ID D8U578_VOLCA Unreviewed; 1126 AA.
AC D8U578;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=VOLCADRAFT_94598 {ECO:0000313|EMBL:EFJ45103.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ45103.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
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; GL378359; EFJ45103.1; -; Genomic_DNA.
DR RefSeq; XP_002953779.1; XM_002953733.1.
DR AlphaFoldDB; D8U578; -.
DR STRING; 3068.D8U578; -.
DR GeneID; 9616934; -.
DR KEGG; vcn:VOLCADRAFT_94598; -.
DR eggNOG; KOG0355; Eukaryota.
DR InParanoid; D8U578; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000001058; 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:UP000001058};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 439..553
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 1126 AA; 127918 MW; CC7E0827840C2FE1 CRC64;
MYQKKTQLEH IILRPDTYIG STERQPNTIW VHNGQKMELK TVNYPPGLYK IFDEILVNAA
DNKVRDPTMD TIKVDVDPAN NSIRVWNSGR GIPVEVHKEE GVYVPELIFG HLLTSSNYND
SEKKITGGRN GYGAKLANIF STEFTVETCD GSRQRRYKQT FTNNMQQKGT PKITDCKASD
NWTCITFKPD LAKFGMSELD EDIVSVLRRR VFDMAGVLGK GVKVFYNGER LSIKSFQEYV
DMYLGPKVKR TWFRGVPHDN GIPRFCERLN DRWEICISLT DGSFQQVSFV NAISTQKGGT
HVEYIVNQIV KHCIEKLSKK TAKTTAIKPA MVRNHLWIFL NCYVENPAFD SQASPFKIVL
LTKETLTLRS TSFGSKCELP IPLLDKVLKA GLSDSIIKYA EFKSQKDLKK GDGVKRSRLV
GMAKLDDAND AGGPRSTDCT LILTEGDSAK SLAVSGLGVV GRNHYGVFPL RGKLLNVREA
SAVQIAANQE IQNIKQIMGL QHGRVYDSTS SLRYGHLMIM TDQDHDGSHI KGLIMNFMHS
FFPSLLKIPG FMLEFITPIV KARRGRETKV FYTMPEYEAW KESLDNNTSG WDIKYYKGLG
TSTKEEAQEY FSRLNLHRKE FVWTGDEDGD AIELAFSKKR VDDRKEWLSN FVPGTYLDQS
AEKISYADFI NKELILFSRA DLDRSIPNVL DGLKPGQRKI MFACFKRNLK KDIKVAQLSA
YVAEHSAYHH GEQSLASTIV NLAQDFVGSN NINLLHPSGQ FGTRLQGGKD AASARYIYTR
LEKLTRHLFN EHDDVLLKYL NEEGQSIEPE WYLPILPTVL VNGAEGIGTG WSTFIPNYNP
RDIIANLRRL LNGEEQDPLH PWYRGFTGTI TEVPHKSGSR SYVVGGLVAQ TGPNTIEVTE
LPVRKWTQDY KEFLETLLRP QDKDEAPLIA DYHEHHSDSN VHFVVELLPG KLDELLATPG
GLEAKFKLQA KVTTSNMMLF QKDGIIKHYQ SPEAIIAEFF ELRLDYYEKR RIAMLRFAQM
DQMRADNKVR FILAVVHGKL EVRNRKRVDI EKDLEAQGFD RMSKTNTATK VNLSIPVVQS
CMLNPSFNFV DRSTTYLLRG TMRTARRRAR RANQVTSTCY PCQFTA
//
