ID L5LVM9_MYODS Unreviewed; 278 AA.
AC L5LVM9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Deoxyribonuclease {ECO:0000256|PIRNR:PIRNR000988};
GN ORFNames=MDA_GLEAN10007738 {ECO:0000313|EMBL:ELK30085.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK30085.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the DNase I family.
CC {ECO:0000256|ARBA:ARBA00007359, ECO:0000256|PIRNR:PIRNR000988}.
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; KB107323; ELK30085.1; -; Genomic_DNA.
DR RefSeq; XP_015419511.1; XM_015564025.1.
DR AlphaFoldDB; L5LVM9; -.
DR GeneID; 102755462; -.
DR CTD; 1775; -.
DR eggNOG; ENOG502SGB6; Eukaryota.
DR OrthoDB; 5396078at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IEA:UniProtKB-EC.
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:SF29; DEOXYRIBONUCLEASE-1-LIKE 2; 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 Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000988-2};
KW Endonuclease {ECO:0000256|PIRNR:PIRNR000988};
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:UP000010556};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..278
FT /note="Deoxyribonuclease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003970648"
FT DOMAIN 26..268
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR000988-1"
FT ACT_SITE 150
FT /evidence="ECO:0000256|PIRSR:PIRSR000988-1"
FT DISULFID 189..225
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000988-2"
SQ SEQUENCE 278 AA; 30896 MW; 8F4D88D3FB7E9225 CRC64;
MGRPRALLAA LWALGAAGAA ALRIGAFNIQ SFGDSKVLDS DCASVIAQIL AGYDITLVQE
VRDPDLSAVS MLMEQINSVS RHQYSYVSSE PLGRDQYKEM YLFVYRKDAV SVVDTYQYPD
PEDTFSREPF VVKFSAPNSA AKELVLVPLH AAPHHAVAEI DALYDVYLDI IDKWGTDDML
FLGDFNADCS YVKEQDWPSI RLRSSEVFKW LIPDSADTTV GNSDCAYDRI VVCGAHLRRS
LKPQSATVHN FQEVFGLDQT QALAISDHFP VEVTLKPH
//
