MTD1_DESNO
ID MTD1_DESNO Reviewed; 415 AA.
AC P05302;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Type II methyltransferase M.DdeI {ECO:0000303|PubMed:12654995};
DE Short=M.DdeI {ECO:0000303|PubMed:2823226};
DE EC=2.1.1.37 {ECO:0000305|PubMed:2823226};
DE AltName: Full=Cytosine-specific methyltransferase DdeI;
DE AltName: Full=Modification methylase DdeI;
GN Name=ddeIM; Synonyms=ddeM;
OS Desulfomicrobium norvegicum (strain DSM 1741 / NCIMB 8310) (Desulfovibrio
OS baculatus (strain Norway 4)) (Desulfovibrio desulfuricans (strain Norway
OS 4)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=52561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS A METHYLASE.
RX PubMed=2823226; DOI=10.1093/nar/15.20.8249;
RA Sznyter L.A., Slatko B., Moran L., O'Donnell K.H., Brooks J.E.;
RT "Nucleotide sequence of the DdeI restriction-modification system and
RT characterization of the methylase protein.";
RL Nucleic Acids Res. 15:8249-8266(1987).
RN [2]
RP NOMENCLATURE.
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 methylase that recognizes the double-stranded sequence 5'-
CC CTNAG-3', methylates C-1 on both strands, and protects the DNA from
CC cleavage by the DdeI endonuclease. {ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:2823226}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018,
CC ECO:0000305|PubMed:2823226};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; Y00449; CAA68505.1; -; Genomic_DNA.
DR AlphaFoldDB; P05302; -.
DR SMR; P05302; -.
DR STRING; 52561.SAMN05421830_1265; -.
DR REBASE; 3357; M.DdeI.
DR PRO; PR:P05302; -.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..415
FT /note="Type II methyltransferase M.DdeI"
FT /id="PRO_0000087873"
FT DOMAIN 1..373
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 415 AA; 47081 MW; 34DF5968E0414EED CRC64;
MNIIDLFAGC GGFSHGFKMA GYNSILAIEK DLWASQTYSF NNPNVSVITE DITTLDPGDL
KISVSDVDGI IGGPPCQGFS LSGNRDQKDP RNSLFVDFVR FVKFFSPKFF VMENVLGILS
MKTKSRQYVK DIIAEEFSNV GYKVCVIILN ACDYGVPQSR QRVFFIGLKS DRPLNQQILT
PPSKVIESEY TSLEEAISDL PVIEAGEGGE VQDYPVAPRN KYQENMRKGS TCVYNHVAMR
HTQRLVDRFA AIKFGQSVKH VSEEHSQRKR GDANSISGKV FSQNNMRPYP YKPCPTVAAS
FQSNFIHPFY NRNFTAREGA RIQSFPDTYI FQGKRTTMSW EKHLSQYQQI GNAVPPLLAQ
ALAERISWYF ENINLINDSN VSIKRMVQRS FMSQLNLENN VNVRQDDNYD KVHSF
