ID MTM2_METJA Reviewed; 530 AA. AC Q58843; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Type II methyltransferase M.MjaII {ECO:0000303|PubMed:12654995}; DE Short=M.MjaII {ECO:0000303|PubMed:12654995}; DE EC=2.1.1.113; DE AltName: Full=N-4 cytosine-specific methyltransferase MjaII; GN Name=mjaIIM; OrderedLocusNames=MJ1448; 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: An alpha subtype methylase that recognizes the double- CC stranded sequence 5'-GGNCC-3', methylates C-5 on both strands, and CC protects the DNA from cleavage by the MjaII 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L77117; AAB99457.1; -; Genomic_DNA. DR PIR; G64480; G64480. DR RefSeq; WP_010870968.1; NC_000909.1. DR AlphaFoldDB; Q58843; -. DR STRING; 243232.MJ_1448; -. DR REBASE; 3896; M.MjaII. DR PaxDb; 243232-MJ_1448; -. DR EnsemblBacteria; AAB99457; AAB99457; MJ_1448. DR GeneID; 1452352; -. DR KEGG; mja:MJ_1448; -. DR eggNOG; arCOG00890; Archaea. DR HOGENOM; CLU_039482_0_0_2; -. DR InParanoid; Q58843; -. DR OrthoDB; 38200at2157; -. DR PhylomeDB; Q58843; -. DR PRO; PR:Q58843; -. 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; 2. 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; 2. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2. 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..530 FT /note="Type II methyltransferase M.MjaII" FT /id="PRO_0000087937" SQ SEQUENCE 530 AA; 63755 MW; FF6F29ADD080060C CRC64; MNLDAWLDIQ PAKKLYTIKE ASRILTKKFG KEIKEHNISY LVQYGRVNKY KIKNRVYVDI DEVENYYKKL FFEKRKEWEE KLGFKLDWDL AFDLLSEKER TKHVHGIHPY KGKFIPQLVE YFLKRHFNVG DIIIDPFMGS GTTLVQCMEM GINSIGIDIS PFNCLIAEVK LQKYDIQKLK KILLDMLNKT KEFSKNLGDD EFVKEMDKLI EKYNKKYFTL EYKRKLSKKE IDEDSYSEKI MEMFYLEYKK LKEKYCKNDD EFDDIFKDKP FLYKWYSPRI RAELNFYLNL IKDCRDETIK KVAMIILSRT ARSVRGTTHF DLATLKEPVF DPYYCYKHKK ICRPVQTILR HLEEYTNDVI SRIEEFSKIR KDAYYLIING DSRTVDIEEE LKKHPNFYEL YKNKKIDGIF TSPPYLGQID YHEQHAYAYE LFDIPRLDEL EIGPKFKGSS KKAQKEYIEG ISDVLINMKR FLNEDAKIFI VVNDKKNLYK EIFEKSGLIL VREFKRPVLN RTERDRNPYY ESIFELKMEE //