ID A0A484B4H8_DRONA Unreviewed; 1467 AA.
AC A0A484B4H8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=AWZ03_010837 {ECO:0000313|EMBL:TDG42731.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG42731.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG42731.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG42731.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG42731.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
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:TDG42731.1}.
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 EMBL; LSRL02000202; TDG42731.1; -; Genomic_DNA.
DR STRING; 7232.A0A484B4H8; -.
DR OMA; TWTQDFK; -.
DR Proteomes; UP000295192; 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:UP000295192};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 471..588
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1116..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1173..1223
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1286..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1409
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1467 AA; 167038 MW; D28EC2B625592487 CRC64;
MSFNDVTCSL PRVVLIRAII NFSIPTPKHV HHRSSNMENG KGAMSIEQMY QKKSQLEHIL
LRPDSYIGSV EFTKELMWVH DAEKNRMVQR EISFVPGLYK IFDEILVNAA DNKQRDKSMN
TIKVDIDPER NIVSIWNNGQ GIPVTMHKEE NMYVPTMIFG HLLTSSNYND DEKKVTGGRN
GYGAKLCNIF SSSFTVETAT KQYKKSFKQT WGNNMSKAGD PIIKDFNGSD YTRITFSPDL
SKFKMESLDS DIVALMSRRA YDIAASTKGV SVFLNGTKVP VRGFKEYIDL FVKNTDDDAG
QPIKVVYEAC GERWEVACCP SDRGFQQVSF VNSIATTKGG RHVDHVVDNV IKQLIEVLKK
KNKNGISIKP FQVRNHLWIF VNCLIENPTF DSQTKENMTL QAKSFGSKCT FSEKFIANVA
KAGIVESVLA WAKFKAQNDI AKTGGKKSHK IKGIPKLEDA NEAGTKNSIN CTLILTEGDS
AKSLAVSGLG VIGRNYYGVF PLRGKLLNVR EATFKQLTEN AEINNLCKII GLQYKKKYLT
MDDLKTLRYG KVMIMTDQDQ DGSHIKGLLI NFIHTNWPEL LRLPFLEEFI TPIVKATKKN
EEISFYSLPE FEEWKMDTPN HHTYNIKYYK GLGTSTSKEA KEYFQDMERH RILFKYDGQV
DDDNIVMAFA KKHVESRKTW LTNHMDEVKR RKQLGLPERY LYTKGTKHVS YSDFINLELV
LFSNADNERS IPSLVDGLKP GQRKVMFTCF KRNDKREVKV AQLSGSVAEM SAYHHGEMSL
QMTIVNLAQN FVGSNNINLL EPRGQFGTRL TGGKDCASAR YIFTLMSPLT RLIYHPLDDP
LLQYQVDDGQ RIEPLWYIPI IPMVLVNGAE GIGTGWSTKI ANYNPRDMIT NLRRMINNEE
PLPLHPWYKN FTGTMEYVSD GRYVHSGNVQ ILPDNRIEIT ELPIGVWTQN YKENVLEVLS
NGTEKVKAII SDYREYHTDT TVRFVISFAP GEFERLRSEE GGFHRVLKLS SSISTNQMHA
FDENNCLRRF PTPKDILLEF YKLRLEYYNR RKDYLVGQLT AQADRLSDQA RFILEKCEKK
LVIENKQRKM MIDELIKRGY RPDPVKEWQR RIKMEDVEAA EDDDEEEESA VGTTSKKIKK
EVDPEKAFQK LTEVKKFDYL LGMSMWMLTE ERKNELLKQR DLKIAELDNL MKKTPSHLWL
DDLDNLEQKL TEVEEKERLE EQGINLKQAK AMKGQKPAAG RAKKGGKSAG NADIFPDPIG
ERVAFKVTDE IIKKFQAATN TAVKTKERMT KAKAIKKEET TADKEVDDFD LLVEGGAPKT
SPKAKKAPKK EPAEKKPKKQ NGDGLKQGKL DFSKGKKKES LDSSGELAEE VPRVERPGRR
AASKKINYSF LISDEEGEEH DETNNDNDDD MDDSPIKRPA AKRQREDDSS GGAKKKAAAK
KARALDSESS DDDVVGVDDD DDSDFEA
//
