ID   MTM5_METJA              Reviewed;         292 AA.
AC   Q58893;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Type II methyltransferase M.MjaV {ECO:0000303|PubMed:12654995};
DE            Short=M.MjaV {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.113;
DE   AltName: Full=N-4 cytosine-specific methyltransferase MjaV;
GN   Name=mjaVM; OrderedLocusNames=MJ1498;
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'-GTAC-3', methylates C-4 on both strands, and protects the
CC       DNA from cleavage by the MjaV endonuclease.
CC       {ECO:0000303|PubMed:12654995}.
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; AAB99509.1; -; Genomic_DNA.
DR   PIR; A64487; A64487.
DR   RefSeq; WP_010871021.1; NC_000909.1.
DR   AlphaFoldDB; Q58893; -.
DR   SMR; Q58893; -.
DR   STRING; 243232.MJ_1498; -.
DR   REBASE; 3897; M.MjaV.
DR   PaxDb; 243232-MJ_1498; -.
DR   EnsemblBacteria; AAB99509; AAB99509; MJ_1498.
DR   GeneID; 1452405; -.
DR   KEGG; mja:MJ_1498; -.
DR   eggNOG; arCOG00115; Archaea.
DR   HOGENOM; CLU_024927_2_3_2; -.
DR   InParanoid; Q58893; -.
DR   OrthoDB; 38200at2157; -.
DR   PhylomeDB; Q58893; -.
DR   PRO; PR:Q58893; -.
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:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF33; TYPE II METHYLTRANSFERASE M.MJAV; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..292
FT                   /note="Type II methyltransferase M.MjaV"
FT                   /id="PRO_0000087938"
SQ   SEQUENCE   292 AA;  33877 MW;  A5A46D7C8FBD3FE3 CRC64;
     MEINKIYCMD CLEGMKQLKD KTVDVVVTSP PYNIGIKYNK YSDNLSREDY LNWIEEVVKE
     IKRVLKDDGS FFINVGYTAK DPWIAFDVAN VIRKHFKLQN TIHWVKSIAI QKEDVGNYPN
     IIGDIAVGHY KPINSDRFLS IMHEYIFHFT KNGNVKLDKL AIGVPYQDKS NIKRFNRKGD
     LRDRGNTWFI PYETIQSKEK ERPHPATFPP KLPEMCIKLH GVKKTNLVLD PFMGIGSTAI
     ACIRLGIDYI GFEIDEYYCR VAEERIKKEL LKTDGKFDNV KNKNIITLDA FI
//