RF1_CHLP8
ID RF1_CHLP8 Reviewed; 357 AA.
AC B3QRH7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Cpar_0069;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=517417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327;
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., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
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}.
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DR EMBL; CP001099; ACF10497.1; -; Genomic_DNA.
DR RefSeq; WP_012501332.1; NC_011027.1.
DR AlphaFoldDB; B3QRH7; -.
DR SMR; B3QRH7; -.
DR STRING; 517417.Cpar_0069; -.
DR EnsemblBacteria; ACF10497; ACF10497; Cpar_0069.
DR KEGG; cpc:Cpar_0069; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_10; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000008811; 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.
FT CHAIN 1..357
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000093437"
FT MOD_RES 234
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 40468 MW; 6895C9D03C4E61EF CRC64;
MFDKLQSIKD KYLTIEQQLS DPEVAADQNR FRKLNKEYSG LREIVRAYDN WRSAKQQLDE
TLAMQKSEED PEMRALAAAE AEELQERLPE LEQNLKILLL PKDEADTRNA IIEIRAGTGG
DEAGLFAADL MRMYQRYAER QGWSCQTLDV SEGSVPGSLK EVSLEVSGHD VYGILKFESG
VHRVQRVPET ETQGRIHTSA ASVAVLPEAE EVDVEIRKDD LQMDTFRSGG KGGQNVNKVE
TAVRITHVPS GIVVACQEER SQLQNRERAM KMLRSKLYDI KITEQLQSRA DLRRSMVATG
DRSAKIRTYN FPQSRVTDHR IGFTTHALPQ VMQGELEPII DALRMHDQAE RLKAETN