Reviewed,
UniProtKB/Swiss-Prot P14230 (MTSM_SERMA)
Last modified
June 16, 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 SmaI Short name=M.SmaI EC=2.1.1.113 Alternative name(s): N-4 cytosine-specific methyltransferase SmaI | ||
| Gene names |
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| Organism | Serratia marcescens | ||
| Taxonomic identifier | 615 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia |
Protein attributes
| Sequence length | 292 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 CCCGGG, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the SmaI endonuclease. |
| Catalytic activity | S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N(4)-methylcytosine. |
| Sequence similarities | Belongs to the N(4)/N(6)-methyltransferase family. N(4) subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Restriction system |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Gene Ontology (GO) | |
| Biological process | DNA methylation on cytosine 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 (cytosine-N4-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 – 292 | 292 | Modification methylase SmaI | PRO_0000087932 | |||
Sequences
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References
| [1] | "Cloning, characterization and heterologous expression of the SmaI restriction-modification system." Heidmann S., Seifert W., Kessler C., Domdey H. Nucleic Acids Res. 17:9783-9796(1989) [PubMed: 2690008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BMTU 1373. |
| [2] | "M.Smal is an N4-methylcytosine specific DNA-methylase." Klimasauskas S., Steponaviciene D., Maneliene Z., Petrusyte M., Butkus V., Janulaitis A. Nucleic Acids Res. 18:6607-6609(1990) [PubMed: 2251121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Characterization of the SmaI restriction and modification enzymes." Dunbar J.C., Withers B. Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| X16458 Genomic DNA. Translation: CAA34479.1. M98769 Genomic DNA. Translation: AAA26570.1. | |
| PIR | S06036. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1G60 based on UniProtKB P23192. |
| ModBase | Search... |
Protein family/group databases | |
| REBASE | 3505. M.SmaI. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.113. 457. |
Family and domain databases | |
| InterPro | IPR002941. DNA_methylase_N4/N6. IPR001091. MeTrfase_CN4. IPR017985. MeTrfase_CN4_CS. [Graphical view] |
| Pfam | PF01555. N6_N4_Mtase. 1 hit. [Graphical view] |
| PRINTS | PR00508. S21N4MTFRASE. |
| PROSITE | PS00093. N4_MTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MTSM_SERMA | ||||||||
| Accession | Primary (citable) accession number: P14230 | ||||||||
| 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


