ID   RF1_EDWI9               Reviewed;         360 AA.
AC   C5B814;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=NT01EI_1564;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR68750.1; -; Genomic_DNA.
DR   RefSeq; WP_015870908.1; NC_012779.2.
DR   AlphaFoldDB; C5B814; -.
DR   SMR; C5B814; -.
DR   STRING; 67780.B6E78_01015; -.
DR   EnsemblBacteria; ACR68750; ACR68750; NT01EI_1564.
DR   GeneID; 7961045; -.
DR   KEGG; eic:NT01EI_1564; -.
DR   PATRIC; fig|634503.3.peg.1398; -.
DR   HOGENOM; CLU_036856_0_1_6; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001485; 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..360
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000202692"
FT   REGION          285..304
FT                   /note="Disordered"
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   360 AA;  40313 MW;  461C4AE25912D635 CRC64;
     MKPSIVAKLE ALQERHEEVQ ALLGDAGVIA DQDRFRALSR EYAQLTDVSH CFLAWRQVQD
     DLTTAEMLLD DPEMRDMAQE ELKEARGRLA ELEQQLQILL LPKDPDDERD CFLEVRAGTG
     GDEAALFAGD LFRMYSRYAE ARRWRIEIMS ASEGEHGGYK EVIARVSGDG AYGRLKFESG
     GHRVQRVPAT ESQGRIHTSA CTVAVMPAVP EAELPQINPA DLRIDTYRSS GAGGQHVNTT
     DSAIRITHLP TGIVVECQDE RSQHKNKAKA MSVLGARIRA AEIAKRQQEE ASTRRNLLGS
     GDRSDRVRTY NFPQGRVTDH RINLTLYRLD EVMEGKLDNL IEPIVQEHQA DQLSALAEQE