ID A0A2P6TW43_CHLSO Unreviewed; 1565 AA.
AC A0A2P6TW43;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=C2E21_2888 {ECO:0000313|EMBL:PRW58281.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW58281.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW58281.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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:PRW58281.1}.
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DR EMBL; LHPG02000005; PRW58281.1; -; Genomic_DNA.
DR STRING; 3076.A0A2P6TW43; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000239899; 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:UP000239899};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 453..575
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1565 AA; 171608 MW; 4C4ABF7B0F4896BF CRC64;
MEIDSENVAQ PVKAPKAKAK AAKPAAGGGG KTIEETYQKL SQLEHILLRP DTYIGSTEAQ
EQQLWVHDGD RMVFKNIRFV PGLYKIFDEI LVNAADNKVR DPTMDTLRVD VDAAKGCIKV
LNSGAGIPVE IHQKEGIYVP ELIFGNLLTS SNYNDNEKKV TGGRNGYGAK LANIFSTKFV
VETCDGKRGR RYKQTFSKNM SKKGEPVITD CGKDENWTCI TFYPDLERFG MTELEEETVQ
LMRKRVYDMA GILGKTVKVY LNGTRLKVKT FQEYVEMYLG PKESGVPRVY ERFSDRWEVC
VATTEGQFNQ VSFVNAICTS KGGTHVNYIA DQVVKNLCEM INKKDKKANV KPFMAKNYLW
VFVNCLIENP AFDSQTKDTL TLRASSFGSK CELPDPFLKK VANCGVVDLI LSFASFKADK
ELKKGDGAKR QRLTGIPKLE DANDAGGRSS EHCTLILTEG DSAKSLAVAG LSVVGRDRFG
VFPLRGKLLN VRDASAAQIT GNAEIQNIKQ ILGLQHGKVY SDVKSLRYGH LMIMTDQDHD
GSHIKGLLMN YFHHFYPSLL KLPGFLVEFI TPIIKVTKGK ESIAFYTLPE YEEWKEHTNL
RGWSIKYYKG LGTSTAAEAK HYFANIQSHR KEFTWDGEDD GKALEMAFSK KKVEERKQWL
QSFVPGTFLD QSVDTISYSD FVHKELILFS RADLERSIPC MVDGLKPGQR KIMFACFKRN
LKSDIKVAQL SGYVAEHSAY HHGEASLSGT IVGLAQDFVG SNNINYLVPQ GQFGTRLQGG
KDAASARYIF TRLAPMTRHL YNEHDDRLLA YLTEEGQSIE PEWYMPIVPT VLVNGAEGIG
TGWSTSIPNY NPRDLVANLR RMLDGEQPEP MKPWYRGFKG TIEEVPTKTS GKSYQICGVI
NQVDDTTLEI TELPIRKWTQ DYKEFLEDMV KPEDKNATPF IQDYKEYHTD VSVKFRITLS
EAKMREALAA GLLDKFKLKS KISTGNMMLF NSDGVIQKYA TPEDILRDFY DLRLQFYAKR
RAALLRAAEA DLCRISNKVR FILAVVSGEL KLSNRRKADI EAELEDEGYD KLPSQKKAKA
QAAADPEEEG EEGAEVAGAS YDYLLSMPLS SLTLEKVEAL KKEADDWKET VERLRGTTEK
DMWRTDLEAF EIALDEYEEE QERSQAQLAR QQAKAAKHQA ALQKKATTKG KKKKGHEWSD
DEDELSDSEN DFEDDDFEDF RKPKAAAKPR QRAAPAPRAV PAASGATSMQ TSQQTGTTVG
TKRSAGGAAA KKPAAAKPAA ALPPKAPAAP PPPPPAEEEM SLMARLAGRM GALGLSPKSA
AAAPAAPAAA AAAPAASGRT TSAGGRPGRA AAAAAAKKTS KIVVISEEED ESEPSSASEE
ESDDEVNSPA VKPEPKKRGR GGAAAAKNTL AAKAMANAGK QQAAAPAQAA YDFALVDDDE
VAASPLPAPK PKVQRMRPSP FNKQSGVAKG AKAAAGPSKL GGGAKAAAAA PAGKGKAKKV
VDDSEDEDEE DVIDMSVSPA PARVAVPRRG AAAKKPVSYR EASDSEGEED ASSSEEEGSD
YAPSD
//
