ID B0WRP3_CULQU Unreviewed; 1358 AA.
AC B0WRP3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=6042239 {ECO:0000313|EnsemblMetazoa:CPIJ010018-PA};
GN ORFNames=CpipJ_CPIJ010018 {ECO:0000313|EMBL:EDS33447.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS33447.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS33447.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ010018-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ010018-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; DS232058; EDS33447.1; -; Genomic_DNA.
DR RefSeq; XP_001851377.1; XM_001851325.1.
DR STRING; 7176.B0WRP3; -.
DR EnsemblMetazoa; CPIJ010018-RA; CPIJ010018-PA; CPIJ010018.
DR KEGG; cqu:CpipJ_CPIJ010018; -.
DR VEuPathDB; VectorBase:CPIJ010018; -.
DR VEuPathDB; VectorBase:CQUJHB005928; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; B0WRP3; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000002320; 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 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:UP000002320};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 471..588
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1113..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1358 AA; 153722 MW; 07062DCB21406348 CRC64;
MFDKSLIFVF SPPLHLHHPQ AAFAANQNGS GAGATASPKV GGKSIEKIYQ KKSQLEHILL
RPDTYIGSVE QLKETQWIYD TEANKMIQKE ITFVPGLYKI FDEILVNAAD NKQRDAKMTA
IKIDINQETN TISIWNNGQG IPVVMHKEEK MYVPTMIFGH LLTSSNYNDE EQKVTGGRNG
YGAKLCNIFS TKFTVETASK QYKKAFKQTW GDNMSKASEP KIKEGASGED YTKITFSPDL
TKFKMEKLDD DIVGLMSRRA FDVAASTRGV AVYLNGKKLP IKNFKDYIDL YVKEQQEDVS
APIKVCYENA NERWEVAVAI SEKGFQQVSF VNSIATTKGG RHVDYVTDMI VKQLIEVLKK
KNKGGINIKP FQVKNHMWVF INCLIVNPTF DSQTKENMTL QAKSFGSKCA LSEKFITAVS
KSGIVESVLQ WAKFKAQTEL NKASGSKKSK IKGVPKLEDA NDAGTKNSLN CTLILTEGDS
AKTLAVSGLG VVGRDTYGVF PLRGKLLNVR EATHKQILEN AEINNLIKIL GLQYKKKYLT
IDDLKTLRYG KVMIMTDQDQ DGSHIKGLLI NFIHTNWPEL LRLPFLEEFI TPIVKATKKN
GEELSFFSLP EFEEWKTETA NSHTYNIKYY KGLGTSTSKE AKEYFQNMER HRILFTYDTS
TDDDAITMAF AKKCVDQRKE WLTAHMEENR HRKLVGLPER YLYTKTTRAI SYKEFINLEL
VLFSNSDNVR SIPCVLDGLK PGQRKVMFTC FKRNDKREVK VAQLAGSVAE MSAYHHGEQS
LCSTIVNLAQ NFVGSNNINL LYPGGQFGTR LAGGKDSASP RYIFTMMSAL TRLIFHPLDD
PLLEYQYDDN QKIEPLWYLP IIPMVLVNGS EGIGTGWSTK IPLHNPRDII ANLRRMLNGE
EPKVLHPWYK NFRGSVEVVG PQKYLTVGNL SLLENQKIEI SELPIGTWTQ VYKENTLEPL
LHGSEKQKAV ISDYKEYNTD TTVRFVVSFL PGEFDKLYAE DGGFHRVFKL TSSISTTCMH
AFDDKNYLRR YEHANDIFQE YYKIRLDFYH KRKAYLEGML QAEADRLTDQ ARFIMEKCDR
TLVVENKKRK VMIDELIKRG YRPDPVKEWK RKVALEEDEE AEEPEEEGAE EEDTKPGKSA
AKKPVDPEKA FQRLTDVKKF DYLLGMSMWM LTDERKNELL KQRDNKLSEL SAIKAKTSEV
LWTDDLDALA KKLDEVEEKE RLDAISTEKK LKGAAAKGGA GRVKTLGKKN AIDETKPSAL
GEEVKFKVTE ELLKKYEKLA AGPANPRVKK EKKEPGEGGA EGGADEFDAL VEGKKPAAAK
VKKEPKEPKV KKEKKDKDGT KQTKLNFGKA AAGKGRVS
//
