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Y126_METJA
ID   Y126_METJA              Reviewed;          98 AA.
AC   Q57590;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Putative protein adenylyltransferase MJ0126;
DE            EC=2.7.7.n1 {ECO:0000250|UniProtKB:A0A0B0QJN8};
DE   AltName: Full=Putative antitoxin MJ0126;
GN   OrderedLocusNames=MJ0126;
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 antitoxin component of a putative type VII toxin-
CC       antitoxin (TA) system. Neutralizes cognate toxic MJ0125 by di-
CC       AMPylation. {ECO:0000250|UniProtKB:Q8ECH7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC         Evidence={ECO:0000250|UniProtKB:Q8ECH7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + O-(5'-adenylyl)-L-tyrosyl-[protein] = diphosphate + O-
CC         [5'-(adenylyl-(5'->3')-adenylyl)]-L-tyrosyl-[protein];
CC         Xref=Rhea:RHEA:66528, Rhea:RHEA-COMP:13846, Rhea:RHEA-COMP:17046,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83624,
CC         ChEBI:CHEBI:167160; Evidence={ECO:0000250|UniProtKB:Q8ECH7};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8ECH7};
CC       Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:Q8ECH7};
CC   -!- SUBUNIT: Probably forms a complex with cognate toxin MJ0125.
CC       {ECO:0000250|UniProtKB:Q8ECH7}.
CC   -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98106.1; -; Genomic_DNA.
DR   RefSeq; WP_010869619.1; NC_000909.1.
DR   AlphaFoldDB; Q57590; -.
DR   SMR; Q57590; -.
DR   STRING; 243232.MJ_0126; -.
DR   EnsemblBacteria; AAB98106; AAB98106; MJ_0126.
DR   GeneID; 1450968; -.
DR   KEGG; mja:MJ_0126; -.
DR   eggNOG; arCOG01206; Archaea.
DR   HOGENOM; CLU_130257_10_3_2; -.
DR   InParanoid; Q57590; -.
DR   OMA; GEMNDDS; -.
DR   OrthoDB; 108900at2157; -.
DR   PhylomeDB; Q57590; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Toxin-antitoxin system;
KW   Transferase.
FT   CHAIN           1..98
FT                   /note="Putative protein adenylyltransferase MJ0126"
FT                   /id="PRO_0000106705"
FT   MOTIF           31..45
FT                   /note="GSX(10)DXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT   BINDING         75
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
SQ   SEQUENCE   98 AA;  11605 MW;  0748F07131F29685 CRC64;
     MKTLSEIKEI LRKHKKELKE KYKVKSIAIF GSYARNEQTE TSDIDILIDY YEPISLLKLI
     ELENYLSDLL EIKVDLITKN SIHNPYVKKS IEEDLIYI
 
 
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