ID A0A0N5ASB9_9BILA Unreviewed; 1441 AA.
AC A0A0N5ASB9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000767801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000767801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) 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}.
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DR STRING; 451379.A0A0N5ASB9; -.
DR WBParaSite; SMUV_0000767801-mRNA-1; SMUV_0000767801-mRNA-1; SMUV_0000767801.
DR Proteomes; UP000046393; Unplaced.
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 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 462..579
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1108..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1153..1218
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1257..1277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1322
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1441 AA; 164982 MW; D7AC50D4E2B56AC0 CRC64;
MKLCLGGGDG KENLEENPMD VFTSIDKQTK RLSIEKIYQK KSQLEHILLR PDTYIGSIEH
TDRAPMWVYD QAQGRIVQRE ISYAPGLYKI FDEILVNAAD NKQRDPKMNL IRINIDKEKN
TVSVFNNGRG IPVVFHKVEK MYVPELIFGT LLTSSNYNDD ERKVTGGRNG YGAKLCNIFS
TEFTVETSSK EYGKRFKQTW INNMTKDADA TVTKCTGEDF TRITFKPDLA KFKMSELDDD
IVSLMCRRAY DIAGSIKGVK VYLNNQVLPV QGFKQYVEQY AKYNLDSQGE PYKIAYEQVN
ERWEVALTVS EKGFQQVSFA NSIATTKGGR HVDYVADQIT SKLIETIKKK IGKSGINIKP
FQIKNHMWIF VNSLIENPTF DSQTKETMTL QSKSFGSKCD LSEKFIATVM KCGIVEAVMA
WVRFKQQENM DKKCSSKKTS KIKGVPKLED ANEAGTKNSS LCTLILTEGD SAKSLAVSGL
GVVGRDKYGV FPLRGKMLNV REGSHKQIME NAEVNALIKI IGLQYRMKYD KDDDMKSLRY
GKVMVMADQD QDGSHIKGLV INFIHYNWPN LIKRNFVEEF ITPIVKATKG KEEISFFSLP
EYAEWRNSTE NWKSYRIKYY KGLGTSTSKE AKEYFTDMAR HRIKFRYAGD DDDNCIDMAF
SKKKCEERKE WLTKWMAERK ERREHGLTEE YLYDKETRAV SFKDFVNKEL VLFSNADNER
SIPSLVDGLK PGQRKVLFTC FKRADKKEVK VAQLAGAVGE MSAYHHGEQS LMSTIVNLAQ
DFVGSNNINL LLPIGQFGTR LQGGKDSASP RYIFTQLNPV TRALFPSVDE NVLRFLFEEN
QRIEPEWYCP VIPTVLVNGA EGIGTAWSTK IPNYNPREIV ENMRKLIRGE EPTPMVPWFK
NFCGTIEQLD QQRFVCSGEV AVLSEDTIEI TELPIRTWTQ TYKETVLEPF LDGTEKQPAI
IQDFKEYHTD TTVKFVVKMA PQKLREAQAE GLHKVFKLQT AINTSSMVLF DPLGCLRKFN
TVMEICQEFF ETRKRKYIER KAFQEGMLKA QSERLSNQAR FILGKIKGEI LIENKRKAAI
VEQLVKKGFD PDPVKKWREY VKKKEMENNG EVGVDDDDES QDNEESSSTV SNSNKEMEMK
LQDYDYLVGM AILKLSEEEK DKLIRESDEK LEELKRLQNT TWAEMWNADL DNFLVELEKQ
EAKELADANI QIQNAAKKLL KDTTGRKKKG TLLAREVLPD PNGVRVVPKL EYMKEKYEAK
KNSNGEPKTR KPRAPKQAKD LTVCLTKFFA RAQKKNKKES ELSDDEDADN FVIEDNEGTS
DLFDDKDDSA ESGGFSKKKV EKQSKQSTKP AKKKVTSEAS NSITNYFQKP TTSKKRAVSD
DDDSITEISV SPKAPRENIR KRTAVKYNYD DELSDDSDVE TYGRKKRGRK IESDDEFVLS
D
//
