ID   RF1_CAMC5               Reviewed;         355 AA.
AC   A7GW12;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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};
GN   OrderedLocusNames=Ccur92_01000; ORFNames=CCV52592_0740;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) 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; CP000767; EAT99666.1; -; Genomic_DNA.
DR   RefSeq; WP_011991680.1; NC_009715.2.
DR   AlphaFoldDB; A7GW12; -.
DR   SMR; A7GW12; -.
DR   STRING; 360105.CCV52592_0740; -.
DR   EnsemblBacteria; EAT99666; EAT99666; CCV52592_0740.
DR   KEGG; ccv:CCV52592_0740; -.
DR   HOGENOM; CLU_036856_0_1_7; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000006380; 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..355
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004872"
FT   REGION          283..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         231
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   355 AA;  39619 MW;  0AC376C0C6DC8872 CRC64;
     MFADKLRPFL DRYNEISALL GDPNIINDIE KMTKLSKEQS SIEPIKNAAS QYLQTLDDIE
     ENKALLDDAE LGELAREELK SAQIRKEELE NEIKILLLPK DPNDDKNIFL EIRAGTGGDE
     AALFVGDLFN AYIRYADLRG YKFEIVSQSE GSAGGFKEII LLIKGKGAYS RLKFEGGTHR
     VQRVPETESQ GRVHTSAVTV AIMPEVEDSE IEINPNDLRI DVMRSSGHGG QSVNTTDSAV
     RITHIPTGLV VTNQDGKSQH KNKEAAMKVL KARLYEMQEA ERIAKETSER KSQVGTGDRS
     GRIRTYNFPQ NRISDHRINL TLYRLDAIMA GGLFDEIIEP LIAHHQAEAI TDAGL