SRP54_SCHPO
ID SRP54_SCHPO Reviewed; 522 AA.
AC P21565;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Signal recognition particle 54 kDa protein homolog;
DE Short=SRP54;
GN Name=srp54; ORFNames=SPCC188.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2557350; DOI=10.1083/jcb.109.6.3223;
RA Hann B.C., Poritz M.A., Walter P.;
RT "Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue
RT to the 54-kD subunit of the signal recognition particle that in S.
RT cerevisiae is essential for growth.";
RL J. Cell Biol. 109:3223-3230(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP MUTAGENESIS OF GLN-110; LYS-114; THR-115; ASP-138; ARG-194 AND THR-248.
RX PubMed=7969124; DOI=10.1128/mcb.14.12.7839-7854.1994;
RA Althoff S.M., Stevens S.W., Wise J.A.;
RT "The Srp54 GTPase is essential for protein export in the fission yeast
RT Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 14:7839-7854(1994).
CC -!- FUNCTION: Binds to the signal sequence of presecretory protein when
CC they emerge from the ribosomes and transfers them to TRAM
CC (translocating chain-associating membrane protein).
CC -!- SUBUNIT: Fungal signal recognition particle consists of a 7S RNA
CC molecule (scR1) and at least six protein subunits: srp72, srp68, srp54,
CC sec65, srp21 and srp14. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Has a two domain structure: the G-domain binds GTP; the M-
CC domain binds the 7S RNA in presence of srp19 and also binds the signal
CC sequence.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000305}.
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DR EMBL; X51613; CAA35951.1; -; Genomic_DNA.
DR EMBL; M55518; AAA35344.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB41226.1; -; Genomic_DNA.
DR PIR; A33644; A33644.
DR RefSeq; NP_588209.1; NM_001023199.2.
DR AlphaFoldDB; P21565; -.
DR SMR; P21565; -.
DR BioGRID; 275858; 5.
DR IntAct; P21565; 3.
DR MINT; P21565; -.
DR STRING; 4896.SPCC188.06c.1; -.
DR iPTMnet; P21565; -.
DR MaxQB; P21565; -.
DR PaxDb; P21565; -.
DR PRIDE; P21565; -.
DR EnsemblFungi; SPCC188.06c.1; SPCC188.06c.1:pep; SPCC188.06c.
DR GeneID; 2539290; -.
DR KEGG; spo:SPCC188.06c; -.
DR PomBase; SPCC188.06c; srp54.
DR VEuPathDB; FungiDB:SPCC188.06c; -.
DR eggNOG; KOG0780; Eukaryota.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; P21565; -.
DR OMA; DTAGRHK; -.
DR PhylomeDB; P21565; -.
DR Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR PRO; PR:P21565; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IPI:PomBase.
DR GO; GO:0008312; F:7S RNA binding; IPI:PomBase.
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; IMP:PomBase.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:PomBase.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR022941; SRP54.
DR InterPro; IPR006325; SRP54_euk.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR11564; PTHR11564; 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; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01425; SRP54_euk; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..522
FT /note="Signal recognition particle 54 kDa protein homolog"
FT /id="PRO_0000101201"
FT REGION 1..295
FT /note="G-domain"
FT REGION 296..522
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"
FT MUTAGEN 110
FT /note="Q->K,R: Lethal."
FT /evidence="ECO:0000269|PubMed:7969124"
FT MUTAGEN 114
FT /note="K->G,R: Lethal."
FT /evidence="ECO:0000269|PubMed:7969124"
FT MUTAGEN 115
FT /note="T->N: Lethal."
FT /evidence="ECO:0000269|PubMed:7969124"
FT MUTAGEN 138
FT /note="D->N: Lethal."
FT /evidence="ECO:0000269|PubMed:7969124"
FT MUTAGEN 194
FT /note="R->L,H: Cold-sensitive."
FT /evidence="ECO:0000269|PubMed:7969124"
FT MUTAGEN 248
FT /note="T->N: Cold-sensitive."
FT /evidence="ECO:0000269|PubMed:7969124"
FT MUTAGEN 248
FT /note="T->R,K: Lethal."
FT /evidence="ECO:0000269|PubMed:7969124"
SQ SEQUENCE 522 AA; 56698 MW; EA21E48F82CC97C1 CRC64;
MVFADLGRRL NSALGDFSKA TSVNEELVDT LLKNICTALL ETDVNVRLVQ ELRSNIKKKI
NVSTLPQGIN GKRIVQKAVF DELCSLVDPK VDAFTPKKGR PSVIMMVGLQ GSGKTTTCSK
LALHYQRRGL KSCLVAADTF RAGAFDQLKQ NAIKARVPYF GSYTETDPVV IAKEGVDKFK
NDRFDVIIVD TSGRHQQEQE LFAEMVEISD AIRPDQTIMI LDASIGQAAE SQSKAFKETA
DFGAVIITKL DGHAKGGGAL SAVAATKTPI VFIGTGEHIN DLERFSPRSF ISKLLGLGDL
EGLMEHVQSL DFDKKNMVKN LEQGKFTVRD FRDQLGNIMK LGPLSKMASM IPGMSNMMNG
MNDEEGSLRM KRMLYIVDSM TEQELDSDGL LFVEQPSRVL RVARGSGTSV LEVEETISQV
RVFAQMAKKI GGKDGILGKL GGNPAAALKK DPRQLAAMQK RMQAMGMGGG MPGLNPGSMN
FGDISKMANM LMGGGGPGGA GGMDFSGMLN QFQNMQKPPR RR
