Q9LAI0 (T2BLB_BACSQ) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 33. History...
Names and origin
|Protein names||Recommended name:|
Type-2 restriction enzyme BslI subunit beta
Endonuclease BslI subunit beta
Type II restriction enzyme BslI subunit beta
Type IIT restriction enzyme BslI subunit beta
|Organism||Bacillus sp. (strain NEB-606)|
|Taxonomic identifier||114630 [NCBI]|
|Taxonomic lineage||Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus|
|Sequence length||301 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Recognizes the double-stranded sequence 5'-CCN7GG-3' and cleaves after N-7.
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Binds 1 zinc ion per subunit.
Heterotetramer of two alpha and two beta subunits. The alpha subunit is believed to be responsible for DNA recognition, while the beta subunit is thought to mediate cleavage.
Could be used to screen carcinogenic mutations in a restriction endonuclease-mediated selective PCR (or REMS-PCR) assay. In particular, could be used to detect the vast majority of mutations that occur at codons 12 or 13 of the Ras oncogenes that encode glycine (codons GGN) at those positions.
Is one of the thermostable restriction enzymes that remain active after 20 to 30 cycles of thermal PCR cycling.
|Biological process||Restriction system|
|Technical term||Direct protein sequencing|
|Gene Ontology (GO)|
|Biological_process||DNA restriction-modification system|
Inferred from electronic annotation. Source: UniProtKB-KWnucleic acid phosphodiester bond hydrolysis
Inferred from electronic annotation. Source: GOC
|Molecular_function||Type II site-specific deoxyribonuclease activity|
Inferred from electronic annotation. Source: UniProtKB-ECmetal ion binding
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 301||301||Type-2 restriction enzyme BslI subunit beta||PRO_0000077284|
|Zinc finger||62 – 82||21||CHC2-type|
|Mutagenesis||62||1||C → K: Loss of activity. Ref.2|
|Mutagenesis||66||1||H → K: 50% of wild-type activity. Ref.2|
|Mutagenesis||79||1||C → K: 10% of wild-type activity. Ref.2|
|Mutagenesis||82||1||C → K: 10% of wild-type activity. Ref.2|
|||"Cloning, expression, and purification of a thermostable nonhomodimeric restriction enzyme, BslI."|
Hsieh P.-C., Xiao J.-P., O'Loane D., Xu S.-Y.
J. Bacteriol. 182:949-955(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, CHARACTERIZATION.
|||"Glucocorticoid receptor-like Zn(Cys)4 motifs in BslI restriction endonuclease."|
Scheuring Vanamee E., Hsieh P.-C., Zhu Z., Yates D., Garman E., Xu S.-Y., Aggarwal A.K.
J. Mol. Biol. 334:595-603(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ZINC-BINDING, ABSORPTION SPECTROSCOPY, MUTAGENESIS OF CYS-62; HIS-66; CYS-79 AND CYS-82.
|Accession||Primary (citable) accession number: Q9LAI0|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Prokaryotic Protein Annotation Program|
|Restriction enzymes and methylases|
Classification of restriction enzymes and methylases and list of entries