[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=HPA1; Duesterhoeft A., Kroeger M.; Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
[2]	DISCUSSION OF SEQUENCE. DOI=10.1016/0378-1119(94)00779-R; PubMed=7607523 [NCBI, ExPASy, EBI, Israel, Japan] Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S., Meyer-Rogge S., Moestl D.; "Organization and gene expression within restriction-modification systems of Herpetosiphon giganteus."; Gene 157:43-47(1995).

Comments

FUNCTION: This methylase recognizes the double-stranded sequence GRCGYC, causes specific methylation on C-? on both strands, and protects the DNA from cleavage by the HgiEI 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

X55143; CAA38947.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S21955; S21955.

3D structure databases

HSSP

P20589; 1DCT. [HSSP ENTRY / PDB]

ModBase

P25267.

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.

PROSITE

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

ProtoNet

P25267.

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 >126`	`>126`	`Modification methylase HgiGI.`	`PRO_0000087891`
`ACT_SITE`	`75 75`		`By similarity.`
`NON_TER`	`126 126`

Sequence information

Length: 126 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 13871 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: FF3695B03BC02399 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTIDLFAGC GGMSLGFMQA GFEIVAAVDN WRPAITTYQQ NFIHPIHELD LAEVDEAISL 

        70         80         90        100        110        120 
IKTYSPELII GGPPCQDFSS AGKRDEGLGR ANLTLDFVKI VLAIQPAWVI MENVERARLS 


KIHQQA

P25267 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