ID A0A1E3PNV1_9ASCO Unreviewed; 1303 AA.
AC A0A1E3PNV1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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};
DE Flags: Fragment;
GN ORFNames=NADFUDRAFT_21822 {ECO:0000313|EMBL:ODQ67105.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ67105.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ67105.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ67105.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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}.
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DR EMBL; KV454407; ODQ67105.1; -; Genomic_DNA.
DR STRING; 857566.A0A1E3PNV1; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000095009; 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; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000095009};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 544..658
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1265..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1303
FT /evidence="ECO:0000313|EMBL:ODQ67105.1"
SQ SEQUENCE 1303 AA; 148100 MW; 6A4910985BB647A2 CRC64;
MSDISDDDFI IDDNDSDFVI DEPVIKPAAK KKNIVGAKRA PLATKKTPVA KKAKTTTKPI
IRKSPFDIIP ETTPIPVPLL NSASTPPVDY EAPNNNAVDI EKSASSTYQK LTQLEHILKR
PDTYIGSVEP TDQQMWVYDE TANSMVWKSV TIVPGLYKIF DEILVNAADN KIRDPAMDEL
RVDIDVENNT VSIFNNGKGI PIQMHEKENM YIPELIFGNL LTSSNYDDDQ KKVTGGRNGY
GAKLCNIFST EFILETADMA TNLVYKQVWS GNMSKVTTPR ITTPKKPTQY TKIIFKPDLK
LFNMTKIDTD LVSVMMRRVY DLAGTNSKVK VYLNKERLKV KDFKSYVEMF LKAMAKAEYE
QNGLVADEAA LAALPKPKIV HEIINDRWEV AFGVSDGNFN QVSFVNSIAT TSGGTHVNYI
ADQLTTKILE HVKKKAKSAQ LRISQIRGNM FLFVNCLIEN PAFTSQTKEQ LTTKVSAFGS
KCVLPEDFVK KVLKTSIVDS VMEIASRNAD KDLKKTDGNR KKRLTGFVNL EDANKAGTRE
GYKCTLILTE GISALSLAVA GLAVVGRDYY GAYPLRGKLL NVREASHDQI MKNNEIQAIK
QIMGLQHKKH YTSTNELRYG HIMIMTDQDH DGSHIKGLII NFLDSSFPGL LEIPGFLVEF
VTPIVKVSIK RGNRIVKVIP FFSMPEFEYW RDTEGRNCSW THKYYKGLGS SKPEESREYF
SQLDNHFKTF HALQNGDQEL IELAFSKKKT DHRKDWLRNF QPGTHLDHEI TEIPISEFIN
KELILFSMAD NIRSIPSVLD GFKPGQRKVL YACFKRNLKS EIKVGSLAAY AVEHTGYHHG
EQSLVQTIIG LAQDFVGSNN LYLLNPNGSF GTRATGGKDA AAARYIFTEL NELTRKIFPI
SDDPLLNYLM DDKDTVEPEW YTPIIPMVLV NGAEGIGTGW STNIPCYNPL EIVDNLRKLM
AGEEMVSLSP WYRGWNGILE PMGPERFRTS GIINKIDDNT IEITELPIKM WTISMKEFLL
NNIKKDRNDS GWIEDMTEDH GIGIRFVVKL TEAEMRKTES IGFYERFKLN MSISLSNMIA
FDAQNRIKKY ASPEEIISDF YPIRLDFYQR RKDNLTNQLQ NQLEKLSQQA RFVKMIIEKE
LVVTKRKRDE IVKELQTLEF PRIGKDGIPV FSRIADDEVE LGDAEEDDDG LSRKQRILIS
DFDYLLGMPI WSLTYERYEK LLKERNGKET ELIALLRLSA KDLWNIDLDD FVKGWNNFME
FDHEKRSSLI PKKKSTAKKG RKTKVDDDDF APGATKKKKT AVK
//
