ID A0A1W0A0R4_9STRA Unreviewed; 299 AA.
AC A0A1W0A0R4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Endonuclease {ECO:0008006|Google:ProtNLM};
GN ORFNames=THRCLA_03862 {ECO:0000313|EMBL:OQS03847.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS03847.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS03847.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS03847.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {ECO:0000256|ARBA:ARBA00010052}.
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:OQS03847.1}.
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; JNBS01000748; OQS03847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0A0R4; -.
DR STRING; 74557.A0A1W0A0R4; -.
DR OrthoDB; 5487361at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR640255-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217}.
FT DOMAIN 55..273
FT /note="DNA/RNA non-specific endonuclease"
FT /evidence="ECO:0000259|SMART:SM00892"
FT DOMAIN 56..273
FT /note="Extracellular Endonuclease subunit A"
FT /evidence="ECO:0000259|SMART:SM00477"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ SEQUENCE 299 AA; 33572 MW; FA2B1E44A233C3D6 CRC64;
MGALVGAVAT LSVVDLLIRD EQQEEEKKSS IVPQEQELLH EAIRYGVPSM QNVKIRQGYA
LGYDRRLRNA AWVAEYITKE SLEKNGDVNR LKSSFKVDPT TPTAFRVTPA EYQNSGYDRG
HLAPARDMNS SQPAINESFL MTNISPQVSK FNRGYWSRLE GFVRHLANYY GAAYVITGPL
FLPQKTKEGD GYTVSYPIIG TPLNGIAVPT HFFKVILIEK KGKKGQKLKY LATGFVLPNQ
GIADKIPLSS FVMPLDMIER YSGLVFFDKL ERPSLLPLCD DTKCELKAIE FQKQVKAIE
//