ID J4ICG2_9APHY Unreviewed; 1571 AA.
AC J4ICG2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=FIBRA_08613 {ECO:0000313|EMBL:CCM06356.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM06356.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM06356.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM06356.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(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; HE797302; CCM06356.1; -; Genomic_DNA.
DR RefSeq; XP_012185639.1; XM_012330249.1.
DR STRING; 599839.J4ICG2; -.
DR GeneID; 24101256; -.
DR HOGENOM; CLU_001935_1_1_1; -.
DR InParanoid; J4ICG2; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000006352; 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 Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 529..643
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1174
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1571 AA; 175798 MW; F2D4729F91D034E9 CRC64;
MSSSEENFNL DAISGSGSDS EGYAPAPKKS LKTAPKAKPA SKAAKLSTKP KAVPRKKVLV
DKNDNADSDT EMRNSDDDAG PSAPAPAAPA KKKTASETYT KVLSQLEHIL KRPDSYIGSV
ETITQPMWAW DSDRKLMVYK EIKYVPGFFK IVDEILVNAA DNKINDPSMD TIKVTIDPRN
NVISVYNSGR GIPIEMHSKE KIYIPELIFG HLLSSSNYDD DEKKLTGGRN GYGAKLANIY
SVEFTIDTAD KNTGQKYVQT WTDNMSKMGK AKITKNSRGE EYTRVTFKPD LKRFGMDSID
EDTVALLKKR VHDIAGTVKD VKVFLNDERL KIKNFKQYVE LYLNSAAEQA ADASGGAAQA
KQTMIYEQIG TRWEVAFAVS EGAFQQVSFA NSISTVKGGT HVQYIADQLA KNLVTFISKK
NKAATVKPPQ IKNHMWIFVN ALIENPTFDS QTKETLTLPS AKFGTKPSLS EEFMKKVQKS
VIVDHILNWA KFKADQQLKK TDGSRRNRLS GLPKLSDANN AGTRKASECT LILTEGDSAK
TLAVAGLSVV GRDNYGVFPL RGKLLNVRDA KHDQIMKNEE IQNIKKILGL QHNKDYKDVS
GLRYGQLMIM TDQDHDGSHI KGLLINYFEH FYPSLLKVPH FLVEFVTPII RATKGTQLIE
FYTIPEYEQW LEETPNSASW RAKYLKGLGT SKDEDARRYF KLMRKHRIAF STIKEGDRDS
IELAFSKKRA DDRKEWLRQF KPGTFLDHTQ GEIGFTDFIN RELILFSMAD NIRSIPSVAD
GLKPVQRKVI WACFKRKLKG EIKVAQLVGH VSEHAQYHHG EQSLMMTIVN LAQDFVGGNN
LNLMMPNGQF GTRDQGGKDH ASARYIYTEL SPATRAVFHP GDDPLMKYLT DDGHLIEPEY
YMPTVPMVLI NGAEGIGTGW STNIPCYNPE DIVANLRRLM AGEEQLPMLP WWRGFKGTIK
KTSDYRYDVS GIVTKLDDTT FEITELPIHK WTQNYKVELE AMCGEKGDGP VKDYKEYHNN
MNVHFVVHME PKAVEKAESQ GLLEFFRLTG KINTSNMICF DFEGKIKKYN TPEEIIEDFY
PQRLAYYQKR KDFMANELSD ELDKLNNQIR FIQMIIDREL AVSNRKKVDI VADLRKKEFR
PFPKVSKAKA KASETTELVE VNEDEEDEED SGPAGSASDF DYLLGMAIWS LTKEKMEKLR
QQAKQTEGEL LILLERTPIQ IWQCDLDRFL EEWRATCEQW DAKIISADAS GNKKGKRKQP
TLKAAMKKAA GDDDSEDDFK PTKAAAKAKK TTEPKPAPAK KLPQADPSSS KVDEDEQKKP
VAKKPTKKQI KDDPDSDFEV IQQKPAPKKA AAKKLAKIES ESELEMIDGR LASANKGKAQ
DSDIEMISLV LKDSDKGKAP AVPKRKSPDA ENSDSDSFTV PLKKSKPSPA QATVTDFFDK
VPTAKKTTVR KPSSSKPAPA KKTATKVVDS DDEDELMDED DPPPPPAPRK PIARKPSSSK
SALAKKPATK KVVESDDDIS ADELAAVAPI TTRNEAPRRA ARGGAKKYIE IPSSSEGEGG
GKDGSEFEDF D
//
