ID   RF1_PELPB               Reviewed;         357 AA.
AC   B4SAR5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Ppha_0078;
OS   Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=324925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5477 / BU-1;
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., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL   Submitted (JUN-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001110; ACF42434.1; -; Genomic_DNA.
DR   RefSeq; WP_012506932.1; NC_011060.1.
DR   AlphaFoldDB; B4SAR5; -.
DR   SMR; B4SAR5; -.
DR   STRING; 324925.Ppha_0078; -.
DR   EnsemblBacteria; ACF42434; ACF42434; Ppha_0078.
DR   KEGG; pph:Ppha_0078; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_10; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002724; 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_1000093483"
FT   MOD_RES         234
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   357 AA;  40716 MW;  5DDE0F795CEA014B CRC64;
     MLDKLQSIKE KHLDLEQLLS DPNAAADQVR FRKLNKEYSD LREIVQAYDL YAATKTELDE
     SRQLLKSESD AEMKELVQAE ISELQKKLPE LEQQLKILLL PKEEADSRNV IIEIRAGTGG
     EEAALFAADL TRMYQRYAEH QGWQCETLHF NESSVPGGFR EITLSVNGHD VYGTMKYESG
     VHRVQRVPDT ETQGRIHTSA VSVAVLPEAE EVDVEIRRED LRFDTYRSGG KGGQNVNKVE
     TAVRITHMPT GIVSACQEQR SQLQNKERAM QMLRTKLYDI QLAEQQQQRA DLRRSMVTTG
     DRSAKIRTYN YPQSRVTDHR IAFTSHALPQ ILQGDLQDII NALKMHDQAA RLQAELV