ID A0A1E4T1G0_9ASCO Unreviewed; 1403 AA.
AC A0A1E4T1G0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=CANARDRAFT_198612 {ECO:0000313|EMBL:ODV85564.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV85564.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; KV453852; ODV85564.1; -; Genomic_DNA.
DR STRING; 983967.A0A1E4T1G0; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000094801; 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 Reference proteome {ECO:0000313|Proteomes:UP000094801};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 493..609
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 157856 MW; F1F0CA9E453EEF68 CRC64;
MSDFEDDDFI MEDSPPPTST KKKQPLSNST NTTSNSAAPK KQKTSASDQY QKLSQLEHIL
KRPDTYIGSV ERIESEQWVL NEEMETMEKK TVSIVPGLFK IFDEILVNAA DNKIRDPSMK
KIDIKIDPEN NVISVRNDGK GIPVEIHDKE QIYIPELIFG NLLTSSNYDD DQKKVTGGRN
GFGAKLCNIF STEFTIQTAD KSDNKLYSQT WKDNMSKAGK AKITAMKSQA EFTEVTFKPD
LAKFNMENLD EDILGVLKRR VYDLCGTVRG VKVSLNGKLL KINNFKQYVE MYVRALEKAK
NLDDGTPEPV KLEDGKLLPP AENLPTVVHQ IVDDRWEIAF SLSDGNFNQV SFVNSIATTS
GGTHVENVAN LLVTKIMDQI KKKNKKAMIK PFQIKNNMFL FINCLIENPA FTSQTKEQLT
TRASQFGGKK LELPDLFVKR VLNSGIVDNV MNIVAANADK ALKKNDGSRK SRITGYPKLE
DANKAGTKEG GKCTLILTEG DSALTLAVAG LAVVGRDYYG CYPLRGKMLN VREASADQIM
KNAEIQAIKQ IMGLQHKKRY DITNVSSLRY GHIMIMTDQD HDGSHIKGLI INFLETSFPG
LLEIPEFLIE FITPIVKVTI MSGPKKKSVI SFYNMPEYEE WRDTEGKTCS YKQKYYKGLG
TSSAQEAREY FSRLDKHLKK FHSLVEDDKA LIDLAFSKKK ADDRKEWLRG FVPGTFLDPT
LQVIPISDFI NKELILFSMA DNIRSIPSVL DGFKPSQRKI LYGCYKRNLN GEIKVSQLAG
YIGEHTGYHH GDASLIQSIV SLAQDFVGAN NLNILKPLGG FGSRAVGGKD ASAPRYIFTE
LTPITRKAFN PEDNPLLTYL QDDEQTVEPE WFLPVLPMLL VNGSDGIGSG WSTNIPPFNP
KDIIHNIRAL MTGDEMMDMI PWFKGWEGTI TRVSSDRFKV EGNIEEIDEN TLEITELPAR
MWTITMKEYL LLGLGGNEKQ KPWIKDMEEQ HGVGIRFIVK LSDEEMEKAR RTGLKEKFKL
ISSISTSNMV AFDPQGRIKK YDHVNQIIED YYHVRLEYYQ RRKDYLATQF SNQLEKLSCQ
ARFVKMIIEN ELVVSNRKRA ALIEELQKLN FPGFDKNGVV IRVKAEEISS DDDDDASAAA
DTTLTTTVVN NNTSVASAYD YLLGMQIWAL TRERYEKLLK QKDEKETELN ILLGKSAKDL
WNEDLDAFLI AWDDFLRDDE ESRRSAVPDA NGKKKRAPVR KPKLPLKSNK ITMLDDDAVA
PKEETSKKAA EPEFKSVFGS NKVKESSSPG QNFSNFSAAF SAFSGDATGV DKNDQAPKKA
SSIFQKSKKP ASNPKKIISS EDEDVELHSL NSDSEDEVVI PAARSAAVGS RRKAAPRKSY
AIDSFDEDDE VSEDDDESYD DFE
//
