ID   RF1_VIBPA               Reviewed;         362 AA.
AC   Q87RN4;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE            Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN   Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=VP0743;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR   EMBL; BA000031; BAC59006.1; -; Genomic_DNA.
DR   RefSeq; NP_797122.1; NC_004603.1.
DR   RefSeq; WP_005456867.1; NC_004603.1.
DR   AlphaFoldDB; Q87RN4; -.
DR   SMR; Q87RN4; -.
DR   STRING; 223926.28805729; -.
DR   EnsemblBacteria; BAC59006; BAC59006; BAC59006.
DR   GeneID; 1188238; -.
DR   KEGG; vpa:VP0743; -.
DR   PATRIC; fig|223926.6.peg.710; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_6; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..362
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177767"
FT   MOD_RES         237
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   362 AA;  40294 MW;  CA09EA91772CE382 CRC64;
     MKASILTKLE TLVERYEEVQ HLLGDPDVIG DQDKFRALSK EYSQLEEVTK CFQAYQQAQD
     DLAAAEEMAK EDDEEMREMA QEEIKDAKEA IERLADELQI LLLPKDPNDD RNCFLEIRAG
     AGGDEAGIFA GDLFRMYSKY AEKRGWRIEV MSSNEAEHGG YKEMIAKVSG DGAYGVLKFE
     SGGHRVQRVP ATESQGRVHT SACTVAVMAE IPEADLPEIK AADLKIDTFR ASGAGGQHVN
     TTDSAIRITH LPTGTVVECQ DERSQHKNKA KAMAVLAARI VQAEQERRAA EVSDTRRNLL
     GSGDRSDRIR TYNYPQGRVS DHRINLTIYR LNEVMEGDLQ SLIDPVVQEH QADQLAALAE
     NA