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Database: UniProt
Entry: Y1217_METJA
LinkDB: Y1217_METJA
Original site: Y1217_METJA 
ID   Y1217_METJA             Reviewed;          98 AA.
AC   Q58614;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-NOV-2023, entry version 101.
DE   RecName: Full=Putative protein adenylyltransferase MJ1217;
DE            EC=2.7.7.108 {ECO:0000250|UniProtKB:A0A0B0QJN8};
DE   AltName: Full=Putative antitoxin MJ1217;
GN   OrderedLocusNames=MJ1217;
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 MJ1216 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=2.7.7.108;
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 MJ1216.
CC       {ECO:0000250|UniProtKB:Q8ECH7}.
CC   -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR   EMBL; L77117; AAB99218.1; -; Genomic_DNA.
DR   PIR; H64451; H64451.
DR   RefSeq; WP_010870729.1; NC_000909.1.
DR   AlphaFoldDB; Q58614; -.
DR   SMR; Q58614; -.
DR   STRING; 243232.MJ_1217; -.
DR   PaxDb; 243232-MJ_1217; -.
DR   EnsemblBacteria; AAB99218; AAB99218; MJ_1217.
DR   GeneID; 1452113; -.
DR   KEGG; mja:MJ_1217; -.
DR   eggNOG; arCOG01206; Archaea.
DR   HOGENOM; CLU_130257_10_3_2; -.
DR   InParanoid; Q58614; -.
DR   OMA; YVRQEQT; -.
DR   OrthoDB; 64953at2157; -.
DR   PhylomeDB; Q58614; -.
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   CDD; cd05403; NT_KNTase_like; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   PANTHER; PTHR33571:SF14; PROTEIN ADENYLYLTRANSFERASE MJ0128-RELATED; 1.
DR   PANTHER; PTHR33571; SSL8005 PROTEIN; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 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 MJ1217"
FT                   /id="PRO_0000107219"
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;  11559 MW;  074E10CA476F74D1 CRC64;
     MKTLSEIKEI LRKHKKILKE KYKVKSIAIF GSYAREEQKE TSDIDILIDY YEPISLLKLI
     ELENYLSDLL GIKVDLITKN SIHNPYVKKS IEEDLIYI
//
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