Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
an N6-[small archaeal modifier protein]-[protein]-L-lysine + H2O
a [protein]-L-lysine + a small archaeal modifier protein
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
SAMP1 + [molybdopterin synthase MoaE]-L-lysine
N6-SAMP1-[protein]-L-lysine + H2O
SAMP1 + [protein]-L-lysine
N6-SAMP2-[protein]-L-lysine + H2O
SAMP2 + [protein]-L-lysine
N6-[SAMP1]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP1
N6-[SAMP3]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP3
additional information
?
-
an N6-[small archaeal modifier protein]-[protein]-L-lysine + H2O
a [protein]-L-lysine + a small archaeal modifier protein
Hvo_2505 mixed with Ta0895_VSGG-Ta0547 results cleavage products at 18 kDa (Ta0547) and 14 kDa (Ta0895_VSGG). Hvo_2505 is active at 24°C, 37°C and 48°C cleaving a substantial percentage of Ta0895_VAGG-ScRpn11 and Ta0895_VSGG-Ta0547. No cleavage activity is detected at lower (10°C) temperature. Inactive on Ta1019-ScRpn11 and Mbur_1415-ScRpn11 fusion protein substrates
-
-
?
an N6-[small archaeal modifier protein]-[protein]-L-lysine + H2O
a [protein]-L-lysine + a small archaeal modifier protein
Hvo_2505 mixed with Ta0895_VSGG-Ta0547 results cleavage products at 18 kDa (Ta0547) and 14 kDa (Ta0895_VSGG). Hvo_2505 is active at 24°C, 37°C and 48°C cleaving a substantial percentage of Ta0895_VAGG-ScRpn11 and Ta0895_VSGG-Ta0547. No cleavage activity is detected at lower (10°C) temperature. Inactive on Ta1019-ScRpn11 and Mbur_1415-ScRpn11 fusion protein substrates
-
-
?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
-
-
?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
SAMP1 + [molybdopterin synthase MoaE]-L-lysine
the enzyme cleaves isopeptide-liked SAMP1 from molybdopterin synthase MoaE. It also cleaves linear fusions of SAMP to molybdopterin synthase MoaE
-
-
?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
-
-
?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
SAMP1 + [molybdopterin synthase MoaE]-L-lysine
the enzyme cleaves isopeptide-liked SAMP1 from molybdopterin synthase MoaE. It also cleaves linear fusions of SAMP to molybdopterin synthase MoaE
-
-
?
N6-SAMP1-[protein]-L-lysine + H2O
SAMP1 + [protein]-L-lysine
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins
-
-
?
N6-SAMP1-[protein]-L-lysine + H2O
SAMP1 + [protein]-L-lysine
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins
-
-
?
N6-SAMP2-[protein]-L-lysine + H2O
SAMP2 + [protein]-L-lysine
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins
-
-
?
N6-SAMP2-[protein]-L-lysine + H2O
SAMP2 + [protein]-L-lysine
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins
-
-
?
N6-[SAMP1]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP1
MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1
-
-
?
N6-[SAMP1]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP1
MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1
-
-
?
N6-[SAMP3]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP3
MoaE, i.e. molybdopterin synthase large subunit homolog
SAMP3 protein conjugates are dependent on the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease JAMM1
-
?
N6-[SAMP3]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP3
MoaE, i.e. molybdopterin synthase large subunit homolog
SAMP3 protein conjugates are dependent on the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease JAMM1
-
?
additional information
?
-
the enzyme can cleave proteins attached to SAMP1 by linear and isopeptide bonds. The enzyme is inactive in hydrolyzing the amide bond that links aminomethylcoumarin to the C-terminus of monomeric ubiquinone or diglycine
-
-
?
additional information
?
-
-
the enzyme can cleave proteins attached to SAMP1 by linear and isopeptide bonds. The enzyme is inactive in hydrolyzing the amide bond that links aminomethylcoumarin to the C-terminus of monomeric ubiquinone or diglycine
-
-
?
additional information
?
-
JAMM1 is a metalloprotease with relatively broad substrate specificity, able to cleave a wide variety of proteins conjugated to SAMP3 as well as SAMP1/2
-
-
?
additional information
?
-
-
JAMM1 is a metalloprotease with relatively broad substrate specificity, able to cleave a wide variety of proteins conjugated to SAMP3 as well as SAMP1/2
-
-
?
additional information
?
-
JAMM1 is a metalloprotease with relatively broad substrate specificity, able to cleave a wide variety of proteins conjugated to SAMP3 as well as SAMP1/2
-
-
?
additional information
?
-
the enzyme can cleave proteins attached to SAMP1 by linear and isopeptide bonds. The enzyme is inactive in hydrolyzing the amide bond that links aminomethylcoumarin to the C-terminus of monomeric ubiquinone or diglycine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
1 * 16771, calculated from sequence, MALTI-TOF, the negative surface charge of the enzyme may account for the 1000 Da discrepancy between the molecular mass of the enzyme estimated by SDS-PAGE compared to its theoretical molecular mass
monomer
1 * 26000, SDS-PAGE, the negative surface charge of the enzyme may account for the 1000 Da discrepancy between the molecular mass of the enzyme estimated by SDS-PAGE compared to its theoretical molecular mass
monomer
-
1 * 16771, calculated from sequence, MALTI-TOF, the negative surface charge of the enzyme may account for the 1000 Da discrepancy between the molecular mass of the enzyme estimated by SDS-PAGE compared to its theoretical molecular mass
-
monomer
-
1 * 26000, SDS-PAGE, the negative surface charge of the enzyme may account for the 1000 Da discrepancy between the molecular mass of the enzyme estimated by SDS-PAGE compared to its theoretical molecular mass
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Miranda, H.V.; Antelmann, H.; Hepowit, N.; Chavarria, N.E.; Krause, D.J.; Pritz, J.R.; Bsell, K.; Becher, D.; Humbard, M.A.; Brocchieri, L.; Maupin-Furlow, J.A.
Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism
Mol. Cell. Proteomics
13
220-239
2013
Haloferax volcanii (D4GTS4), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GTS4)
brenda
Hepowit, N.L.; Uthandi, S.; Miranda, H.V.; Toniutti, M.; Prunetti, L.; Olivarez, O.; De Vera, I.M.; Fanucci, G.E.; Chen, S.; Maupin-Furlow, J.A.
Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-like small archaeal modifier proteins (SAMPs) from protein-conjugates
Mol. Microbiol.
86
971-987
2012
Haloferax volcanii (D4GTS4), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GTS4)
brenda
Cao, S.; Hepowit, N.; Maupin-Furlow, J.A.
Ubiquitin-like protein SAMP1 and JAMM/MPN+ metalloprotease HvJAMM1 constitute a system for reversible regulation of metabolic enzyme activity in archaea
PLoS ONE
10
e0128399
2015
Haloferax volcanii (D4GTS4), Haloferax volcanii DSM 3757 (D4GTS4)
brenda
Varga, S.; Pathare, G.R.; Baka, E.; Boicu, M.; Kriszt, B.; Szekacs, A.; Zinzula, L.; Kukolya, J.; Nagy, I.
Enhancing recombinant protein solubility with ubiquitin-like small archeal modifying protein fusion partners
J. Microbiol. Methods
118
113-122
2015
Haloferax volcanii (D4GTS4), Haloferax volcanii, Haloferax volcanii ATCC 29605 (D4GTS4)
brenda