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RF1_ERYLH
ID   RF1_ERYLH               Reviewed;         355 AA.
AC   Q2N5U6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=ELI_14265;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594;
RX   PubMed=19168610; DOI=10.1128/jb.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC64945.1; -; Genomic_DNA.
DR   RefSeq; WP_011415767.1; NC_007722.1.
DR   AlphaFoldDB; Q2N5U6; -.
DR   SMR; Q2N5U6; -.
DR   STRING; 314225.ELI_14265; -.
DR   EnsemblBacteria; ABC64945; ABC64945; ELI_14265.
DR   KEGG; eli:ELI_14265; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008808; 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..355
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004889"
FT   MOD_RES         231
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   355 AA;  38725 MW;  2524A205D010EC52 CRC64;
     MTIPATRLDQ IANRFAELEA RMASGTLEGE EFVQASRDYA ELEPVAKVAA EVKAMREEIG
     GLEEMLADPE MKAMAQEELA AIREALPEKE RQLAIAMLPK DSADNKPAML EIRAGTGGDE
     AALFAGDLYR MYERFAGEQG WKVEPVSMNA SEVGGFKEIV ANVSGTGVFA KLKFESGVHR
     VQRVPETESG GRIHTSAATV AVLPEPDEVD VQIDDKDLKI DIYRASGAGG QHVNTTDSAV
     RITHLPTGIV VQQQDERSQH KNKAKAMQVL RTRLYDHLRE QSQGEEAAAR KAMVGSGDRS
     ERIRTYNFPQ GRVTDHRIGL TLHKLDEIIA GPGLGELVGA LIAEDEAKRL AALSE
 
 
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