P00473 (MTH2_HAEPH) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 79.
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 HhaII Short name=M.HhaII EC=2.1.1.72 Alternative name(s): Adenine-specific methyltransferase HhaII | ||
| Gene names |
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| Organism | Haemophilus parahaemolyticus | ||
| Taxonomic identifier | 735 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus![]() |
Protein attributes
| Sequence length | 228 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This methylase recognizes the double-stranded sequence GANTC, causes specific methylation on A-2 on both strands, and protects the DNA from cleavage by the HhaII endonuclease. |
| 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. |
| Caution | Strain ATCC 10014 was originally thought to originate from H.haemolyticus. |
| Sequence caution | The sequence K00508 differs from that shown. Reason: |
Ontologies
| Keywords | |
|---|---|
| Biological process | Restriction system |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| 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 – 228 | 228 | Modification methylase HhaII | PRO_0000087972 | |||
Sequences
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References
| [1] | "Overproduction and purification of the M.HhaII methyltransferase from Haemophilus haemolyticus." Chandrasegaran S., Wu L.P., Valda E., Smith H.O. Gene 74:15-21(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10014 / CCUG 3716 / NCTC 8479. |
| [2] | "The nucleotide sequence of the HhaII restriction and modification genes from Haemophilus haemolyticus." Schoner B., Kelly S., Smith H.O. Gene 24:227-236(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10014 / CCUG 3716 / NCTC 8479. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M24624 Genomic DNA. Translation: AAA24963.1. K00508 Genomic DNA. No translation available. |
| PIR | XYHIH2. JS0103. |
3D structure databases | |
| ProteinModelPortal | P00473. |
| ModBase | Search... |
Protein family/group databases | |
| REBASE | 3422. M.HhaII. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002295. D21N6_MeTrfase. IPR002941. DNA_methylase_N4/N6. [Graphical view] |
| Pfam | PF01555. N6_N4_Mtase. 1 hit. [Graphical view] |
| PRINTS | PR00506. D21N6MTFRASE. |
| PROSITE | PS00092. N6_MTASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MTH2_HAEPH | ||||||||
| Accession | Primary (citable) accession number: P00473 | ||||||||
| 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
