Reviewed, UniProtKB/Swiss-Prot P25263 (MTC1_HERAU)

Names and origin

Protein names

Recommended name:
    Modification methylase HgiCI
      Short name=M.HgiCI
    EC=2.1.1.37
Alternative name(s):
    Cytosine-specific methyltransferase HgiCI

Gene names

Name:

hgiCIM

Organism

Herpetosiphon aurantiacus (Herpetosiphon giganteus)

Taxonomic identifier

65 [NCBI]

Taxonomic lineage

Bacteria › Chloroflexi › Herpetosiphonales › Herpetosiphonaceae › Herpetosiphon

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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.
Sequence similarities	Belongs to the C5-methyltransferase family.

Ontologies

Keywords
Biological process	Restriction system
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Biological process	DNA methylation Inferred from electronic annotation. Source: InterPro DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA (cytosine-5-)-methyltransferase activity Inferred from electronic annotation. Source: EC DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	Modification methylase HgiCI		PRO_0000087886
Sites
	Active site	75	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25263-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: EDB427C9D66CD971	FASTA	420	47,641
	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

References

[1]	"Cloning and molecular characterization of the HgiCI restriction/modification system from Herpetosiphon giganteus Hpg9 reveals high similarity to BanI." Erdmann D., Duesterhoeft A., Kroeger M. Eur. J. Biochem. 202:1247-1256(1991) [PubMed: 1662609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: HPG9.
[2]	Kroeger M. Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Organization and gene expression within restriction-modification systems of Herpetosiphon giganteus." Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S., Meyer-Rogge S., Moestl D. Gene 157:43-47(1995) [PubMed: 7607523] [Abstract] Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X55138 Genomic DNA. Translation: CAA38933.1.
PIR	S19707.
3D structure databases
HSSP	HSSP built from PDB template 6MHT based on UniProtKB P05102.
ModBase	Search...
Protein family/group databases
REBASE	3415. M.HgiCI.
Enzyme and pathway databases
BRENDA	2.1.1.37. 291850.
Family and domain databases
InterPro	IPR001525. C5_DNA_meth. IPR018117. C5_DNA_meth_AS. [Graphical view]
PANTHER	PTHR10629. C5_DNA_meth. 1 hit.
Pfam	PF00145. DNA_methylase. 1 hit. [Graphical view]
PRINTS	PR00105. C5METTRFRASE.
TIGRFAMs	TIGR00675. dcm. 1 hit.
PROSITE	PS00094. C5_MTASE_1. 1 hit. PS00095. C5_MTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MTC1_HERAU

Accession

Primary (citable) accession number: P25263

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	November 1, 1995
Last modified:	May 5, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)