ID A0A0B2W309_TOXCA Unreviewed; 964 AA.
AC A0A0B2W309;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=K12D12.1 {ECO:0000313|EMBL:KHN88343.1};
GN ORFNames=Tcan_15694 {ECO:0000313|EMBL:KHN88343.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN88343.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN88343.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN88343.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN88343.1}.
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DR EMBL; JPKZ01000253; KHN88343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2W309; -.
DR STRING; 6265.A0A0B2W309; -.
DR OMA; AFESLWP; -.
DR Proteomes; UP000031036; 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:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 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 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; 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 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 497..614
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 964 AA; 109398 MW; B0B8844D7FDFFB4D CRC64;
MLLRVLPQTR GGALRIGCSK CGWRAVLIRH LPKRFRSCAV DGFMRRACCP LVTFDRSSSS
ATRTFPVKKE KYQHISPLKH VLLRPDTYVG SVLPSEEQSV YLYETQSKRM VKQVVSYIPA
LLKIFDEVLV NAADNKQRDP RMTAIRVTID RDNNEVSVWN DGEGIPVEMH SEEGVYVPSL
IFGTLLTSSN YDDSEVKIIG GRNGFGAKLC NIFSTEFTVE TSSSNSGKRF RQTWHNNMSK
CDEALVEVIP EGTSDFTKVT FKPDIEKFHM KELDEVAIGL MQRRVIDVAG TLKGVDVFLN
GQKIDVHGFR DYVRLYIGKN DMAATDSEKG ETYVFSEVND RWQVAVALSD IGFEQISFVN
NIATTKGGRH VDYVCDQIVS RIKEEVELRC GTKKSVRPLQ VKNCMRLFLN SFIENPAFDS
QTKEYLSSAP KAFGSKCVMS DAFFKELFAR TDIVESIMRD INKRELRSLN RSNGRELSDL
HKLEEAGDAG TNRSRQCTLI VTEGDSAKAL AVAGLAVVGR KYFGVFPLRG KLTNVRGLDE
KTSLQNAEVS ALIRILGLKF GEDYSSDEKR NELRYGHLMI MTDQDEDGAH IRGLIVNFLH
SFWPSLIRSD FIQYFITPLL KVRSGSEVIP FYSNAEFERW KRDCVDSTKY SLKYYKGLGT
SSAQEAREYF AAMDRHRMQF VYGGKEDDEN IELAFDKNRA DDRKIWISSN SREKVSSKKI
EDANRRTYSE FINEELIEFS RLDIRRSVPS AIDGLKPSQR KVLYTMMQRF EKGEVRVVQL
AGAIAHFCAY HHGEQPLINT IVRLAQDFVG SNNINLLQPI GQFGTRLAGG EDCASARYIY
TALSPLTRWI FPRADDSVLS YMEEDNMRIE PQWFCPIIPM VLVNGAEGIG TGWSTKVLCY
NPKQIINNVQ RMIDGQSLQK MLPFYRKFTG AVKEISDGRF EMSGAIMLQP SRNNSLTFQA
LHFV
//
