ID SRP54_DICDI Reviewed; 542 AA.
AC Q75K18; Q552P1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Signal recognition particle subunit SRP54;
DE EC=3.6.5.4 {ECO:0000250|UniProtKB:P61011};
DE AltName: Full=Signal recognition particle 54 kDa protein;
GN Name=srp54; ORFNames=DDB_G0275455;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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 As part of the SRP complex, associates with the SRP receptor (SR)
CC component srpra to target secretory proteins to the endoplasmic
CC reticulum membrane. Binds to the signal sequence of presecretory
CC proteins when they emerge from the ribosomes. Displays basal GTPase
CC activity, and stimulates reciprocal GTPase activation of the SR subunit
CC SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with
CC the SR subunit srpra. SR compaction and GTPase mediated rearrangement
CC of SR drive SRP-mediated cotranslational protein translocation into the
CC ER (By similarity). Requires the presence of srp9/srp14 and/or srp19 to
CC stably interact with RNA (By similarity).
CC {ECO:0000250|UniProtKB:P61010, ECO:0000250|UniProtKB:P61011}.
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:0000250|UniProtKB:P61011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P61011};
CC -!- SUBUNIT: Component of a signal recognition particle (SRP) complex that
CC consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC subunits: srp72, srp68, srp54, srp19, srp14 and srp9.
CC {ECO:0000250|UniProtKB:P61011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61011}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P61011}.
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:0000250|UniProtKB:P61011}.
CC -!- DOMAIN: The M domain binds the 7SL RNA in presence of srp19 and binds
CC the signal sequence of presecretory proteins.
CC {ECO:0000250|UniProtKB:P61011}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69478.1; -; Genomic_DNA.
DR RefSeq; XP_643640.1; XM_638548.1.
DR AlphaFoldDB; Q75K18; -.
DR SMR; Q75K18; -.
DR STRING; 44689.Q75K18; -.
DR PaxDb; 44689-DDB0232373; -.
DR EnsemblProtists; EAL69478; EAL69478; DDB_G0275455.
DR GeneID; 8620227; -.
DR KEGG; ddi:DDB_G0275455; -.
DR dictyBase; DDB_G0275455; srp54.
DR eggNOG; KOG0780; Eukaryota.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; Q75K18; -.
DR OMA; GMTGQDA; -.
DR PhylomeDB; Q75K18; -.
DR Reactome; R-DDI-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR PRO; PR:Q75K18; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR GO; GO:0008312; F:7S RNA binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; GTP-binding; Hydrolase;
KW Nucleotide-binding; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..542
FT /note="Signal recognition particle subunit SRP54"
FT /id="PRO_0000327678"
FT REGION 1..295
FT /note="G-domain"
FT REGION 296..542
FT /note="M-domain"
FT BINDING 108..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 542 AA; 57610 MW; F5AE74963AD00D20 CRC64;
MVLADLGNQL SSALRSLNET TIVNEDTINQ LLKEVGNALS KSDVSMSLII QMRKNIKDKI
KLDQMAAGLN KRKIIKQVVF DELIRLLDPG VPLWKPTKGK SNIVMFVGLQ GAGKTTSVTK
LAYFYKKKGF STAIVCADTF RAGAFDQVRH NAAKAKIHYY GSETEKDPVV VARTGVDIFK
KDGTEIIIVD TSGRHKQDSE LFEEMKQIET AVKPDNCIFV MDSSIGQAAY EQATAFRSSV
KVGSIIITKM DGNSMGGGAI SAVAATNTPI IFIGTGEHLT DLELFDPSTF VSKLLGYGDM
KGMLEKIKEV IPEDSTSLKE IAQGKFTLRS MQQQFQQIMQ LGPIDKLVQM IPGMNQLPQL
QGNEGGLKLK AYINILDSLS EKELDGKKPI TQKRIITIAQ GSGRHPNEVV ELLEQHKTFE
KLIGKGGPGG GLGSLMAGKG GPKNMEQAMK QMNANGGMQG LMNSLKGMGG MGDLAKMFGG
GGGGGGGMPS MGDLAKMMGG MGGGGRGGGG MPNMGDLAKM MGGMGGGAGK GGQNGFPNLD
LD
//
