ID A0A1J1HH63_PLARL Unreviewed; 1534 AA.
AC A0A1J1HH63;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=PRELSG_1317600 {ECO:0000313|EMBL:CRH03817.1};
OS Plasmodium relictum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:CRH03817.1, ECO:0000313|Proteomes:UP000220158};
RN [1] {ECO:0000313|EMBL:CRH03817.1, ECO:0000313|Proteomes:UP000220158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGS1 {ECO:0000313|EMBL:CRH03817.1,
RC ECO:0000313|Proteomes:UP000220158};
RG Pathogen Informatics;
RL Submitted (APR-2015) 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; LN835308; CRH03817.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PRELSG_1317600; -.
DR OMA; NESMDYN; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000220158; Chromosome 13.
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:UP000220158};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 482..597
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 262..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1142..1169
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1473..1491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1534 AA; 176799 MW; B9374CB2720623FE CRC64;
MSKKKTIEER YQKKSQIEHI LLRPDTYIGS VEMHTQFLWV WNKNKNRMIQ KNITYVPGLY
KIFDEIIVNA ADVKAREKNK CENPMTCIKI EVNRENNKIS VFNDGEGIPV EMHKEMNIYV
PHMIFGELLT SDNYDDEEDR ITGGRNGFGA KLTNIFSKEF IVQCGDAKRK KEFKMTWTNN
MSKFSEPQIK TYNGKDFVKV TFKPDLSKFG MTAMDDDIES LIYKRVYDLA GTCNVKVFLN
GTRLGVKDFK SYVDLYLKDN SSNANSKTQN SSSETIANQN FTNPENSEAN DLEESPKSNI
NGNVNDDEEI VKIHEKQHRW EIVISRSDGS QFQQVSFVNS ICTTKGGSHV NYIVDQLLNA
LSKKANAKNK GGMEIKSGHI KNHLWVFVNC LIVNPTFDSQ TKETLTTKPV KFGSKCILSD
KTINSVLKSS ILSNILLWAQ AKAQVELKKK MKAGSSKARE RIIGIPKLED ANDAGSKYSQ
ECTLILTEGD SAKTSCLAGL SIVGRDRYGV FPLKGKLLNV RDASFKQLMD NKEIQNIFRI
MGLDITDKNK NDIKGLRYGS LMIMTDQDYD GSHIKGLLIN MIHKFWPSLL KHKGFLSEFV
TPIVKVQKGN QEHSFFTIAE YEQWKENTNL AGWKIKYYKG LGTSTDKEFK QYFSDIKNHK
IVFLWTGDRD GDSIDMAFSK KRIEDRKVWL QNFIIGSYVD HKEKDLSFYD FVNKELIYYS
RYDTERSIPN IMDGWKPGQR KVLYGCFKRN LKNECKVAQL VGYIAEHSAY HHGESSLQQT
IINMAQTFVG SNNINFLEPC GQFGSRKEGG KDASAARYIF TKLASSTRYI FNEYDDPILK
YLNEEGQKIE PQYYIPVIPT ILVNGCEGIG TGYSSFIPNY NYKDIINNIK RYINKEPLIP
MIPWYKDFKG RIESNGKTGY ETIGIIKKLD EETLEITELP IKKWTQDYKE FLEELLTDEK
NQLIIDYIDN SSHEDICFTI KMDPNKLKKA EEEGLEKVFK LKSTLTTTNM TLFDPNLKLQ
RYSTELDILK EFCFHRLKAY QSRKDYLISK LEKEKKIISN KAKFILAIVN NELIVNKKKR
RVIVEELYRR GYDPYKDINK LSKKEIFEQE LLENAENLED NEEIIAGISL KDYDYLLGMP
IYSLTLEKVE ELLAQHKEKE RELEILKNIT IETMWLKDIE KVEEAVELQR NIELANREES
NKFKVAKRQG INAFRRKKKK KKLSTDESEG DTTDSSDFIL NTLNIKKKKK DNNNNNKRLK
KVDDRNYNKS SLLYNSELDY SLSCTKTFDD TNISDTSPIL NRIINKKNIN NNNTKENNDY
FSSNNNKALN ESSFNKTNSI YKLNNENDIN SSKYSDKKSS YFFDLSHDSD TNNQNKKNIS
SNNVNDKNDI SNSHSITPNR QIDISLINSV NMNEFTNVDN NNNNDSLQVD NNQNITISPN
KTININEFSS IKNKLLELEK KKKPRLTLAE KIKMKNSEKI NTEDKQKLET SPTNKPKSSL
LGDDLKSKKG SNIDSESSKG NIESSEDSES SYDI
//
