperone
Biochim. Biophys. Acta
1748
1-8
2005
Escherichia coli
Manually annotated by BRENDA team
Brough, P.A.; Barril, X.; Beswick, M.; Dymock, B.W.; Drysdale, M.J.; Wright, L.; Grant, K.; Massey, A.; Surgenor, A.; Workman, P.
3-(5-Chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides as inhibitors of the Hsp90 molecular chaperone
Bioorg. Med. Chem. Lett.
15
5197-5201
2005
Homo sapiens
Manually annotated by BRENDA team
Zippay, M.L.; Place, S.P.; Hofmann, G.E.
The molecular chaperone Hsc70 from a eurythermal marine goby exhibits temperature insensitivity during luciferase refolding assays
Comp. Biochem. Physiol. A
138A
1-7
2004
Gillichthys mirabilis
Manually annotated by BRENDA team
Takle, H.; McLeod, A.; Andersen, O.
Cloning and characterization of the executioner caspases 3, 6, 7 and Hsp70 in hyperthermic Atlantic salmon (Salmo salar) embryos
Comp. Biochem. Physiol. B Biochem. Mol. Biol.
144
188-198
2006
Salmo salar
Manually annotated by BRENDA team
Kourtidis, A.; Scouras, Z.G.
Analysis and characterization of the transcriptional unit of a new Mytilus galloprovincialis (Mollusca: Bivalvia) hsp70 gene
DNA Seq.
16
36-43
2005
Mytilus galloprovincialis
Manually annotated by BRENDA team
Moro, F.; Fernandez-Saiz, V.; Slutsky, O.; Azem, A.; Muga, A.
Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70. Role of the divergent C-terminal alpha-helical subdomain
FEBS J.
272
3184-3196
2005
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Groemping, Y.; Seidel, R.; Reinstein, J.
Balance of ATPase stimulation and nucleotide exchange is not required for efficient refolding activity of the DnaK chaperone
FEBS Lett.
579
5713-5717
2005
Thermus thermophilus
Manually annotated by BRENDA team
Brunt, S.A.; Silver, J.C.
Molecular cloning and characterization of two different cDNAs encoding the molecular chaperone Hsp90 in the oomycete Achlya ambisexualis
Fungal Genet. Biol.
41
239-252
2004
Achlya ambisexualis
Manually annotated by BRENDA team
Yamashita, M.; Hirayoshi, K.; Nagata, K.
Characterization of multiple members of the HSP70 family in platyfish culture cells: molecular evolution of stress protein HSP70 in vertebrates
Gene
336
207-218
2004
Xiphophorus maculatus (Q8UWM8), Xiphophorus maculatus (Q8UWM9), Xiphophorus maculatus (Q8UWN0)
Manually annotated by BRENDA team
Cheng, Q.; Hallmann, A.; Edwards, L.; Miller, S.M.
Characterization of a heat-shock-inducible hsp70 gene of the green alga Volvox carteri
Gene
371
112-120
2006
Volvox carteri
Manually annotated by BRENDA team
Ravaux, J.; Toullec, J.Y.; Leger, N.; Lopez, P.; Gaill, F.; Shillito, B.
First hsp70 from two hydrothermal vent shrimps, Mirocaris fortunata and Rimicaris exoculata: Characterization and sequence analysis
Gene
386
162-172
2006
Mirocaris fortunata (A1XQQ5), Mirocaris fortunata, Rimicaris exoculata (A1XQQ6), Rimicaris exoculata
Manually annotated by BRENDA team
Newton-Howes, J.; Heath, D.D.; Shoemaker, C.B.; Grant, W.N.
Characterisation and expression of an Hsp70 gene from Parastrongyloides trichosuri
Int. J. Parasitol.
36
467-474
2006
Parastrongyloides trichosuri
Manually annotated by BRENDA team
Boesl, B.; Grimminger, V.; Walter, S.
Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides
J. Biol. Chem.
280
38170-38176
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Swain, J.F.; Schulz, E.G.; Gierasch, L.M.
Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states
J. Biol. Chem.
281
1605-1611
2006
Escherichia coli
Manually annotated by BRENDA team
Andersson, F.I.; Blakytny, R.; Kirstein, J.; Turgay, K.; Bukau, B.; Mogk, A.; Clarke, A.K.
