ID   RF1_GLUOX               Reviewed;         353 AA.
AC   Q5FUR9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=GOX0032;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW59830.1; -; Genomic_DNA.
DR   RefSeq; WP_011251634.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FUR9; -.
DR   SMR; Q5FUR9; -.
DR   STRING; 290633.GOX0032; -.
DR   EnsemblBacteria; AAW59830; AAW59830; GOX0032.
DR   KEGG; gox:GOX0032; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000006375; 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..353
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263280"
FT   MOD_RES         230
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   353 AA;  39444 MW;  43A96C9B80E4FADF CRC64;
     MAFDDRLERI VARSEEVQAL MSSGELTGED FTRLSQEYAE LEPVVASIQA WKSAEEQKAG
     AQALLDDPEM RELAQMELAE IEATLPDLQH ALRLALLPKD AADERSAILE IRPAAGGDEA
     GLFAAELFDA YRRFSEQNGW RFEVMEYAEN EVAGLKEGMA TISGRSVFAR LKYESGVHRV
     QRVPATESQG RIHTSTVTVA VLPEAEEVDV TVNDDDLRID VYRASGAGGQ HVNKTESAVR
     VTHMPSGIVV AMQEEKSQHK NKAKAMKILR ARLYERERAQ LHATRAADRK SQVGTGDRSE
     RIRTYNFPQG RVTDHRINLT LYKIDRIMGG EFDEIIDALT REEQTELLAA EGF