RF1_BURMA
ID RF1_BURMA Reviewed; 360 AA.
AC Q62DF3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=BMAA0504;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000011; AAU46610.1; -; Genomic_DNA.
DR RefSeq; WP_004186862.1; NC_006349.2.
DR RefSeq; YP_105275.1; NC_006349.2.
DR AlphaFoldDB; Q62DF3; -.
DR SMR; Q62DF3; -.
DR STRING; 243160.BMAA0504; -.
DR EnsemblBacteria; AAU46610; AAU46610; BMAA0504.
DR KEGG; bma:BMAA0504; -.
DR PATRIC; fig|243160.12.peg.4011; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_4; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000006693; Chromosome 2.
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..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177649"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40483 MW; CE016622715160DE CRC64;
MKTSMQSKLD QLTTRLAELN DLLSRENVTA DLDQYRKLTR EHAEIGPVVE HYAQWRQARA
DELAAQELLA DASMRDFAED ELRGARDRMG RLAAELQTML LPKDPNDERN IFVEIRAGTG
GDESALFAGN LLRMYLRYAE RQRWQVEMMS ESPSDLGGYK EVIVRIAGYG AYSRLKFESG
GHRVQRVPAT ETQGRIHTSA CTVAVMPEAD EIGEVEINPA DLRIDTFRAS GAGGQHINKT
DSAVRVTHIP TGIVVECQDD RSQHKNKDRA LKVLAARIKD KQYHEQHAKE AATRKSLIGS
GDRSERIRTY NFPQGRMTDH RINLTLYKLE QIMDGDLDEL IAALVSEHQA ELLASLGDAE
