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P23657 (T2P2_PROHU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 PvuII

Short name=R.PvuII
EC=3.1.21.4
Alternative name(s):
Endonuclease PvuII
Type II restriction enzyme PvuII
Gene names
Name:pvuIIR
OrganismProteus hauseri
Taxonomic identifier183417 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes the double-stranded sequence CAGCTG and cleaves after G-3.

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit.

Subunit structure

Homodimer.

Ontologies

Keywords
   Biological processRestriction system
   LigandMagnesium
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
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 – 157157Type-2 restriction enzyme PvuII
PRO_0000077356

Sites

Metal binding581Magnesium 1 By similarity
Metal binding581Magnesium 2 By similarity
Metal binding681Magnesium 1 By similarity

Secondary structure

............................ 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23657 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 2146453E04E65570

FASTA15718,345
        10         20         30         40         50         60 
MSHPDLNKLL ELWPHIQEYQ DLALKHGIND IFQDNGGKLL QVLLITGLTV LPGREGNDAV 

        70         80         90        100        110        120 
DNAGQEYELK SINIDLTKGF STHHHMNPVI IAKYRQVPWI FAIYRGIAIE AIYRLEPKDL 

       130        140        150 
EFYYDKWERK WYSDGHKDIN NPKIPVKYVM EHGTKIY 

« Hide

References

[1]"Complete nucleotide sequence of the PvuII restriction enzyme gene from Proteus vulgaris."
Athanasiadis A., Gregoriu M., Thanos D., Kokkinidis M., Papamatheakis J.
Nucleic Acids Res. 18:6434-6434(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
[2]"Structure of PvuII endonuclease with cognate DNA."
Cheng X., Balendiran K., Schildkraut I., Anderson J.E.
EMBO J. 13:3927-3935(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[3]"Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV."
Athanasiadis A., Vlassi M., Kotsifaki D., Tucker P.A., Wilson K.S., Kokkinidis M.
Nat. Struct. Biol. 1:469-475(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]"How is modification of the DNA substrate recognized by the PvuII restriction endonuclease?"
Horton J.R., Bonventre J., Cheng X.
Biol. Chem. 379:451-458(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).
[5]"Asp34 of PvuII endonuclease is directly involved in DNA minor groove recognition and indirectly involved in catalysis."
Horton J.R., Nastri H.G., Riggs P.D., Cheng X.
J. Mol. Biol. 284:1491-1504(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52681 Genomic DNA. Translation: CAA36904.1.
AF305615 Genomic DNA. Translation: AAA96334.1.
PIRS12163.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EYUX-ray1.78A/B1-157[»]
1F0OX-ray2.50A/B1-157[»]
1H56X-ray3.00A/B2-157[»]
1K0ZX-ray2.05A/B2-157[»]
1NI0X-ray2.50A/B/C1-157[»]
1PVIX-ray2.60A/B1-157[»]
1PVUX-ray2.40A/B2-157[»]
2PVIX-ray1.76A/B1-157[»]
3KSKX-ray2.35A/B2-157[»]
3PVIX-ray1.59A/B1-157[»]
ProteinModelPortalP23657.
SMRP23657. Positions 2-157.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE1542. PvuII.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

ProtClustDBCLSK688103.

Family and domain databases

Gene3D3.40.210.10. 1 hit.
InterProIPR011335. Restrct_endonuc-II-like.
IPR015306. Restrct_endonuc_II_PvuII.
[Graphical view]
PfamPF09225. Endonuc-PvuII. 1 hit.
[Graphical view]
SUPFAMSSF52980. SSF52980. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP23657.

Entry information

Entry nameT2P2_PROHU
AccessionPrimary (citable) accession number: P23657
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 89 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references