ID   Y604_METJA              Reviewed;         100 AA.
AC   Q58021;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative protein adenylyltransferase MJ0604;
DE            EC=2.7.7.n1 {ECO:0000250|UniProtKB:A0A0B0QJN8};
DE   AltName: Full=Putative antitoxin MJ0604;
GN   OrderedLocusNames=MJ0604;
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: Putative antitoxin component of a putative type VII toxin-
CC       antitoxin (TA) system. Its cognate toxin might be MJ0605, which it
CC       might AMPylate. {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   -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98594.1; -; Genomic_DNA.
DR   PIR; D64375; D64375.
DR   RefSeq; WP_010870108.1; NC_000909.1.
DR   AlphaFoldDB; Q58021; -.
DR   SMR; Q58021; -.
DR   STRING; 243232.MJ_0604; -.
DR   EnsemblBacteria; AAB98594; AAB98594; MJ_0604.
DR   GeneID; 1451469; -.
DR   KEGG; mja:MJ_0604; -.
DR   eggNOG; arCOG01195; Archaea.
DR   HOGENOM; CLU_130257_3_2_2; -.
DR   InParanoid; Q58021; -.
DR   OMA; INWSFHR; -.
DR   OrthoDB; 108083at2157; -.
DR   PhylomeDB; Q58021; -.
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..100
FT                   /note="Putative protein adenylyltransferase MJ0604"
FT                   /id="PRO_0000106953"
FT   MOTIF           29..43
FT                   /note="GSX(10)DXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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"
SQ   SEQUENCE   100 AA;  11667 MW;  A259493170FF0BC2 CRC64;
     MNEEKAIKEF VNALKSKYRG RIKKIILFGS YARGDYTEES DIDILIVGDV DFDYVIDLCT
     KLLLKYGVVI NAIVESEELF NKKINWSFHR NVLEEGRVLY