ID   RF1_BURTA               Reviewed;         360 AA.
AC   Q2SUG2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=BTH_I2930;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC38863.1; -; Genomic_DNA.
DR   RefSeq; WP_009888664.1; NZ_CP008786.1.
DR   AlphaFoldDB; Q2SUG2; -.
DR   SMR; Q2SUG2; -.
DR   PRIDE; Q2SUG2; -.
DR   EnsemblBacteria; ABC38863; ABC38863; BTH_I2930.
DR   KEGG; bte:BTH_I2930; -.
DR   HOGENOM; CLU_036856_0_1_4; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001930; 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..360
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263247"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   360 AA;  40529 MW;  06A48A1C69A26330 CRC64;
     MKTSMQSKLD QLTTRLAELN DLLSRENVTA DLDQYRKLTR EHAEIGPVVE HYAQWRQARA
     DELAAQELLA DASMRDFAED ELRGARERMS RLAAELQTML LPKDPNDERN IFVEIRAGTG
     GDESALFAGD LLRMYLRYAE RQRWQVEMMS ESPSDLGGYK EVIVRIAGYG AYSRLKFESG
     GHRVQRVPAT ETQGRIHTSA CTVAVMPEAD EIGEVEINPA DLRIDTFRAS GAGGQHINKT
     DSAVRVTHIP TGIVVECQDD RSQHKNKDRA LKVLAARIKD KQYHEQHAKE AATRKSLIGS
     GDRSERIRTY NFPQGRMTDH RINLTLYKLE QIMDGDLDEL IAALVSEHQA ELLASLGDAE