SRP54_CANAX
ID SRP54_CANAX Reviewed; 556 AA.
AC O42816;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Signal recognition particle 54 kDa protein homolog;
GN Name=SRP54;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B2630;
RA Hosking S.L., Stirling C.J., Egerton M.;
RT "Isolation of the SRP54 homolog from the pathogenic yeast, Candida
RT albicans.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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 seven protein subunits: SRP72, SRP68,
CC SRP54, SEC65, SRP21, SRP14 and SRP7. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AJ222805; CAA10999.1; -; mRNA.
DR AlphaFoldDB; O42816; -.
DR SMR; O42816; -.
DR VEuPathDB; FungiDB:CAWG_01464; -.
DR VEuPathDB; FungiDB:CR_01110W_A; -.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR GO; GO:0008312; F:7S RNA binding; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:EnsemblFungi.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:EnsemblFungi.
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 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..556
FT /note="Signal recognition particle 54 kDa protein homolog"
FT /id="PRO_0000101200"
FT REGION 1..312
FT /note="G-domain"
FT REGION 313..556
FT /note="M-domain"
FT REGION 450..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 207..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 265..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 556 AA; 60701 MW; 0EA14A8FE7B922CF CRC64;
MVLADLGSRL RGALSSVESG SDDEIQQMIK DICSALLESD VNVKLVAKLR GNIKNKIDES
NVSKETSAMN KRKKLQKIIF DELCALVDSN VEPPKPKKLS TSTKTINGKK VRLSKESSHV
IMFVGLQGAG KTTSCTKLAV YYKKRGFKVG LVCADTFRAG AFDQLKQNAI KANIPYYGSY
LEPDPVKIAF EGVQKFKQEK FDIIIVDTSG RHRQEEQLFT EMVQIGEAVQ PTQTIMVMDG
SIGQAAESQA RAFKESSNFG SIILTKMDGH AKGGGAISAV AATKTPIVFI GTGEHVGDLE
IFKPTTFISK LLGIGDIQGL IEHVQSLNLH QDEGHKQTIE HIKEGKFTLR DFQNQMNNFL
KMGPLTNIAS MIPGLSNIMS QVGDEETSKK IKNMIYIMDS MTTKELECDG RIFIKEPSRI
VRVARGSGCA VVEVEMILQQ HRMMSTMAKS AMAAQGGQPG QPGNPMANNP QMQRMMQQAQ
SNPNFMQQAM NMLGGAGGGA GGAGGLAGMM NNPAMMQQAQ QMMRSNPQMM QQAQQMMKNP
GMMQKMMQQF GGMGGM