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P0AEE9 (DMA_ECO57) 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:
DNA adenine methylase

EC=2.1.1.72
Alternative name(s):
DNA adenine methyltransferase
Deoxyadenosyl-methyltransferase
Gene names
Name:dam
Ordered Locus Names:Z4740, ECs4229
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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.

Ontologies

Keywords
   Biological processDNA replication
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

site-specific DNA-methyltransferase (adenine-specific) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278DNA adenine methylase
PRO_0000087992

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

Sequences

Sequence LengthMass (Da)Tools
P0AEE9 [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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58487.1.
BA000007 Genomic DNA. Translation: BAB37652.1.
PIRC86003.
E91157.
RefSeqNP_289926.1. NC_002655.2.
NP_312256.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0AEE9.
SMRP0AEE9. Positions 3-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1230135.
STRING155864.Z4740.

Protein family/group databases

REBASE5592. M.EcoKO157DamP.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58487; AAG58487; Z4740.
BAB37652; BAB37652; BAB37652.
GeneID915915.
958843.
KEGGece:Z4740.
ecs:ECs4229.
PATRIC18358011. VBIEscCol44059_4172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0338.
HOGENOMHOG000281348.
KOK06223.
OMAKFTREIY.
OrthoDBEOG6CS08V.

Enzyme and pathway databases

BioCycECOL386585:GJFA-4199-MONOMER.
ECOO157:DAM-MONOMER.

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...

Entry information

Entry nameDMA_ECO57
AccessionPrimary (citable) accession number: P0AEE9
Secondary accession number(s): P00475
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 66 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