ID A0A0K0DSA3_STRER Unreviewed; 1421 AA.
AC A0A0K0DSA3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000011200.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000011200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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=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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0K0DSA3; -.
DR STRING; 6248.A0A0K0DSA3; -.
DR WBParaSite; SSTP_0000011200.1; SSTP_0000011200.1; SSTP_0000011200.
DR Proteomes; UP000035681; 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; 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:SF62; DNA TOPOISOMERASE 2 TOP-2-RELATED; 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 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:UP000035681};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 479..596
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 162986 MW; 610603E8BFF55902 CRC64;
MSDTDDMDFD GPGPSTSRKT LKEHNGPSKE DLKVFTNIDK KTSNGKPTIE QMYQKKSQLE
HILLRPDTYI GSVEHTDQTP MWIYDMENEK LVQRNISYVP GLYKIYDEIL VNAADNRQRD
RKMNLIKVDI NKQTNTISIF NNGKGIPVAH HGVEKMYVPE LIFGTLLTSS NYNDDEKKTT
GGRNGYGAKL CNIFSTKFTL ETSSSEYKKQ FKQTWINNMT KDKEAEISKS TGEDYTKVTF
TPDLKKFKMK ELDDDIIGLM ARRAYDIAGT TPGVRVYLNG KCIPIKSFKD YAEKYVESMM
DDEAEKPKVI YERVNDRWEV ALTVSEKGFQ SVSFVNSIAT SKGGRHVDYI ADQITSNLID
TIKKKAGGAK SGINVKPFQV KNHMWVFVNC LIENPTFDSQ TKENMTLQAK SFGSKGEMSE
KFYKEALKCG VVEAVLSWVR FKQQEQADKK CSTKKSTKVK GIPKLEDANE AGTKNSYKCT
LILTEGDSAK TLAVSGLGVV GRDYYGVFPL RGKMLNVRDC SMKQINDNQE IGHMIKILGL
QYRLKYETEE ERKTLRYGRV MIMADQDQDG SHIKGLLINW IHCNWPALMK NNFVEEFITP
IVKASKGNTS LSFFSLPEYM EWRNSTDNWK SYKIKYYKGL GTSTSKEAKE YFSDMDRHRI
PFTYSGPECE QAVEMAFSKK KIEARKTWLS NWMREKKERR ENGGIEEYLY NKDTRSVSFV
EFINKELILF SNMDNERSIP CLVDGLKPGQ RKVLFTCFRR ADKKEVKVAQ LAGAVGEMSA
YHHGEQSLMM TIINLAQDYV GSNNINLLLP IGQFGTRLQG GKDSASPRYI FTQLNPVTKA
LFVQDDENVL RFLFEENQKI EPEWYCPIIP MILVNGAEGI GTAWSTKIPN YNPRDVMENI
RRLIRGEEMK KMIPWYKHFE GEIVQVDEQK YISNGRVGLL DDETFEITEL PIKTWTQNYK
EGVLEDLSNS TDKSPAIVQD YKEYHTDQTV KFVIKMTESN LKKALHQGIY DIFKLQTPIN
TSSMVLFDAE GCLRKFESPE QICQEFFVVR KKKYIERKAF LVGMLEAQSK RLSNQARFIM
AKIKGEIVME NRKKKNIVDQ LIKEKFDPDP VKAWKDLCKK KELEMCGEIE IEEEEESLEE
DETSTDAGLK KRLADYDYLV NMALIKLSEE EKDRLLRESQ EKLEELETLK KKTWADLWEH
DLKVFEEALK KQEEKELQDI EGSIKTAQSK LVKGGASSKN RKNKVNVDVS SFKPNPNAEI
VKVEFEALKN KYEKKPKKVK GTTVPKVQGD EAANALENVD LKPPKAKKPK EAKAPKKTTE
KKNKKAVDSE DDSDIMDDSP PMEYSPVPQR RAKRNITKAP VIEMDSDSDI EFIEPTPQSS
QKGTKRKSVT PQKPKKAKKQ KIVESDDEDE SFESFNSDDS Y
//