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity
J. Biol. Chem.
281
5468-5475
2006
Synechococcus elongatus
Manually annotated by BRENDA team
Wegele, H.; Wandinger, S.K.; Schmid, A.B.; Reinstein, J.; Buchner, J.
Substrate transfer from the chaperone Hsp70 to Hsp90
J. Mol. Biol.
356
802-811
2006
Homo sapiens
Manually annotated by BRENDA team
Targosz, A.; Pierzchalski, P.; Krawiec, A.; Szczyrk, U.; Brzozowski, T.; Konturek, S.J.; Pawlik, W.W.
Helicobacter pylori inhibits expression of heat shock protein 70 (HSP70) in human epithelial cell line. Importance of Cag A protein
J. Physiol. Pharmacol.
57
265-278
2006
Homo sapiens
Manually annotated by BRENDA team
Sjoegren, L.L.; MacDonald, T.M.; Sutinen, S.; Clarke, A.K.
Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content
Plant Physiol.
136
4114-4126
2004
Arabidopsis thaliana
Manually annotated by BRENDA team
Chang, L.; Bertelsen, E.B.; Wisen, S.; Larsen, E.M.; Zuiderweg, E.R.; Gestwicki, J.E.
High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
Anal. Biochem.
372
167-176
2008
Escherichia coli
Manually annotated by BRENDA team
Nagy, M.; Akoev, V.; Zolkiewski, M.
Domain stability in the AAA+ ATPase ClpB from Escherichia coli
Arch. Biochem. Biophys.
453
63-69
2006
Escherichia coli
Manually annotated by BRENDA team
Mao, Y.; Deng, A.; Qu, N.; Wu, X.
ATPase domain of Hsp70 exhibits intrinsic ATP-ADP exchange activity
Biochemistry (Moscow)
71
1222-1229
2006
Bos taurus
Manually annotated by BRENDA team
Hawkins, T.A.; Haramis, A.; Etard, C.; Prodromou, C.; Vaughan, C.K.; Ashworth, R.; Ray, S.; Behra, M.; Holder, N.; Talbot, W.S.; Pearl, L.H.; Strahle, U.; Wilson, S.W.
The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis
Development
135
1147-1156
2008
Danio rerio
Manually annotated by BRENDA team
Weitzmann, A.; Baldes, C.; Dudek, J.; Zimmermann, R.
The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum - a quantitative approach
FEBS J.
274
5175-5187
2007
Canis lupus familiaris
Manually annotated by BRENDA team
Loovers, H.M.; Guinan, E.; Jones, G.W.
Importance of Hsp70 ATPase domain in yeast prion propagation
Genetics
175
621-630
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Boshoff, A.; Stephens, L.L.; Blatch, G.L.
The Agrobacterium tumefaciens DnaK: ATPase cycle, oligomeric state and chaperone properties
Int. J. Biochem. Cell Biol.
40
804-812
2008
Agrobacterium tumefaciens
Manually annotated by BRENDA team
Sugimoto, S.; Yoshida, H.; Mizunoe, Y.; Tsuruno, K.; Nakayama, J.; Sonomoto, K.
Structural and functional conversion of molecular chaperone ClpB from the gram-positive halophilic lactic acid bacterium Tetragenococcus halophilus mediated by ATP and stress
J. Bacteriol.
188
8070-8078
2006
Tetragenococcus halophilus
Manually annotated by BRENDA team
McLaughlin, S.H.; Sobott, F.; Yao, Z.P.; Zhang, W.; Nielsen, P.R.; Grossmann, J.G.; Laue, E.D.; Robinson, C.V.; Jackson, S.E.
The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins
J. Mol. Biol.
356
746-758
2006
Homo sapiens
Manually annotated by BRENDA team
Schaupp, A.; Marcinowski, M.; Grimminger, V.; Boesl, B.; Walter, S.
Processing of proteins by the molecular chaperone Hsp104
J. Mol. Biol.
370
674-686
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lee, S.; Choi, J.M.; Tsai, F.T.
Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB
Mol. Cell
25
261-271
2007
Thermus thermophilus
Manually annotated by BRENDA team
Doyle, S.M.; Shorter, J.; Zolkiewski, M.; Hoskins, J.R.; Lindquist, S.; Wickner, S.
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
Nat. Struct. Mol. Biol.
14
114-122
2007
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Colombo, G.; Morra, G.; Meli, M.; Verkhivker, G.
Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution
Proc. Natl. Acad. Sci. USA
105
7976-7981
2008
Homo sapiens
Manually annotated by BRENDA team
Saji, H.; Iizuka, R.; Yoshida, T.; Abe, T.; Kidokoro, S.; Ishii, N.; Yohda, M.
Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, Sulfolobus tokodaii strain 7
Proteins
71
771-782
2008
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Manually annotated by BRENDA team
Needham, P.G.; Masison, D.C.
Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities
Arch. Biochem. Biophys.
478
167-174
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Watanabe, Y.H.; Nakazaki, Y.; Suno, R.; Yoshida, M.
Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity
Biochem. J.
421
71-77
2009
Thermus thermophilus
Manually annotated by BRENDA team
Sugimoto, S.; Saruwatari, K.; Higashi, C.; Tsuruno, K.; Matsumoto, S.; Nakayama, J.; Sonomoto, K.
In vivo and in vitro complementation study comparing the function of DnaK chaperone systems from halophilic lactic acid bacterium Tetragenococcus halophilus and Escherichia coli
Biosci. Biotechnol. Biochem.
72
811-822
2008
Escherichia coli, Tetragenococcus halophilus (Q93R27), Tetragenococcus halophilus JCM 5888 (Q93R27)
Manually annotated by BRENDA team
Polier, S.; Dragovic, Z.; Hartl, F.U.; Bracher, A.
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
Cell
133
1068-1079
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Graf, C.; Stankiewicz, M.; Kramer, G.; Mayer, M.P.
Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine
EMBO J.
28
602-613
2009
Escherichia coli
Manually annotated by BRENDA team
Karradt, A.; Sobanski, J.; Mattow, J.; Lockau, W.; Baier, K.
NblA, a key protein of phycobilisome degradation, interacts with ClpC, a HSP100 chaperone partner of a cyanobacterial Clp protease
J. Biol. Chem.
283
32394-32403
2008
Nostoc sp. PCC 7120 = FACHB-418 (Q8YST5)
Manually annotated by BRENDA team
Werbeck, N.D.; Schlee, S.; Reinstein, J.
Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB
J. Mol. Biol.
378
178-190
2008
Thermus thermophilus
Manually annotated by BRENDA team
Onuoha, S.C.; Coulstock, E.T.; Grossmann, J.G.; Jackson, S.E.
Structural studies on the co-chaperone Hop and its complexes with Hsp90
J. Mol. Biol.
379
732-744
2008
Homo sapiens
Manually annotated by BRENDA team
Bhattacharya, A.; Kurochkin, A.V.; Yip, G.N.; Zhang, Y.; Bertelsen, E.B.; Zuiderweg, E.R.
Allostery in Hsp70 chaperones is transduced by subdomain rotations
J. Mol. Biol.
388
475-490
2009
Thermus thermophilus
Manually annotated by BRENDA team
Southworth, D.R.; Agard, D.A.
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
Mol. Cell
32
631-640
2008
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Xu, Z.; Page, R.C.; Gomes, M.M.; Kohli, E.; Nix, J.C.; Herr, A.B.; Patterson, C.; Misra, S.
Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2
Nat. Struct. Mol. Biol.
15
1309-1317
2008
Homo sapiens
Manually annotated by BRENDA team
Hessling, M.; Richter, K.; Buchner, J.
Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
Nat. Struct. Mol. Biol.
16
287-293
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Bertelsen, E.B.; Chang, L.; Gestwicki, J.E.; Zuiderweg, E.R.
Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
Proc. Natl. Acad. Sci. USA
106
8471-8476
2009
Escherichia coli
Manually annotated by BRENDA team
Nagy, M.; Wu, H.C.; Liu, Z.; Kedzierska-Mieszkowska, S.; Zolkiewski, M.
Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB
Protein Sci.
