ID A0A091D3L7_FUKDA Unreviewed; 279 AA.
AC A0A091D3L7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Deoxyribonuclease {ECO:0000256|PIRNR:PIRNR000988};
GN ORFNames=H920_13786 {ECO:0000313|EMBL:KFO24790.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO24790.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO24790.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO24790.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KN123497; KFO24790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D3L7; -.
DR STRING; 885580.ENSFDAP00000017664; -.
DR eggNOG; ENOG502QQFT; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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:0003779; F:actin binding; IEA:UniProtKB-KW.
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; IPR033125; DNASE_I_2.
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.
DR PROSITE; PS00918; DNASE_I_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
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:UP000028990};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..279
FT /note="Deoxyribonuclease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001872967"
FT DOMAIN 24..271
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR000988-1"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR000988-1"
FT DISULFID 120..123
FT /evidence="ECO:0000256|PIRSR:PIRSR000988-2"
FT DISULFID 192..228
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000988-2"
SQ SEQUENCE 279 AA; 31206 MW; EFA6890D07B308B6 CRC64;
MKLTPVLLAL ASLLQVAVPL KIAAFNIRTF GETKMANATL SNYIVQILSR YDIALIQEVR
DTYLTAVGKL LDELNRDVPD TYHFVVSEPL GRNSYKEQYL YVFRPDRVSV LDSYQYDDGC
EPCGNDTFSR EPAIVRFSSP FTKVRDFAVV PLHAAPTEAV AEIDALYDVY LDVRKKWGLE
DIMLMGDFNA GCSYVSPSQW SSIRLRTNPT FQWLISDTAD TTVTSTHCAY DRVVVAGSLL
QSAVVLDSAA PFDFQAAYVL TDQLAQAISD HYPVEVMLK
//
