ID F2PYI8_TRIEC Unreviewed; 1678 AA.
AC F2PYI8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=TEQG_06009 {ECO:0000313|EMBL:EGE06956.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995753; EGE06956.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TEQG_06009; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_2_1_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
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 556..670
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1678 AA; 187249 MW; 915E534819AC73FD CRC64;
MSSESDFEND GFSSDFAPKP KAKAAPKKAA AAAKPKDAPK KLTQTTLKSK TTSKATSSKK
AARPDPEDEL DSVAEEADSD DADALDSTPP NASKKQKAAP KKAASKPLAN VENGSFTAET
VEGGGSSEKY QKITQLEHIL KRPDTYIGSV ERTEKHMWVY NSTTELMEYR EVSFVPGLYK
IFDEILVNAA DNKQNDPNMS EIRVTLDKEA GEISVWNNGR GIPVEIHKKE QIYIPELIFG
HLLTSSNYND MQEKVTGGRN GYGAKLCNIF SNEFTVETAD SKQKKKFKLT WTNNMSTMGK
AKITECKGDD YTKVTFKPDF AKFGMDGMDD DFEALVKRRV YDMAGTCGTS VKLNGTRIPI
KSFKKYMEMY TKAIKAERGE DSTSASDKND IITESPDRRW EIGFTVSDGS FQQVSFVNSI
ATTSGGTHVN YISDQICNKL ADALKKKNKA GATLKAAQIK NHIFLFVNSQ IVNPAFTSQT
KEQLTTRASQ FGSKCVVSDD FLKKVMKTRV MDDILHFAEK KADQILKKTD GNRRSRMNNP
KLTDANKAGT KDGHHCTLIL TEGDSAKGLA MAGRAVVGPD LFGVFPLRGK LLNVRDASVD
QISKNAEIQN IKNFIGLQHK KEYTDTRGLR YGHLMIMTDQ DHDGSHIKGL LINYLQVAFP
TLLKIPGFLI EFITPIVKVW KGNPKNPTHT KSFFTLPEYE EWKEAHAHDK KWQKKYYKGL
GTSSTEDAQI YFQDLDRHLK QFHTLQDKEA ELIELAFSKK KADERKEWLR QFKPGTYLDH
STDQITYTDF INKELILFSM ADNIRSIPSV VDGLKPGQRK VLYTMFKRNV RKDVKVVELA
GYVSGMTAYQ HGDNSLHTTI VGLAQTFVGS NNINCLEPSG NFGSRLQGGS DSASARYIYT
RLSPFARRLF HQADEPLLVN NIDDGKVIEP ETYVPVVPLI LINGADGIGT GWSTSIPNYN
PEEVVDNLKR LMAGEELVPM KPWFRGFKGE VTGSGDRYKF SGIIKQTADN EVEITELPIR
TWTQDFKDKL EEIIKAEKVP SFIKDYKDYN THTDVHFIIQ MEEKHMKKAL EEGLEEKFKL
VKQIATSNMV AFDAEGRITR YETPEDILRA FYAVRIKLYE KRKQYLLSEL QTQLDKLSNQ
ARFVQMIIDG KLVISKKKKA VLIQELQEKG FKPFPKVVGT PEPGEAGDVE EEEDEEEETT
TAAASSDAYD YLLSMPLWSL TQERVDKLRR QIGDKEMEVD ALIKLSKEDL WRKDLDEFIS
EWRFQLEDEE NRRKKIASRG RRLSAKVKTG SRATAAKKRK AGSGDDSDFD VPKVKKAAVN
RVQPKGGLLD FLSKAKPKPK ATSRVDGADD SDDFEDEVMP KPKSRGAAKE AKAKPAPVPK
RLSDADFMDI DSMGTDNPKR EPSPVEKPKV VDDDSDIEMI PKPTTQRSAR NKQQPKKYHG
FSTSEDEEDD DFDVSAMVKG IDKKKPNTVS TGPTLFSEPS RPAGGSSKLP AKPAKETMEF
DADETDYSKL IPQNSPRRSL LVKPKESKVF SDAEDDIEDE PKPAAKPTAK AKASSSSKST
SKPAAKASTT SARGRPKKAV AAAPEKEKKT LQLSPAAKVY ASKKAKAKKI VDDMSDDDID
AMANDILDSE PEEAVKPSSR ARPSRRAATA AKKPVYALDD DSSEEDGDAA VSSEDFSD
//
