RF1_HELPH
ID RF1_HELPH Reviewed; 352 AA.
AC Q1CV77;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=HPAG1_0078;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84145.1; -; Genomic_DNA.
DR RefSeq; WP_000025116.1; NC_008086.1.
DR AlphaFoldDB; Q1CV77; -.
DR SMR; Q1CV77; -.
DR EnsemblBacteria; ABF84145; ABF84145; HPAG1_0078.
DR KEGG; hpa:HPAG1_0078; -.
DR HOGENOM; CLU_036856_0_1_7; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000008835; 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..352
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263285"
FT REGION 288..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 352 AA; 39628 MW; F1DBE45E2E803319 CRC64;
MSILAEKLSS ILKRYDELTA LLSSAEVISD IKKLTELSKE QSSIEEISIA SKEYLSVLEN
IKENKELLED KELSELAKEE LKILEIQKSD LETAIKQLLI PKDPNDDKNI YLELRAGTGG
NEAGIFVGDL FKAYCRYADL KKWRVEIVSS SENSVGGYKE IIALIKGKGV YSRLKFEAGT
HRVQRVPETE SQGRIHTSAI TVAIMPEVDD VEVSINPSDL KIEVFRAGGH GGQCVNTTDS
AVRITHLPTN ISVSMQDEKS QHKNKDKALK ILKARLYEKQ IEEQQLANAK DRKEQVGSGD
RSERIRTYNY PQNRLSEHRI NLTLYSLEEI MLSGNLDEVI NPLIAHAQSQ FE