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P04392 (DMA_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 97. 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:
DNA adenine methylase

EC=2.1.1.72
Alternative name(s):
Deoxyadenosyl-methyltransferase
M.EcoT4Dam
Gene names
Name:DAM
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Sequence similarities

Belongs to the N(4)/N(6)-methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259DNA adenine methylase
PRO_0000087990

Sites

Binding site71S-adenosyl-L-methionine
Binding site111S-adenosyl-L-methionine; via amide nitrogen
Binding site501S-adenosyl-L-methionine
Binding site1711S-adenosyl-L-methionine

Experimental info

Mutagenesis1261P → S in damh; hypermethylating mutant.
Sequence conflict139 – 1402QY → RF Ref.2
Sequence conflict2091Q → L Ref.2

Secondary structure

............................................. 259
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04392 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: A49401D059A4388D

FASTA25930,417
        10         20         30         40         50         60 
MLGAIAYTGN KQSLLPELKS HFPKYNRFVD LFCGGLSVSL NVNGPVLAND IQEPIIEMYK 

        70         80         90        100        110        120 
RLINVSWDDV LKVIKQYKLS KTSKEEFLKL REDYNKTRDP LLLYVLHFHG FSNMIRINDK 

       130        140        150        160        170        180 
GNFTTPFGKR TINKNSEKQY NHFKQNCDKI IFSSLHFKDV KILDGDFVYV DPPYLITVAD 

       190        200        210        220        230        240 
YNKFWSEDEE KDLLNLLDSL NDRGIKFGQS NVLEHHGKEN TLLKEWSKKY NVKHLNKKYV 

       250 
FNIYHSKEKN GTDEVYIFN 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of a new bacteriophage T4 gene, 69, that spans an origin of DNA replication."
McDonald P.M., Mosig G.
EMBO J. 3:2863-2871(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Single amino acid changes that alter the DNA sequence specificity of the DNA-[N6-adenine] methyltransferase (Dam) of bacteriophage T4."
Miner Z., Schlagman S.L., Hattman S.
Nucleic Acids Res. 17:8149-8157(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT DAMH.
[3]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Structure of the bacteriophage T4 DNA adenine methyltransferase."
Yang Z., Horton J.R., Zhou L., Zhang X.J., Dong A., Zhang X., Schlagman S.L., Kossykh V., Hattman S., Cheng X.
Nat. Struct. Biol. 10:849-855(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01416 Genomic DNA. Translation: CAA25660.1.
K03113 Genomic DNA. Translation: AAA32555.1.
X17641 Genomic DNA. No translation available.
AF158101 Genomic DNA. Translation: AAD42553.1.
PIRXYBPT4. A00554.
RefSeqNP_049647.1. NC_000866.4.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q0SX-ray2.30A1-259[»]
1Q0TX-ray3.10A/B1-259[»]
1YF3X-ray2.29A/B1-259[»]
1YFJX-ray2.69A/B/C/D/E/F1-259[»]
1YFLX-ray3.09A/B/D/E1-259[»]
ProteinModelPortalP04392.
SMRP04392. Positions 1-259.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE2837. M.EcoT4Dam.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258548.

Phylogenomic databases

ProtClustDBCLSP2343847.

Enzyme and pathway databases

BRENDA2.1.1.72. 732.

Family and domain databases

Gene3D1.10.1020.10. 1 hit.
InterProIPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
[Graphical view]
PfamPF02086. MethyltransfD12. 1 hit.
[Graphical view]
PIRSFPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSPR00505. D12N6MTFRASE.
TIGRFAMsTIGR00571. dam. 1 hit.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04392.

Entry information

Entry nameDMA_BPT4
AccessionPrimary (citable) accession number: P04392
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: October 16, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral 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