MTM2_METJA
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 03-AUG-2022, entry version 116.
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 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 OMA; KHGKICK; -.
DR OrthoDB; 63009at2157; -.
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:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 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 Pfam; PF01555; N6_N4_Mtase; 2.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 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