18
287-293
2009
Escherichia coli
Manually annotated by BRENDA team
Neckers, L.; Mollapour, M.; Tsutsumi, S.
The complex dance of the molecular chaperone Hsp90
Trends Biochem. Sci.
34
223-226
2009
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Wisniewska, M.; Karlberg, T.; Lehtioe, L.; Johansson, I.; Kotenyova, T.; Moche, M.; Schueler, H.
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B, and HSPA5/BiP/GRP78
PLoS ONE
5
e8625
2010
Homo sapiens
Manually annotated by BRENDA team
Taldone, T.; Sun, W.; Chiosis, G.
Discovery and development of heat shock protein 90 inhibitors
Bioorg. Med. Chem.
17
2225-2235
2009
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Janin, Y.L.
ATPase inhibitors of heat-shock protein 90, second season
Drug Discov. Today
15
342-353
2010
Homo sapiens
Manually annotated by BRENDA team
Cho, H.J.; Gee, H.Y.; Baek, K.H.; Ko, S.K.; Park, J.M.; Lee, H.; Kim, N.D.; Lee, M.G.; Shin, I.
A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator
J. Am. Chem. Soc.
133
20267-20276
2011
Homo sapiens
Manually annotated by BRENDA team
Gao, X.C.; Zhou, C.J.; Zhou, Z.R.; Wu, M.; Cao, C.Y.; Hu, H.Y.
The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation
J. Biol. Chem.
287
6044-6052
2012
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Gierasch, L.; Bahar, I.
Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs
PLoS Comput. Biol.
6
e1000931
2010
Homo sapiens
-
Manually annotated by BRENDA team
Ngansop, F.; Li, H.; Zolkiewska, A.; Zolkiewski, M.
Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum
Biochem. Biophys. Res. Commun.
439
191-195
2013
Plasmodium falciparum (Q8IB03), Plasmodium falciparum
Manually annotated by BRENDA team
Aguado, A.; Fernandez-Higuero, J.A.; Cabrera, Y.; Moro, F.; Muga, A.
ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins
Biochem. J.
466
561-570
2015
Plasmodium falciparum (Q8IB03)
Manually annotated by BRENDA team
Araujo, T.L.; Borges, J.C.; Ramos, C.H.; Meyer-Fernandes, J.R.; Oliveira Junior, R.S.; Pascutti, P.G.; Foguel, D.; Palhano, F.L.
Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity
Biochemistry
53
2884-2889
2014
Homo sapiens
Manually annotated by BRENDA team
Flores-Perez, U.; Jarvis, P.
Molecular chaperone involvement in chloroplast protein import
Biochim. Biophys. Acta
1833
332-340
2013
Physcomitrium patens, Physcomitrium patens (D2XNF3), Physcomitrium patens (D2XNF4), Pisum sativum, Arabidopsis thaliana (P22953), Arabidopsis thaliana (P22954)
Manually annotated by BRENDA team
Hu, Y.H.; Dang, W.; Zhang, M.; Sun, L.
Japanese flounder (Paralichthys olivaceus) Hsp70: adjuvant effect and its dependence on the intrinsic ATPase activity
Fish Shellfish Immunol.
33
829-834
2012
Paralichthys olivaceus (O93240), Paralichthys olivaceus
Manually annotated by BRENDA team
Yokoyama, Y.; Ohtaki, A.; Jantan, I.; Yohda, M.; Nakamoto, H.
Goniothalamin enhances the ATPase activity of the molecular chaperone Hsp90 but inhibits its chaperone activity
J. Biochem.
157
161-168
2015
Schizosaccharomyces pombe, Synechococcus elongatus, Synechococcus elongatus PCC 7942
Manually annotated by BRENDA team
Cai, K.; Frederick, R.O.; Kim, J.H.; Reinen, N.M.; Tonelli, M.; Markley, J.L.
Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)
J. Biol. Chem.
288
28755-28770
2013
Homo sapiens
Manually annotated by BRENDA team
Yamamoto, S.; Subedi, G.P.; Hanashima, S.; Satoh, T.; Otaka, M.; Wakui, H.; Sawada, K.; Yokota, S.; Yamaguchi, Y.; Kubota, H.; Itoh, H.
ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP)
J. Biol. Chem.
289
9880-9886
2014
Sus scrofa, Sus scrofa (O02705)
Manually annotated by BRENDA team
Yamasaki, T.; Oohata, Y.; Nakamura, T.; Watanabe, Y.H.
Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement
J. Biol. Chem.
290
9789-9800
2015
Thermus thermophilus (Q9RA63), Thermus thermophilus
Manually annotated by BRENDA team
Blamowska, M.; Neupert, W.; Hell, K.
Biogenesis of the mitochondrial Hsp70 chaperone
J. Cell Biol.
199
125-135
2012
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Singh, M.; Shah, V.; Tatu, U.
A novel C-terminal homologue of Aha1 co-chaperone binds to heat shock protein 90 and stimulates its ATPase activity in Entamoeba histolytica
J. Mol. Biol.
426
1786-1798
2014
Entamoeba histolytica (Q5KTW9), Entamoeba histolytica, Entamoeba histolytica HM-1: IMSS (Q5KTW9)
Manually annotated by BRENDA team
Bartolini, M.; Wainer, I.W.; Bertucci, C.; Andrisano, V.
The rapid and direct determination of ATPase activity by ion exchange chromatography and the application to the activity of heat shock protein-90
J. Pharm. Biomed. Anal.
73
77-81
2013
Homo sapiens
Manually annotated by BRENDA team
Tyc, J.; Klingbeil, M.M.; Lukes, J.
Mitochondrial heat shock protein machinery hsp70/hsp40 is indispensable for proper mitochondrial DNA maintenance and replication
mBio
6
e02425-14
2015
Trypanosoma brucei
Manually annotated by BRENDA team
General, I.J.; Liu, Y.; Blackburn, M.E.; Mao, W.; Gierasch, L.M.; Bahar, I.
ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones
PLoS Comput. Biol.
10
e1003624
2014
Escherichia coli
Manually annotated by BRENDA team
Dores-Silva, P.R.; Barbosa, L.R.; Ramos, C.H.; Borges, J.C.
Human mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization
PLoS ONE
10
e0117170
2015
Homo sapiens (P38646), Homo sapiens
Manually annotated by BRENDA team
Liu, S.; Wang, J.; Cong, B.; Huang, X.; Chen, K.; Zhang, P.
Characterization and expression analysis of a mitochondrial heat-shock protein 70 gene from the Antarctic moss Pohlia nutans
Polar Biol.
37
1145-1155
2014
Pohlia nutans
-
Manually annotated by BRENDA team
AhYoung, A.P.; Koehl, A.; Cascio, D.; Egea, P.F.
Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design
Protein Sci.
24
1508-1520
2015
Plasmodium falciparum, Plasmodium falciparum (A0A0L7LXM6)
Manually annotated by BRENDA team
Dhara, A.; Hussain, M.; Datta, D.; Kumar, M.
Insights to the assembly of a functionally active leptospiral ClpP1P2 protease complex along with its ATPase chaperone ClpX
ACS Omega
4
12880-12895
2019
Leptospira interrogans (Q72SG5), Leptospira interrogans, Leptospira interrogans Fiocruz L1-130 (Q72SG5)
Manually annotated by BRENDA team
Ranaweera, C.B.; Glaza, P.; Yang, T.; Zolkiewski, M.
Interaction of substrate-mimicking peptides with the AAA+ ATPase ClpB from Escherichia coli
Arch. Biochem. Biophys.
655
12-17
2018
Escherichia coli
Manually annotated by BRENDA team
Pearl, L.
Review The HSP90 molecular chaperone - an enigmatic ATPase
Biopolymers
105
594-607
2016
Homo sapiens (P07900 and P08238)
Manually annotated by BRENDA team
Krajewska, J.; Arent, Z.; Wieckowski, D.; Zolkiewski, M.; Kedzierska-Mieszkowska, S.
Immunoreactivity of the AAA+ chaperone ClpB from Leptospira interrogans with sera from Leptospira-infected animals
BMC Microbiol.
16
151
2016
Leptospira interrogans
Manually annotated by BRENDA team
Deville, C.; Franke, K.; Mogk, A.; Bukau, B.; Saibil, H.R.
