SEC65_ASHGO
ID SEC65_ASHGO Reviewed; 261 AA.
AC Q756H7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Signal recognition particle SEC65 subunit;
GN Name=SEC65; OrderedLocusNames=AER289W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Signal-recognition-particle assembly has a crucial role in
CC targeting secretory proteins to the rough endoplasmic reticulum
CC membrane. It must be involved intimately in the translocation of a wide
CC variety of protein substrates (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SRP19 family. {ECO:0000305}.
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DR EMBL; AE016818; AAS52970.1; -; Genomic_DNA.
DR RefSeq; NP_985146.1; NM_210500.1.
DR AlphaFoldDB; Q756H7; -.
DR SMR; Q756H7; -.
DR STRING; 33169.AAS52970; -.
DR EnsemblFungi; AAS52970; AAS52970; AGOS_AER289W.
DR GeneID; 4621358; -.
DR KEGG; ago:AGOS_AER289W; -.
DR eggNOG; KOG3198; Eukaryota.
DR HOGENOM; CLU_065433_1_1_1; -.
DR InParanoid; Q756H7; -.
DR OMA; KVKGFKM; -.
DR Proteomes; UP000000591; Chromosome V.
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:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IBA:GO_Central.
DR Gene3D; 3.30.56.30; -; 1.
DR InterPro; IPR002778; Signal_recog_particle_SRP19.
DR InterPro; IPR036521; SRP19-like_sf.
DR PANTHER; PTHR17453; PTHR17453; 1.
DR Pfam; PF01922; SRP19; 1.
DR SUPFAM; SSF69695; SSF69695; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..261
FT /note="Signal recognition particle SEC65 subunit"
FT /id="PRO_0000135204"
SQ SEQUENCE 261 AA; 29514 MW; 2213D3C0B22C7C54 CRC64;
MPKLEEIDDL EDIDNLHMDL AELDASLKTP IAPRLKPTVV RSQDSEPPLF PQIPLEGEQG
PSFTFIDPKS GRVEETTKIT KEDLADLKRF QILYPCYFDK NRTHAQGRQV PLELAVANPL
AKTIADACRE LEVLCVFEGE KTHPQDFGNP GRVRVLLKEN GKAAGKYANK RWLMKNVAKY
LQEHPTTLES LREIPYGPDF EGIEPSKIPL VHGFQMNEIV PLHSPFTMGH PMTKGIYTAP
KVVAPEKQIK APKNKYKVVR R