ID Q9HI41_THEAC Unreviewed; 241 AA. AC Q9HI41; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 29-MAY-2024, entry version 98. DE SubName: Full=Probable apurinic/apyrimidinic endonuclease {ECO:0000313|EMBL:CAC12624.1}; GN OrderedLocusNames=Ta1506 {ECO:0000313|EMBL:CAC12624.1}; OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC OS 15155 / AMRC-C165). OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; OC Thermoplasmataceae; Thermoplasma. OX NCBI_TaxID=273075 {ECO:0000313|EMBL:CAC12624.1, ECO:0000313|Proteomes:UP000001024}; RN [1] {ECO:0000313|EMBL:CAC12624.1, ECO:0000313|Proteomes:UP000001024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165 RC {ECO:0000313|Proteomes:UP000001024}; RX PubMed=11029001; DOI=10.1038/35035069; RA Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C., RA Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.; RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma RT acidophilum."; RL Nature 407:508-513(2000). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Note=Probably binds two magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR604808-2}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|ARBA:ARBA00007092}. 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; AL445067; CAC12624.1; -; Genomic_DNA. DR AlphaFoldDB; Q9HI41; -. DR STRING; 273075.gene:9572738; -. DR PaxDb; 273075-Ta1506m; -. DR EnsemblBacteria; CAC12624; CAC12624; CAC12624. DR KEGG; tac:Ta1506; -. DR eggNOG; arCOG02207; Archaea. DR HOGENOM; CLU_027539_1_3_2; -. DR InParanoid; Q9HI41; -. DR Proteomes; UP000001024; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:TreeGrafter. DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:TreeGrafter. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:TreeGrafter. DR GO; GO:0006284; P:base-excision repair; IEA:TreeGrafter. DR CDD; cd09073; ExoIII_AP-endo; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR020848; AP_endonuclease_F1_CS. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR NCBIfam; TIGR00195; exoDNase_III; 1. DR NCBIfam; TIGR00633; xth; 1. DR PANTHER; PTHR22748; AP ENDONUCLEASE; 1. DR PANTHER; PTHR22748:SF6; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 3: Inferred from homology; KW Endonuclease {ECO:0000313|EMBL:CAC12624.1}; KW Hydrolase {ECO:0000313|EMBL:CAC12624.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2}; KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2}; KW Nuclease {ECO:0000313|EMBL:CAC12624.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001024}. FT DOMAIN 24..232 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" FT ACT_SITE 96 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 135 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 232 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 135 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 137 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 137 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 206 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 232 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" SQ SEQUENCE 241 AA; 28093 MW; 760A2ACF8F6A1293 CRC64; MNGLRAAVKN GAVSVFKQDD YFGIALQETK ADSTSVPEEM YHLGYYLYNN PAKKKGYSGT MSLVREKPID VSYGFENEEG RILNLEFDKF YFINVYFPNA QHGLTRLDMK LDFDEKFLEY SNELRKKKPL IICGDFNVAH EEIDIARPKD NENNAGFTKQ ERDWMTKFLD SGYVDTYRIF MKEGGHYSWW SYRFNARAKN IGWRIDYFVV SDDIRDRVKK AEILETVTGS DHAPVTLEVD L //