ID A0A099P7T3_PICKU Unreviewed; 1396 AA.
AC A0A099P7T3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=JL09_g642 {ECO:0000313|EMBL:KGK40294.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK40294.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
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:KGK40294.1}.
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; JQFK01000003; KGK40294.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:C5L36_0C09810; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR Proteomes; UP000029867; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 462..578
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 257..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 158115 MW; 7CE03816FE5B29B8 CRC64;
MSSDYSDEEP HILKRPDTYI GSVERHTSEQ WVYNEDLKCM EKKTVSIVPG LFKIFDEILV
NAADNKIRDP SMKRIDVIIN EEENVISVKN DGKGIPIEIH DKENIYIPEL IFGNLLTSSN
YDDDQKKVTG GRNGYGAKLC NIFSTEFTVH TADMSHGKEY TQVWRNNMSE VGKPKILNFK
KKNEFTEIIF KPDLSKFGME KLDHDILGVF KRRVYDLCGS VRGIRVTLNG ELLKINNFKQ
YVELYVKAIN KSKEERPHIP VKIETEDGTP LNGESEANTE TSSTPEPSLN ENLPTIVHEI
INDRWEIAFC ISDGSFNQVS FVNSIATTLG GTHVDYVANM LCGKITEQIK KKNKKAIIKP
FQIKSKMFLF INCLVENPAF TSQTKEYLTT QPSKFGGKRL ELPEKFIKKI LNTGIIDEVL
DIVQANADKA LKKTDGAKKS RITGYPKLED ANKAGTREGY KCTLILTEGD SAKSLAVQGL
AVVGRNYYGC FPLRGKVLNV REASTDQIMK NGAIQAIKQI MGLQHKKHYG PDDIKSLRYG
RIMIMADQDH DGSHIKGLLI NFLEASFPGL LEIPNFLIEF ITPIVKITIM SGPNRRKTIP
FYSMPEYEQW RETEGSTCSY KQKYYKGLGT SSAQEMREYF TQLDKHLKRF DALRDEDKSS
IDLAFSKKKA DDRKEWLRNY QPGTYLDSTL SDIPISEFIN KELILFSMAD NVRSIASVMD
GFKPVQRKIL YACYKRNLRD EIKVSQLEGY IAEHTGYHHG DASLMQSIIG LAQDFVGSNN
INLLVPHGGF GSRAAGGKDA AAARYIFTEL SAITRKIFNP LDNPLLTYVQ DDEQTVEPEW
YTPVLPMLLV NGCEGIGSGW STSIPPFNPR DIIENIRLLM DGKEMKEMTP WFKGWTGAII
HEPSKDRWRL EGIIEELDDN TLAISELPAR MWTITMKEFL LNALAGNDKQ KPWIKDMEEE
HGVGVRFIVK LSDEEMEKTR RIGLVERFKL TNTVSSSNMV AFDPSGKIKR YSHANEIIRD
FYYVRLEYYQ KRKNYLVKEY SNQLEKISAQ AKFVKLIIDG ELVVGNKKKT VLIEELRNLD
FPGFDKKNEP IQMKFSSIKD EEEEENDDEV AAPLVDPSAT ADTTETGLIV SNKKTSSMLY
DYLLGMPIWS LTKERYEALL KVRGEKEELL NTLLQKSPKD LWNEDIDEFL AEWEKFLIED
EERKVSSVTG NDNGSTKRKR RAPAKKRETA IKKATVKKES VNNGPAKKKA KTAEAPPPVT
DSVKKSEDIN DFDSIFENFK KVTDTPTSTV ATSSSASSLP LNSEKSQTKA ASKTPVKSKE
APRKKKTAKI VESDISDDES DGSAEFSMSD SNDGEEVVVA PRATRNRRNR TPVKSYTLES
DGEASVIELS EDEEYV
//
