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Q9LAI1 (T2BLA_BACSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type-2 restriction enzyme BslI subunit alpha

Short name=R.BslIalpha
EC=3.1.21.4
Alternative name(s):
Endonuclease BslI subunit alpha
Type II restriction enzyme BslI subunit alpha
Type IIT restriction enzyme BslI subunit alpha
Gene names
Name:bslIRalpha
OrganismBacillus sp. (strain NEB-606)
Taxonomic identifier114630 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes the double-stranded sequence 5'-CCN7GG-3' and cleaves after N-7.

Catalytic activity

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

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.

Domain

One of the zinc-binding motifs may participate in protein-DNA interactions and the other might mediate protein-protein interactions.

Biotechnological use

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.

Biophysicochemical properties

Temperature dependence:

Is one of the thermostable restriction enzymes that remain active after 20 to 30 cycles of thermal PCR cycling.

Ontologies

Keywords
   Biological processRestriction system
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionType II site-specific deoxyribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Type-2 restriction enzyme BslI subunit alpha
PRO_0000077283

Regions

Zinc finger36 – 5318C4-type 1
Zinc finger63 – 8422C4-type 2

Experimental info

Mutagenesis361C → A: 10% of wild-type activity. Ref.2
Mutagenesis391C → A: 10% of wild-type activity. Ref.2
Mutagenesis501C → A: Loss of activity. Ref.2
Mutagenesis531C → A: 10% of wild-type activity. Ref.1 Ref.2
Mutagenesis531C → R: Loss of activity. Ref.1 Ref.2
Mutagenesis631C → A: Loss of activity. Ref.2
Mutagenesis661C → A: 50% of wild-type activity. Ref.2
Mutagenesis791C → A: 50% of wild-type activity. Ref.2
Mutagenesis841C → A: 50% of wild-type activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9LAI1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4969BF02325E12B2

FASTA22525,605
        10         20         30         40         50         60 
MERQLKSIAY AFVANDIDVY IPDGESNCIV VTKLVCKDCG QYWHTSLSEC YFCGTLNFYL 

        70         80         90        100        110        120 
YECNSCGKKY SLTSSSKSCD TDGCNGKLIK RCSNPECISR TNEEIQRATD EQGGVFDLNS 

       130        140        150        160        170        180 
SFNVSLNHCV TCGSKENYYK TYRIYSYRTE VEPNIEALRE FANNNKLNSD EDVIIIKHLV 

       190        200        210        220 
DNVIHYGYIP YSKLDETTEI TTTFSRFSDL VSELFPVNVP PNVTE 

« Hide

References

[1]"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.
[2]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF135191 Genomic DNA. Translation: AAF32530.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE386. BslI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameT2BLA_BACSQ
AccessionPrimary (citable) accession number: Q9LAI1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries