ID A0A0J8U3I0_COCIT Unreviewed; 304 AA. AC A0A0J8U3I0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 24-JAN-2024, entry version 26. DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895}; DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895}; GN ORFNames=CISG_08743 {ECO:0000313|EMBL:KMU81332.1}; OS Coccidioides immitis RMSCC 3703. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides. OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU81332.1, ECO:0000313|Proteomes:UP000054559}; RN [1] {ECO:0000313|Proteomes:UP000054559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559}; RX PubMed=20516208; DOI=10.1101/gr.103911.109; RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J., RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D., RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A., RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J., RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R., RA Taylor J.W., Rounsley S.D.; RT "Population genomic sequencing of Coccidioides fungi reveals recent RT hybridization and transposon control."; RL Genome Res. 20:938-946(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; 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; DS268197; KMU81332.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0J8U3I0; -. DR STRING; 454286.A0A0J8U3I0; -. DR Proteomes; UP000054559; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR013757; Topo_IIA_A_a_sf. DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1. DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000054559}. FT REGION 31..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 122..304 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 41..57 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..166 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..212 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..246 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 257..298 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 304 AA; 34438 MW; 0A183FD7548E68B4 CRC64; MIIDGKLVIS KKRKAKLIEE LKEKGFKPIP KAVDAAKEGE NEPAVEEEEE SEEDEQLSSD VFDYLLGMPL WSLTQERVEK LLRQIGDKEL EIDALIKLSK EDLWKRDLDE FITEWRNQLE DEERRAKKAR SYGRRTSTKL KTAGRAPAGK KRKALGDDDD SDFAPKAKKA TVVNKVKPKG GLLDYLSKPA AKSKTKATRL DSTKEIESRF EQKPRGGYYI SFSDSEDDKD DILSKETDEK ARDPTRPPSP DIPAISDSDD YKPKPAKKAT AVSKKAPKEH DDSDTEIVQR HASEQIAHPK AYRI //