RF1_CAMC1
ID RF1_CAMC1 Reviewed; 355 AA.
AC A7ZB10;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=Ccon26_00470; ORFNames=CCC13826_1805;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-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; CP000792; EAT99101.1; -; Genomic_DNA.
DR RefSeq; WP_012000993.1; NC_009802.2.
DR AlphaFoldDB; A7ZB10; -.
DR SMR; A7ZB10; -.
DR STRING; 360104.CCC13826_1805; -.
DR EnsemblBacteria; EAT99101; EAT99101; CCC13826_1805.
DR KEGG; cco:CCC13826_1805; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_7; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000001121; 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_1000004871"
FT REGION 283..306
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; 39764 MW; E7CE6D30C1D57533 CRC64;
MFADKLHPFL DRYDEISTLL SDPNIANDIE KMTKLSKEQS SIEPVATAAT KYLQILNDIE
ENKALLEDAE LGELAKEELK SLEISREKLE EEIKILLLPK DPNDDKNIFL EIRAGTGGDE
AALFAGDLFN AYIRYAELRG YKFEIVSQSE GNTGGFKEII VLIKGKGAYS RLKFEGGTHR
VQRVPETESQ GRVHTSAVTV AIMPEVEDSE IEINPNDIRV DVMRSSGHGG QSVNTTDSAV
RITHIPTGLV VTNQDGKSQH KNKEAAMKVL KARLYEMQEQ ERLAKETSER KSQVGTGDRS
GRIRTYNYPQ NRISDHRINL TLYRLDAIMA AGLFDEIIEP LITHYQAEAM LEAGI