ID J8PZX9_SACAR Unreviewed; 1427 AA. AC J8PZX9; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 24-JAN-2024, entry version 61. DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635, ECO:0000256|RuleBase:RU362094}; DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|RuleBase:RU362094}; GN ORFNames=SU7_2974 {ECO:0000313|EMBL:EJS41976.1}; OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS41976.1, ECO:0000313|Proteomes:UP000006968}; RN [1] {ECO:0000313|EMBL:EJS41976.1, ECO:0000313|Proteomes:UP000006968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H-6 / AS 2.3317 / CBS 10644 RC {ECO:0000313|Proteomes:UP000006968}; RX PubMed=23368932; DOI=10.1186/1471-2164-14-69; RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A., RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N., RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.; RT "High quality de novo sequencing and assembly of the Saccharomyces RT arboricolus genome."; RL BMC Genomics 14:69-69(2013). CC -!- FUNCTION: Control of topological states of DNA by transient breakage CC and subsequent rejoining of DNA strands. Topoisomerase II makes double- CC strand breaks. {ECO:0000256|RuleBase:RU362094}. 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 ECO:0000256|RuleBase:RU362094}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}. 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:EJS41976.1}. 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; ALIE01000169; EJS41976.1; -; Genomic_DNA. DR HOGENOM; CLU_001935_1_1_1; -. DR OrthoDB; 1944951at2759; -. DR Proteomes; UP000006968; Chromosome XIV. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt. DR CDD; cd16930; HATPase_TopII-like; 1. DR CDD; cd00187; TOP4c; 1. DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1. DR CDD; cd03365; TOPRIM_TopoIIA; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.30.1490.30; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1. DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR013757; Topo_IIA_A_a_sf. DR InterPro; IPR013759; Topo_IIA_B_C. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR002205; Topo_IIA_dom_A. DR InterPro; IPR001154; TopoII_euk. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR031660; TOPRIM_C. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034157; TOPRIM_TopoII. DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1. DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00521; DNA_topoisoIV; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF16898; TOPRIM_C; 1. DR PRINTS; PR01158; TOPISMRASEII. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU362094}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362094}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000006968}; KW Topoisomerase {ECO:0000256|RuleBase:RU362094}. FT DOMAIN 443..557 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT REGION 1078..1101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1174..1216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1237..1294 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1306..1427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1174..1210 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1251..1275 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1276..1294 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1306..1332 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1358..1374 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1404..1427 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1427 AA; 163173 MW; F65666E8992C325C CRC64; MSVEPTSASD RYQKISQLDH ILKRPDTYIG SVETQEQQQW IYDEETDCMI EKNVTIVPGL FKIFDEILVN AADNKVRDLS MKRIDVNINP EENTIEVKND GKGIPVEIHS KEGIYIPELI FGHLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTEFTLET ADLNAGKKYI QKWEKNMSIC NPPKITSYKK GPSYTKVTFR PDLSRFGMES LDNDILGVMR RRVYDINGSV RGINVYLNGK FLKIRNFKNY VELYLKSLEK KRQLDNGQDA TAQTSIPTIL YERINERWEV AFAVSDISFQ QISFVNSIAT TMGGTHVNYV TDQIVRKISD LLKKKNKKSV KPFQIKNNMF IFINCLVENP AFTSQTKEQL TTRVKDFGSR CEIPNEYINK IMKTDLAIKM FEIADANADN ALKKSDGTRK NRITDYPKLQ DANKAGTKAG YKCTLVLTEG DSALSLAVAG LAVVGRDYYG CYPLRGKMLN VREASSDQIS KNAEIQAIKK IMGLQHRKNY EDTKSLRYGH LMIMTDQDHD GSHIKGLIIN FLESSFPGLL DIEGFLLEFI TPIVKVFITK PKKNTISFYN MPDYEKWKQE ESHKFTWKQK YYKGLGTSLA KDIREYFSNL DKHLKIFHSL QGNDKDYIDL AFSKKKADDR KEWLRQYEPG TVLDPTLKEI PISDFINKEL ILFSLADNIR SIPNVLDGFK PGQRKVLYGC FKKNLKSEIK VAQLAPYVGE CTAYHHGEES LAQTIIGLAQ NFVGSNNIYL LLPNGAFGTR ATGGKDAAAS RYIYTELNKL TRMIFHPSDD PLYKYIQDDE KTVEPEWYLP ILPMVLVNGA EGIGTGWSTY IPPFNPLEIV KNIRHLMNNE EMELMHPWFR GWSGTMEEIE PLRYRMYGRI EQVGSNTLEI TELPARTWTS TIKEYLLLGL SGNDKIKPWI KDMEEQHNDN IKFIITLSPE EMAKTRKIGF YERFKLIAPI SLRNMVAFDP SGKIKKYNSV NEILSEFYYI RLEYYQKRKD HMSEILQWEV EKYSFQVKFI KMIIEKELVV TNKPRKAIIQ ELENLGFPRI NKQGQPYYGS PKTEMAEQID DMRSATSDEE DEESSHEDTE TIVNGPEELY GTYEYLLGMK IWSLTKERYE KLLKQKQEKE TELENLLKLS AKDIWIADLE AFDIGYQEFL KRDKDARGGN VPDKGDKSKG KRKRRLADDD EYDPSKKSKK TTAGKRAKKI KMEDIFFERV LLEQKPVTKG KGPTRIKKEN PASISKLNTE GAEESDPSST SSSSIFDIKK EEDKNESGLS KMSDKFKKIS TIFDKVGSAS ATSRENTPDH LTAATTTKPA AAKTASPKPK PVRKPKKIVA LSDESDLEAL DSYNDGEDGT EDEDDAIPQR PRRQRSARAA SAPKKSYAET IELSDDSFIE DDGEQEQESD ASFNEDN //