ID   RF1_RHIEC               Reviewed;         359 AA.
AC   Q2K3T1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 99.
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=RHE_CH03756;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC92505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000133; ABC92505.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_020922380.1; NC_007761.1.
DR   AlphaFoldDB; Q2K3T1; -.
DR   SMR; Q2K3T1; -.
DR   STRING; 347834.RHE_CH03756; -.
DR   EnsemblBacteria; ABC92505; ABC92505; RHE_CH03756.
DR   GeneID; 61482194; -.
DR   KEGG; ret:RHE_CH03756; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   Proteomes; UP000001936; 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..359
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263329"
FT   REGION          280..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   359 AA;  39991 MW;  1A51DDA02EDC0276 CRC64;
     MAKLPVEKMR ELERRFGEIE ARMSAGPAAD VYVKLASEYS ELQPVVTKIR AYEKAVAELA
     DLETLLEDKS VDREMRDLAE LELPEVRARI EALEQEMQIL LLPKDAADEK SAILEIRAGT
     GGSEAALFAG DLFRMYERFA SEKGWKVEVL SASEGEAGGY KEIIATITGR GVFAKLKFES
     GVHRVQRVPE TEAGGRIHTS AATVAVLPEA EEIDIEIRPE DIRIDTMRSS GAGGQHVNTT
     DSAVRITHLP TGIVVTSSEK SQHQNRAKAM QVLRSRLYDA ERQRADSERS ADRKSQVGSG
     DRSERIRTYN FPQGRVTDHR INLTLYKLDR MMEGEIEEVV DALMADYQAS QLAQLGEQQ