P25241 (T3RE_BACC1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 91.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Type III restriction-modification system Bce10987IP enzyme res EC=3.1.21.5 | ||||||
| Gene names |
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| Organism | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 222523 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›  |
Protein attributes
| Sequence length | 987 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This protein cuts the DNA outside of the recognition site. May also act as a helicase involved in unwinding DNA at the cleavage site. Protein only required for restriction but needs the presence of the modification enzyme By similarity. |
| Catalytic activity | Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. |
| Cofactor | Magnesium By similarity. |
| Subunit structure | Contains two different subunits: res and mod. |
| Sequence similarities | Belongs to the type III restriction-modification system res protein family. Contains 1 VRR-NUC domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Restriction system |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Endonuclease Helicase Hydrolase Nuclease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysisInferred from electronic annotation. Source: GOC |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA bindingInferred from electronic annotation. Source: InterPro Type III site-specific deoxyribonuclease activityInferred from electronic annotation. Source: EC helicase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 987 | 987 | Type III restriction-modification system Bce10987IP enzyme res | PRO_0000077376 | |||||
Regions | |||||||||
| Domain | 886 – 974 | 89 | VRR-NUC | ||||||
Experimental info | |||||||||
| Sequence conflict | 410 – 462 | 53 | TFERL…GYFGE → GDYQFIETKAPTGYDLNAKP IPFTITKGQAQVTSVTALNS LTTGSMELMKVDM in CAA43125. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genome organization is not conserved between Bacillus cereus and Bacillus subtilis." Oekstad O.A., Hegna I.K., Lindbaeck T., Rishovd A.-L., Kolstoe A.-B. Microbiology 145:621-631(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987. |
| [3] | "A type-III DNA restriction and modification system in Bacillus cereus?" Hegna I.K., Karlstroem E.S., Lopez R., Kristensen T., Kolstoe A.-B. Gene 114:149-150(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-821. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ007510 Genomic DNA. Translation: CAB40612.1. AE017194 Genomic DNA. Translation: AAS39950.1. X60713 Genomic DNA. Translation: CAA43125.1. |
| PIR | JC1116. S15518. |
| RefSeq | NP_977342.1. NC_003909.8. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 222523.BCE_1019. |
Protein family/group databases | |
| REBASE | 2841. BceSI. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAS39950; AAS39950; BCE_1019. |
| GeneID | 2750767. |
| KEGG | bca:BCE_1019. |
| PATRIC | 18850934. VBIBacCer118379_0972. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3587. |
| HOGENOM | HOG000218980. |
| KO | K01156. |
| OMA | FAWLLEF. |
| ProtClustDB | PRK15483. |
Enzyme and pathway databases | |
| BRENDA | 3.1.21.5. 648. |
Family and domain databases | |
| InterPro | IPR006935. Helicase/UvrB_dom. IPR014883. VRR_NUC. [Graphical view] |
| Pfam | PF04851. ResIII. 1 hit. PF08774. VRR_NUC. 1 hit. [Graphical view] |
| SMART | SM00990. VRR_NUC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | T3RE_BACC1 | ||||||||
| Accession | Primary (citable) accession number: P25241 Secondary accession number(s): Q9XBI5 | ||||||||
| 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 |