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Y1216_METJA
ID   Y1216_METJA             Reviewed;         121 AA.
AC   Q58613;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Putative RNase MJ1216;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE   AltName: Full=Putative toxin MJ1216;
GN   OrderedLocusNames=MJ1216;
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       antitoxin MJ1215 or MJ1217. Neutralization may be due to AMPylation by
CC       antitoxin. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- SUBUNIT: Homodimer, probably forms a complex with antitoxin MJ1215 or
CC       MJ1217. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- PTM: Modified by antitoxin MJ1215 or MJ1217; 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; AAB99217.1; -; Genomic_DNA.
DR   PIR; G64451; G64451.
DR   RefSeq; WP_010870728.1; NC_000909.1.
DR   AlphaFoldDB; Q58613; -.
DR   SMR; Q58613; -.
DR   STRING; 243232.MJ_1216; -.
DR   EnsemblBacteria; AAB99217; AAB99217; MJ_1216.
DR   GeneID; 1452112; -.
DR   KEGG; mja:MJ_1216; -.
DR   eggNOG; arCOG05024; Archaea.
DR   HOGENOM; CLU_142825_3_3_2; -.
DR   InParanoid; Q58613; -.
DR   OMA; WRAMAGM; -.
DR   OrthoDB; 112390at2157; -.
DR   PhylomeDB; Q58613; -.
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..121
FT                   /note="Putative RNase MJ1216"
FT                   /id="PRO_0000158263"
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   121 AA;  14498 MW;  F95805B623D85298 CRC64;
     MPKRDIKAFL YDILEYMDDI INFTKNMEYE EFINNKAIKY AVVRCLEVIG EAVKKIPKDI
     REKYPHIPFK ELAGMRDKLI HQYFGVDYLT VWETAKYEIP EIKKEFEKII KDIEGKDENS
     L
 
 
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