[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=HPG9; DOI=10.1016/0378-1119(92)90484-7; PubMed=1644308 [NCBI, ExPASy, EBI, Israel, Japan] Erdmann D., Horst G., Duesterhoeft A., Kroeger M.; "Stepwise cloning and genetic organization of the seemingly unclonable HgiCII restriction-modification system from Herpetosiphon giganteus strain Hpg9, using PCR technique."; Gene 117:15-22(1992).
[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 GGWCC, causes specific methylation on C-? on both strands and protects the DNA from cleavage by the HgiCII 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

X55139; CAA38935.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC1165; JC1165.

3D structure databases

HSSP

P05102; 1FJX. [HSSP ENTRY / PDB]

ModBase

P25264.

Protein family/group databases

REBASE

3416; M.HgiCII.

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.

ProtoNet

P25264.

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`	`1 437`	`437`	`Modification methylase HgiCII.`	`PRO_0000087887`
`ACT_SITE`	`75 75`		`By similarity.`

Sequence information

Length: 437 AA [This is the length of the unprocessed precursor]

Molecular weight: 49622 Da [This is the MW of the unprocessed precursor]

CRC64: 721217050B382081 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKQFRFIDLF AGIGGFRLGL EAVGGICVGS AEIDQQAIKV YRQNWPTDRS EHNLGDITTL 

        70         80         90        100        110        120 
QQLPAHDLVV GGVPCQPWSI AGKNQAFDDP RGQLWADVIR LVRINQPKAF IFENVKGLID 

       130        140        150        160        170        180 
PRNRLCLESI LDSFKAEGYN VYYKLLNSFD YGVAQNRDRV FIIGIQQKLG VPDFSFPEYS 

       190        200        210        220        230        240 
ESEQRLYDIL DNLQTPSIIP ESLPIQRNLF GERIEVGFNK LTPRGAFNDF FILNDIRNGP 

       250        260        270        280        290        300 
TSIHSWEIYA TTEREKQICT TIMRNRGNPR YGDCDGNPMS YQDIADLVVD LAESELQVLI 

       310        320        330        340        350        360 
QKRILRQYED GKYEFFNRRL SGGIDGTYRI FLPHARFFGR LTARGMHDEI AEISVSGATA 

       370        380        390        400        410        420 
EAYKQNFIQQ ILIPKRHRPI TVNEAARIQG FPATFKFHSN QSANFRLIGN SVAPPVIMAL 

       430 
GKALPNDHLF EPELCEV

P25264 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