ID A0A0L7M802_PLAF4 Unreviewed; 1343 AA.
AC A0A0L7M802;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=PFDG_03941 {ECO:0000313|EMBL:KOB88946.1};
OS Plasmodium falciparum (isolate Dd2).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57267 {ECO:0000313|EMBL:KOB88946.1, ECO:0000313|Proteomes:UP000054282};
RN [1] {ECO:0000313|Proteomes:UP000054282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum Dd2.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Kodira C., Zeng Q., O'Leary S., Yandava C., Alvarado L., Wirth D.,
RA Volkman S., Hartl D.;
RT "The genome sequence of Plasmodium falciparum Dd2.";
RL Submitted (SEP-2006) 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}.
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DR EMBL; GG701838; KOB88946.1; -; Genomic_DNA.
DR EnsemblProtists; KOB88946; KOB88946; PFDG_03941.
DR OMA; TWTQDFK; -.
DR Proteomes; UP000054282; 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:UP000054282};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 493..608
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 260..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1153..1180
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1261..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 154965 MW; 185A3E2DBA403DDD CRC64;
MAKNKTIEER YQKKSQIEHI LLRPDTYIGS VEMHTQLLWV WNKEKNRMVQ KNITYVPGLY
KIFDEIIVNA ADVKAREKEK SENPMTCIKI EINKENKRIS VYNDGEGIPV DIHKEMNIYV
PHMIFGELLT SDNYDDAEDR ITGGRNGFGA KLTNIFSKEF IVQCGDSSRK KEFKMTWSDN
MSKFSEPHIK NYNGKDYVKV TFKPDLNKFG MTEMDDDIES LLFKRVYDLA GTCSVRVYLN
GQRLAVKDFK SYVDLYLKDN SNDNKNNKGQ NDNNNNNNNN NDENANQNND NLDVSLSNEP
ADGTPTKNNN NNNNNNDEDE IVKIHEKQHR WEIVVSKSDG SQFQQVSFVN SICTTKGGSH
VNYIVEQLLS SLSKKANAKN KGGMEIKSGH IRNHLWVFVN CLIVNPTFDS QTKETLTTKP
VKFGSKCILS DKTINNVLKS PILSNILLWA QAKAQVELKK KMKAGSSKAR ERIIGIPKLE
DANDAGSKYS QECTLILTEG DSAKTSCLAG LSIVGRDKYG VFPLKGKLLN VRDASFKQLM
DNKEIQNIFR IMGLDITDKN KDDIKGLRYG SLMIMTDQDY DGSHIKGLLI NMIHKFWPSL
LKHKGFLSEF VTPIVKVQKG SQEYSFFTIA EYEQWKENTN LLGWKIKYYK GLGTSTDREF
KQYFSDIKNH KIMFLWTGDR DGDSIDMAFS KKRIEDRKLW LQNFILGSYV DHKEKDLSYY
DFVNKELIYY SRYDTERSIP NIMDGWKPGQ RKVLYGCFKR NLRNECKVAQ LVGYIAEHSA
YHHGESSLQQ TIINMAQTFV GSNNINFLEP CGQFGSRKEG GKDASAARYI FTKLASSTRS
IFNEYDDPIL KYLNEEGQKI EPQYYIPVIP TILVNGCEGI GTGYSSFIPN YNYKDIIDNI
KRYINKEPLI PMVPWYKDFK GRIESNGKTG YETIGIINKI DNDTLEITEL PIKKWTQDYK
EFLEELLTDE KHQLILDYID NSSHEDICFT IKMDPAKLQK AEEEGLEKVF KLKSTLTTTN
MTLFDPNLKL QRYSTELDIL KEFCYQRLKA YENRKSYLIS KLEKEKRIIS NKTKFILAIV
NNELIVNKKK KKVLVEELYR KGYDPYKDIN KIKKEEIFEQ ELLDAADNPE DNEEIIAGIT
VKDYDYLLSM PIFSLTLEKV EDLLTQLKEK ERELEILRNI TVETMWLKDI EKVEEAIEFQ
RNVELSNREE SNKFKVARKQ GPSSMKKKKK KKKLSSDEES EGGDTSDSSE FLVNTLNIKK
NTNKKTTTSS NNVNNSKKRL RKADDLNSNE LDNTLSVSKT FDDNNNLTDN TPLINRLNDE
NNEFSSNNVD NKSTNKNSRK KKP
//
