ID   NUC1_CUNEE              Reviewed;         252 AA.
AC   P81203;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Nuclease C1;
DE            EC=3.1.30.-;
GN   Name=NUC1CE;
OS   Cunninghamella echinulata var. echinulata.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Cunninghamella.
OX   NCBI_TaxID=76406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 15-252, AND PROTEIN SEQUENCE OF 1-49.
RC   STRAIN=ATCC 36190 / DSM 1905 / NRRL 3655;
RX   PubMed=9746353; DOI=10.1046/j.1432-1327.1998.2560112.x;
RA   Ho H.-C., Liu F.-C., Chung J.-G., Chen L.-Y.;
RT   "Purification, characterization and complete amino acid sequence of
RT   nuclease C1 from Cunninghamella echinulata var. echinulata.";
RL   Eur. J. Biochem. 256:112-118(1998).
CC   -!- FUNCTION: This enzyme has both RNase and DNase activity.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- SUBCELLULAR LOCATION: Secreted.
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}.
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; AF043517; AAC78769.2; -; mRNA.
DR   AlphaFoldDB; P81203; -.
DR   SMR; P81203; -.
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; Endonuclease; Hydrolase; Magnesium; Manganese;
KW   Metal-binding; Nuclease; Secreted.
FT   CHAIN           1..252
FT                   /note="Nuclease C1"
FT                   /id="PRO_0000178671"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10047"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   252 AA;  27499 MW;  2FA49B158AAABEC6 CRC64;
     SPNSESILQF GDPGTARDFL ERESYVISYN RRDRVASWTG EHLTADSLKT GDGVDRDHSK
     FKEDPDVPSL FRSTLADYSG SGFDRGHMAP AGDAVATQPA MDQTFYLSNM SPQVGIGFNR
     HYWAYLEGFC RSLTKKFSDV YVFTGPLFLP TKGSDGKYTV TYNVLQGNVA VPTHFYKVIL
     VPQGDNKYAY GAFILPNQAI DTKTPLTNFK VKLTDVEKAS GLTFFDKLDV STLGDLCAAT
     TCAVSSSGGG DA