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P0AEE8 (DMA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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):
DNA adenine methyltransferase
Deoxyadenosyl-methyltransferase
M.EcoDam
Gene names
Name:dam
Ordered Locus Names:b3387, JW3350
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Methylates DNA within the sequence GATC and protects the DNA from cleavage by the restriction endonuclease MboI. Although it shares sequence specificity with a number of type II restriction endonucleases and methylases, it is thought to act in postreplication mismatch repair rather than as a part of a restriction modification system. May also play a role in DNA replication.

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 – 278278DNA adenine methylase
PRO_0000087991

Sites

Binding site101S-adenosyl-L-methionine By similarity
Binding site141S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site541S-adenosyl-L-methionine By similarity
Binding site1811S-adenosyl-L-methionine By similarity

Secondary structure

........................................... 278
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEE8 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: B2FA5D1FDC863CB9

FASTA27832,100
        10         20         30         40         50         60 
MKKNRAFLKW AGGKYPLLDD IKRHLPKGEC LVEPFVGAGS VFLNTDFSRY ILADINSDLI 

        70         80         90        100        110        120 
SLYNIVKMRT DEYVQAAREL FVPETNCAEV YYQFREEFNK SQDPFRRAVL FLYLNRYGYN 

       130        140        150        160        170        180 
GLCRYNLRGE FNVPFGRYKK PYFPEAELYH FAEKAQNAFF YCESYADSMA RADDASVVYC 

       190        200        210        220        230        240 
DPPYAPLSAT ANFTAYHTNS FTLEQQAHLA EIAEGLVERH IPVLISNHDT MLTREWYQRA 

       250        260        270 
KLHVVKVRRS ISSNGGTRKK VDELLALYKP GVVSPAKK 

« Hide

References

« Hide 'large scale' references
[1]"The isolation and characterization of the Escherichia coli DNA adenine methylase (dam) gene."
Brooks J.E., Blumenthal R.M., Gingeras T.R.
Nucleic Acids Res. 11:837-851(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of three genes in the dam-containing operon of Escherichia coli."
Lyngstadaas A., Lobner-Olesen A., Boye E.
Mol. Gen. Genet. 247:546-554(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The Escherichia coli dam gene is expressed as a distal gene of a new operon."
Jonczyk P., Hines R., Smith D.W.
Mol. Gen. Genet. 217:85-96(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
Strain: K12.
[6]"The role of the preserved sequences of Dam methylase."
Guyot J.-B., Grassi J., Hahn U., Guschlbauer W.
Nucleic Acids Res. 21:3183-3190(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01600 Genomic DNA. Translation: AAA23664.1.
V00272 Genomic DNA. Translation: CAA23530.1.
Z19601 Genomic DNA. Translation: CAA79668.1.
U18997 Genomic DNA. Translation: AAA58184.1.
U00096 Genomic DNA. Translation: AAC76412.1.
AP009048 Genomic DNA. Translation: BAE77904.1.
X15162 Genomic DNA. Translation: CAA33254.1.
PIRXYECDA. A00555.
RefSeqNP_417846.1. NC_000913.3.
YP_492045.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G1PX-ray1.89A/B1-278[»]
2OREX-ray2.99D/E/F1-278[»]
4GBEX-ray2.66D/E/F1-278[»]
4GOLX-ray2.57D/E/F1-278[»]
4GOMX-ray2.45D/E/F1-278[»]
4GONX-ray2.72D/E/F1-278[»]
4GOOX-ray2.70D/E/F1-278[»]
ProteinModelPortalP0AEE8.
SMRP0AEE8. Positions 3-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47948N.
IntActP0AEE8. 24 interactions.
MINTMINT-1230150.
STRING511145.b3387.

Chemistry

ChEMBLCHEMBL1075075.

Protein family/group databases

REBASE2396. M.EcoKDam.

Proteomic databases

PaxDbP0AEE8.
PRIDEP0AEE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76412; AAC76412; b3387.
BAE77904; BAE77904; BAE77904.
GeneID12932866.
947893.
KEGGecj:Y75_p3789.
eco:b3387.
PATRIC32122206. VBIEscCol129921_3480.

Organism-specific databases

EchoBASEEB0200.
EcoGeneEG10204. dam.

Phylogenomic databases

eggNOGCOG0338.
HOGENOMHOG000281348.
KOK06223.
OMAKFTREIY.
OrthoDBEOG6CS08V.
PhylomeDBP0AEE8.

Enzyme and pathway databases

BioCycEcoCyc:EG10204-MONOMER.
ECOL316407:JW3350-MONOMER.

Gene expression databases

GenevestigatorP0AEE8.

Family and domain databases

Gene3D1.10.1020.10. 1 hit.
3.40.50.150. 2 hits.
InterProIPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF02086. MethyltransfD12. 1 hit.
[Graphical view]
PIRSFPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSPR00505. D12N6MTFRASE.
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00571. dam. 1 hit.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AEE8.
PROP0AEE8.

Entry information

Entry nameDMA_ECOLI
AccessionPrimary (citable) accession number: P0AEE8
Secondary accession number(s): P00475, Q2M752
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 81 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene