ID J8PZX9_SACAR Unreviewed; 1427 AA. AC J8PZX9; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 20-DEC-2017, entry version 31. DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094}; DE EC=5.99.1.3 {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; OC Saccharomycetes; 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 CC breakage and subsequent rejoining of DNA strands. Topoisomerase II CC makes double-strand breaks. {ECO:0000256|RuleBase:RU362094}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|RuleBase:RU362094}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. CC {ECO:0000256|RuleBase:RU362094}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblFungi; EJS41976; EJS41976; SU7_2974. DR OrthoDB; EOG092C08KH; -. DR Proteomes; UP000006968; Chromosome XIV. DR GO; GO:0034506; C:chromosome, centromeric core domain; IEA:EnsemblFungi. DR GO; GO:0097047; C:DNA replication termination region; IEA:EnsemblFungi. DR GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi. DR GO; GO:0000795; C:synaptonemal complex; IEA:EnsemblFungi. DR GO; GO:0035327; C:transcriptionally active chromatin; IEA:EnsemblFungi. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi. DR GO; GO:0140082; F:SUMO-ubiquitin ligase activity; IEA:EnsemblFungi. DR GO; GO:0006333; P:chromatin assembly or disassembly; IEA:EnsemblFungi. DR GO; GO:0031055; P:chromatin remodeling at centromere; IEA:EnsemblFungi. DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi. DR GO; GO:0006265; P:DNA topological change; IEA:EnsemblFungi. DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblFungi. DR GO; GO:0044774; P:mitotic DNA integrity checkpoint; IEA:EnsemblFungi. DR GO; GO:0051306; P:mitotic sister chromatid separation; IEA:EnsemblFungi. DR GO; GO:0000019; P:regulation of mitotic recombination; IEA:EnsemblFungi. DR GO; GO:0097046; P:replication fork progression beyond termination site; IEA:EnsemblFungi. DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:EnsemblFungi. DR CDD; cd00075; HATPase_c; 1. DR CDD; cd03365; TOPRIM_TopoIIA; 1. DR Gene3D; 1.10.268.10; -; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR Gene3D; 3.90.199.10; -; 1. DR InterPro; IPR024946; Arg_repress-like_C. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR002205; Topo_IIA_A/C. 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; IPR018522; TopoIIA_CS. DR InterPro; IPR031660; TOPRIM_C. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034157; TOPRIM_TopoII. DR PANTHER; PTHR10169; PTHR10169; 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 SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR SUPFAM; SSF56719; SSF56719; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006968}; KW DNA-binding {ECO:0000256|RuleBase:RU362094}; KW Isomerase {ECO:0000256|RuleBase:RU362094}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362094}; KW Reference proteome {ECO:0000313|Proteomes:UP000006968}; KW Topoisomerase {ECO:0000256|RuleBase:RU362094}. FT DOMAIN 443 557 Toprim. {ECO:0000259|PROSITE:PS50880}. FT COILED 1126 1149 {ECO:0000256|SAM:Coils}. 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 //