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P24289

- NUP1_PENCI

UniProt

P24289 - NUP1_PENCI

Protein

Nuclease P1

Gene
N/A
Organism
Penicillium citrinum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    • Comment

    Functioni

    Hydrolyzes only single-stranded DNA and RNA without apparent specificity for bases.

    Catalytic activityi

    Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products.

    Cofactori

    Binds 3 zinc ions.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1 – 11Zinc 3
    Metal bindingi6 – 61Zinc 3
    Metal bindingi45 – 451Zinc 1
    Metal bindingi60 – 601Zinc 1
    Metal bindingi116 – 1161Zinc 1
    Metal bindingi120 – 1201Zinc 1
    Metal bindingi120 – 1201Zinc 3
    Metal bindingi126 – 1261Zinc 2
    Metal bindingi149 – 1491Zinc 2
    Metal bindingi153 – 1531Zinc 2

    GO - Molecular functioni

    1. endonuclease activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. nucleic acid binding Source: InterPro

    GO - Biological processi

    1. DNA catabolic process Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclease P1 (EC:3.1.30.1)
    Alternative name(s):
    Deoxyribonuclease P1
    Endonuclease P1
    OrganismiPenicillium citrinum
    Taxonomic identifieri5077 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 270270Nuclease P1PRO_0000058003Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi72 ↔ 217
    Disulfide bondi80 ↔ 85
    Glycosylationi92 – 921N-linked (GlcNAc...)
    Glycosylationi138 – 1381N-linked (GlcNAc...)
    Glycosylationi184 – 1841N-linked (GlcNAc...)
    Glycosylationi197 – 1971N-linked (GlcNAc...)

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    Secondary structure

    1
    270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi19 – 2911
    Turni34 – 374
    Helixi38 – 403
    Helixi43 – 486
    Turni51 – 533
    Helixi54 – 607
    Turni68 – 703
    Helixi76 – 794
    Helixi86 – 9712
    Helixi104 – 12017
    Helixi124 – 1274
    Helixi130 – 1334
    Turni134 – 1363
    Beta strandi138 – 1414
    Beta strandi144 – 1474
    Helixi148 – 1536
    Helixi155 – 1617
    Helixi166 – 18116
    Helixi186 – 1938
    Helixi201 – 21818
    Helixi226 – 2283
    Beta strandi229 – 2324
    Helixi236 – 26328

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AK0X-ray1.80A1-270[»]
    ProteinModelPortaliP24289.
    SMRiP24289. Positions 1-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24289.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the nuclease type I family.Curated

    Family and domain databases

    Gene3Di1.10.575.10. 1 hit.
    InterProiIPR008947. PLipase_C/P1_nuclease.
    IPR003154. S1/P1nuclease.
    [Graphical view]
    PfamiPF02265. S1-P1_nuclease. 1 hit.
    [Graphical view]
    SUPFAMiSSF48537. SSF48537. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P24289-1 [UniParc]FASTAAdd to Basket

    « Hide

    WGALGHATVA YVAQHYVSPE AASWAQGILG SSSSSYLASI ASWADEYRLT    50
    SAGKWSASLH FIDAEDNPPT NCNVDYERDC GSSGCSISAI ANYTQRVSDS 100
    SLSSENHAEA LRFLVHFIGD MTQPLHDEAY AVGGNKINVT FDGYHDNLHS 150
    DWDTYMPQKL IGGHALSDAE SWAKTLVQNI ESGNYTAQAI GWIKGDNISE 200
    PITTATRWAS DANALVCTVV MPHGAAALQT GDLYPTYYDS VIDTIELQIA 250
    KGGYRLANWI NEIHGSEIAK 270
    Length:270
    Mass (Da):29,227
    Last modified:March 1, 1992 - v1
    Checksum:iFA9D25FE75A526EF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti270 – 2701Missing.

    Sequence databases

    PIRiS17828.

    Cross-referencesi

    Sequence databases

    PIRi S17828.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AK0 X-ray 1.80 A 1-270 [» ]
    ProteinModelPortali P24289.
    SMRi P24289. Positions 1-264.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P24289.

    Family and domain databases

    Gene3Di 1.10.575.10. 1 hit.
    InterProi IPR008947. PLipase_C/P1_nuclease.
    IPR003154. S1/P1nuclease.
    [Graphical view ]
    Pfami PF02265. S1-P1_nuclease. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48537. SSF48537. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of nuclease P1 from Penicillium citrinum."
      Maekewa K., Tsunasawa S., Dibo G., Sakiyama F.
      Eur. J. Biochem. 200:651-661(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Crystal structure of Penicillium citrinum P1 nuclease at 2.8-A resolution."
      Volbeda A., Lahm A., Sakiyama F., Suck D.
      EMBO J. 10:1607-1618(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    3. "Recognition of single-stranded DNA by nuclease P1: high resolution crystal structures of complexes with substrate analogs."
      Romier C., Dominguez R., Lahm A., Dahl O., Suck D.
      Proteins 32:414-424(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiNUP1_PENCI
    AccessioniPrimary (citable) accession number: P24289
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3