ID   RF1_GRABC               Reviewed;         352 AA.
AC   Q0BUJ8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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};
GN   OrderedLocusNames=GbCGDNIH1_0606;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61504.1; -; Genomic_DNA.
DR   RefSeq; WP_011631313.1; NC_008343.2.
DR   AlphaFoldDB; Q0BUJ8; -.
DR   SMR; Q0BUJ8; -.
DR   STRING; 391165.GbCGDNIH1_0606; -.
DR   GeneID; 69744860; -.
DR   KEGG; gbe:GbCGDNIH1_0606; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OrthoDB; 9806673at2; -.
DR   Proteomes; UP000001963; 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   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.70.1660; -; 1.
DR   Gene3D; 6.10.140.1950; -; 1.
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   NCBIfam; TIGR00019; prfA; 1.
DR   PANTHER; PTHR43804; LD18447P; 1.
DR   PANTHER; PTHR43804:SF7; LD18447P; 1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; Release factor; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263281"
FT   MOD_RES         229
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   352 AA;  39011 MW;  A3816F05C06376CB CRC64;
     MSFTANLDRI VARAEELRAS LSEGLNGDSF AAASRELAEL EPVVARIEEL WAAERGLAEA
     EAMLADPDMR ELAESEAEIL REKLPSLTRE IRIALLPKDE ADERSAILEI RPAAGGDEAS
     LFAAQLFSMY QRYAEIRGWR FEILEYDDTG LGGLKGGMAE ITGRSVFARL KYESGVHRVQ
     RVPATESQGR IHTSTVTVAV LPEAEDVDVQ VDEGDLRIDV YRASGAGGQH VNKTESAVRI
     THLPSGIVVA MQEEKSQHKN RAKAMKILKA RLYEQQRAAL HASRAADRRA QVGTGDRSER
     IRTYNFPQGR VSDHRINLTL YKIDRVMLGE LDDFVDALTA EDQAARLSAQ EL
//