NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 33694 / HB101;
DOI=10.1093/nar/15.1.313; PubMed=3029675 [NCBI, ExPASy, EBI, Israel, Japan]
Som S., Bhagwat A.S., Friedman S.;
"Nucleotide sequence and expression of the gene encoding the EcoRII modification enzyme.";
Nucleic Acids Res. 15:313-332(1987).

Comments

FUNCTION: This methylase recognizes the double-stranded sequence CCWGG, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the EcoRII endonuclease.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
SUBUNIT: Monomer.
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

X05050; CAA28725.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25871; XYECR2.

RefSeq

YP_724464.1; -.

3D structure databases

HSSP

P05102; 6MHT. [HSSP ENTRY / PDB]

ModBase

P05101.

Protein family/group databases

REBASE

3396; M.EcoRII.

Ontologies

GO:0003886;	Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from electronic annotation from EC).
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.

Genome annotation databases

GeneID

4246757; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 477`	`477`	`Modification methylase EcoRII.`	`PRO_0000087874`
`ACT_SITE`	`186 186`		`By similarity.`

Sequence information

Length: 477 AA [This is the length of the unprocessed precursor]

Molecular weight: 54556 Da [This is the MW of the unprocessed precursor]

CRC64: 9E595D3809BCCAEA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEFELLAQD LLEKAEAEEQ LRQENDKKLL GQVLEIYDQK YVAELLRKVG KNEWSRETLN 

        70         80         90        100        110        120 
RWINGKCSPK TLTLAEEELL RKMLPEAPAH HPDYAFRFID LFAGIGGIRK GFETIGGQCV 

       130        140        150        160        170        180 
FTSEWNKEAV RTYKANWFND AQEHTFNLDI REVTLSDKPE VPENDAYAYI NEHVPDHDVL 

       190        200        210        220        230        240 
LAGFPCQPFS LAGVSKKNSL GRAHGFECEA QGTLFFDVAR IIRAKKPAIF VLENVKNLKS 

       250        260        270        280        290        300 
HDKGKTFKVI MDTLDELGYE VADAAEMGKN DPKVIDGKHF LPQHRERIVL VGFRRDLNIH 

       310        320        330        340        350        360 
QGFTLRDISR FYPEQRPSFG ELLEPVVDSK YILTPKLWEY LYNYAKKHAA KGNGFGFGLV 

       370        380        390        400        410        420 
NPENKESIAR TLSARYHKDG SEILIDRGWD MATGETDFAN EENQAHRPRR LTPRECARLM 

       430        440        450        460        470 
GFEKVDGRPF RIPVSDTQSY RQFGNSVVVP VFEAVAKLLE PYILKAVNAD SCKVERI

P05101 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