P24289 (NUP1_PENCI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Nuclease P1 EC=3.1.30.1 Alternative name(s): Deoxyribonuclease P1 Endonuclease P1
Organism	Penicillium citrinum
Taxonomic identifier	5077 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Secreted
Ligand	Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	DNA catabolic process Inferred from electronic annotation. Source: InterPro nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endonuclease 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

Nuclease P1

PRO_0000058003

Sites

Metal binding

1

1

Zinc 3

Metal binding

6

1

Zinc 3

Metal binding

45

1

Zinc 1

Metal binding

60

1

Zinc 1

Metal binding

116

1

Zinc 1

Metal binding

120

1

Zinc 1

Metal binding

120

1

Zinc 3

Metal binding

126

1

Zinc 2

Metal binding

149

1

Zinc 2

Metal binding

153

1

Zinc 2

Amino acid modifications

Glycosylation

92

1

N-linked (GlcNAc...)

Glycosylation

138

1

N-linked (GlcNAc...)

Glycosylation

184

1

N-linked (GlcNAc...)

Glycosylation

197

1

N-linked (GlcNAc...)

Disulfide bond

72 ↔ 217

Disulfide bond

80 ↔ 85

Natural variations

Natural variant

270

1

Missing.

Secondary structure

1

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270

Helix Strand Turn

Details...

Helix

3 – 16

14

Helix

19 – 29

11

Turn

34 – 37

4

Helix

38 – 40

3

Helix

43 – 48

6

Turn

51 – 53

3

Helix

54 – 60

7

Turn

68 – 70

3

Helix

76 – 79

4

Helix

86 – 97

12

Helix

104 – 120

17

Helix

124 – 127

4

Helix

130 – 133

4

Turn

134 – 136

3

Beta strand

138 – 141

4

Beta strand

144 – 147

4

Helix

148 – 153

6

Helix

155 – 161

7

Helix

166 – 181

16

Helix

186 – 193

8

Helix

201 – 218

18

Helix

226 – 228

3

Beta strand

229 – 232

4

Helix

236 – 263

28

Sequences

	Sequence		Length	Mass (Da)
	P24289 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: FA9D25FE75A526EF	FASTA	270	29,227
	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

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

PIR

S17828.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AK0	X-ray	1.80	A	1-270	[»]

ProteinModelPortal

P24289.

SMR

P24289. Positions 1-264.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.575.10. 1 hit.

InterPro

IPR008947. PLipase_C/P1_nuclease.
IPR003154. S1/P1nuclease.
[Graphical view]

Pfam

PF02265. S1-P1_nuclease. 1 hit.
[Graphical view]

SUPFAM

SSF48537. PLC_Nuclease. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P24289.

Entry information

Entry name

NUP1_PENCI

Accession

Primary (citable) accession number: P24289

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program