[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=P9; DOI=10.1093/nar/16.10.4369; PubMed=2837733 [NCBI, ExPASy, EBI, Israel, Japan] Sullivan K.M., Saunders J.R.; "Sequence analysis of the NgoPII methyltransferase gene from Neisseria gonorrhoeae P9: homologies with other enzymes recognizing the sequence 5'-GGCC-3'."; Nucleic Acids Res. 16:4369-4387(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=P9; DOI=10.1007/BF00334379; PubMed=2501649 [NCBI, ExPASy, EBI, Israel, Japan] Sullivan K.M., Saunders J.R.; "Nucleotide sequence and genetic organization of the NgoPII restriction-modification system of Neisseria gonorrhoeae."; Mol. Gen. Genet. 216:380-387(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 33084 / F62 / M-1914; DOI=10.1016/0378-1119(93)90509-2; PubMed=8406039 [NCBI, ExPASy, EBI, Israel, Japan] Gunn J.S., Stein D.C.; "Natural variation of the NgoII restriction-modification system of Neisseria gonorrhoeae."; Gene 132:15-20(1993).

Comments

FUNCTION: This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the NgoPII endonuclease.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
SIMILARITY: Belongs to the C5-methyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X06965; CAA30038.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52661; CAA36888.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L14564; AAA17019.1; ALT_INIT; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S00920; CTNHP2.

3D structure databases

HSSP

P20589; 1DCT. [HSSP ENTRY / PDB]

ModBase

P08455.

Protein family/group databases

REBASE

3464; M.NgoPII.

Ontologies

GO:0003886;	Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0006306;	Biological process: DNA methylation (inferred from electronic annotation from InterPro).
GO:0009307;	Biological process: DNA restriction-modification system (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001525; C5_DNA_meth.
Graphical view of domain structure.

PANTHER

PTHR10629; C5_DNA_meth; 1.

Pfam

PF00145; DNA_methylase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00105; C5METTRFRASE.

TIGRFAMs

TIGR00675; dcm; 1.

PROSITE

PS00094; C5_MTASE_1; 1.
PS00095; C5_MTASE_2; 1.

Other

ProtoNet

P08455.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Methyltransferase; Restriction system; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 330`	`330`	`Modification methylase NgoPII.`	`PRO_0000087900`
`ACT_SITE`	`73 73`		`By similarity.`

Sequence information

Length: 330 AA [This is the length of the unprocessed precursor]

Molecular weight: 37222 Da [This is the MW of the unprocessed precursor]

CRC64: 0A384A98B1EB03E1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIISLFSGC GGLDLGFEKA GFEIPAANEY DKTIWATFKA NHPKTHLIEG DIRKIKEEDF 

        70         80         90        100        110        120 
PEEIDGIIGG PPCQSWSEAG ALRGIDDARG QLFFDYIRIL KSKQPKFFLA ENVSGMLANR 

       130        140        150        160        170        180 
HNGAVQNLLK MFDGCGYDVT LTMANAKDYG VAQERKRVFY IGFRKDLEIK FSFPKGSTVE 

       190        200        210        220        230        240 
DKDKITLKDV IWDLQDTAVP SAPQNKTNPD AVNNNEYFTG SFSPIFMSRN RVKAWDEQGF 

       250        260        270        280        290        300 
TVQASGRQCQ LHPQAPKMEK HGANDYRFAA GKETLYRRMT VREVARIQGF PDNFKFIYQN 

       310        320        330 
VNDAYKMIGN AVPVNLAYEI AAAIKKTLER

P08455 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools