ID A0A0K0EWL4_STRVS Unreviewed; 497 AA.
AC A0A0K0EWL4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
OS Strongyloides venezuelensis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0091600.1};
RN [1] {ECO:0000313|Proteomes:UP000035680}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A, De Silva N.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SVE_0091600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER).
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- DOMAIN: The M domain binds the 7SL RNA in presence of SRP19 and binds
CC the signal sequence of presecretory proteins.
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- DOMAIN: The NG domain, also named G domain, is a special guanosine
CC triphosphatase (GTPase) domain, which binds GTP and forms a guanosine
CC 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in
CC the SRP receptor subunit SRPRA. The two NG domains undergo cooperative
CC rearrangements upon their assembly, which culminate in the reciprocal
CC activation of the GTPase activity of one another. SRP receptor
CC compaction upon binding with cargo-loaded SRP and GTPase rearrangement
CC drive SRP-mediated cotranslational protein translocation into the ER.
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|RuleBase:RU364034}.
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DR AlphaFoldDB; A0A0K0EWL4; -.
DR STRING; 75913.A0A0K0EWL4; -.
DR WBParaSite; SVE_0091600.1; SVE_0091600.1; SVE_0091600.
DR Proteomes; UP000035680; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:UniProtKB-UniRule.
DR CDD; cd17875; SRP54_G; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 1.
DR HAMAP; MF_00306; SRP54; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR006325; SRP54_euk.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR NCBIfam; TIGR01425; SRP54_euk; 1.
DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF02978; SRP_SPB; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU364034};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU364034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364034};
KW Reference proteome {ECO:0000313|Proteomes:UP000035680};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU364034};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU364034};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW ECO:0000256|RuleBase:RU364034}.
FT DOMAIN 269..282
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
SQ SEQUENCE 497 AA; 55062 MW; C4D116BC87BBD70C CRC64;
MVLADLGRRI RVAIGKLGQA TVINEEEVKV MLNEVCAALL ESDVNIKLVK KLKDNCFKKI
NNEELLGGVN KRRVIQKTVF QELLALVDPG VAPYTPVKGK ANVIMFVGLQ GAGKTTTCTK
MAYYYQKKGW RTCLVCADTF RAGAFDQLKQ NATKARIPFY GSYTEMDPVV IAADGVEKFK
KEGFEIIIVD TSGRHKQEAS LFEEMLQVSN AVSPNNVVFV MDASIGQALE AQAKSFHETV
PVGSVIITKL DSHAKGGGAL SAVAATGSPV IFIGTGEHID EFETFKPKQF ISKLLGMGDL
EGLVEKVSEI SNMQDSAELL KRIKGGIFTL RDMYEQFQSI QKMGPFNQIM GMIPGFGPDF
LSKGNEQESQ NRLKRMMTIM DSMADKELDH PKATELFQKE HTRVTRVSKG SGTTEIEVVE
LLNQYKKFAD LIKKMGSMKG LFKGGDMNPM NMNPNQMMAL NKQMSKMIDP RMLQQMGGMA
GLQNCIFQNK AFQKLKK
//
