ID   RF1_BURCM               Reviewed;         360 AA.
AC   Q0BIQ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Bamb_0414;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI85973.1; -; Genomic_DNA.
DR   RefSeq; WP_006755622.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BIQ0; -.
DR   SMR; Q0BIQ0; -.
DR   STRING; 339670.Bamb_0414; -.
DR   EnsemblBacteria; ABI85973; ABI85973; Bamb_0414.
DR   GeneID; 44691099; -.
DR   GeneID; 60996938; -.
DR   KEGG; bam:Bamb_0414; -.
DR   PATRIC; fig|339670.21.peg.1199; -.
DR   eggNOG; COG0216; Bacteria.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000000662; 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.
FT   CHAIN           1..360
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004863"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   360 AA;  40642 MW;  83FB348C09D78CA3 CRC64;
     MKTSMQRKLD QLSTRLAELN DLLSRENVTA DLDQYRRLTR EHAELGPVVE QYALWRQSRN
     DETAAQELLA DASMRDFAED EIRSARERMV RLEAELQKML LPKDPNDDRN IFLEIRAGAG
     GDESALFAGD LLRMYLRFAE RQRWQVEMMS ESASDLGGYK EVIVRIAGQG AYSRLKFESG
     GHRVQRVPAT ETQGRIHTSA CTVAVMPEAD EIGEVEINPA DLRIDTFRAS GAGGQHINKT
     DSAVRVTHIP TGIVVECQDD RSQHKNKDRA LKVLAARIKD KQYHEQHAKE AATRKSLIGS
     GDRSERIRTY NFPQGRMTDH RINLTLYRLE ALMDGDLDEL IGALVTEHQA ELLASLGDTD