Reviewed,
UniProtKB/Swiss-Prot P25240 (MT57_ECOLX)
Last modified
January 19, 2010.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 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 – 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: 1334261] [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: 1334260] [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 | |
| SMR | P25240. Positions 16-259. |
| ModBase | Search... |
Protein family/group databases | |
| REBASE | 5234. M.Eco57I. |
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. [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 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


