ID A0A183T0W5_SCHSO Unreviewed; 1267 AA.
AC A0A183T0W5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=SSLN_LOCUS10114 {ECO:0000313|EMBL:VDL96499.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001050001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SSLN_0001050001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL96499.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDL96499.1,
RC ECO:0000313|Proteomes:UP000275846};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYSU01035653; VDL96499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183T0W5; -.
DR STRING; 70667.A0A183T0W5; -.
DR WBParaSite; SSLN_0001050001-mRNA-1; SSLN_0001050001-mRNA-1; SSLN_0001050001.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; 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 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000275846};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 449..566
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1081..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1128..1178
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1182..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 144153 MW; C05BB831742BAD84 CRC64;
MADVQLANGD VPEDGIVDPA KKRLSVERIY QKKTQLEHIL IRPDTYIGSV ERATTLMWLY
DKEKQAMIQK EITYTPGLYK IYDEILGLLT IYLYFLKKSM LRTTRLTLKR RPFYNLIRIW
NNGAGIPVVH HRVEKMFVPS LIFGHLLTSS NYDDTEKKVT GGRNGFGAKL CNIFSRKFVV
ETSSKEHKKC FKQTWIDNMT KTSEPRITAS AGEDFTCISF YPDLARFGMT ELEADTVALF
ERRAYDIAAS TRGVKVILNG VRVPIKNFKD YVDLYLKDKG EDGEVVYECV NPRWEVAVAA
SNLGFQQVSF VNSIATTKGG KHIDYISDQV ANKLVDVVKK KSGKSGVTVK SFQIRSHMWV
FVNCLIENPS FDSQTKEFMT LQSKSFGSTC VLSEKFINQV GLSNVLSWVR FKAQEKMDKQ
CHKSKHVKLK GIPKLDDAND AGTKNSAACT LILTEGDSAK TLAVAGLSVV GRDRYGVFPL
RGKLLNVREA SSKQIMENAE INNLIKILGL QYKNKYETPE SVATLRYGKI MIMTDQDQDG
SHIKGLLISF IHHNWPKLLH HNFLEEFITP IVKVFKGKQE LAFYSIPEFE EWQKTTSNWH
TWRVKYYKGL GTSTSKEAKD YFSDMTRHRI RFRYSGPEDD ASITLAFNKN KSDDRKSWLT
TWMNERKRRV ELGLPEDYLY GSGTHAITYS DFVHKELILF SNMDNERSIP SLVDGLKPGQ
RKVLYTCLKR NLVKEIKVAQ LSGSVAEMSS YHHGEASLMG TIIGLAQDFV GSNNLNLLMP
HGQFGTRLSG GKDAASPRYI FTSLSPFTRK IFSERDDAIL HYLFEDNQRI EPYWYIPVIP
MVLINGADGI GTGWGTKIPN YDVMEVISNL RRMIDGADPL PMLPSFRDFR GVIQELGDNR
YVVFGEIAIL DEQTVEITEL PVRVWTQSYK EGVLEVMLNG SEKVPASILD YKEYHTDATV
RFVVRMTPEK LREAEAIGLH KFFKLSTAMT TNSMVLFDHM GCVKRYASVS EILKEFFELR
LEWYNKRKSY LEGMLSAEAR RLENQARFVL EKIQGKISIE NRAKRDLIRL LKEHNYEPDP
VHAWKESAGE GEEEDSEEQG GDASTSSAAA DYNYILGMPL WSLTKERKDD LLAQRDKKQA
ELTELLSKSA RRLWRDDLDE LEADRQKDMQ SLIEAAEKKM SKQTASGRNV PSKASKSVKQ
TLPDPLGKRI VPVVDPEHLK KVEAVKRKAT RVRDANAAVD PNAGEPNDTS SSQLVSLRFH
IGGFRAF
//
