RF1_GRABC
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 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};
GN OrderedLocusNames=GbCGDNIH1_0606;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; 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 EnsemblBacteria; ABI61504; ABI61504; GbCGDNIH1_0606.
DR GeneID; 56915014; -.
DR KEGG; gbe:GbCGDNIH1_0606; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_5; -.
DR OMA; ISDHRVG; -.
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 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..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