ID   MTMV_KOCVA              Reviewed;         454 AA.
AC   P14244;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Type II methyltransferase M.MvaI {ECO:0000303|PubMed:12654995};
DE            Short=M.MvaI {ECO:0000303|PubMed:2690010};
DE            EC=2.1.1.113;
DE   AltName: Full=Modification methylase MvaI;
DE   AltName: Full=N-4 cytosine-specific methyltransferase MvaI;
GN   Name=mvaIM {ECO:0000303|PubMed:2690010};
OS   Kocuria varians (Micrococcus varians).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=1272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RFL19;
RX   PubMed=2690010; DOI=10.1093/nar/17.23.9823;
RA   Klimasauskas S., Timinskas A., Menkevicius S., Butkiene D., Butkus V.,
RA   Janulaitis A.;
RT   "Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases:
RT   similarity to adenine and cytosine-C5 DNA-methylases.";
RL   Nucleic Acids Res. 17:9823-9832(1989).
RN   [2]
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, recognizes the double-stranded
CC       sequence 5'-CCWGG-3', methylatES C-2 on both strands, and protects the
CC       DNA from cleavage by the MvaI 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; X16985; CAA34854.1; -; Genomic_DNA.
DR   PIR; S07539; S07539.
DR   AlphaFoldDB; P14244; -.
DR   SMR; P14244; -.
DR   REBASE; 3450; M.MvaI.
DR   KEGG; ag:CAA34854; -.
DR   BRENDA; 2.1.1.113; 3359.
DR   PRO; PR:P14244; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
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; -; 2.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Restriction system; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..454
FT                   /note="Type II methyltransferase M.MvaI"
FT                   /id="PRO_0000087929"
SQ   SEQUENCE   454 AA;  53072 MW;  B0330A9DF037E93A CRC64;
     MEYLNDKDQH LIDKLSKKIN DNNQYLGFLN TNTKELTHRY HIYPAMMIPQ LAKEFIELTQ
     QVKPEIKKLY DPFMGSGTSL VEGLAHGLEV YGTDINPLSQ MMSKAKTTPI EPSKLSRAIS
     DLEYSIREMT ILYHEGNYKI SNLPDFDRID FWFKEEVIIS LQLIKNCINE FIEDDLKTFF
     MAAFSETVRH VSNTRNNEFK LYRMAPEKLE IWNPNVTEEF LKRVYRNELG NMDFYRQLEN
     VGNYSPKTII NKQSNIKLPE EFKDEMFDIV VTSPPYGDSK TTVAYGQFSR LSAQWLDLKI
     DDETKINQLD NVMLGGKTDK NIIVNDVLEY LNSPTSKSVF NLISHKDEKR ALEVLQFYVD
     LDKSIKETTR VMKPESYQFW VVANRTVKMI SIPTDIIISE LFKKYNVHHL YSFYRKIPNK
     RMPSKNSPTN KIGNHSVTMT SEIILMLKNY INKS