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Database: UniProt
Entry: A0A3Q3WDW8_MOLML
LinkDB: A0A3Q3WDW8_MOLML
Original site: A0A3Q3WDW8_MOLML 
ID   A0A3Q3WDW8_MOLML        Unreviewed;       289 AA.
AC   A0A3Q3WDW8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Deoxyribonuclease {ECO:0000256|PIRNR:PIRNR000988};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000012843.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000012843.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-
CC         phosphooligonucleotide end-products.; EC=3.1.21.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000688};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.
CC       Secreted {ECO:0000256|ARBA:ARBA00004613}. Zymogen granule
CC       {ECO:0000256|ARBA:ARBA00024324}.
CC   -!- SIMILARITY: Belongs to the DNase I family.
CC       {ECO:0000256|ARBA:ARBA00007359, ECO:0000256|PIRNR:PIRNR000988}.
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DR   AlphaFoldDB; A0A3Q3WDW8; -.
DR   STRING; 94237.ENSMMOP00000012843; -.
DR   Ensembl; ENSMMOT00000013055.1; ENSMMOP00000012843.1; ENSMMOG00000009865.1.
DR   OMA; KMSNQTV; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0042588; C:zymogen granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0004536; F:DNA nuclease activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR   CDD; cd10282; DNase1; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR018057; Deoxyribonuclease-1_AS.
DR   InterPro; IPR016202; DNase_I.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   PANTHER; PTHR11371; DEOXYRIBONUCLEASE; 1.
DR   PANTHER; PTHR11371:SF27; DEOXYRIBONUCLEASE-1; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   PIRSF; PIRSF000988; DNase_I_euk; 1.
DR   PRINTS; PR00130; DNASEI.
DR   SMART; SM00476; DNaseIc; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS00919; DNASE_I_1; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000988-2};
KW   Endonuclease {ECO:0000256|PIRNR:PIRNR000988};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000988};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR000988};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..289
FT                   /note="Deoxyribonuclease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018785586"
FT   DOMAIN          28..275
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000988-1"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000988-1"
FT   DISULFID        125..128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000988-2"
FT   DISULFID        197..233
FT                   /note="Essential for enzymatic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000988-2"
SQ   SEQUENCE   289 AA;  32687 MW;  C9C7F599BD224ABC CRC64;
     LTTKMHSVCA FGLFLALLHL SNSLLLGAFN IKTFGNKKAS NMTLMNIIST IVHRYDIILI
     QEVRDNNLSA TKKLMERVNK GSHPFRYSHI VSEPLGRSSY KERYLFLYRE ETVSVAKSYT
     YDDGCESCGT DTFSREPFVV MFSSKYTAVR DFVLIPQHTS PDFAVAELNA LYDVVADVRT
     RWKTKDIVLL GDFNAGCNYV VDSEWQQIRL FTDKNFHWLI KNDADTTVTT TNCPYDRIVV
     TNDMMRGVVP GSAETYNYMM DLALSHSLAL AVSDHFPVEV QLAGKALAV
//
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