NUP1_PENCI
ID NUP1_PENCI Reviewed; 270 AA.
AC P24289;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Nuclease P1 {ECO:0000303|PubMed:1915339};
DE EC=3.1.30.1 {ECO:0000250|UniProtKB:Q9SXA6};
DE AltName: Full=Deoxyribonuclease P1 {ECO:0000303|PubMed:1915339};
DE AltName: Full=Endonuclease P1 {ECO:0000303|PubMed:1915339};
OS Penicillium citrinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5077;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1915339; DOI=10.1111/j.1432-1033.1991.tb16228.x;
RA Maekewa K., Tsunasawa S., Dibo G., Sakiyama F.;
RT "Primary structure of nuclease P1 from Penicillium citrinum.";
RL Eur. J. Biochem. 200:651-661(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=1710977; DOI=10.1002/j.1460-2075.1991.tb07683.x;
RA Volbeda A., Lahm A., Sakiyama F., Suck D.;
RT "Crystal structure of Penicillium citrinum P1 nuclease at 2.8-A
RT resolution.";
RL EMBO J. 10:1607-1618(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ZINC,
RP GLYCOSYLATION AT ASN-92; ASN-138 AND ASN-197, AND DISULFIDE BONDS.
RX PubMed=9726413;
RX DOI=10.1002/(sici)1097-0134(19980901)32:4<414::aid-prot2>3.0.co;2-g;
RA Romier C., Dominguez R., Lahm A., Dahl O., Suck D.;
RT "Recognition of single-stranded DNA by nuclease P1: high resolution crystal
RT structures of complexes with substrate analogs.";
RL Proteins 32:414-424(1998).
CC -!- FUNCTION: Hydrolyzes only single-stranded DNA and RNA without apparent
CC specificity for bases. {ECO:0000250|UniProtKB:Q9SXA6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.30.1;
CC Evidence={ECO:0000250|UniProtKB:Q9SXA6};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:9726413};
CC Note=Binds 3 divalent metal cations. {ECO:0000269|PubMed:9726413};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the nuclease type I family. {ECO:0000305}.
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DR PIR; S17828; S17828.
DR PDB; 1AK0; X-ray; 1.80 A; A=1-270.
DR PDBsum; 1AK0; -.
DR AlphaFoldDB; P24289; -.
DR SMR; P24289; -.
DR ChEMBL; CHEMBL4802006; -.
DR DrugBank; DB03011; Adenosine-5'-(Dithio)Phosphate.
DR DrugBank; DB02980; Thymidine-5'-(dithio)phosphate.
DR iPTMnet; P24289; -.
DR EvolutionaryTrace; P24289; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Glycoprotein; Hydrolase; Metal-binding; Nuclease; Secreted; Zinc.
FT CHAIN 1..270
FT /note="Nuclease P1"
FT /id="PRO_0000058003"
FT REGION 116..164
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
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:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 6
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
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:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 73..78
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 116
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 126
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT BINDING 153
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
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:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0"
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 ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0"
FT DISULFID 72..217
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT DISULFID 80..85
FT /evidence="ECO:0000269|PubMed:9726413,
FT ECO:0007744|PDB:1AK0"
FT VARIANT 270
FT /note="Missing"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1AK0"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:1AK0"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:1AK0"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1AK0"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1AK0"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1AK0"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 166..181
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1AK0"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1AK0"
FT HELIX 236..263
FT /evidence="ECO:0007829|PDB:1AK0"
SQ SEQUENCE 270 AA; 29227 MW; FA9D25FE75A526EF CRC64;
WGALGHATVA YVAQHYVSPE AASWAQGILG SSSSSYLASI ASWADEYRLT SAGKWSASLH
FIDAEDNPPT NCNVDYERDC GSSGCSISAI ANYTQRVSDS SLSSENHAEA LRFLVHFIGD
MTQPLHDEAY AVGGNKINVT FDGYHDNLHS DWDTYMPQKL IGGHALSDAE SWAKTLVQNI
ESGNYTAQAI GWIKGDNISE PITTATRWAS DANALVCTVV MPHGAAALQT GDLYPTYYDS
VIDTIELQIA KGGYRLANWI NEIHGSEIAK
