ID RF1_CLOAB Reviewed; 359 AA.
AC Q97F68;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 116.
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=CA_C2884;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80827.1; -; Genomic_DNA.
DR PIR; H97254; H97254.
DR RefSeq; NP_349487.1; NC_003030.1.
DR RefSeq; WP_010966168.1; NC_003030.1.
DR AlphaFoldDB; Q97F68; -.
DR SMR; Q97F68; -.
DR STRING; 272562.CA_C2884; -.
DR GeneID; 44999372; -.
DR KEGG; cac:CA_C2884; -.
DR PATRIC; fig|272562.8.peg.3068; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_9; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000000814; 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 Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 6.10.140.1950; -; 1.
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 NCBIfam; TIGR00019; prfA; 1.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..359
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177660"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 359 AA; 40975 MW; 93F77680F2A92EF5 CRC64;
MLERLEFIES KYDELSVKIS DPSVMANQSE WQKLCKEHSE VENIVLKYRE YKKAKEDLEA
DKEMLRDKID AELKEMVEEE IKELEKSVVD YEEELRVMLL PKDPNDSKNV FVEIRGGTGG
EEAALFAADL FRMYTRYAER QGWHTEVMSA NETDIGGFKE IVFMVKGNGA YSRMKYESGT
HRVQRVPNTE SSGRIHTSAA TVAVLPEVDD VDIEINPNDI RIDVFRASGH GGQCVNTTDS
AVRITHLPTG IVVSCQDEKR QLKNKEKAMK VLRARLYEKA EAERNAGIAE NRRNQVGSGD
RSERIRTYNF PQGRITDHRI GLTIYKLEQF LDGDIDEVIN GLITAEQAEK MKEMGNTKD
//
