P23192 (MTM2_MORBO) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 75.
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 MboII Short name=M.MboII EC=2.1.1.72 Alternative name(s): Adenine-specific methyltransferase MboII DNA MTase MboIIA | ||
| Gene names |
| ||
| Organism | Moraxella bovis | ||
| Taxonomic identifier | 476 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Moraxella › ![]() |
Protein attributes
| Sequence length | 260 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | This methylase recognizes the double-stranded sequence GAAGA, causes specific methylation on A-5, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme. |
| Catalytic activity | S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. |
| Subunit structure | Homodimer. |
| 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 | 3D-structure |
| 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 – 260 | 260 | Modification methylase MboII | PRO_0000087967 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 4 – 9 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 12 – 18 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 24 – 29 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 39 – 41 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 46 – 63 | 18 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 64 – 74 | 11 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 76 – 88 | 13 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 92 – 99 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 109 – 111 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 125 | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 132 – 134 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 141 – 151 | 11 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 170 – 173 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 199 – 209 | 11 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 215 – 220 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 225 – 232 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 236 – 242 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 244 – 255 | 12 | ||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Cloning and characterization of the MboII restriction-modification system." Bocklage H., Heeger K., Mueller-Hill B. Nucleic Acids Res. 19:1007-1013(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10900 / DSM 6328 / LMG 986 / NCTC 11013. |
| [2] | "Crystal structure of MboIIA methyltransferase." Osipiuk J., Walsh M.A., Joachimiak A. Nucleic Acids Res. 31:5440-5448(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X56977 Genomic DNA. Translation: CAA40297.1. | ||||||||||||
| PIR | S26835. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P23192. | ||||||||||||
| SMR | P23192. Positions 1-256. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| REBASE | 3441. M1.MboII. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002941. DNA_methylase_N4/N6. IPR002052. DNA_methylase_N6_adenine_CS. IPR001091. RM_Methylase. [Graphical view] | ||||||||||||
| Pfam | PF01555. N6_N4_Mtase. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00508. S21N4MTFRASE. | ||||||||||||
| PROSITE | PS00092. N6_MTASE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P23192. | ||||||||||||
Entry information
| Entry name | MTM2_MORBO | ||||||||
| Accession | Primary (citable) accession number: P23192 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
