ID A0A250XNU3_9CHLO Unreviewed; 1094 AA.
AC A0A250XNU3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=CEUSTIGMA_g12183.t1 {ECO:0000313|EMBL:GAX84761.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX84761.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX84761.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX84761.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-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:GAX84761.1}.
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DR EMBL; BEGY01000135; GAX84761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250XNU3; -.
DR STRING; 1157962.A0A250XNU3; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000232323; 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 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 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; 2.
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:UP000232323};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 402..529
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 703..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 120674 MW; 7C71AC7B55F6F797 CRC64;
MEAAQFKRLS HREHVLLRPD MYVGPTTPET TAAYVLGAEK AGGGGAEKGG GMVLRTDIQY
VPALLKIFDE ILVNAIDHCV RSRQMQTASD DVQPTKRIDV SIGEDGSVTV SNDGDGIPVE
RTGDGMYVPE LIFGHLLTSA NYDDAADGGG GRTIGGQNGI GAKACNILSK YFEVDVVDRK
RGLRFRQRFE HNMSVTLPPE VEKSRLKRSY TTVKAFDKYV GLFLAEGQPH AYARVAGWEI
AAAFLEEGTG LRQVSFVNGV ATLRGGRHVD HVVQQISRRL CDLVEKRRKG GGGSGSGSPK
PQYVKDNLLV FVRATVPNPK FDSQAKETLT TPVSQFGQKV EVPDAFVEKL YRIEGLVVRL
VGLSGVAMDR EAKKSDGSKR ARVSVPKLED AEWAGTGRSD KCTLILTEGD SAKASAVSGM
SVVGRDRFGV FPLRGKVLNV CDVSADKVSS NAEISAIKKI LGLQTGKAYA SAAELRYGRV
MLMTDADTDG SHIKGLVMNL FMQQWPSLLR LDGFFCALLT PVVKAFFPPP RPPLEFYNAS
EFEAWRQENP GLASKCNSKY YKGLGTSTAE EAREWFRRMR IRGHAGGAGK GLRQEAGRRP
QGVAPHVRAV QDDRVRQVRR ALLRLRGARA GALQQLRRAA VHPVGGGRAE SVAAEGNTRV
LQAEAERRQA GDAGGAARCL RRGGHLLPPR GGVHAGHPGV HGAGLRGQRQ QRPAPVANRA
VRDPPRGREA DADVLTTLTD DGVPIEPKHF LPVLPIVLLN GATGIGTGYS TTVPSYNPRE
VADAVRAWID RRGERWMEGR ERLEPWCAGH LGKIEATGED LSKRRSRGVV TRSAPKAAVV
SELPIGMWTD DFREALEALV ERCDDIRSFS NESSEATVRF TVQFSYETAA DSWLARSATD
ERLTRLEAEL RMVGTRGLGT GNMHLFNARS QIQRFESAEQ ILEAFCEVRL EGYVRRRQIQ
IARAIEEACT LKNRVRFVEL VVDGSLNLHD EHVEKAMEAV GLMRKYDHSK EDQDHSKEDQ
EDHRKDDHND RGYGYLLSMP MRSMTHQRLS KLRALQDEKQ RTVEALEADD ALQMWRRDID
YFMAVYDGCE KKTP
//
