ID   MTM4_NEIGO              Reviewed;         312 AA.
AC   P31033;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   13-SEP-2023, entry version 86.
DE   RecName: Full=Type II methyltransferase M.NgoMIV {ECO:0000303|PubMed:12654995};
DE            Short=M.NgoMIV {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase NgoMIV;
DE   AltName: Full=DNA methylase M.NgoMI {ECO:0000303|PubMed:1321116};
DE            Short=M.NgoMI {ECO:0000303|PubMed:1321116};
DE   AltName: Full=Modification methylase NgoMIV;
GN   Name=ngoMIVM;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=MS11;
RX   PubMed=1321116; DOI=10.1128/jb.174.15.4899-4906.1992;
RA   Stein D.C., Chien R., Seifert H.S.;
RT   "Construction of a Neisseria gonorrhoeae MS11 derivative deficient in NgoMI
RT   restriction and modification.";
RL   J. Bacteriol. 174:4899-4906(1992).
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, recognizes the double-stranded sequence 5'-
CC       GCCGGC-3', methylates C-2 on both strands, and protects the DNA from
CC       cleavage by the NgoMIV endonuclease. {ECO:0000269|PubMed:1321116,
CC       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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
CC   -!- CAUTION: Was originally known as M.NgoMI. {ECO:0000305|PubMed:1321116}.
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DR   EMBL; M86915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A42709; A42709.
DR   AlphaFoldDB; P31033; -.
DR   SMR; P31033; -.
DR   REBASE; 165908; M.Nse506ORF6588P.
DR   PRO; PR:P31033; -.
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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
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   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; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 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..312
FT                   /note="Type II methyltransferase M.NgoMIV"
FT                   /id="PRO_0000087899"
FT   DOMAIN          3..311
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   312 AA;  35226 MW;  319E20242B873452 CRC64;
     MQFTSLEICA GAGGQALGLE RAGFSHVALI EIEPSACQTL RLNRPDWNVI EGDVRLFQGE
     GYDGIDLLAG GVPCPPFSKA GKQLGKDDER DLFPEAIRLA KETDPKAIML ENVRGLLDPK
     FENYRNHITE QFAKLGYLGQ WKLLYAADYG VSQLRPRVLF VALKNEYTNF FKWPEPNSEQ
     PKTVGELLFD LMSENNWQGA HNWRLKAAQI APTLVAVQKN TAVLTWDLHD PNAHGRSWVW
     MVQVCGIVRR LKTFTGMPRL TVRMTARIQG FPDDWQFFGK KTPMYRQIGN AFPPPVAEAV
     GRQIIKALKK EN
//