ID   RF1_CHLL2               Reviewed;         357 AA.
AC   B3EE55;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Clim_0083;
OS   Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 245 / NBRC 103803 / 6330;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium limicola DSM 245.";
RL   Submitted (MAY-2008) 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; CP001097; ACD89189.1; -; Genomic_DNA.
DR   RefSeq; WP_012465070.1; NC_010803.1.
DR   AlphaFoldDB; B3EE55; -.
DR   SMR; B3EE55; -.
DR   STRING; 290315.Clim_0083; -.
DR   EnsemblBacteria; ACD89189; ACD89189; Clim_0083.
DR   KEGG; cli:Clim_0083; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_10; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008841; 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..357
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093436"
FT   MOD_RES         234
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   357 AA;  40798 MW;  DEA49FD5D0603C75 CRC64;
     MFDKLQSIKE KHLDLEQQLA DPSAASDQNR FRKLNKEYSD LKEIVHAFDR YSLARKQLEE
     SRELLGSEKD PQMRELVQME IEDLQEKLPE LEQQLKVLLL PKDEADSRNV IMEIRAGTGG
     DEAALFAADL LRMYQRYAER QGWKCVLLDY TESSVPGGFR EVTLEVSGHD VFATMKYESG
     VHRVQRVPDT ETQGRIHTSA ASVAVLPEAE EVDVEIRRDD LRFDTYRSGG KGGQNVNKVE
     TAVRITHLPT GIVAACQEER SQLQNKERAM TMLRTKLYDI QLAEQQQQRA DLRRSMVSTG
     DRSAKIRTYN YPQSRVTDHR IGFTSHALPQ IMQGEIGDVI EALKLHDQTA RLQAEQV