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Protein

Type-2 restriction enzyme PvuII

Gene

pvuIIR

Organism
Proteus hauseri
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi58Magnesium 1By similarity1
Metal bindingi58Magnesium 2By similarity1
Metal bindingi68Magnesium 1By similarity1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000773561 – 157Type-2 restriction enzyme PvuIIAdd BLAST157

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 25Combined sources20
Turni31 – 33Combined sources3
Helixi36 – 46Combined sources11
Beta strandi55 – 57Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi66 – 73Combined sources8
Turni74 – 76Combined sources3
Beta strandi78 – 80Combined sources3
Beta strandi84 – 86Combined sources3
Helixi88 – 95Combined sources8
Beta strandi99 – 105Combined sources7
Beta strandi108 – 115Combined sources8
Helixi117 – 133Combined sources17
Helixi146 – 152Combined sources7
Beta strandi153 – 155Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
PIRiS12163.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi1542. PvuII.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23657.

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.
ProtoNetiSearch...

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 2, 2016
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.