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P25263 (MTC1_HERAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modification methylase HgiCI

Short name=M.HgiCI
EC=2.1.1.37
Alternative name(s):
Cytosine-specific methyltransferase HgiCI
Gene names
Name:hgiCIM
OrganismHerpetosiphon aurantiacus (Herpetosiphon giganteus)
Taxonomic identifier65 [NCBI]
Taxonomic lineageBacteriaChloroflexiHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceInferred 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 class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 SAM-dependent MTase C5-type domain.

Ontologies

Keywords
   Biological processRestriction system
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Modification methylase HgiCI
PRO_0000087886

Regions

Domain2 – 417416SAM-dependent MTase C5-type

Sites

Active site751 By similarity

Sequences

Sequence LengthMass (Da)Tools
P25263 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: EDB427C9D66CD971

FASTA42047,641
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55138 Genomic DNA. Translation: CAA38933.1.
PIRS19707.

3D structure databases

ProteinModelPortalP25263.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3415. M.HgiCI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
SUPFAMSSF53335. SSF53335. 2 hits.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTC1_HERAU
AccessionPrimary (citable) accession number: P25263
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries