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P23657

- T2P2_PROHU

UniProt

P23657 - T2P2_PROHU

Protein

Type-2 restriction enzyme PvuII

Gene

pvuIIR

Organism
Proteus hauseri
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 2520
    Turni31 – 333
    Helixi36 – 4611
    Beta strandi55 – 573
    Beta strandi58 – 603
    Beta strandi66 – 738
    Turni74 – 763
    Beta strandi78 – 803
    Beta strandi84 – 863
    Helixi88 – 958
    Beta strandi99 – 1057
    Beta strandi108 – 1158
    Helixi117 – 13317
    Helixi146 – 1527
    Beta strandi153 – 1553

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MSHPDLNKLL ELWPHIQEYQ DLALKHGIND IFQDNGGKLL QVLLITGLTV    50
    LPGREGNDAV DNAGQEYELK SINIDLTKGF STHHHMNPVI IAKYRQVPWI 100
    FAIYRGIAIE AIYRLEPKDL EFYYDKWERK WYSDGHKDIN NPKIPVKYVM 150
    EHGTKIY 157
    Length:157
    Mass (Da):18,345
    Last modified:November 1, 1991 - v1
    Checksum:i2146453E04E65570
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52681 Genomic DNA. Translation: CAA36904.1.
    AF305615 Genomic DNA. Translation: AAA96334.1.
    PIRiS12163.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52681 Genomic DNA. Translation: CAA36904.1 .
    AF305615 Genomic DNA. Translation: AAA96334.1 .
    PIRi S12163.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 92 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