ID   NUC1_SYNRA              Reviewed;         320 AA.
AC   P81204; Q9UVC4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Nuclease;
DE            EC=3.1.30.-;
DE   AltName: Full=Sr-nuclease;
DE   Flags: Precursor;
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-320, AND MUTAGENESIS OF
RP   HIS-155.
RX   PubMed=10191256; DOI=10.1042/bj3390261;
RA   Ho H.-C., Liao T.-H.;
RT   "Protein structure and gene cloning of Syncephalastrum racemosum
RT   nuclease.";
RL   Biochem. J. 339:261-267(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 71-110 AND 145-153, COFACTOR, SUBUNIT, AND
RP   GLYCOSYLATION.
RX   PubMed=8489265; DOI=10.1006/abbi.1993.1254;
RA   Chen L.-Y., Ho H.-C., Tsai Y.-C., Liao T.-H.;
RT   "Deoxyribonuclease of Syncephalastrum racemosum -- enzymatic properties and
RT   molecular structure.";
RL   Arch. Biochem. Biophys. 303:51-56(1993).
CC   -!- FUNCTION: This enzyme has both RNase and DNase activity.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8489265};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:8489265};
CC   -!- SUBUNIT: Homodimer; as a result of non-covalent interactions and not
CC       through the disulfide linkages between the two monomers.
CC       {ECO:0000269|PubMed:8489265}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:8489265}.
CC   -!- MISCELLANEOUS: The active site contains 1 hydrated divalent metal
CC       cation that has only 1 direct interaction with the protein; all other
CC       interactions are via water molecules. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AF043515; AAC69516.1; -; mRNA.
DR   EMBL; AF043727; AAF21658.1; -; Genomic_DNA.
DR   PIR; S33276; S33276.
DR   AlphaFoldDB; P81204; -.
DR   SMR; P81204; -.
DR   iPTMnet; P81204; -.
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   Gene3D; 3.40.570.10; -; 1.
DR   InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   InterPro; IPR040255; Non-specific_endonuclease.
DR   PANTHER; PTHR13966; PTHR13966; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SUPFAM; SSF54060; SSF54060; 1.
DR   PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; Secreted; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..70
FT                   /evidence="ECO:0000269|PubMed:10191256,
FT                   ECO:0000269|PubMed:8489265"
FT                   /id="PRO_0000019922"
FT   CHAIN           71..320
FT                   /note="Nuclease"
FT                   /id="PRO_0000019923"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10047"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8489265"
FT   DISULFID        312..317
FT   MUTAGEN         155
FT                   /note="H->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10191256"
SQ   SEQUENCE   320 AA;  35316 MW;  9C29F093ABB7A7DE CRC64;
     MPIIRRTSRA TASSSKSATS SILRQAILVF TGFLLGALFM VFVPSLYNAA EPSSLHRLMN
     PIRRNTLSAR ASSDILKLGN PGPVSDLLER SGYILSYNRR DRLAHWVGEH LTSASLQAGQ
     GVDRDKSNFQ EDTDIPEMFR AHLKDYVSSG YDRGHQAPAA DDLSSQEAMD ETFLLSNMAP
     QVGVGFNRHY WAYLEGFMRD LTQNFTDVYV YTGPLFLPSA ASTGRKNPAY SIEYPFLGAT
     TPNVPVPTHF FKIALTTTAS SEYALGAFVL PNQAIDSSTP LTNFKVELEA IEKAAGLVFF
     DKLDRSKFAD LCSKTTCQVR