P0AEE9 (DMA_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: DNA adenine methylase EC=2.1.1.72 Alternative name(s): DNA adenine methyltransferase Deoxyadenosyl-methyltransferase | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 278 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 process | DNA replication |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA replication Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | nucleic acid binding Inferred from electronic annotation. Source: InterPro site-specific DNA-methyltransferase (adenine-specific) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 278 | 278 | DNA adenine methylase | PRO_0000087992 | |||||
Sites | |||||||||
| Binding site | 10 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 14 | 1 | S-adenosyl-L-methionine; via amide nitrogen By similarity | ||||||
| Binding site | 54 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 181 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG58487.1. BA000007 Genomic DNA. Translation: BAB37652.1. |
| PIR | C86003. E91157. |
| RefSeq | NP_289926.1. NC_002655.2. NP_312256.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0AEE9. |
| SMR | P0AEE9. Positions 3-270. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-1230135. |
| STRING | 155864.Z4740. |
Protein family/group databases | |
| REBASE | 5592. M.EcoKO157DamP. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAG58487; AAG58487; Z4740. BAB37652; BAB37652; BAB37652. |
| GeneID | 915915. 958843. |
| KEGG | ece:Z4740. ecs:ECs4229. |
| PATRIC | 18358011. VBIEscCol44059_4172. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0338. |
| HOGENOM | HOG000281348. |
| KO | K06223. |
| OMA | KARRTIS. |
| ProtClustDB | PRK10904. |
Enzyme and pathway databases | |
| BioCyc | ECOL386585:GJFA-4199-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.1020.10. 1 hit. |
| InterPro | IPR023095. Ade_MeTrfase_dom_2. IPR002052. DNA_methylase_N6_adenine_CS. IPR012263. M_m6A_EcoRV. IPR012327. MeTrfase_D12. [Graphical view] |
| Pfam | PF02086. MethyltransfD12. 1 hit. [Graphical view] |
| PIRSF | PIRSF000398. M_m6A_EcoRV. 1 hit. |
| PRINTS | PR00505. D12N6MTFRASE. |
| TIGRFAMs | TIGR00571. dam. 1 hit. |
| PROSITE | PS00092. N6_MTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DMA_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AEE9 Secondary accession number(s): P00475 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Restriction enzymes and methylases Classification of restriction enzymes and methylases and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
