ID   MTP2_NEIGO              Reviewed;         330 AA.
AC   P08455;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   07-JUL-2009, entry version 70.
DE   RecName: Full=Modification methylase NgoPII;
DE            Short=M.NgoPII;
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase NgoPII;
GN   Name=ngoPIIM; Synonyms=dcrM;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P9;
RX   MEDLINE=88247748; PubMed=2837733; DOI=10.1093/nar/16.10.4369;
RA   Sullivan K.M., Saunders J.R.;
RT   "Sequence analysis of the NgoPII methyltransferase gene from Neisseria
RT   gonorrhoeae P9: homologies with other enzymes recognizing the sequence
RT   5'-GGCC-3'.";
RL   Nucleic Acids Res. 16:4369-4387(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P9;
RX   MEDLINE=89313677; PubMed=2501649; DOI=10.1007/BF00334379;
RA   Sullivan K.M., Saunders J.R.;
RT   "Nucleotide sequence and genetic organization of the NgoPII
RT   restriction-modification system of Neisseria gonorrhoeae.";
RL   Mol. Gen. Genet. 216:380-387(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33084 / F62 / M-1914;
RX   MEDLINE=94010340; PubMed=8406039; DOI=10.1016/0378-1119(93)90509-2;
RA   Gunn J.S., Stein D.C.;
RT   "Natural variation of the NgoII restriction-modification system of
RT   Neisseria gonorrhoeae.";
RL   Gene 132:15-20(1993).
CC   -!- FUNCTION: This methylase recognizes the double-stranded sequence
CC       GGCC, causes specific methylation on C-3 on both strands, and
CC       protects the DNA from cleavage by the NgoPII endonuclease.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
CC       homocysteine + DNA containing 5-methylcytosine.
CC   -!- SIMILARITY: Belongs to the C5-methyltransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X06965; CAA30038.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X52661; CAA36888.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L14564; AAA17019.1; ALT_INIT; Unassigned_DNA.
DR   PIR; S00920; CTNHP2.
DR   HSSP; P20589; 1DCT.
DR   REBASE; 3464; M.NgoPII.
DR   REBASE; 3609; M.NgoLII.
DR   BRENDA; 2.1.1.37; 588.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR001525; C5_DNA_meth.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   PANTHER; PTHR10629; C5_DNA_meth; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Restriction system; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    330       Modification methylase NgoPII.
FT                                /FTId=PRO_0000087900.
FT   ACT_SITE     73     73       By similarity.
SQ   SEQUENCE   330 AA;  37222 MW;  0A384A98B1EB03E1 CRC64;
     MKIISLFSGC GGLDLGFEKA GFEIPAANEY DKTIWATFKA NHPKTHLIEG DIRKIKEEDF
     PEEIDGIIGG PPCQSWSEAG ALRGIDDARG QLFFDYIRIL KSKQPKFFLA ENVSGMLANR
     HNGAVQNLLK MFDGCGYDVT LTMANAKDYG VAQERKRVFY IGFRKDLEIK FSFPKGSTVE
     DKDKITLKDV IWDLQDTAVP SAPQNKTNPD AVNNNEYFTG SFSPIFMSRN RVKAWDEQGF
     TVQASGRQCQ LHPQAPKMEK HGANDYRFAA GKETLYRRMT VREVARIQGF PDNFKFIYQN
     VNDAYKMIGN AVPVNLAYEI AAAIKKTLER
//