ID   MTF7_NEIGO              Reviewed;         374 AA.
AC   Q59606;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Type II methyltransferase M.NgoFVII {ECO:0000303|PubMed:12654995};
DE            Short=M.NgoFVII {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase NgoFVII;
DE   AltName: Full=Modification methylase NgoFVII;
GN   Name=ngoFVIIM; Synonyms=dcmG {ECO:0000303|PubMed:7607490};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=1291C;
RX   PubMed=7607490; DOI=10.1016/0378-1119(94)00649-d;
RA   Stein D.C., Gunn J.S., Radlinska M., Piekarowicz A.;
RT   "Restriction and modification systems of Neisseria gonorrhoeae.";
RL   Gene 157:19-22(1995).
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       GCSGC-3', methylates C-5 on both strands, and protects the DNA from
CC       cleavage by the NgoFVII endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:7607490}.
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}.
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DR   EMBL; U43736; AAA86270.1; -; Genomic_DNA.
DR   PIR; T10165; T10165.
DR   AlphaFoldDB; Q59606; -.
DR   SMR; Q59606; -.
DR   REBASE; 162055; M.BsuBS38ORF584P.
DR   REBASE; 296184; M.Bve83ORF3864P.
DR   REBASE; 3611; M.NgoFVII.
DR   PRO; PR:Q59606; -.
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; 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; 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..374
FT                   /note="Type II methyltransferase M.NgoFVII"
FT                   /id="PRO_0000087898"
FT   DOMAIN          16..344
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   374 AA;  42073 MW;  6210BA089D906894 CRC64;
     MLSKQISNLN SSSNKPKILS LFSGCGGLDL GFHQAGCETV WANDFSHWAC ESFRKNIGDV
     IVEGDIEQIN PNDPTIPDCD IILGGFPCQD FSMIWKQPGL EGERGNLYKS FLRFVNAKKP
     KVFVAENVKG LLTANKKKAI QQIITDFENC GYYVQANVYN FAEFGVPQFR ERVLIVGVRL
     DTGFDFRHPE PTHNETGENG LKPYVTAGQA ISNIPQNASN NELLKISDKT RRMLELIPEG
     GNFTDIPKDH PLYVKGMISH VYRRMHRNEP SKTIIAAGGG GTWGYHFPEP RAFTNRERAR
     LQSFPDDFEF VGSTTEVRRQ IGNAVPPQGV VELAKSILPI FSDNYEKVDL HEKLVEEKEI
     LFHDRLSKIR GGKQ