ID B7P6J4_IXOSC Unreviewed; 538 AA.
AC B7P6J4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
DE Flags: Fragment;
GN ORFNames=IscW_ISCW024091 {ECO:0000313|EMBL:EEC02216.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC02216.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC02216.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW024091-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW024091-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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=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|RuleBase:RU362094}.
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DR EMBL; ABJB010797884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS646419; EEC02216.1; -; Genomic_DNA.
DR RefSeq; XP_002408893.1; XM_002408849.1.
DR AlphaFoldDB; B7P6J4; -.
DR STRING; 6945.B7P6J4; -.
DR PaxDb; 6945-B7P6J4; -.
DR EnsemblMetazoa; ISCW024091-RA; ISCW024091-PA; ISCW024091.
DR KEGG; isc:IscW_ISCW024091; -.
DR VEuPathDB; VectorBase:ISCI016225; -.
DR VEuPathDB; VectorBase:ISCP_030498; -.
DR VEuPathDB; VectorBase:ISCW024091; -.
DR HOGENOM; CLU_006146_1_0_1; -.
DR InParanoid; B7P6J4; -.
DR OMA; RDGKTHH; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 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 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; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR005737; TopoIV_B_Gneg.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF4; DNA TOPOISOMERASE 4 SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01098; TOPISMRASE4B.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 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|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 397..514
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 538
FT /evidence="ECO:0000313|EMBL:EEC02216.1"
SQ SEQUENCE 538 AA; 59099 MW; 135B0D4B4624DF95 CRC64;
MYTRTDNPLH IVQEVIDNAA DEALAGFART LTVTLLEDGG IQVEDDGRGI PVGLHPEENA
PVVELVFTRL HAGGKFDKLN GGAYAFSGGL HGVGVSVTNA LSRRLEVLVW RDGQANEIVF
ADGELEQPLT QTGTVGKRKT GTRVRVWPDP KYFDSAQIPL AQLTHILHSK AVLLEGVTVE
LVQQKTGQRQ QWCYEDGLRG YLQEEMDGVE LLVPLFEGRQ YAPQDDDNFS AGEGAHWVVA
WALDSNIVRE SYVNLIPTPA GGTHESGLRD GLYQAVRSFA ELHSLIPKGV KLQAEDVFAR
ASFVLSAKVL DPQFQGQIKE KLNSRDAVRL VSGYVRNALE LHLHANVDQG RKLAEVAVRQ
AQARTRSAQK VEKRKSSGVA VLPGKLTDCE SHDLESSELF LVEGDSAGGS AKMGRDKEFQ
AILPLRGKVL NAWEVDKDRL FANQEIHDIS VAIGVDPHDA QSEPDLSGLR YGRICILSDA
DVDGSHIQVL LLTLFFRHFP KLIEAGHVYV ARPPLFRVDV PAAGKRPARK IYCLDQGE
//
