ID   Y1296_METAC             Reviewed;         116 AA.
AC   Q8TR85;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Putative RNase MA_1296;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE   AltName: Full=Putative toxin MA_1296;
GN   OrderedLocusNames=MA_1296;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- FUNCTION: Probable toxic component of a putative type VII toxin-
CC       antitoxin (TA) system, probably an RNase. Probably neutralized by
CC       cognate antitoxin MA_1295. Neutralization may be due to AMPylation by
CC       MA_1295. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- SUBUNIT: Homodimer, probably forms a complex with cognate antitoxin
CC       MA_1295. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- PTM: Modified by cognate antitoxin MA_1295; probably at least 2
CC       successive AMPylation events occur on Tyr-82.
CC       {ECO:0000250|UniProtKB:A0A0B0QJR1}.
CC   -!- SIMILARITY: Belongs to the HepT RNase toxin family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM04715.1; -; Genomic_DNA.
DR   RefSeq; WP_011021317.1; NC_003552.1.
DR   AlphaFoldDB; Q8TR85; -.
DR   SMR; Q8TR85; -.
DR   STRING; 188937.MA_1296; -.
DR   EnsemblBacteria; AAM04715; AAM04715; MA_1296.
DR   GeneID; 1473184; -.
DR   KEGG; mac:MA_1296; -.
DR   HOGENOM; CLU_142825_3_3_2; -.
DR   InParanoid; Q8TR85; -.
DR   OMA; WRAMAGM; -.
DR   OrthoDB; 112390at2157; -.
DR   PhylomeDB; Q8TR85; -.
DR   Proteomes; UP000002487; 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 MA_1296"
FT                   /id="PRO_0000158258"
FT   MOTIF           75..82
FT                   /note="RX(4)HXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   MOD_RES         82
FT                   /note="O-di-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
SQ   SEQUENCE   116 AA;  13470 MW;  BAD71D0E652F99FD CRC64;
     MKKDDRVYLN HILQSVSLIE KYTEDLTEEE FLSNSLFQDA TIRQIQIIGE ATKNLSKSLR
     DKYPQVHWRG IAGMRDKLIH DYFGVDINAV WDTIKEDIPA LKKIVLEIIQ DLNGNP