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P24504 (NUP3_PENSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nuclease PA3

EC=3.1.3.6
Alternative name(s):
Deoxyribonuclease PA3
Endonuclease PA3
OrganismPenicillium sp.
Taxonomic identifier5081 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaePenicillium

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

A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactor

Binds 3 zinc ions.

Subcellular location

Secreted.

Sequence similarities

To A.oryzae nuclease S1, and barley nuclease.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Nuclease PA3
PRO_0000058004

Sites

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

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Ref.1
Glycosylation1381N-linked (GlcNAc...) Ref.1
Glycosylation1841N-linked (GlcNAc...) Ref.1
Glycosylation1971N-linked (GlcNAc...) Ref.1
Disulfide bond72 ↔ 217 By similarity
Disulfide bond80 ↔ 85 By similarity

Sequences

Sequence LengthMass (Da)Tools
P24504 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: EF52CFDBBA4F16EF

FASTA27029,215
        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 
ESGNYTAQAT GWIKGDNISE PITTATRWAS DANALVCTVV MPHGAAALQT GDLYPTYYDS 

       250        260        270 
VIDTIELQIA KGGYRLANWI NEIHGSEIAK 

« Hide

References

[1]"Primary structure of a nuclease (nuclease PA3) from a Penicillium sp."
Tabata N., Kazama H., Ohgi K., Irie M.
Agric. Biol. Chem. 55:461-469(1991) [PubMed: 1369324] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Purification and characterization of a nuclease (3'-nucleotidase) from a Penicillium sp."
Kazama H., Tabata N., Ohgi K., Irie M.
Chem. Pharm. Bull. 38:3081-3085(1990) [PubMed: 1964878] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-30 AND 268-270.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRJE0408.

3D structure databases

ProteinModelPortalP24504.
SMRP24504. Positions 1-264.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008947. PLipase_C/P1_nuclease.
IPR003154. S1/P1nuclease.
[Graphical view]
Gene3DG3DSA:1.10.575.10. Phospholipase_C/P1_nuclease. 1 hit.
PfamPF02265. S1-P1_nuclease. 1 hit.
[Graphical view]
SUPFAMSSF48537. PLC_Nuclease. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNUP3_PENSQ
AccessionPrimary (citable) accession number: P24504
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: October 19, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program