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Database: UniProt
Entry: A0A4T0X6Z3_9ASCO
LinkDB: A0A4T0X6Z3_9ASCO
Original site: A0A4T0X6Z3_9ASCO 
ID   A0A4T0X6Z3_9ASCO        Unreviewed;       331 AA.
AC   A0A4T0X6Z3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   08-NOV-2023, entry version 12.
DE   RecName: Full=Endonuclease {ECO:0000256|RuleBase:RU366055};
DE            EC=3.1.30.- {ECO:0000256|RuleBase:RU366055};
GN   ORFNames=CANINC_000708 {ECO:0000313|EMBL:TID30792.1};
OS   [Candida] inconspicua.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=52247 {ECO:0000313|EMBL:TID30792.1, ECO:0000313|Proteomes:UP000307173};
RN   [1] {ECO:0000313|EMBL:TID30792.1, ECO:0000313|Proteomes:UP000307173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 180 {ECO:0000313|EMBL:TID30792.1,
RC   ECO:0000313|Proteomes:UP000307173};
RX   PubMed=31105748; DOI=10.3389/fgene.2019.00383;
RA   Mixao V., Hansen A.P., Saus E., Boekhout T., Lass-Florl C., Gabaldon T.;
RT   "Whole-Genome Sequencing of the Opportunistic Yeast Pathogen Candida
RT   inconspicua Uncovers Its Hybrid Origin.";
RL   Front. Genet. 10:383-383(2019).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU366055};
CC   -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC       {ECO:0000256|ARBA:ARBA00010052, ECO:0000256|RuleBase:RU366055}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TID30792.1}.
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DR   EMBL; SELW01000121; TID30792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4T0X6Z3; -.
DR   STRING; 52247.A0A4T0X6Z3; -.
DR   Proteomes; UP000307173; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd00091; NUC; 1.
DR   Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 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:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR   PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW   ECO:0000256|RuleBase:RU366055}; Hydrolase {ECO:0000256|RuleBase:RU366055};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR640255-2,
KW   ECO:0000256|RuleBase:RU366055};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU366055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000307173};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..331
FT                   /note="Endonuclease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020685491"
FT   DOMAIN          87..306
FT                   /note="DNA/RNA non-specific endonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00892"
FT   DOMAIN          88..306
FT                   /note="Extracellular Endonuclease subunit A"
FT                   /evidence="ECO:0000259|SMART:SM00477"
FT   REGION          25..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..47
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ   SEQUENCE   331 AA;  36653 MW;  169F591F23B4BADF CRC64;
     MFKHGFVLPA VIPGASALFF WGGSSSSTST PTQAPPVPPP PPMGAPLGAP NNGKDTSTTK
     STNNADDINP SAFFKYGFPG PVHDMGTHSE FVSVYDRQTR NPYYVVEHIT ADSIKKGDTN
     GDRKNSVFKE DESIPVKFRA LLRDYFRSGY DRGHQAPAAD AKFSQTAMDE TFYLSNMSPQ
     VGAGFNRDYW AHFEDFCRRL TGEYRSVRIV TGPLYLPKKC DDGKYRVTYE VIGNPPNIAV
     PTHFFKLVVG EKSLKRNAGS EDIAVAAFVM PNAIIPNEVP LKSFQVPVES LERSSGLEFL
     KLVPQKQVKE LCKEVSCEII VREFNNALPK K
//
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