ID   MTM1_METJA              Reviewed;         303 AA.
AC   Q58392;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Type II methyltransferase M.MjaI {ECO:0000303|PubMed:12654995};
DE            Short=M.MjaI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.113;
DE   AltName: Full=N-4 cytosine-specific methyltransferase MjaI;
GN   Name=mjaIM; OrderedLocusNames=MJ0985;
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).
RN   [2]
RP   CHARACTERIZATION.
RA   Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.;
RT   "Method for screening restriction endonucleases.";
RL   Patent number WO9911821, 11-MAR-1999.
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A beta subtype methylase that recognizes the double-stranded
CC       sequence 5'-CTAG-3', methylates C-1 on both strands, and protects the
CC       DNA from cleavage by the MjaI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L77117; AAB98988.1; -; Genomic_DNA.
DR   PIR; A64423; A64423.
DR   RefSeq; WP_010870499.1; NC_000909.1.
DR   AlphaFoldDB; Q58392; -.
DR   SMR; Q58392; -.
DR   STRING; 243232.MJ_0985; -.
DR   REBASE; 3889; M.MjaI.
DR   EnsemblBacteria; AAB98988; AAB98988; MJ_0985.
DR   GeneID; 1451883; -.
DR   KEGG; mja:MJ_0985; -.
DR   eggNOG; arCOG00115; Archaea.
DR   HOGENOM; CLU_024927_2_2_2; -.
DR   InParanoid; Q58392; -.
DR   OMA; MIEMWDD; -.
DR   OrthoDB; 63009at2157; -.
DR   PhylomeDB; Q58392; -.
DR   PRO; PR:Q58392; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IBA:GO_Central.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..303
FT                   /note="Type II methyltransferase M.MjaI"
FT                   /id="PRO_0000087936"
SQ   SEQUENCE   303 AA;  35518 MW;  6D4DB9B36EA90E80 CRC64;
     MMSIDITTNH KIIFGDARKM DEIEDESVHL VVTSPPYPMI EMWDELFKML NLEINKRWME
     MENEEDEEKK EKLIMQIYNL MHQTLYPVWE EVYRVLVPGG IACINIGDAT RKINGVFRLF
     PNHSKIIENF EKIGFVTLPY ILWKKPSNKP NAFLGSGFLP PNAYVTLDVE YILIFRKGKP
     RKFKPKDPLR YASAYTKEER DRWFSQIWEI VGDKQTHPKI ERRTASFPEE IPRRLIRMFS
     IIGDTVLDPF LGTGTTVKAA IELKRNSIGY EIDKSLKPII EEKIGIKQKR IGMDFNVEFI
     NRG