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Database: UniProt
Entry: Q76C33_TRIVC
LinkDB: Q76C33_TRIVC
Original site: Q76C33_TRIVC 
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}.
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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
//
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