ID   RF1_BUCBP               Reviewed;         362 AA.
AC   P59456;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=bbp_161;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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; AE016826; AAO26894.1; -; Genomic_DNA.
DR   RefSeq; WP_011091295.1; NC_004545.1.
DR   AlphaFoldDB; P59456; -.
DR   SMR; P59456; -.
DR   STRING; 224915.bbp_161; -.
DR   EnsemblBacteria; AAO26894; AAO26894; bbp_161.
DR   GeneID; 56470704; -.
DR   KEGG; bab:bbp_161; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_6; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000601; 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..362
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177648"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   362 AA;  41467 MW;  8D6C3CC0B676A45D CRC64;
     MKSSMMKKLE SLHRRYEEIE SMLSDRTVIS NQEKFRELSQ EYLKLSDINY CFVQWKNCNH
     DVIETKLLLL DSELHDVAEQ ELQMLSKKMK KIETEIQVLL LPCDPNDQQN CFLEIRSASG
     GDEAAIFSGD LFRMYIKYSE FQNWKTNIIH MTHSLKGGYK DIIVKITGKG SYGKLKFESG
     GHRVQRVPKT ESQGRVHTST CIVAVIPVVP KKEIEKVNIN DLKIDTFRSS GAGGQHVNTT
     DSAVRITHIP SGQVVECQDE RSQHKNKAKA LSVLVSRIKA AELYNQRKKN AIQRRDLLGT
     GMRSDRNRTY NFAQNRVTDH RINLVVYCLD EVLDGKLDVL IEPIIQEHNA DVLSNLSNIE
     FL