ID   RF1_ACIAD               Reviewed;         362 AA.
AC   Q6F9S2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 111.
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=ACIAD2418;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG69191.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR543861; CAG69191.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004928334.1; NC_005966.1.
DR   AlphaFoldDB; Q6F9S2; -.
DR   SMR; Q6F9S2; -.
DR   STRING; 62977.ACIAD2418; -.
DR   EnsemblBacteria; CAG69191; CAG69191; ACIAD2418.
DR   GeneID; 45234727; -.
DR   KEGG; aci:ACIAD2418; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_6; -.
DR   OrthoDB; 928964at2; -.
DR   BioCyc; ASP62977:ACIAD_RS11050-MON; -.
DR   Proteomes; UP000000430; 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_0000177621"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   362 AA;  40724 MW;  FB996DAB6BA58DA9 CRC64;
     MKESLRLRLD QLCDRHEELT ALLADAEVIS DNKRFRKLSR EHSDLNEIVD VWSKYRQAEE
     DIETAESMLS DPDFKDMAQE EIKENRALIE QLEGDLNILM IPKDPNDANA AYLEVRAGTG
     GDEAAIFSGD LFRMYSKYAE SRGWRIEVLS ENEGEHGGYK EVICRVDGDG VYGRLKFESG
     AHRVQRVPAT ESQGRVHTSA CTVAILPEVD VDTTVEINPA DLRIDTYRAS GAGGQHINKT
     DSAVRITHVP TGVVVECQEE RSQHKNKAKA MALLVSRLEN AKRAAQETAT SEMRRDLVGS
     GDRSERIRTY NYPQGRMTDH RINLTLYKLD AIMEGDLTEL LDSLHREYQA DQLAMLAQEN
     GG