[1]	PROTEIN SEQUENCE. PubMed=1369324 [NCBI, ExPASy, EBI, Israel, Japan] Tabata N., Kazama H., Ohgi K., Irie M.; "Primary structure of a nuclease (nuclease PA3) from a Penicillium sp."; Agric. Biol. Chem. 55:461-469(1991).
[2]	PROTEIN SEQUENCE OF 1-30 AND 268-270. PubMed=1964878 [NCBI, ExPASy, EBI, Israel, Japan] Kazama H., Tabata N., Ohgi K., Irie M.; "Purification and characterization of a nuclease (3'-nucleotidase) from a Penicillium sp."; Chem. Pharm. Bull. 38:3081-3085(1990).

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.
SIMILARITY: To A.oryzae nuclease S1, and barley nuclease.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

JE0408; JE0408.

3D structure databases

HSSP

P24289; 1AK0. [HSSP ENTRY / PDB]

SMR

P24504; 1-264.

ModBase

P24504.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0008254;	Molecular function: 3'-nucleotidase activity (inferred from electronic annotation from EC).
GO:0004519;	Molecular function: endonuclease activity (inferred from electronic annotation from InterPro).
GO:0003676;	Molecular function: nucleic acid binding (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006308;	Biological process: DNA catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003154; S1/P1nuclease.
Graphical view of domain structure.

Pfam

PF02265; S1-P1_nuclease; 1.
Pfam graphical view of domain structure.

ProtoNet

P24504.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Endonuclease; Glycoprotein; Hydrolase; Metal-binding; Nuclease; Secreted; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 270`	`270`	`Nuclease PA3.`	`PRO_0000058004`
`METAL`	`1 1`		`Zinc 3 (By similarity).`
`METAL`	`6 6`		`Zinc 3 (By similarity).`
`METAL`	`45 45`		`Zinc 1 (By similarity).`
`METAL`	`60 60`		`Zinc 1 (By similarity).`
`METAL`	`116 116`		`Zinc 1 (By similarity).`
`METAL`	`120 120`		`Zinc 1 (By similarity).`
`METAL`	`120 120`		`Zinc 3 (By similarity).`
`METAL`	`126 126`		`Zinc 2 (By similarity).`
`METAL`	`149 149`		`Zinc 2 (By similarity).`
`METAL`	`153 153`		`Zinc 2 (By similarity).`
`CARBOHYD`	`92 92`		`N-linked (GlcNAc...).`
`CARBOHYD`	`138 138`		`N-linked (GlcNAc...).`
`CARBOHYD`	`184 184`		`N-linked (GlcNAc...).`
`CARBOHYD`	`197 197`		`N-linked (GlcNAc...).`
`DISULFID`	`72 217`		`By similarity.`
`DISULFID`	`80 85`		`By similarity.`

Sequence information

Length: 270 AA [This is the length of the unprocessed precursor]

Molecular weight: 29215 Da [This is the MW of the unprocessed precursor]

CRC64: EF52CFDBBA4F16EF [This is a checksum on the sequence]

        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

P24504 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools