SRP54_YARLI
ID SRP54_YARLI Reviewed; 536 AA.
AC Q99150; Q6C2Z6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Signal recognition particle 54 kDa protein homolog;
DE Short=SRP54;
GN Name=SRP54; OrderedLocusNames=YALI0F03839g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 32338 / CX-161-1B;
RX PubMed=9178502;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<499::aid-yea100>3.0.co;2-m;
RA Lee I.H., Ogrydziak D.M.;
RT "Yarrowia lipolytica SRP54 homolog and translocation of Kar2p.";
RL Yeast 13:499-513(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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). {ECO:0000250}.
CC -!- SUBUNIT: Fungal signal recognition particle consists of a 7S RNA
CC molecule (SCR1) and at least seven protein subunits: SRP72, SRP68,
CC SRP54, SEC65, SRP21, SRP14 and SRP7. {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; U42418; AAC49735.1; -; Genomic_DNA.
DR EMBL; CR382132; CAG77773.1; -; Genomic_DNA.
DR RefSeq; XP_504966.1; XM_504966.1.
DR AlphaFoldDB; Q99150; -.
DR SMR; Q99150; -.
DR STRING; 4952.CAG77773; -.
DR EnsemblFungi; CAG77773; CAG77773; YALI0_F03839g.
DR GeneID; 2908963; -.
DR KEGG; yli:YALI0F03839g; -.
DR VEuPathDB; FungiDB:YALI0_F03839g; -.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; Q99150; -.
DR OMA; DTAGRHK; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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: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:EnsemblFungi.
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; 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 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; SSF47364; SSF47364; 1.
DR SUPFAM; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01425; SRP54_euk; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..536
FT /note="Signal recognition particle 54 kDa protein homolog"
FT /id="PRO_0000101202"
FT REGION 1..297
FT /note="G-domain"
FT REGION 298..536
FT /note="M-domain"
FT BINDING 110..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 192..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 250..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 409
FT /note="G -> E (in Ref. 1; AAC49735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 57081 MW; 8148B5313CB372A9 CRC64;
MVLEDLGKRI NGAFANLSKG GDIDEALDAM LKEVCSALLE SDVNIKLVSQ LRQKVKNSVK
ATPNGASKKK VIQKALFDEL VNLVGVDESA ASAAKFKPQK GKSNVVMFVG LQGSGKTTSC
TKLAVYYQRR GFKVGLVCAD TFRAGAFDQL KQNATKAKIP FFGSYTETDP VAVAAEGVAK
FKKEKFEIII VDTSGRHRQE SELFTEMVDI GAAVKPDSTI MVLDASIGQA AEPQSRAFKD
ASDFGSIILT KMDGHAKGGG AISAVAATNT PIIFIGTGEH IHDLEAFSPK QFISKLLGIG
DLQGLMETMQ SLNLDQKKTM EHIQEGIFTL ADLRDQMGNM LKMGSLSSIA GMIPGLSGMA
SSISDEEGTR RIKRMIYILD SMNQKELDSD GSIFKEVPSR ITRVARGSGT SIREVEEVLQ
QQKMMASMAS RMGGKNGMMS RMQNAQNNPA QMAAAQRRAQ QMMGGGAGGM PGMGGMPGMG
GMPGMGGMPG MGGGMPDMSA LQGMFPGGMP DMGQMMNMVQ NNPQMKAMAR SMGLGI
