RF1_BRUME
ID RF1_BRUME Reviewed; 359 AA.
AC Q8YJ95;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=BMEI0191;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL51373.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL51373.1; ALT_INIT; Genomic_DNA.
DR PIR; AB3276; AB3276.
DR RefSeq; WP_004686702.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YJ95; -.
DR SMR; Q8YJ95; -.
DR STRING; 224914.BMEI0191; -.
DR EnsemblBacteria; AAL51373; AAL51373; BMEI0191.
DR GeneID; 29594610; -.
DR KEGG; bme:BMEI0191; -.
DR PATRIC; fig|224914.52.peg.1312; -.
DR eggNOG; COG0216; Bacteria.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000000419; Chromosome I.
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.
FT CHAIN 1..359
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177644"
FT REGION 283..309
FT /note="Disordered"
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 359 AA; 39909 MW; 9B447F031AD72D84 CRC64;
MIALPQDRMD QLLKRFSMIE SQMANNPDSD TYVKLASEYS ELQDVVGKIR ELSDARMEAS
DLAAMRDDAS TDAEMRALAV EELPEVEKRI AVLEQDVQIL LLPKDAADDK NAILEIRAGT
GGLEAALFAG DLFRMYERYA AEKGWRVELV SASEGDAGGY KEIIATVSGK GVFSKLKFES
GVHRVQRVPE TEAGGRIHTS AATVAVLPEA EDIDIEIRNE DIRIDTMRAS GAGGQHVNTT
DSAVRITHIP TGIMVVQAEK SQHQNRARAM QILRARLYDM ERQKAESERS QARRSQVGSG
DRSERIRTYN FPQGRVTDHR INLTLYKLDR VMEGELDELV DALISDHQTA LLAELGEQP
