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P20589 (MTH3_HAEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 HaeIII

Short name=M.HaeIII
EC=2.1.1.37
Alternative name(s):
Cytosine-specific methyltransferase HaeIII
Gene names
Name:haeIIIM
OrganismHaemophilus aegyptius
Taxonomic identifier197575 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the HaeIII 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Modification methylase HaeIII
PRO_0000087878

Regions

Domain1 – 327327SAM-dependent MTase C5-type

Sites

Active site711 Ref.3

Secondary structure

.................................................................. 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20589 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 928C6D5390DBED25

FASTA33037,686
        10         20         30         40         50         60 
MNLISLFSGA GGLDLGFQKA GFRIICANEY DKSIWKTYES NHSAKLIKGD ISKISSDEFP 

        70         80         90        100        110        120 
KCDGIIGGPP CQSWSEGGSL RGIDDPRGKL FYEYIRILKQ KKPIFFLAEN VKGMMAQRHN 

       130        140        150        160        170        180 
KAVQEFIQEF DNAGYDVHII LLNANDYGVA QDRKRVFYIG FRKELNINYL PPIPHLIKPT 

       190        200        210        220        230        240 
FKDVIWDLKD NPIPALDKNK TNGNKCIYPN HEYFIGSYST IFMSRNRVRQ WNEPAFTVQA 

       250        260        270        280        290        300 
SGRQCQLHPQ APVMLKVSKN LNKFVEGKEH LYRRLTVREC ARVQGFPDDF IFHYESLNDG 

       310        320        330 
YKMIGNAVPV NLAYEIAKTI KSALEICKGN 

« Hide

References

[1]"Cloning and analysis of the HaeIII and HaeII methyltransferase genes."
Slatko B.E., Croft R., Moran L.S., Wilson G.G.
Gene 74:45-50(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11116 / CCUG 25716 / NCTC 8502.
[2]Zhang B.-H., Wilson G.G.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11116 / CCUG 25716 / NCTC 8502.
[3]"Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase."
Chen L., McMillan A.M., Chang W., Ezak-Nipkay K., Lane W.S., Verdine G.L.
Biochemistry 30:11018-11025(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 62-81.
[4]"The crystal structure of HaeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing."
Reinisch K.M., Chen L., Verdine G.L., Lipscomb W.N.
Cell 82:143-153(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24625 Genomic DNA. Translation: AAA24970.1.
AF051375 Genomic DNA. Translation: AAC05696.1.
PIRJS0102.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCTX-ray2.80A/B1-324[»]
3UBTX-ray2.50A/B/Y1-330[»]
ProteinModelPortalP20589.
SMRP20589. Positions 1-324.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3410. M.HaeIII.

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. 1 hit.
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...

Other

EvolutionaryTraceP20589.

Entry information

Entry nameMTH3_HAEAE
AccessionPrimary (citable) accession number: P20589
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 86 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references