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P24289

- NUP1_PENCI

UniProt

P24289 - NUP1_PENCI

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Protein

Nuclease P1

Gene
N/A
Organism
Penicillium citrinum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

        10         20         30         40         50
WGALGHATVA YVAQHYVSPE AASWAQGILG SSSSSYLASI ASWADEYRLT
60 70 80 90 100
SAGKWSASLH FIDAEDNPPT NCNVDYERDC GSSGCSISAI ANYTQRVSDS
110 120 130 140 150
SLSSENHAEA LRFLVHFIGD MTQPLHDEAY AVGGNKINVT FDGYHDNLHS
160 170 180 190 200
DWDTYMPQKL IGGHALSDAE SWAKTLVQNI ESGNYTAQAI GWIKGDNISE
210 220 230 240 250
PITTATRWAS DANALVCTVV MPHGAAALQT GDLYPTYYDS VIDTIELQIA
260 270
KGGYRLANWI NEIHGSEIAK
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 29, 2014
This is version 82 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