ID   RF1_CUPMC               Reviewed;         360 AA.
AC   Q1LIF3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 88.
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=Rmet_3201;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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=ABF10073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000352; ABF10073.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029308602.1; NC_007973.1.
DR   AlphaFoldDB; Q1LIF3; -.
DR   SMR; Q1LIF3; -.
DR   STRING; 266264.Rmet_3201; -.
DR   PRIDE; Q1LIF3; -.
DR   EnsemblBacteria; ABF10073; ABF10073; Rmet_3201.
DR   KEGG; rme:Rmet_3201; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_4; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002429; Chromosome.
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..360
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263328"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   360 AA;  40131 MW;  75AF63471AC5448F CRC64;
     MKASISTKLD QLAERLDEVN ALLAREDATA NMDQYRKLSR EHAELSPVAE QYGQYRQAQD
     DLATAQALLD DPEMKEFAAD EIDAARERLQ SLENSLQTLL LPKDPNDDRN LLLEIRAGTG
     GEESALFAAD LLRMYTRYAE RRRWQVEIMS ESPSDLGGYK EVIVRIAGDA AFSRLKFESG
     GHRVQRVPAT ESQGRIHTSA CTVAVMPEAD EVGEVEINPS DLRVDTFRAS GAGGQHVNKT
     DSAVRLTHLP TGIVVECQDD RSQHRNKEKA MKVLAARIKD MQLRAAQAKE ANTRRNLIGS
     GDRSDRIRTY NFPQGRVTDH RINLTLYKID MIMDGDLDEL ISALSAEHQA DQLAALGEES