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 18-APR-2012, entry version 64. DE RecName: Full=Peptide chain release factor 1; DE Short=RF-1; GN Name=prfA; OrderedLocusNames=bbp_161; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX MEDLINE=22426901; 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 CC of translation in response to the peptide chain termination codons CC UAG and UAA (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Methylated by PrmC. Methylation increases the termination CC efficiency of RF1 (By similarity). CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release CC factor family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016826; AAO26894.1; -; Genomic_DNA. DR RefSeq; NP_777789.1; NC_004545.1. DR ProteinModelPortal; P59456; -. DR SMR; P59456; 8-353. DR EnsemblBacteria; EBBUCT00000002444; EBBUCP00000002268; EBBUCG00000002444. DR GeneID; 1058129; -. DR GenomeReviews; AE016826_GR; bbp_161. DR KEGG; bab:bbp161; -. DR PATRIC; 21245099; VBIBucAph80364_0156. DR eggNOG; COG0216; -. DR HOGENOM; HBG629764; -. DR KO; K02835; -. DR OMA; SVMLEIR; -. DR ProtClustDB; PRK00591; -. DR BioCyc; BAPH224915:BBP_161-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:InterPro. DR HAMAP; MF_00093; Rel_fac_1; 1; -. DR InterPro; IPR005139; PCRF. DR InterPro; IPR000352; Pep_chain_release_fac_I_II. DR InterPro; IPR004373; PrfA. DR PANTHER; PTHR11075:SF9; PrfA; 1. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR TIGRFAMs; TIGR00019; PrfA; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis. FT CHAIN 1 362 Peptide chain release factor 1. FT /FTId=PRO_0000177648. FT MOD_RES 235 235 N5-methylglutamine (By similarity). 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 //