Q9LAI1 (T2BLA_BACSQ) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 35. History...
Names and origin
|Protein names||Recommended name:|
Type-2 restriction enzyme BslI subunit alpha
Endonuclease BslI subunit alpha
Type II restriction enzyme BslI subunit alpha
Type IIT restriction enzyme BslI subunit alpha
|Organism||Bacillus sp. (strain NEB-606)|
|Taxonomic identifier||114630 [NCBI]|
|Taxonomic lineage||Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus|
|Sequence length||225 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 2 zinc ions 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.
One of the zinc-binding motifs may participate in protein-DNA interactions and the other might mediate protein-protein interactions.
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 – 225||225||Type-2 restriction enzyme BslI subunit alpha||PRO_0000077283|
|Zinc finger||36 – 53||18||C4-type 1|
|Zinc finger||63 – 84||22||C4-type 2|
|Mutagenesis||36||1||C → A: 10% of wild-type activity. Ref.2|
|Mutagenesis||39||1||C → A: 10% of wild-type activity. Ref.2|
|Mutagenesis||50||1||C → A: Loss of activity. Ref.2|
|Mutagenesis||53||1||C → A: 10% of wild-type activity. Ref.1 Ref.2|
|Mutagenesis||53||1||C → R: Loss of activity. Ref.1 Ref.2|
|Mutagenesis||63||1||C → A: Loss of activity. Ref.2|
|Mutagenesis||66||1||C → A: 50% of wild-type activity. Ref.2|
|Mutagenesis||79||1||C → A: 50% of wild-type activity. Ref.2|
|Mutagenesis||84||1||C → A: 50% 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, MUTAGENESIS OF CYS-53.
|||"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 CYSTEINE RESIDUES.
|Accession||Primary (citable) accession number: Q9LAI1|
|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