RF1_BRUA4
ID RF1_BRUA4 Reviewed; 357 AA.
AC A6WXQ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Oant_1036;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS13757.1; -; Genomic_DNA.
DR RefSeq; WP_012091207.1; NC_009667.1.
DR AlphaFoldDB; A6WXQ3; -.
DR SMR; A6WXQ3; -.
DR STRING; 439375.Oant_1036; -.
DR PRIDE; A6WXQ3; -.
DR EnsemblBacteria; ABS13757; ABS13757; Oant_1036.
DR KEGG; oan:Oant_1036; -.
DR PATRIC; fig|439375.7.peg.1086; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_5; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR PhylomeDB; A6WXQ3; -.
DR Proteomes; UP000002301; Chromosome 1.
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..357
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000004924"
FT REGION 282..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 39778 MW; AF001DFCF6AC89E2 CRC64;
MIALPQDRMD QLLKRFSMIE SQMANNPDSE TYVKLASEYS ELQEVVGKIR ELTDSRKEAV
DLAAMRDDAS TDAEMRALAL EELPGVEKRI EGLEQEVQIL LLPKDAADEK NAILEIRAGT
GGLEAALFAG DLFRMYERYA AEKGWRVELV SASEGDAGGY KEIIATVSGK GVFSKLKFES
GVHRVQRVPE TEAGGRIHTS AATVAVLPEA EDIDIEIRNE DIRIDTMRAS GAGGQHVNTT
DSAVRITHIP TGIMVVQAEK SQHQNRARAM QILRARLYDM ERQKADTERS ESRRSQVGSG
DRSERIRTYN FPQGRVTDHR INLTLYKLDR VMEGDLDELV DALISDHQTA LLTELGH
