ID   Y101_METAC              Reviewed;         119 AA.
AC   Q8TUG6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Putative RNase MA_0101;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE   AltName: Full=Putative toxin MA_0101;
GN   OrderedLocusNames=MA_0101;
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_102. Neutralization may be due to AMPylation by
CC       MA_102. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- SUBUNIT: Homodimer, probably forms a complex with cognate antitoxin
CC       MA_102. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- PTM: Modified by cognate antitoxin MA_102; probably at least 2
CC       successive AMPylation events occur on Tyr-84.
CC       {ECO:0000250|UniProtKB:A0A0B0QJR1}.
CC   -!- SIMILARITY: Belongs to the HepT RNase toxin family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM03555.1; -; Genomic_DNA.
DR   RefSeq; WP_011020160.1; NC_003552.1.
DR   AlphaFoldDB; Q8TUG6; -.
DR   SMR; Q8TUG6; -.
DR   STRING; 188937.MA_0101; -.
DR   EnsemblBacteria; AAM03555; AAM03555; MA_0101.
DR   GeneID; 1471993; -.
DR   KEGG; mac:MA_0101; -.
DR   HOGENOM; CLU_142825_3_3_2; -.
DR   InParanoid; Q8TUG6; -.
DR   OMA; RHAYHAT; -.
DR   OrthoDB; 112390at2157; -.
DR   PhylomeDB; Q8TUG6; -.
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..119
FT                   /note="Putative RNase MA_0101"
FT                   /id="PRO_0000158257"
FT   MOTIF           77..84
FT                   /note="RX(4)HXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   MOD_RES         84
FT                   /note="O-di-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
SQ   SEQUENCE   119 AA;  13853 MW;  C9B86D6B64B927A2 CRC64;
     MKEKREFRDY LSDIFDAIEK IENFTQDISF DAFVEDEMRV FAVVRALEII GEAAKNVPLE
     IKENYPSVPW KEMARTRDKL IHSYFGVDLN VVWKTVNKNL PPLKDQISEI LKDLGNTSS