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Y125_METJA
ID   Y125_METJA              Reviewed;         116 AA.
AC   Q57589;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Putative RNase MJ0125;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE   AltName: Full=Putative toxin MJ0125;
GN   OrderedLocusNames=MJ0125;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Probable toxic component of a putative type VII toxin-
CC       antitoxin (TA) system, probably an RNase. Probably neutralized by
CC       cognate antitoxin MJ0126. Neutralization may be due to AMPylation by
CC       MJ0126. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- SUBUNIT: Homodimer, probably forms a complex with cognate antitoxin
CC       MJ0126. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- PTM: Modified by cognate antitoxin MJ0126; probably at least 2
CC       successive AMPylation events occur on Tyr-83.
CC       {ECO:0000250|UniProtKB:A0A0B0QJR1}.
CC   -!- SIMILARITY: Belongs to the HepT RNase toxin family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98105.1; -; Genomic_DNA.
DR   PIR; E64315; E64315.
DR   RefSeq; WP_010869618.1; NC_000909.1.
DR   AlphaFoldDB; Q57589; -.
DR   SMR; Q57589; -.
DR   STRING; 243232.MJ_0125; -.
DR   EnsemblBacteria; AAB98105; AAB98105; MJ_0125.
DR   GeneID; 1450967; -.
DR   KEGG; mja:MJ_0125; -.
DR   eggNOG; arCOG05024; Archaea.
DR   HOGENOM; CLU_142825_3_3_2; -.
DR   InParanoid; Q57589; -.
DR   OMA; EQFTTGI; -.
DR   OrthoDB; 112390at2157; -.
DR   PhylomeDB; Q57589; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0110001; C:toxin-antitoxin complex; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   InterPro; IPR008201; HepT-like.
DR   Pfam; PF01934; DUF86; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nuclease; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..116
FT                   /note="Putative RNase MJ0125"
FT                   /id="PRO_0000158259"
FT   MOTIF           76..83
FT                   /note="RX(4)HXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   MOD_RES         83
FT                   /note="O-di-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
SQ   SEQUENCE   116 AA;  13970 MW;  7A77740A495160EF CRC64;
     MPKRDIKAFL YDILSYMDDI INFTKDMDYE EFINNKAIKY AVIRCLEVIG EAVKKIPKDI
     REKYPHIPFK ELAGMRDKLI HQYFGVDYLT VWETAKYEIP EIKKEFEKII KDLEEK
 
 
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