[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=HPG9; PubMed=1662609 [NCBI, ExPASy, EBI, Israel, Japan] Erdmann D., Duesterhoeft A., Kroeger M.; "Cloning and molecular characterization of the HgiCI restriction/modification system from Herpetosiphon giganteus Hpg9 reveals high similarity to BanI."; Eur. J. Biochem. 202:1247-1256(1991).
[2]	SEQUENCE REVISION. Kroeger M.; Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
[3]	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 GGYRCC, causes specific methylation on C-5 on both strands, and protects the DNA from cleavage by the HgiCI 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

X55138; CAA38933.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S19707; S19707.

3D structure databases

HSSP

P05102; 6MHT. [HSSP ENTRY / PDB]

ModBase

P25263.

Protein family/group databases

REBASE

3415; M.HgiCI.

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

P25263.

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`	`1 420`	`420`	`Modification methylase HgiCI.`	`PRO_0000087886`
`ACT_SITE`	`75 75`		`By similarity.`

Sequence information

Length: 420 AA [This is the length of the unprocessed precursor]

Molecular weight: 47641 Da [This is the MW of the unprocessed precursor]

CRC64: EDB427C9D66CD971 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKFIDLFAG IGGMRLGFEQ AMHELGIETA CVLSSEIDKH AQTTYAMNFH EQSQGDITQI 

        70         80         90        100        110        120 
QDFPSFDFLL AGFPCQPFSY AGKQKGFGDT RGTLFFEIER ILKAYRPKGF LLENVRGLTT 

       130        140        150        160        170        180 
HDKGRTFKTI LQKLHELNYG VYLILNSSNF QVPQNRLRVY IVGLDQSQPE LTITSHIGAT 

       190        200        210        220        230        240 
DSHKFKQLSN QASLFDTNKI MLVRDILEDH PLDKYNCSTD FVNKLLAFIG HPIKLNGKRL 

       250        260        270        280        290        300 
IDYRNGNSIH SWELGIKGEC TSDEIQFMNA LIANRRKKHF GAHQDGKKLT IEQIKTFFEH 

       310        320        330        340        350        360 
DDLDSIMQSL ITKGYLQEVN GRFNPVAGNM SFEVFKFLDP DSVSITLVSS DAHKIGVVHQ 

       370        380        390        400        410        420 
NRIRRITPRE CARLQGFPDS FQFHPKDSLA YRQFGNSVSV PVVKAVILDL FKSADLASCF

P25263 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