ID Q76C33_TRIVC Unreviewed; 1089 AA.
AC Q76C33;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 104.
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 Name=top2 {ECO:0000313|EMBL:BAD02210.1};
OS Trichophyton verrucosum (Cattle ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63417 {ECO:0000313|EMBL:BAD02210.1};
RN [1] {ECO:0000313|EMBL:BAD02210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KMU 4066 {ECO:0000313|EMBL:BAD02210.1};
RX PubMed=14527738; DOI=10.1016/S0923-1811(03)00150-6;
RA Kanbe T., Suzuki Y., Kamiya A., Mochizuki T., Kawasaki M., Fujihiro M.,
RA Kikuchi A.;
RT "Species-identification of dermatophytes Trichophyton, Microsporum and
RT Epidermophyton by PCR and PCR-RFLP targeting of the DNA topoisomerase II
RT genes.";
RL J. Dermatol. Sci. 33:41-54(2003).
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 ---------------------------------------------------------------------------
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; AB110283; BAD02210.1; -; Genomic_DNA.
DR AlphaFoldDB; Q76C33; -.
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 Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 425..539
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1043..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1070
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAD02210.1"
FT NON_TER 1089
FT /evidence="ECO:0000313|EMBL:BAD02210.1"
SQ SEQUENCE 1089 AA; 123668 MW; 87006472166830D0 CRC64;
KITQLEHILK RPDTYIGSVE RTEKHMWVYN STTELMEYRE VSFVPGLYKI FDEILVNAAD
NKQNDPNMSE IRVTLDKEAG EISVWNNGRG IPVEIHKKEQ TYIPELIFGH LLTSSNYNDM
QEKVTGGRNG YGAKLCNIFS NEFTVETADS KQKKKFKLTW TNNMSTMGKA KITECKGDDY
TKVTFKPDFA KFGMDGMDDD FEALVKRRVY DMAGTCGTAV KLNGTRIPIK SFKKYMEMYT
KAIKAERGED PTSASDKNDI ITESPDRRWE IGFTVSDGSF QQVSFVNSIA TTSGGTHVNY
ISDQICNKLA DALKKKNKTG ATLKAAQIKN HIFLFVNSQI VNPAFTSQTK EQLTTRPSQF
GSKCVVSDDF LKKVMKTRVM DDILHFAEKK ADQILKKTDG NRRSRMNNPK LTDANKAGTK
DGHHCTLILT EGDSAKGLAM AGRAVVGPDL FGVFPLRGKL LNVRDASVDQ ISKNAEIQNI
KNFIGLQHKK EYTDTRGLRY GHLMIMTDQD HDGSHIKGLL INYLQVAFPT LLKIPGFLIE
FITPIVKVWK GDPKNPTHSK SFFTIPEYEE WKEAHAHDKK WQKKYYKGLG TSSTEDAQIY
FQDLDRHLKQ FHTLQDKEAE LIELAFSKKK ADERKEWLRQ FKPGTYLDHS TDQITYTDFI
NKELILFSMA DNIRSIPSVV DGLKPGQRKV LYTMFKRNVR KDIKVVELAG YVSGMTAYQH
GDNSLHTTIV GLAQTFVGSN NINCLEPSGN FGSRLQGGSD SASARYIYTR LSPFARRLFH
QADEPLLVNN VDDGKVIEPE TYVPVVPLIL INGADGIGTG WSTSIPNYNP EEVVDNLKRL
MVGEELVPMK PWFRGFKGEV SGSGDRYKFS GIIKQTADNE VEITELPIRT WTQDFKDKLE
EIIKAEKVPS FIKDYKDYNT HTNVHFIIQM EEKHMKKALE EGLEEKFKLV KQIATSNMVA
FDAEGRITRY ETPEDILRAF YAVRIKLYEK RKQYLLSELQ TQLDKLSNQA RFVQMIIDGE
LVISKKKKAV LIQELQEKGF KPFPKVVGTP EPGEAGDVEE EEDEEEETTT AAVSSDAYDY
LLSMPLWSL
//