NUP3_PENSQ
ID NUP3_PENSQ Reviewed; 270 AA.
AC P24504;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Nuclease PA3 {ECO:0000303|PubMed:1369324};
DE EC=3.1.3.6 {ECO:0000269|PubMed:1964878};
DE AltName: Full=Deoxyribonuclease PA3 {ECO:0000303|PubMed:1369324};
DE AltName: Full=Endonuclease PA3 {ECO:0000303|PubMed:1369324};
OS Penicillium sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5081;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1369324; DOI=10.1271/bbb1961.55.461;
RA Tabata N., Kazama H., Ohgi K., Irie M.;
RT "Primary structure of a nuclease (nuclease PA3) from a Penicillium sp.";
RL Agric. Biol. Chem. 55:461-469(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-30 AND 268-270, FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=1964878; DOI=10.1248/cpb.38.3081;
RA Kazama H., Tabata N., Ohgi K., Irie M.;
RT "Purification and characterization of a nuclease (3'-nucleotidase) from a
RT Penicillium sp.";
RL Chem. Pharm. Bull. 38:3081-3085(1990).
CC -!- FUNCTION: Hydrolyzes only single-stranded DNA and RNA without apparent
CC specificity for bases. {ECO:0000269|PubMed:1964878}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000269|PubMed:1964878};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:1964878};
CC Note=Binds 3 divalent metal cations. {ECO:0000269|PubMed:1964878};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the nuclease type I family. {ECO:0000305}.
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DR PIR; JE0408; JE0408.
DR AlphaFoldDB; P24504; -.
DR SMR; P24504; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR CDD; cd11010; S1-P1_nuclease; 1.
DR Gene3D; 1.10.575.10; -; 1.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR003154; S1/P1nuclease.
DR PANTHER; PTHR33146; PTHR33146; 1.
DR Pfam; PF02265; S1-P1_nuclease; 1.
DR SUPFAM; SSF48537; SSF48537; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Metal-binding; Nuclease; Secreted; Zinc.
FT CHAIN 1..270
FT /note="Nuclease PA3"
FT /id="PRO_0000058004"
FT REGION 116..164
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 1..6
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 1
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 6
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 45..51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 45
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 60..63
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 73..78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 116
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 126
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 153
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT SITE 45
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24021"
FT SITE 48
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 72..217
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT DISULFID 80..85
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
SQ SEQUENCE 270 AA; 29215 MW; EF52CFDBBA4F16EF CRC64;
WGALGHATVA YVAQHYVSPE AASWAQGILG SSSSSYLASI ASWADEYRLT SAGKWSASLH
FIDAEDNPPT NCNVDYERDC GSSGCSISAI ANYTQRVSDS SLSSENHAEA LRFLVHFIGD
MTQPLHDEAY AVGGNKINVT FDGYHDNLHS DWDTYMPQKL IGGHALSDAE SWAKTLVQNI
ESGNYTAQAT GWIKGDNISE PITTATRWAS DANALVCTVV MPHGAAALQT GDLYPTYYDS
VIDTIELQIA KGGYRLANWI NEIHGSEIAK
