Nuclease PA3 - Penicillium sp.

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Reviewed, UniProtKB/Swiss-Prot P24504 (NUP3_PENSQ)

Last modified June 16, 2009. Version 47. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein names	Recommended name: Nuclease PA3 EC=3.1.3.6 Alternative name(s): Endonuclease PA3 Deoxyribonuclease PA3
Organism	Penicillium sp.
Taxonomic identifier	5081 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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

Keywords
Cellular component	Secreted
Ligand	Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'-nucleotidase activity Inferred from electronic annotation. Source: EC endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

270

Nuclease PA3

PRO_0000058004

Sites

Metal binding

1

Zinc 3 By similarity

Metal binding

1

Zinc 3 By similarity

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 3 By similarity

Metal binding

1

Zinc 2 By similarity

Metal binding

1

Zinc 2 By similarity

Metal binding

1

Zinc 2 By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Ref.1

Glycosylation

1

N-linked (GlcNAc...) Ref.1

Glycosylation

1

N-linked (GlcNAc...) Ref.1

Glycosylation

1

N-linked (GlcNAc...) Ref.1

Disulfide bond

By similarity

Disulfide bond

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P24504-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: EF52CFDBBA4F16EF
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270

29,215

        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

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.

Cross-references

Sequence databases
PIR	JE0408.
3D structure databases
HSSP	HSSP built from PDB template 1AK0 based on UniProtKB P24289.
SMR	P24504. Positions 1-264.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.3.6. 276590.
Family and domain databases
InterPro	IPR008947. Phospholipase_C/P1_nuclease. IPR003154. S1/P1nuclease. [Graphical view]
Gene3D	G3DSA:1.10.575.10. Phospholipase_C/P1_nuclease. 1 hit.
Pfam	PF02265. S1-P1_nuclease. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUP3_PENSQ

Accession

Primary (citable) accession number: P24504

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information