ID A0A194PUX2_PAPXU Unreviewed; 1574 AA.
AC A0A194PUX2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=RR46_09113 {ECO:0000313|EMBL:KPI97206.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI97206.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI97206.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI97206.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI97206.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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; KQ459590; KPI97206.1; -; Genomic_DNA.
DR STRING; 66420.A0A194PUX2; -.
DR Proteomes; UP000053268; 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: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 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:UP000053268};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 449..566
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1147..1204
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1310..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1574 AA; 179082 MW; 39442787195CF857 CRC64;
MQSATQNGTS EAAPPAKGQK GTIEKIYQKK SQLEHILLRP DTYIGSVERA TETMWVFDKE
KECMVQKELT FVPGLYKIYD EILVNAADNK QRDSKMDVIR IDINQEQNTI SVYNNGCGIP
VVMHKDEKMY VPTMIFGHLL TSSNYNDEEE KVTGGRNGYG AKLCNIFSTK FTVETASRQY
KKHFKQTWGC NMTKASEPKV KEAGKDDDFT KVTFSPDLAK FKMDKLEDDI VALMSRRAYD
VAASSQGVKV YLNGERLKIN KFKDYVDLYI KGKEDENGQP LKVVYEKVND RWEVALTLSD
RGFQQVSFVN SIATTKGGKH VDTVADSVVK NVLEVLKKKN KGGVNIKPFQ VKNHMWVFIN
CLIVNPTFDS QTKENMTLQA KSFGSKCNFS EKFINAVTKS GLVESVLTWA KFKAQTELVK
ASGKKQSKLK GIPKLEDAND AGTKNSHLCT LILTEGDSAK TLAVSGLSVV GRDHYGVFPL
KGKPLNVRDA SHKQVLENVE INNLIKILGL QYKKKYNSLD DLKTLRYGKV MIMADQDQDG
SHIKGLIINF IHHNWPELLK LPFLEEFITP IVKATKKDKE ISFYSLPEFE EWKRETENHH
TFNIKYYKGL GTSTSKEAKE YFQNMERHRI KFRYSGPTDD HHIELAFSKK GADQRKEWLT
NHMDEVKRRK EIGLSERYLY TKETKAVTYS DFINLELVLF SNGDNVRSIP SMVDGLKPGQ
RKVIFTCIKR NDKREVKVAQ LAGSVAEHSA YHHGEQSLAM TIVNLAQNYV GSNNINLLEP
RGQFGTRLCG GKDSASPRYI FTLMSPLTRL VFHPHDDPLL IHEFEDNQKI EPVHYVPILP
MVLVNGAEGI GTGWSTKIPN YNPRDIVANI RRMLDGEEPK TMHPWYKNFR GTIESFGDKY
VISGEAAVLP GEKIEITELP VGIWTQNYKE NVLEPMLGNE KVKPLISEYR EYNTDTTVRF
VVSLLPGKLA EVEAEGIHKV FKLQTTISMT CMNAFDHNNC LKKYDKVEEV LREFYDLRLR
YYLRRKDFLE GQLQAEADKL TNQARFILEK CDKGLVIENK KRKAMVEELI KRGYAPDPIA
DWKKRASKMQ GLEAVEEEQQ ESEEEVEPED NKGKPVDPEK AFQQLKEVKK FNYLLGMSMW
MLTKEKKDEL LKQRDQKLSE LEILKAKTPA MLWREDLDAF LVRLEEVEEK ERNEENTVNK
KSSKAMAANK KNRKSLFDII PAENGRRIEP KISEDLIKRI QAAEKAKTRK EIKKEYDPFA
CILAHESAKG WFGSLWSGNQ CACVHQISIV LSCNSQDDPT GVTPPTSGEK KPKGRVKKEK
PEKEKVEKTD GLKQTKLAFK KEPKKKKMTF SGSSSGEMSE SDVEMVEPPA PRERGSARRA
ATKVQKYKDG SDDSDSNEEL ELHDNKVDSE GERPRVLSLS DDDDFNVKKN ANKKPAEMDS
DCLFDSLIEE TKKEQPTNNH AEPTTILSSD EEEAELSPPK KKPAPKRKLL NTNKEKKEDK
PKKRPAKVLL SADSDDDSIF DTKKDKKANP KKKAKKKAGS DSEEEDVISS SPVAARGKAR
ARPQAKYNFS DDSE
//
