Reviewed,
UniProtKB/Swiss-Prot P08455 (MTP2_NEIGO)
Last modified
March 3, 2009.
Version 69.
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 NgoPII Short name=M.NgoPII EC=2.1.1.37 Alternative name(s): Cytosine-specific methyltransferase NgoPII | ||||
| Gene names |
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| Organism | Neisseria gonorrhoeae | ||||
| Taxonomic identifier | 485 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 330 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the NgoPII endonuclease. |
| Catalytic activity | S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine. |
| Sequence similarities | Belongs to the C5-methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Restriction system |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| 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 (cytosine-5-)-methyltransferase activity Inferred from electronic annotation. Source: EC DNA bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Sequence analysis of the NgoPII methyltransferase gene from Neisseria gonorrhoeae P9: homologies with other enzymes recognizing the sequence 5'-GGCC-3'." Sullivan K.M., Saunders J.R. Nucleic Acids Res. 16:4369-4387(1988) [PubMed: 2837733] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: P9. |
| [2] | "Nucleotide sequence and genetic organization of the NgoPII restriction-modification system of Neisseria gonorrhoeae." Sullivan K.M., Saunders J.R. Mol. Gen. Genet. 216:380-387(1989) [PubMed: 2501649] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: P9. |
| [3] | "Natural variation of the NgoII restriction-modification system of Neisseria gonorrhoeae." Gunn J.S., Stein D.C. Gene 132:15-20(1993) [PubMed: 8406039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33084 / F62 / M-1914. |
Cross-references
Sequence databases | |
|---|---|
| X06965 Genomic DNA. Translation: CAA30038.1. Different initiation. X52661 Genomic DNA. Translation: CAA36888.1. Different initiation. L14564 Unassigned DNA. Translation: AAA17019.1. Different initiation. | |
| PIR | CTNHP2. S00920. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DCT based on UniProtKB P20589. |
| ModBase | Search... |
Protein family/group databases | |
| REBASE | 3464. M.NgoPII. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.37. 588. |
Family and domain databases | |
| InterPro | IPR001525. C5_DNA_meth. IPR018117. C5_DNA_meth_AS. [Graphical view] |
| PANTHER | PTHR10629. C5_DNA_meth. 1 hit. |
| Pfam | PF00145. DNA_methylase. 1 hit. [Graphical view] |
| PRINTS | PR00105. C5METTRFRASE. |
| TIGRFAMs | TIGR00675. dcm. 1 hit. |
| PROSITE | PS00094. C5_MTASE_1. 1 hit. PS00095. C5_MTASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MTP2_NEIGO | ||||||||
| Accession | Primary (citable) accession number: P08455 | ||||||||
| 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


