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RF1_THEPX
ID   RF1_THEPX               Reviewed;         356 AA.
AC   B0K1F7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-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};
GN   OrderedLocusNames=Teth514_0094;
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter;
OC   unclassified Thermoanaerobacter.
OX   NCBI_TaxID=399726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-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; CP000923; ABY91416.1; -; Genomic_DNA.
DR   RefSeq; WP_009051984.1; NC_010320.1.
DR   AlphaFoldDB; B0K1F7; -.
DR   SMR; B0K1F7; -.
DR   PRIDE; B0K1F7; -.
DR   EnsemblBacteria; ABY91416; ABY91416; Teth514_0094.
DR   KEGG; tex:Teth514_0094; -.
DR   HOGENOM; CLU_036856_0_1_9; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002155; 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..356
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093517"
FT   MOD_RES         232
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   356 AA;  40600 MW;  34E33F3C27A47CBB CRC64;
     MIDKLQAIED RYVELSQKIS DPNIISNVNE WRKYVKEHAA IEDIVLKYRE YKKVLEDIEA
     TKELLSSNDE ELKEMAEEEL SQLEEKKEKL LEEIKILLIP KDPNDEKNVI MEIRAGAGGE
     EAALFAHDLF RMYSMYAEKK GWKVEIMSSN ETDIGGFKEV ILNISGKGSY SRLKYESGVH
     RVQRVPTTEA GGRIHTSTAT VAVLPEVEEV DVEINPNDIK VDVFRSGGHG GQSVNTTDSA
     VRVTHIPTGI VVTCQDERSQ IQNRERALKI LRAKLYEMAL QEQQREIAET RKSQVGTGER
     SERIRTYNYP QGRVTDHRIG LTLYRLQEVL DGDLDEIIDA LILNDQAEKL KNMNLN
 
 
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