RF1_ALKMQ
ID RF1_ALKMQ Reviewed; 357 AA.
AC A6TK43;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Amet_0331;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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; CP000724; ABR46561.1; -; Genomic_DNA.
DR RefSeq; WP_011971469.1; NC_009633.1.
DR AlphaFoldDB; A6TK43; -.
DR SMR; A6TK43; -.
DR STRING; 293826.Amet_0331; -.
DR EnsemblBacteria; ABR46561; ABR46561; Amet_0331.
DR KEGG; amt:Amet_0331; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_9; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000001572; 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_1000057611"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 40305 MW; B468AE4979D70ADC CRC64;
MLDKLAFLQE KYEDLGEKIS DPEIINDQVQ WQKLIKEHSE IEPIVMKYRE YKTTQQALGE
TKEIMHDKAT DAELKEMAKM EVEELEESIV EMEEQLKVML LPTDPNDDKN VIVEIRGGAG
GDEAGLFAAV LFRMYTRYAE RSGWKVEMMS LNESGVGGYK EVIFMIKGKG AYSQLKYESG
AHRVQRIPTT ESGGRIHTST ATVVIMPEAE DVGEVNIDTN ELRIDVFRSS GNGGQSVNTT
DSAVRITHLP TGLVVSCQDG KSQLKNKEKA MKVLKSRLLD QMIQEQDAEI SQDRRSKVGT
GDRSERIRTY NFPQGRVTDH RINVTVYKLD AFLDGEINEM IDSLITSAQA EKMQEVQ