ID A0A267H9T8_9PLAT Unreviewed; 1536 AA.
AC A0A267H9T8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig014497g1 {ECO:0000313|EMBL:PAA94319.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA94319.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA94319.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA94319.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA94319.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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:PAA94319.1}.
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DR EMBL; NIVC01000012; PAA94319.1; -; Genomic_DNA.
DR STRING; 282301.A0A267H9T8; -.
DR Proteomes; UP000215902; 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; SM00387; HATPase_c; 1.
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:UP000215902};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 456..575
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA94319.1"
SQ SEQUENCE 1536 AA; 171919 MW; 097E5AEBE39BCE6E CRC64;
AKMSSETDNL GPLASPLSDA ANRFGGGSGK QRMSVEKIYQ KKTQLEHILL RPDTYIGSVE
SVRQNMWVYD STAKRMIERE ITFVPGLYKI FDEVLVNAAD NKQRDPGMSC IRITISKEDN
LIEVWNNGKG IPVVEHKKEK LYVPTLIFGH LLTSSNFNDS EKKTTGGRNG YGAKLCNVYS
RQFTVETSCK ESGKRFQQTW TDNMGKAGEA KIMKNGAEDY TKVSFKPDLT KFGMTELDDD
TIALFSRRAF DIAGTCSGVR VFLNGEKLPV TSFKDYYRLY LTEKEDKEVA IIKSGRWELA
VCLSNDGFKQ VSFVNSIATT KGGRHVDFVC DLLLKRLVDA IDGKCKADKK NLKGSIKPAF
VKNHLWIFCN CLIENPSFDS QTKEFMTLQA KKFGSAPELD DKFFKKLLSE DCGIVRCVLE
YADFKTNKAL NQRTKASKKT FHEKLDHANN AGKGECVLIL TEGDSAKSLA VAGASSLPDG
RDRFGVFPLK GKLLNVREAS KDQLMNNKEI KVIQDAVNLQ YGKKYNTVED LKSLRYRHIM
IMTDQDQDGS HIKGLIINFI HFFWPELLRH DFLQEFITPI VKVTKRDQVK AFYSMPEFDE
WRGQTPDWHK WHVKYYKGLG TSTAKEGREY FRDMRRHCVR FIRRDQTDEE SILMAFGKNA
DMRKDWLLKF MDDRKRRADL GLPEAYLYEK TTREISYNDF VHKELVLFSN ADNERSIPSL
VDGLKPGQRK VMYTCFKRNL LKEIKVAQLA GSVSEISAYH HGEASLVGTI INLAQDFVGS
NNLNLLMPNG QFGSRLQGGK DAAAARYIHT CLSPLARIIF NPNDEPMLEY NVDDNQRVEP
VWYIPIIPMV LINGADGIGT GWSTKIPNYS VDDVIANLRR MLRDEEPRDM LPSYRGFTGI
IRQTDAQRYV SYGEVRTFGD ANVVEITELP VKVWSEPYQD SVLKVGVEGG DGAGGGAGGK
KKTDRKESKP NEQLLEDFNN YCSDTHVRLV VKLKPEQMAN ARQVGLHKYF KLQNTFSTSS
MVLFDRNCCL KRYDSVLDIL REFYSLRLEW YEKRKAYLLG RLGSESLLLD NQARFVQEKI
DNLIRIENVA KKKIVAILVE RGYDSDPVKA WRSQQPYYQQ LQQIAKSAGT AAAGADEDAA
TADDDDDEAA AADAGQSVAD FDYILRMPLW SLTLERKEKL LKDRADKAEQ MRVLRAKTPK
DLWSEDLDEL EAKMRQIGEE TAKADRKAAR GKAKRAGSDD DDFESDGDDS GEEYGKKKKP
KKKPAGKKAG KGAAGAAIEL PRVSPTVVEP AMEEPAKPKQ PRAPKAPKAA KEPKDSSKQL
KLSDMGVSVG KQAAASKKTK KSDDPFASSS DDNDETDEKV KLPLWKRVSL SKPEAAADLA
EFAGASSSAG TTETAATTKP KKRMLGPNTL PEPAMPAAKK PRQKKPAAPK ADKDDKKKSK
PKATKKSKKA MWGSSDDDNT SASSDANDSD NVGASDNDDE GGEAAGSPPP PPRERTERRG
AAAKAKYVFD DSSEDDDNQM AGGGRKRRDS LDSVDD
//
