ID   RF1_AQUAE               Reviewed;         362 AA.
AC   O67032;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Peptide chain release factor 1;
DE            Short=RF-1;
GN   Name=prfA; OrderedLocusNames=aq_876;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC06991.1; -; Genomic_DNA.
DR   PIR; E70375; E70375.
DR   RefSeq; NP_213594.1; NC_000918.1.
DR   RefSeq; WP_010880532.1; NC_000918.1.
DR   AlphaFoldDB; O67032; -.
DR   SMR; O67032; -.
DR   STRING; 224324.aq_876; -.
DR   EnsemblBacteria; AAC06991; AAC06991; aq_876.
DR   KEGG; aae:aq_876; -.
DR   PATRIC; fig|224324.8.peg.682; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_0; -.
DR   InParanoid; O67032; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000798; 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..362
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177624"
FT   MOD_RES         237
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  41834 MW;  CCC91D0043653244 CRC64;
     MLKEAYISRL DKLQEKYRKL QEELSKPEVI QDVEKYKKLS KELKELQEIN ELYERYKKAQ
     KELKEAKELL KSSDKDLREL AEEEVNRLTE EMKKLEEELK VHLVPKDPND TKNVILEIRA
     GAGGEEAALF AADLFRMYQK YAEEKGWKVS ILSSNKTGLG GYKEVIALIE GEGAYSRLKY
     ESGVHRVQRV PVTESSGRIH TSTATVAVLP EVDETDIKIK PEELKIETFR ASGAGGQYVN
     TTETAVRITH IPTGIVVQCQ DERSQFQNKQ KALKILYAKL KDYYERKKQE EIAKERKEQV
     GTGERSEKIR TYNFPQNRVT DHRINLTLYK LQDVLEGKLD EIIDALRAKE IEKKLELVEK
     EG