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
//