P25240 (MT57_ECOLX) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 65.
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: Modification methylase Eco57IB Short name=M.Eco57IB EC=2.1.1.72 Alternative name(s): Adenine-specific methyltransferase Eco57IB | ||||
| Gene names |
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| Organism | Escherichia coli | ||||
| Taxonomic identifier | 562 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia![]() |
Protein attributes
| Sequence length | 544 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | This methylase recognizes the double-stranded sequence 5'-CTGAAG-3' in one strand and 5'-CTTCAG-3' in the other, causes specific methylation on A-5 on one strand, and protects the DNA from cleavage by the Eco57I endonuclease. |
| Catalytic activity | S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. |
| Subunit structure | Monomer. |
| 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 | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | DNA methylation on adenine Inferred from electronic annotation. Source: GOC 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 – 544 | 544 | Modification methylase Eco57IB | PRO_0000087940 | |||
Sequences
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References
| [1] | "Cloning and sequence analysis of the genes coding for Eco57I type IV restriction-modification enzymes." Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S., Butkus V. Nucleic Acids Res. 20:6051-6056(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: RFL57. |
| [2] | "Purification and properties of the Eco57I restriction endonuclease and methylase -- prototypes of a new class (type IV)." Janulaitis A., Petrusyte M., Maneliene Z., Klimasauskas S., Butkus V. Nucleic Acids Res. 20:6043-6049(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M74821 Genomic DNA. Translation: AAA23388.1. X61122 Genomic DNA. Translation: CAA43433.1. |
| PIR | S26425. |
3D structure databases | |
| ProteinModelPortal | P25240. |
| ModBase | Search... |
Protein family/group databases | |
| REBASE | 5234. M.Eco57I. |
Proteomic databases | |
| PRIDE | P25240. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR003356. DNA_methylase_A-5. IPR002052. DNA_methylase_N6_adenine_CS. IPR002296. N12N6_MeTrfase. [Graphical view] |
| Pfam | PF02384. N6_Mtase. 1 hit. [Graphical view] |
| PRINTS | PR00507. N12N6MTFRASE. |
| PROSITE | PS00092. N6_MTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MT57_ECOLX | ||||||||
| Accession | Primary (citable) accession number: P25240 | ||||||||
| 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
