NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NCTC 3438;
PubMed=1856224 [NCBI, ExPASy, EBI, Israel, Japan]
Sugisaki H., Yamamoto K., Takanami M.;
"The HgaI restriction-modification system contains two cytosine methylase genes responsible for modification of different DNA strands.";
J. Biol. Chem. 266:13952-13957(1991).

Comments

FUNCTION: This methylase recognizes the strands carrying the 5'-GACGC-3' sequence, causes specific methylation on C-3, and protects the DNA from cleavage by the HgaI endonuclease.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
MISCELLANEOUS: The HgaI modification system consists of two cytosine methylase genes responsible for modification of different strands in the target DNA.
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

D17388; BAA04207.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D90363; BAA14378.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39467; A39467.

3D structure databases

ModBase

P25283.

Protein family/group databases

REBASE

3651; M2.HgaI.

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.

PROSITE

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

ProtoNet

P25283.

Other

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`	`1 358`	`358`	`Modification methylase HgaIB.`	`PRO_0000087880`
`ACT_SITE`	`81 81`		`By similarity.`

Sequence information

Length: 358 AA [This is the length of the unprocessed precursor]

Molecular weight: 40690 Da [This is the MW of the unprocessed precursor]

CRC64: 0373563207685A91 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKINAMSLFS SAGIGELDLH KGNLNFVVAN ELLKKRADTY QFFYPETKMF QGDISDEKLK 

        70         80         90        100        110        120 
REILLSAQQN NVKFLLATPP CQGLSSVGKN KHQDHFIKDN RNFLIFEVFE FIDVLNLDFI 

       130        140        150        160        170        180 
LIENVPRFIE MYFPYNGQLL LLEEILKIKY ASKYQIDIVI LNAKDYGICQ SRPRAIIKMY 

       190        200        210        220        230        240 
KYGITWKLPT IQAEISLQRA IGHLPPLEPG EVSSIKWHSA PNVKPSIIEA IRHTKPGTSA 

       250        260        270        280        290        300 
ISNPIFYPKK DNGERIKGFH NTYKRMEWDK PAPARTTYSG SISSHNNIHP GRLQLDGTYS 

       310        320        330        340        350 
DPRVLSLLET FIVSSIDENI EFPPGSSETY IRTIIGEAIP PKLLSAICFP DGENINVK

P25283 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