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Information on EC 3.6.5.4 - signal-recognition-particle GTPase

for references in articles please use BRENDA:EC3.6.5.4
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IUBMB 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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This record set is specific for:
UNIPROT: Q8U070
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Word Map
  • 3.6.5.4
  • gtpases
  • ribonucleoprotein
  • co-translational
  • translocons
  • srp-dependent
  • thylakoids
  • sec
  • exit
  • light-harvesting
  • myopathy
  • secyeg
  • cotranslationally
  • universally
  • gtp-binding
  • myositis
  • translocase
  • presecretory
  • tetraloops
  • insertase
  • polytopic
  • anti-srp
  • methionine-rich
  • ribosome-associated
  • rna-protein
  • preproteins
  • protein-targeting
  • signal-anchor
  • m-domain
  • ribosome-bound
  • chromodomains
  • medicine
  • polymyositis
  • protein-conducting
  • anti-signal
  • protein-rna
  • chlorophyll-binding
  • gtp-bound
  • walter
  • multispanning
  • imnms
  • sequence-binding
  • myositis-specific
  • tail-anchored
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Reaction Schemes
Synonyms
signal recognition particle, srp54, srp receptor, srp19, cpsrp43, cpsrp54, cpsrp, srp14, sralpha, cpftsy, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
signal recognition particle
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SRP19
accessory subunit of the signal recognition particle, SRP54 and SRP19 are the two RNA binding components forming the core of the signal recognition particle, SRP19 acts as a molecular scaffold and a chaperone, assisting the SRP RNA in adopting the conformation required for its optimal interaction with the essential subunit SRP54, and proper assembly of a functional SRP
SRP54
GTPase subunit of the signal recognition particle, SRP54 and SRP19 are the two RNA binding components forming the core of the signal recognition particle
GTPase
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guanine triphosphatase
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guanosine 5'-triphosphatase
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guanosine triphosphatase
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ribosomal GTPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9059-32-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SRP54_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
443
0
49879
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
subunit SRP54, X-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GDP-bound subunit SRP54 and free subunit SRP19 are crystallized by hanging drop vapour diffusion method, crystals of SRP54 grow in 1.0-1.3 M lithium sulfate and 100 mM sodium acetate pH 5.0, crystals of SRP19 grow in 1.2-1.3 M sodium malonate and 100 mM sodium acetate pH 5.0
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heat selective precipitation, cobalt-chelating affinity chromatography, gel filtration, and ion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834(DE3)-Rosetta2 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Egea, P.F.; Napetschnig, J.; Walter, P.; Stroud, R.M.
Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus
PLoS ONE
3
e3528
2008
Pyrococcus furiosus (Q8U070), Pyrococcus furiosus
Manually annotated by BRENDA team