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Database: UniProt
Entry: Q0N2R8_BOMMO
LinkDB: Q0N2R8_BOMMO
Original site: Q0N2R8_BOMMO 
ID   Q0N2R8_BOMMO            Unreviewed;       501 AA.
AC   Q0N2R8;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   08-NOV-2023, entry version 77.
DE   RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
GN   Name=SRP54 {ECO:0000313|EMBL:ABH10803.1};
GN   Synonyms=778481 {ECO:0000313|EnsemblMetazoa:NP_001091776.1};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000313|EMBL:ABH10803.1};
RN   [1] {ECO:0000313|EMBL:ABH10803.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hu Z.G., Chen K.P., Yao Q.;
RT   "Signal Recognition Particle of Bombyx mori.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001091776.1}
RP   IDENTIFICATION.
RC   STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001091776.1};
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) 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   EMBL; DQ646413; ABH10803.1; -; mRNA.
DR   RefSeq; NP_001091776.1; NM_001098306.1.
DR   AlphaFoldDB; Q0N2R8; -.
DR   EnsemblMetazoa; NM_001098306.1; NP_001091776.1; GeneID_778481.
DR   GeneID; 778481; -.
DR   KEGG; bmor:778481; -.
DR   CTD; 6729; -.
DR   HOGENOM; CLU_009301_6_1_1; -.
DR   OrthoDB; 1110531at2759; -.
DR   Proteomes; UP000005204; 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   2: Evidence at transcript level;
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:UP000005204};
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   501 AA;  55144 MW;  C396E190E27C30C5 CRC64;
     MVLADLGRKI TTALQSLSRA TIINEEVLNS MLKQICAALL EADVNIRLVK NLRENVRAVI
     DFDEMAGGLN KRRMIQSAVF KELVKLVDPG VKPYQPVKGK PNVIMYVGLQ GSGKTTTCTK
     LAYHYLRKNW KSCLVCADTF RAGAYDQVKQ NCTKARIPFY GSYTEVDPVV IATTGVDMFK
     KQGLEMIIVD TSGRHKQEES LFEEMLAVAT AIKPDNIIFV MDATIGQACE AQARAFKDKV
     DIGSVIITKL DGHAKGGGAL SAVAATQSPI IFIGTGEHID DLEPFKTKPF IKKLLGMGDI
     EGLLDKVNEL KLDDNDELLE KLKHGQFTLR AMYEQFQNIM KMGPFSQIMG MIPGFSQDLM
     SKGSEQESMA KLKLLMTIMD SMNEGELDNR DGAKLFSKQP TRITRVAQGA GVTERDVKDL
     IAQYTKFAAV VKKMGGIKGL FKGGDMAKNV NQTQMVKLNQ QMAKMMDPRL LQQMGGMSGL
     HNMMRQLQQG SSGMGGLMGG K
//
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