ID A0A2P6TJG2_CHLSO Unreviewed; 783 AA.
AC A0A2P6TJG2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=C2E21_7085 {ECO:0000313|EMBL:PRW39388.1};
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:PRW39388.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW39388.1, 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=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 GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {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:PRW39388.1}.
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DR EMBL; LHPG02000014; PRW39388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6TJG2; -.
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; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 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 InterPro; IPR002288; DNA_gyrase_B_C.
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; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 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|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 567..680
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 300..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 82879 MW; 1FBC54C20528641D CRC64;
MRACIVRAAR AARQCARLAS SPLQPAAATS SVALRSSQLL IARGEPQQGR RLSTAAAAAS
RSPAASAAAA EVAEPAAAEA STSYGAQQIQ VLQGLEPVRK RPGMYIGSTG QRGLHHLVYE
ILDNAIDEVQ AGFATEVYVE LDLTSGWVTI SDNGRGIPTD IHPATGKSAL ETVLTVLHAG
GKFGGDSSGY AVSGGLHGVG VSVVNALSNQ LEVTVWRGSK QFSQSFSRGV AQGPLQEAAA
APAANGRQPR NGTQVRFIYD DTIFSKTATF DPDTIRSRLR ELAFLNSRAT IFFRVLDGKS
GKAASSSSSN GSSGGSSAAA SGKAAAASSS SSSSGGSAAA ALAAEAAATL SPAAAQAAAD
GWEVLHFAGG LAEYVRYLNR DKAAIHEPIC FSKQVNGFTV EVALQWCSDA FSDTIIGFVN
SIKTVDGGTH IDGAKAALTR TVNSLARKLK VLKEGDANLA GDYIREGLGA VVSVKVPNPE
FEGQTKTRLG NPEVRKVVEG VVGAEASEAL EMDPTTLNTV LAKAMQAFKA AEAAKKAREL
VRRKSVLTKS TLPGKLADCA STNRDECEIF LVEGDSAGGS TKQARDRRTQ AVLPLRGKIL
NVERQDDAKL YKSSEISNLI VGLGLGLKGE DLGALRYGKI IILTDADVDG AHIRTLLLTF
LFRYQRQLFE QGYVYVGVPP LYKLEVGRKA QYCYTEEELK AATAQLTPGS YHVQRFKGLG
EMMPEQLWQT TLNPATRTLR KLTIEDAAEA SHMFALLMGD KVGPRRELIE RHGSRLALEE
LDI
//
