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Database: UniProt
Entry: G4VKV4_SCHMA
LinkDB: G4VKV4_SCHMA
Original site: G4VKV4_SCHMA 
ID   G4VKV4_SCHMA            Unreviewed;       538 AA.
AC   G4VKV4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_059540.1};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_059540.1}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_059540.1,
RC   ECO:0000313|WBParaSite:Smp_059540.2};
RG   WormBaseParasite;
RL   Submitted (DEC-2018) 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   RefSeq; XP_018653348.1; XM_018798403.1.
DR   SMR; G4VKV4; -.
DR   STRING; 6183.G4VKV4; -.
DR   EnsemblMetazoa; Smp_059540.1; Smp_059540.1; Smp_059540.
DR   EnsemblMetazoa; Smp_059540.2; Smp_059540.2; Smp_059540.
DR   GeneID; 8353184; -.
DR   KEGG; smm:Smp_059540; -.
DR   WBParaSite; Smp_059540.1; Smp_059540.1; Smp_059540.
DR   WBParaSite; Smp_059540.2; Smp_059540.2; Smp_059540.
DR   CTD; 8353184; -.
DR   eggNOG; KOG0780; Eukaryota.
DR   HOGENOM; CLU_009301_6_1_1; -.
DR   OMA; GMTGQDA; -.
DR   OrthoDB; 1110531at2759; -.
DR   Proteomes; UP000008854; 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:UP000008854};
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   538 AA;  57942 MW;  68C24C412C7931A8 CRC64;
     MVLAELGRKI TNALRSLGNA TIINEDVLNS LLKEICTALI EADVNIRLVK QLRENVRAVI
     DFDEMAAGLN KRKIIQSAVF KELVHLVDPQ VKAWQPARGS SNVIMLVGLQ GCGKTTTATK
     LAYFYQRKGW KTCMICADTF RAGAFDQLKQ NATKARIPFY GSYTETDPVV IARDGVQKFV
     EEKFEIIIVD TSGRHRQEDS LFEEMLQVSN AIEPDHVIYV LDASIGQACE AQASAFKAKV
     DVSSVIVTKL DGHAKGGGAL SAVAATHSPI TFIGTGEHVE DFEQFRVQPF VQKLLGLGDL
     EGLVERVTEL KLDENEELVK KLKQGVFTLR NMYEQFQNIL KIGSFSQVLS AIPGLGQDLL
     ANDQESHRRL KRLMTIMDSM NDYELDSDEG GRLFNRQPGR TLRVARGAGV SQAEVKLLLT
     QHNKFYMVVK KMGGIKGLFQ TGSKSGAMGG IGGGPGGVGS GGGAGGSGNT PSLAEMAAAS
     RSVSAGQMAK LNQSMAKVLD PRILQQMGGM AGLQNMMRQL QAGGGFGPFG GGGGGRLG
//
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