P50178 (MTL22_LACLC) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 59.
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 LlaDCHIB Short name=M.LlaDCHI B Short name=M.LlaDCHIB EC=2.1.1.72 Alternative name(s): Adenine-specific methyltransferase LlaDCHIB M.LlaII B | ||||
| Gene names |
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| Encoded on | Plasmid pSRQ700 | ||||
| Organism | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) | ||||
| Taxonomic identifier | 1359 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus › ![]() |
Protein attributes
| Sequence length | 269 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands, and protects the DNA from cleavage by the LlaDCHI endonuclease. |
| Catalytic activity | S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. |
| Miscellaneous | The LlaII restriction system has two different methylases. |
| 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 | Plasmid |
| 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 – 269 | 269 | Modification methylase LlaDCHIB | PRO_0000087954 | |||
Sequences
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References
| [1] | "Cloning and sequencing of LlaDCHI restriction/modification genes from Lactococcus lactis and relatedness of this system to the Streptococcus pneumoniae DpnII system." Moineau S., Walker S.A., Vedamuthu E.R., Vandenbergh P.A. Appl. Environ. Microbiol. 61:2193-2202(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DCH-4. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U16027 Genomic DNA. Translation: AAB06312.1. |
| RefSeq | NP_116732.1. NC_002798.1. |
3D structure databases | |
| ProteinModelPortal | P50178. |
| ModBase | Search... |
Protein family/group databases | |
| REBASE | 3663. M2.LlaDCHI. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1113499. |
Phylogenomic databases | |
| ProtClustDB | CLSK785445. |
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... |
Entry information
| Entry name | MTL22_LACLC | ||||||||
| Accession | Primary (citable) accession number: P50178 | ||||||||
| 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
