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Information on EC 3.6.5.4 - signal-recognition-particle GTPase and Organism(s) Canis lupus familiaris and UniProt Accession P61010
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3.6.5.4 signal-recognition-particle GTPaseIUBMB Comments
Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).
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Word Map
- 3.6.5.4
- gtpases
- ribonucleoprotein
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co-translational
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translocons
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srp-dependent
- thylakoids
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sec
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exit
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light-harvesting
- myopathy
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secyeg
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cotranslationally
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universally
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gtp-binding
- myositis
- translocase
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presecretory
- tetraloops
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insertase
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polytopic
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anti-srp
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methionine-rich
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ribosome-associated
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rna-protein
- preproteins
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protein-targeting
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signal-anchor
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m-domain
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ribosome-bound
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chromodomains
- medicine
- polymyositis
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protein-conducting
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anti-signal
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protein-rna
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chlorophyll-binding
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gtp-bound
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walter
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multispanning
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imnms
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sequence-binding
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myositis-specific
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tail-anchored
The taxonomic range for the selected organisms is: Canis lupus familiaris
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
signal recognition particle, srp54, srp receptor, srp19, cpsrp43, cpsrp54, cpsrp, srp14, sralpha, cpftsy, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GTPase
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-
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guanine triphosphatase
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-
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guanosine 5'-triphosphatase
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-
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guanosine triphosphatase
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ribosomal GTPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (protein-synthesis-assisting)
Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).
CAS REGISTRY NUMBER
COMMENTARY
9059-32-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
P61010; P06625
peripheral membrane SRalpha subunit, the transmembrane SRbeta subunit is anchoring SRalpha on the endoplasmic reticulum membrane
P61010; P06625
peripheral membrane SRalpha subunit, the transmembrane SRbeta subunit is anchoring SRalpha on the endoplasmic reticulum membrane
additional information
P61010; P06625
the domain of SRalpha that binds SRbeta does so by binding directly to the nucleotide bound form of the GTPase domain of SRbeta. Additional level of regulation of SRP receptor function based on regulated dissociation of the receptor subunits
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SRP receptor alpha and beta subunits
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
P61010; P06625
deletion of the N-terminal transmembrane domain of SRbeta does not effect receptor dimerization but reveals a cryptic translocation signal that overlaps the GTPase domain. Deletion of the G-1 region, (SRbetaD5) which comprises part of the SRbeta GTPase domain, abolishes binding to SRalpha. A mutant SRbeta containing an amino acid substitution allows the GTPase domain to bind XTP dimerizes with SRalpha most efficiently in the presence of XTP or XDP, but not ATP
physiological function
P61010; P06625
the signal recognition particle (SRP) is a ribonucleoprotein complex with a key role in targeting and insertion of membrane proteins. The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRalpha in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle. The architecture of the TC and its stimulation by RNA has been described for the bacterial SRP system while this information is lacking for other domains of life
additional information
P61010; P06625
analysis of binding of wild-type and mutant SRalpha and SRbeta by gel filtration and immunoprecipitation, overview. SRX2, the minimum SRbeta binding domain of SRalpha, binds to the GTPase domain of SRbeta, no other regions of SRalpha are observed to bind to SRbeta. Structural basis for conserved regulation and adaptation of the signal recognition particle targeting complex, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
P61010; P06625
the signal recognition particle (SRP) receptor is a heterodimer of two polypeptides (SRalpha and SRbeta) that each contain a GTP binding domain. The GTP binding domain in the peripheral membrane SRalpha subunit has a well defined role in regulating targeting of SRP ribosome-nascent chain complexes to the translocon. Without bound GTP, the empty form of the SRbeta GTPase domain is unable to dimerize with SRalpha
additional information
P61010; P06625
determination of the crystal structure of the GTPase heterodimers, and structure comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SRalpha and SRbeta complex, X-ray diffraction structure determination and analysis
P61010; P06625
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D181N
G118L
G118L/D181N
H119L
K75I
K75I/H119L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a null mutant phenotype and no binding of SRalpha
N178K
additional information
D181N
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows the wild-type phenotype and binding of SRalpha at wild-type level, but no binding in absence of GTP. SRalpha binding to D181N can be restored to some level by adding back nucleotide, i.e. GTP, GDP, XTP or XDP, but not with ATP
G118L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and binding of SRalpha at wild-type level
G118L/D181N
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta) and weak binding of SRalpha
H119L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows the wild-type phenotype and binding of SRalpha at wild-type level
K75I
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and no binding of SRalpha
N178K
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and weak binding of SRalpha
additional information
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SRbetaC1-deltaTM, hydrolysis of XTP favored over GTP
additional information
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SRbeta-deltaloop, hydrolysis of XTP favored over GTP
additional information
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SRbeta-deltaTM, hydrolysis of XTP favored over GTP
additional information
-
Srbeta-loop2, hydrolysis of XTP favored over GTP
additional information
P61010; P06625
construction of several deletion mutants: SRbeta-DELTATM, SRbetaDELTA4, SRbetaDELTA5, SRbeta1C1-DELTATM, SRbeta-DELTAloop, and SRbeta-loop2, phenotypes, altered SRalpha binding of the truncated mutants, overview. Deletion of the last 6 amino-acids from the carboxyl-terminus of the SRbeta GTPase domain results in a molecule (SRbetaC1) with primarily type I topology, similar to SRbeta
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Conolly, T.; Gilmore, R.
The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide
Cell
57
599-610
1989
Canis lupus familiaris
Conolly, T.; Gilmore, R.
GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor
J. Cell Biol.
123
799-807
1993
Canis lupus familiaris
Zopf, D.; Bernstein, H.D.; Walter, P.
GTPase domain of the 54-kD subunit of the mammalian signal recognition particle is required for protein translocation but not for signal sequence binding
J. Cell Biol.
120
1113-1121
1993
Canis lupus familiaris
Miller, J.D.; Tajima, S.; Lauffer, L.; Walter, P.
The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alph subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane
J. Cell Biol.
128
273-282
1995
Canis lupus familiaris
Bacher, G.; Pool, M.; Dobberstein, B.
The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor
J. Cell Biol.
146
723-730
1999
Canis lupus familiaris
Legate, K.R.; Falcone, D.; Andrews, D.W.
Nucleotide-dependent binding of the GTPase domain of the signal recognition particle receptor beta-subunit to the alpha-subunit
J. Biol. Chem.
275
27439-27446
2000
Canis lupus familiaris
Wild, K.; Bange, G.; Motiejunas, D.; Kribelbauer, J.; Hendricks, A.; Segnitz, B.; Wade, R.C.; Sinning, I.
Structural basis for conserved regulation and adaptation of the signal recognition particle targeting complex
J. Mol. Biol.
428
2880-2897
2016
Canis lupus familiaris (P61010 AND P06625)
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