Reviewed,
UniProtKB/Swiss-Prot P10484 (T1M1_ECOLX)
Last modified
September 22, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Type I restriction enzyme EcoR124II M protein Short name=M.EcoR124II EC=2.1.1.72 | ||||
| Gene names |
| ||||
| Encoded on | Plasmid IncFIV R124/3 | ||||
| Organism | Escherichia coli | ||||
| Taxonomic identifier | 562 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 520 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Methylation of specific adenine residues; required for both restriction and modification activities By similarity. The EcoR124/3 I enzyme recognizes 5'-GAAN7RTCG-3'. |
| Catalytic activity | S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. |
| Subunit structure | The type I restriction/modification system is composed of three polypeptides R, M and S. |
| Miscellaneous | Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases. |
| Sequence similarities | Belongs to the N(4)/N(6)-methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Restriction system |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Plasmid |
| Gene Ontology (GO) | |
| Biological process | DNA methylation Inferred from electronic annotation. Source: InterPro DNA restriction-modification systemInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | DNA binding Inferred from electronic annotation. Source: InterPro N-methyltransferase activityInferred 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 – 520 | 520 | Type I restriction enzyme EcoR124II M protein | PRO_0000088023 | |||||
Regions | |||||||||
| Region | 198 – 203 | 6 | S-adenosyl-L-methionine binding By similarity | ||||||
| Region | 230 – 232 | 3 | S-adenosyl-L-methionine binding By similarity | ||||||
Sites | |||||||||
| Binding site | 254 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Sequences
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References
| [1] | "Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes." Price C., Lingner J., Bickle J., Firman T.A., Glover S.W. J. Mol. Biol. 205:115-125(1989) [PubMed: 2784505] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| X13145 Genomic DNA. Translation: CAA31541.1. | |
| PIR | S02166. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:17004N. |
Protein family/group databases | |
| REBASE | 3391. M.EcoR124II. 3392. M.EcoR124I. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.72. 246. |
Family and domain databases | |
| InterPro | IPR003356. DNA_methylase_A-5. IPR002052. DNA_methylase_N6_adenine_CS. IPR002296. N12N6_MeTrfase. IPR004546. Restrict_endonuc_I_EcoRI_M. [Graphical view] |
| Pfam | PF02384. N6_Mtase. 1 hit. [Graphical view] |
| PRINTS | PR00507. N12N6MTFRASE. |
| TIGRFAMs | TIGR00497. hsdM. 1 hit. |
| PROSITE | PS00092. N6_MTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | T1M1_ECOLX | ||||||||
| Accession | Primary (citable) accession number: P10484 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
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


