ID   MTD1_NEIMC              Reviewed;         420 AA.
AC   Q9RLM4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-SEP-2023, entry version 76.
DE   RecName: Full=Type II methyltransferase M.NmeDI {ECO:0000303|PubMed:12654995};
DE            Short=M.NmeDI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase NmeDIP;
DE   AltName: Full=Probable modification methylase NmeDIP;
GN   Name=nmeDIMP;
OS   Neisseria meningitidis serogroup C.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=135720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2120 / Serogroup C / Serotype NT;
RX   PubMed=10671450; DOI=10.1128/jb.182.5.1296-1303.2000;
RA   Claus H., Friedrich A., Frosch M., Vogel U.;
RT   "Differential distribution of novel restriction-modification systems in
RT   clonal lineages of Neisseria meningitidis.";
RL   J. Bacteriol. 182:1296-1303(2000).
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       RCCGGB-3', methylates C-2 on both strands, and protects the DNA from
CC       cleavage by the NmeDI endonuclease. {ECO:0000303|PubMed:12654995}.
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   -!- 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; AJ238948; CAB59897.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RLM4; -.
DR   SMR; Q9RLM4; -.
DR   REBASE; 4188; M.NmeDI.
DR   PRO; PR:Q9RLM4; -.
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; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..420
FT                   /note="Type II methyltransferase M.NmeDI"
FT                   /id="PRO_0000087902"
FT   DOMAIN          56..411
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   420 AA;  47931 MW;  6E2472BA070354C9 CRC64;
     MMSLKIQPAV PKKSDKPSAT NRDCQNFKRE KNNLPFQLTD KSCNLDISIR QERKKTLIFS
     FFSGAGFLDL GFELSGFDIA FVNEVHPPFL EAYKYSRSRM DIPKPKYGYF KGSIDECLYA
     EKAKDLAGWV KKEKQNGIIV GFIGGPPCPD FSIAGKNKGK DGENGKLSQS YVDLICKNQP
     DFFVFENVKG LYRTAKHREF FNALKRQLSD FGYVCTEKLI NAIEYGVPQD RERIILVGFL
     SQHVDALQKF DWDAHISFPD ALEKDWPTTE EVGRVVSQPA NIYPELTVQY WFNRNGVDTH
     PNASKHFQPR AGLEKFQTIS EGDDKKKSYK RLHRWRYSPT AAYGNNEVHI HPYLPRRISA
     AEALAIQSLP KEFELPDNMT LSNMFKTIGN GVPFLAAKGI AMTLKSYLEN HYERTKTDGC
//