Two-step activation mechanism of the ClpB disaggregase for sequential substrate threading by the main ATPase motor
Cell Rep.
27
3433-3446.e4
2019
Escherichia coli (P63284)
Manually annotated by BRENDA team
Tripathi, P.; Parijat, P.; Patel, V.K.; Batra, J.K.
The amino-terminal domain of Mycobacterium tuberculosis ClpB protein plays a crucial role in its substrate disaggregation activity
FEBS Open Bio
8
1669-1690
2018
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Rotanova, T.V.; Andrianova, A.G.; Kudzhaev, A.M.; Li, M.; Botos, I.; Wlodawer, A.; Gustchina, A.
New insights into structural and functional relationships between LonA proteases and ClpB chaperones
FEBS Open Bio
9
1536-1551
2019
Escherichia coli (P63284), Thermus thermophilus (Q9RA63)
Manually annotated by BRENDA team
Johnston, D.M.; Miot, M.; Hoskins, J.R.; Wickner, S.; Doyle, S.M.
Substrate discrimination by ClpB and Hsp104
Front. Mol. Biosci.
4
36
2017
Saccharomyces cerevisiae, Thermus thermophilus (Q9RA63)
Manually annotated by BRENDA team
Krajewska, J.; Arent, Z.; Zolkiewski, M.; K?dzierska-Mieszkowska, S.
Isolation and identification of putative protein substrates of the AAA+ molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans
Int. J. Mol. Sci.
19
E1234
2018
Leptospira interrogans, Leptospira interrogans B42
Manually annotated by BRENDA team
Yokoyama, Y.; Ohtaki, A.; Jantan, I.; Yohda, M.; Nakamoto, H.
Goniothalamin enhances the ATPase activity of the molecular chaperone Hsp90 but inhibits its chaperone activity
J. Biochem.
157
161-168
2015
Schizosaccharomyces pombe, Synechococcus elongatus, Synechococcus elongatus PCC 7942
Manually annotated by BRENDA team
Xu, M.; Marsh, H.; Sevier, C.
A conserved cysteine within the ATPase domain of the endoplasmic reticulum chaperone BiP is necessary for a complete complement of BiP activities
J. Mol. Biol.
428
4168-4184
2016
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Cabrera, Y.; Dublang, L.; Fernandez-Higuero, J.; Albesa-Jove, D.; Lucas, M.; Viguera, A.; Guerin, M.; Vilar, J.; Muga, A.; Moro, F.
Regulation of human Hsc70 ATPase and chaperone activities by Apg2 role of the acidic subdomain
J. Mol. Biol.
431
444-461
2019
Homo sapiens
Manually annotated by BRENDA team
Dutkiewicz, R.; Nowak, M.; Craig, E.; Marszalek, J.
Fe-S cluster Hsp70 chaperones the ATPase cycle and protein interactions
Methods Enzymol.
595
161-184
2017
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Schulze, A.; Beliu, G.; Helmerich, D.; Schubert, J.; Pearl, L.; Prodromou, C.; Neuweiler, H.
Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism
Nat. Chem. Biol.
12
628-635
2016
Saccharomyces cerevisiae (P02829), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Goloubinoff, P.; Sassi, A.S.; Fauvet, B.; Barducci, A.; De Los Rios, P.
Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins
Nat. Chem. Biol.
14
388-395
2018
Escherichia coli
Manually annotated by BRENDA team
Mercier, R.; Wolmarans, A.; Schubert, J.; Neuweiler, H.; Johnson, J.; LaPointe, P.
The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation
Nat. Commun.
10
1273
2019
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Krajewska, J.; Modrak-Wojcik, A.; Arent, Z.J.; Wieckowski, D.; Zolkiewski, M.; Bzowska, A.; Kedzierska-Mieszkowska, S.
Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans
PLoS ONE
12
e0181118
2017
Escherichia coli, Leptospira interrogans
Manually annotated by BRENDA team
Fernandez-Higuero, J.A.; Aguado, A.; Perales-Calvo, J.; Moro, F.; Muga, A.
Activation of the DnaK-ClpB complex is regulated by the properties of the bound substrate
Sci. Rep.
8
5796
2018
Escherichia coli
Manually annotated by BRENDA team