NUS1_ASPOR
ID NUS1_ASPOR Reviewed; 287 AA.
AC P24021; Q00235;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Nuclease S1 {ECO:0000303|PubMed:8597544};
DE EC=3.1.30.1 {ECO:0000269|PubMed:28036383};
DE AltName: Full=Deoxyribonuclease S1 {ECO:0000303|PubMed:8597544};
DE AltName: Full=Endonuclease S1 {ECO:0000303|PubMed:8597544};
DE AltName: Full=Single-stranded-nucleate endonuclease {ECO:0000303|PubMed:8597544};
DE Flags: Precursor;
GN Name=nucS {ECO:0000303|PubMed:8597544};
GN ORFNames=AO090001000075 {ECO:0000312|EMBL:BAE56634.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=8597544; DOI=10.1007/bf00169939;
RA Lee B.R., Kitamoto K., Yamada O., Kumagai C.;
RT "Cloning, characterization and overproduction of nuclease S1 gene (nucS)
RT from Aspergillus oryzae.";
RL Appl. Microbiol. Biotechnol. 44:425-431(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [3]
RP PROTEIN SEQUENCE OF 21-287.
RX PubMed=1939022; DOI=10.1093/oxfordjournals.jbchem.a123534;
RA Iwamatsu A., Aoyama H., Dibo G., Tsunasawa S., Sakiyama F.;
RT "Amino acid sequence of nuclease S1 from Aspergillus oryzae.";
RL J. Biochem. 110:151-158(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF 21-287 IN COMPLEX WITH SUBSTRATE
RP AND ZINC, GLYCOSYLATION AT ASN-112 AND ASN-248, DISULFIDE BONDS,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF
RP ASP-65; LYS-68 AND ASN-154, AND ACTIVITY REGULATION.
RX PubMed=28036383; DOI=10.1371/journal.pone.0168832;
RA Koval T., Ostergaard L.H., Lehmbeck J., Norgaard A., Lipovova P.,
RA Duskova J., Skalova T., Trundova M., Kolenko P., Fejfarova K., Stransky J.,
RA Svecova L., Hasek J., Dohnalek J.;
RT "Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae
RT Responsible for Substrate Recognition, Cleavage, Non-Specificity, and
RT Inhibition.";
RL PLoS ONE 11:e0168832-e0168832(2016).
CC -!- FUNCTION: Hydrolyzes only single-stranded DNA and RNA without apparent
CC specificity for bases. {ECO:0000269|PubMed:28036383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.30.1;
CC Evidence={ECO:0000269|PubMed:28036383};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:28036383};
CC Note=Binds 3 divalent metal cations. {ECO:0000269|PubMed:28036383};
CC -!- ACTIVITY REGULATION: Inhibited by inorganic phosphate (Pi).
CC {ECO:0000269|PubMed:28036383}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mg/ml for ssDNA {ECO:0000269|PubMed:28036383};
CC KM=0.16 mg/ml for RNA {ECO:0000269|PubMed:28036383};
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the nuclease type I family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D45902; BAA08310.1; -; Genomic_DNA.
DR EMBL; AP007154; BAE56634.1; -; Genomic_DNA.
DR PIR; JX0180; JX0180.
DR RefSeq; XP_001818636.1; XM_001818584.2.
DR PDB; 5FB9; X-ray; 1.50 A; A/B=21-287.
DR PDB; 5FBA; X-ray; 1.80 A; A=21-287.
DR PDB; 5FBB; X-ray; 1.75 A; A/B=21-287.
DR PDB; 5FBC; X-ray; 1.75 A; A=21-287.
DR PDB; 5FBD; X-ray; 1.75 A; A=21-287.
DR PDB; 5FBF; X-ray; 1.04 A; A=21-287.
DR PDB; 5FBG; X-ray; 1.97 A; A/B=21-287.
DR PDBsum; 5FB9; -.
DR PDBsum; 5FBA; -.
DR PDBsum; 5FBB; -.
DR PDBsum; 5FBC; -.
DR PDBsum; 5FBD; -.
DR PDBsum; 5FBF; -.
DR PDBsum; 5FBG; -.
DR AlphaFoldDB; P24021; -.
DR SMR; P24021; -.
DR iPTMnet; P24021; -.
DR EnsemblFungi; BAE56634; BAE56634; AO090001000075.
DR GeneID; 5990607; -.
DR KEGG; aor:AO090001000075; -.
DR VEuPathDB; FungiDB:AO090001000075; -.
DR HOGENOM; CLU_044365_0_0_1; -.
DR OMA; WDTSIPN; -.
DR PRO; PR:P24021; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IDA:AspGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IDA:AspGD.
DR CDD; cd11010; S1-P1_nuclease; 1.
DR Gene3D; 1.10.575.10; -; 1.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
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; Reference proteome;
KW Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1939022"
FT CHAIN 21..287
FT /note="Nuclease S1"
FT /id="PRO_0000058010"
FT REGION 135..183
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 21..26
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 21
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 65..71
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF"
FT BINDING 80..83
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBD,
FT ECO:0007744|PDB:5FBF, ECO:0007744|PDB:5FBG"
FT BINDING 80
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 93..98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT SITE 65
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:28036383"
FT SITE 68
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9,
FT ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB,
FT ECO:0007744|PDB:5FBC, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT DISULFID 92..236
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT DISULFID 100..105
FT /evidence="ECO:0000269|PubMed:28036383,
FT ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA,
FT ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC,
FT ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF,
FT ECO:0007744|PDB:5FBG"
FT MUTAGEN 65
FT /note="D->N: Impaired activity."
FT /evidence="ECO:0000269|PubMed:28036383"
FT MUTAGEN 68
FT /note="K->N: Reduced activity."
FT /evidence="ECO:0000269|PubMed:28036383"
FT MUTAGEN 154
FT /note="N->A,S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:28036383"
FT CONFLICT 140
FT /note="I -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:5FBF"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:5FBF"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:5FBF"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:5FBF"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5FBF"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:5FBF"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:5FBF"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:5FBF"
FT TURN 203..207
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:5FBF"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:5FBF"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:5FBF"
FT HELIX 255..283
FT /evidence="ECO:0007829|PDB:5FBF"
SQ SEQUENCE 287 AA; 31146 MW; 604713F2DD57B6D9 CRC64;
MPRLLPISAA TLALAQLTYG WGNLGHETVA YIAQSFVASS TESFCQNILG DDSTSYLANV
ATWADTYKYT DAGEFSKPYH FIDAQDNPPQ SCGVDYDRDC GSAGCSISAI QNYTNILLES
PNGSEALNAL KFVVHIIGDI HQPLHDENLE AGGNGIDVTY DGETTNLHHI WDTNMPEEAA
GGYSLSVAKT YADLLTERIK TGTYSSKKDS WTDGIDIKDP VSTSMIWAAD ANTYVCSTVL
DDGLAYINST DLSGEYYDKS QPVFEELIAK AGYRLAAWLD LIASQPS
