ID   RF1_CAMFF               Reviewed;         355 AA.
AC   A0RRK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=CFF8240_1719;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-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; CP000487; ABK82988.1; -; Genomic_DNA.
DR   RefSeq; WP_002850812.1; NC_008599.1.
DR   AlphaFoldDB; A0RRK4; -.
DR   SMR; A0RRK4; -.
DR   STRING; 360106.CFF8240_1719; -.
DR   EnsemblBacteria; ABK82988; ABK82988; CFF8240_1719.
DR   GeneID; 61065531; -.
DR   KEGG; cff:CFF8240_1719; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_7; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000760; 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.
FT   CHAIN           1..355
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004873"
FT   REGION          278..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..298
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;  39881 MW;  6DA865F73A5AC912 CRC64;
     MLADKLRPFI DRYNELNSIL SDPEVINDIS RMTKLSKEQR NLESIKDATQ RYLSILNGIE
     ENKTLLEDPE LGELAKDELK ALETELPKLE EEIKLLLLPK DPNDEKNIFL ELRAGTGGDE
     AALFVGDLAT AYIRYTEERG YKYEIVSSSE GSAGGYKELI LLIKGEGAYS RLKYEGGTHR
     VQRVPETESQ GRVHTSAITV AIMPEVEDSE IDINPNDLKI DVMRSSGHGG QSVNTTDSAV
     RVTHIPTGLV VVNQDGKSQH KNKDAAIKVL KARLYDMQER ERREKESKER KDQVGTGDRS
     GRIRTYNYPQ NRISDHRINL TLYRLDAIMA AGLFDEIIDP LIAHYQAEAI ANAGL