ID A0A068Y8E7_ECHMU Unreviewed; 1647 AA.
AC A0A068Y8E7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CUT98959.1};
RN [1] {ECO:0000313|EMBL:CUT98959.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CUT98959.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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; LN902845; CUT98959.1; -; Genomic_DNA.
DR STRING; 6211.A0A068Y8E7; -.
DR eggNOG; KOG0355; Eukaryota.
DR OMA; TWTQDFK; -.
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 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 455..572
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1107..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1154..1204
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1316..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1647 AA; 183382 MW; 402A40B31EC1D496 CRC64;
MADISSVNGI PNIIEKAAPA APTKKRLSVE RIYQKKTQLE HILIRPDTYI GSVSRTTTMM
WVFDREKEAM VQREITYTPG LYKIFDEILV NAADNKIRDP TMNCIRIDIK PAENLIRVWN
NGAGIPVVHH KVENMYVPSL IFGHLLTSSN YDDTEQKVTG GRNGYGAKLC NIFSKRFVVE
TSSKENKKCF KQTWVDNMTK TSEPKINPNS GEDFTCVSFC PDLDRFGMTE LDADTVALFE
RRAYDVAAST CGVKVFLNGQ RIPIKNFKDY VDLYLKGKGE DGDSAPAVYE SVNPRWEIAV
APSTVGFQQV SFVNSIATTK GGKHVDYIVD QVVGKLIDIV KKKSGKSGVS IKNFQIRSHM
WVFINCLVVN PTFDSQTKEF MSLEAKCFGS TCQLTEKFIN HVSKSGIVES VLSWVRFKAQ
EKMDKQCHKS KHAKLKGIPK LDDANDAGTK NSQHCTLILT EGDSAKSLAV AGLGVVGRDR
YGVFPLRGKL LNVREAPTRQ IMENAEINNL IKILGLQYKN KYESQDSLVN LRYGKIMIMT
DQDQDGSHIK GLLISFIHHN WPNLLRHNFL EQFITPIVKV FKGKQEIAFY SIPEFEEWQK
STLNWHTWRV KYYKGLGTST SKEAKEYFSD MARHRIRFRY SGPEDDSGIM LAFNKNKINE
RKQWLTAWME EKRRRTELGL PEDYLYGVGT HAITYHDFIH KELVLFSNMD NERSIPSLVD
GLKPGQRKVM FTCLKRNQVK EIKVAQLCGA VAEMSSYHHG EVSLMGTIIG LAQDFVGSNN
LNLLMPYGQF GTRLSGGKDS ASARYIFTAL SPLTRKIFHE NDDPILNYLF EDNQKIEPAW
YMPVIPMVLI NGAEGIGTGW STKVPNYDTN EVIANLRRML DGVEPLPMLP SYRGYRGKIV
EVGENRYVLF GEIAVLDDQT VEITELPAKT WTQCYKETVL EPMLNGTEKV PVSISDYKEY
HTDVTVRFVV QMTQEKLREA ESMGLHKFFK LAIPMTTNSM VLFDHTGCLK RYTSAQEILR
SFYTLRLEWY DRRKAYMEGM LSAEARRLEN QARFVMEKIG GVITIENRSK RDLVRLLRGS
RYDPDPVRAW KECIDKLAAI EEATAARRQA GEPVDEAEGG DGSGVTVDED VARGAADYNY
ILGMPLWSLS KERKEDLLAQ RDKKQAELAT LMRRTNKDLW REDLDELEAA IKKYETERQK
DLEDLINAAE KKVAKQASSQ LKGGRSAAAK GAAAALTKGM RQTRPDPLGR RVEPVVDPEL
ARKAEAQVCR EAKRKAAAAG SGKAADDDFL ADMDDEDSQF GGNAPQPLFK RLSGTVDSED
GNTALNTLAS APLTKRGSGA GSRGGGRGRG KGASAGVKRS SARKVRQKKL TFDSSEDEND
ADNVSDDASD VSEFAPFKGG TGVGPVMSLA ERVRNQPPRR TAAATTKRYS FYDSEGYEDG
VQSSEEEVFT AVDHGQGDKA IVLSSPVKQP SSPTIIQPQT DAIGKSKSGT TVWPISYKEP
ATVATRMPSS TRGGRTGSSR RGANAGGGGG QRGGARLTTA AKSTGVKRLM EETDSDTPGG
ANNKSDDADK IFIPDSPVAP ARTKAARSAQ RKVQYFFGSD SDEVVEVDSV SDKGVDSVDG
SNVKPRGKMG AKRKRFNSDS DEDYVPE
//
