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P24289 (NUP1_PENCI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclease P1

EC=3.1.30.1
Alternative name(s):
Deoxyribonuclease P1
Endonuclease P1
OrganismPenicillium citrinum
Taxonomic identifier5077 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 3 zinc ions.

Subcellular location

Secreted.

Sequence similarities

Belongs to the nuclease type I family.

Ontologies

Keywords
   Cellular componentSecreted
   LigandMetal-binding
Zinc
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processDNA catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Nuclease P1
PRO_0000058003

Sites

Metal binding11Zinc 3
Metal binding61Zinc 3
Metal binding451Zinc 1
Metal binding601Zinc 1
Metal binding1161Zinc 1
Metal binding1201Zinc 1
Metal binding1201Zinc 3
Metal binding1261Zinc 2
Metal binding1491Zinc 2
Metal binding1531Zinc 2

Amino acid modifications

Glycosylation921N-linked (GlcNAc...)
Glycosylation1381N-linked (GlcNAc...)
Glycosylation1841N-linked (GlcNAc...)
Glycosylation1971N-linked (GlcNAc...)
Disulfide bond72 ↔ 217
Disulfide bond80 ↔ 85

Natural variations

Natural variant2701Missing.

Secondary structure

............................................ 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24289 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: FA9D25FE75A526EF

FASTA27029,227
        10         20         30         40         50         60 
WGALGHATVA YVAQHYVSPE AASWAQGILG SSSSSYLASI ASWADEYRLT SAGKWSASLH 

        70         80         90        100        110        120 
FIDAEDNPPT NCNVDYERDC GSSGCSISAI ANYTQRVSDS SLSSENHAEA LRFLVHFIGD 

       130        140        150        160        170        180 
MTQPLHDEAY AVGGNKINVT FDGYHDNLHS DWDTYMPQKL IGGHALSDAE SWAKTLVQNI 

       190        200        210        220        230        240 
ESGNYTAQAI GWIKGDNISE PITTATRWAS DANALVCTVV MPHGAAALQT GDLYPTYYDS 

       250        260        270 
VIDTIELQIA KGGYRLANWI NEIHGSEIAK 

« Hide

References

[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).

Cross-references

Sequence databases

PIRS17828.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AK0X-ray1.80A1-270[»]
ProteinModelPortalP24289.
SMRP24289. Positions 1-264.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.575.10. 1 hit.
InterProIPR008947. PLipase_C/P1_nuclease.
IPR003154. S1/P1nuclease.
[Graphical view]
PfamPF02265. S1-P1_nuclease. 1 hit.
[Graphical view]
SUPFAMSSF48537. SSF48537. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP24289.

Entry information

Entry nameNUP1_PENCI
AccessionPrimary (citable) accession number: P24289
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references