ID   RF1_POLSJ               Reviewed;         373 AA.
AC   Q12F86;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Bpro_0850;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE42806.1; -; Genomic_DNA.
DR   RefSeq; WP_011481808.1; NC_007948.1.
DR   AlphaFoldDB; Q12F86; -.
DR   SMR; Q12F86; -.
DR   STRING; 296591.Bpro_0850; -.
DR   PRIDE; Q12F86; -.
DR   EnsemblBacteria; ABE42806; ABE42806; Bpro_0850.
DR   KEGG; pol:Bpro_0850; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_4; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001983; Chromosome.
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..373
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263313"
FT   MOD_RES         245
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   373 AA;  40936 MW;  A56336C8A4F9E89E CRC64;
     MKPFLRQTLD RQLLRLHELD SLLSATDVVS DLDRFRALTR EHAEASVVAE QYTRLTSREA
     DLASAEGMLA EAKDDPEMAA MAEEEIAAAK LDIAQLDEAL QLMLIPKDPD DARAAFIEIR
     AGTGGDESAL FAGDLFRMYT RFAERNRWQV EIISESPSEL GGYKEVVLRM DGPTDATGVG
     VYGKLRFESG GHRVQRVPAT ETQGRIHTSA CTVAVLPEPD EAVAIQINPA DLRIDTYRAS
     GAGGQHINKT DSAVRITHIP TGIVAECQDD RSQHRNKAKA LQVLSARIVE KDRSERAAKD
     AAMRKGLVGS GDRSDRIRTY NFPQGRLTDH RINLTLYKLL AIMEGDLGDV ITALQVARGA
     EQLAELETAS NGF