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P23657

- T2P2_PROHU

UniProt

P23657 - T2P2_PROHU

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Protein

Type-2 restriction enzyme PvuII

Gene

pvuIIR

Organism
Proteus hauseri
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581Magnesium 1By similarity
Metal bindingi58 – 581Magnesium 2By similarity
Metal bindingi68 – 681Magnesium 1By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

REBASEi1542. PvuII.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme PvuII (EC:3.1.21.4)
Short name:
R.PvuII
Alternative name(s):
Endonuclease PvuII
Type II restriction enzyme PvuII
Gene namesi
Name:pvuIIR
OrganismiProteus hauseri
Taxonomic identifieri183417 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157Type-2 restriction enzyme PvuIIPRO_0000077356Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2520Combined sources
Turni31 – 333Combined sources
Helixi36 – 4611Combined sources
Beta strandi55 – 573Combined sources
Beta strandi58 – 603Combined sources
Beta strandi66 – 738Combined sources
Turni74 – 763Combined sources
Beta strandi78 – 803Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 958Combined sources
Beta strandi99 – 1057Combined sources
Beta strandi108 – 1158Combined sources
Helixi117 – 13317Combined sources
Helixi146 – 1527Combined sources
Beta strandi153 – 1553Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23657.
SMRiP23657. Positions 2-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23657.

Family & Domainsi

Family and domain databases

Gene3Di3.40.210.10. 1 hit.
InterProiIPR011335. Restrct_endonuc-II-like.
IPR015306. Restrct_endonuc_II_PvuII.
[Graphical view]
PfamiPF09225. Endonuc-PvuII. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

P23657-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSHPDLNKLL ELWPHIQEYQ DLALKHGIND IFQDNGGKLL QVLLITGLTV
60 70 80 90 100
LPGREGNDAV DNAGQEYELK SINIDLTKGF STHHHMNPVI IAKYRQVPWI
110 120 130 140 150
FAIYRGIAIE AIYRLEPKDL EFYYDKWERK WYSDGHKDIN NPKIPVKYVM

EHGTKIY
Length:157
Mass (Da):18,345
Last modified:November 1, 1991 - v1
Checksum:i2146453E04E65570
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52681 Genomic DNA. Translation: CAA36904.1.
AF305615 Genomic DNA. Translation: AAA96334.1.
PIRiS12163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52681 Genomic DNA. Translation: CAA36904.1 .
AF305615 Genomic DNA. Translation: AAA96334.1 .
PIRi S12163.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EYU X-ray 1.78 A/B 1-157 [» ]
1F0O X-ray 2.50 A/B 1-157 [» ]
1H56 X-ray 3.00 A/B 2-157 [» ]
1K0Z X-ray 2.05 A/B 2-157 [» ]
1NI0 X-ray 2.50 A/B/C 1-157 [» ]
1PVI X-ray 2.60 A/B 1-157 [» ]
1PVU X-ray 2.40 A/B 2-157 [» ]
2PVI X-ray 1.76 A/B 1-157 [» ]
3KSK X-ray 2.35 A/B 2-157 [» ]
3PVI X-ray 1.59 A/B 1-157 [» ]
ProteinModelPortali P23657.
SMRi P23657. Positions 2-157.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 1542. PvuII.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P23657.

Family and domain databases

Gene3Di 3.40.210.10. 1 hit.
InterProi IPR011335. Restrct_endonuc-II-like.
IPR015306. Restrct_endonuc_II_PvuII.
[Graphical view ]
Pfami PF09225. Endonuc-PvuII. 1 hit.
[Graphical view ]
SUPFAMi SSF52980. SSF52980. 1 hit.
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiT2P2_PROHU
AccessioniPrimary (citable) accession number: P23657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 26, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

External Data

Dasty 3