ID M3HI84_CANMX Unreviewed; 1427 AA.
AC M3HI84;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635, ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|RuleBase:RU362094};
GN ORFNames=G210_2691 {ECO:0000313|EMBL:EMG47037.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47037.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47037.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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:EMG47037.1}.
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DR EMBL; AOGT01001758; EMG47037.1; -; Genomic_DNA.
DR STRING; 1245528.M3HI84; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_1_1; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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 GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
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; 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; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 498..614
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1427
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1427 AA; 160908 MW; E77E971F6C6A5A99 CRC64;
MSDSESDYYT DGSDEDFGST SSSKSTTKKN ASSKKQPLAD STNNTSSSSS NGKPSGASET
YQKLSQLEHI LKRPDTYIGS VEKTSIEMWC FDADTESMVF KEVTIVPGLY KIFDEILVNA
ADNKIRDPTM KNIRVKIDPE NNVIEVMNDG KGIPVEMHTK EKMYIPELIF GNLLTSSNYD
DNEKKVTGGR NGFGAKLCNI FSTEFEVETA DLNMGKLYKQ TWTDNMTKVT TPKITKLKTK
KEYTKITFKP DLSKFDMDSL DADLLSVLRR RVYDLCGTVK NCNIYLNDKK LSISSFKSYV
EMYVKAIKER SPEPEPTEDG ALKNYTTIVH EVFNDRWEVA FAVSDGSFNQ VSFVNSIATT
SGGTHVKYVS DQIINKLIEA ISKKEKGKKK IMVRPQEVRD NMFLFVNCLI ENPAFTSQTK
EQLTTKVSQF GGKDKFVAND NLINRILKTS IVEKIRSIAR ANEDKALQKA DGSRKSRIKG
QVSLVDANKA GTKDGQKCTL ILTEGLSALN LAVAGLAVVG RDFYGCFPLR GKLLNVREAS
ADQIAKNAEI NALKQIVGLQ HKKTYTPENI KSLRYGHIMI MTDQDQDGSH IKGLIINFLE
TSFPGLLDIP GFLLEFITPI VKVTIKTRGT GASRVIPFYT MPEFEKWRDD EGTRCRWTHK
YYKGLGTSTP MEAREYFTAL DRHLKKFHAL QGDDASFIDL AFSKKKADER KEWLQGYVPG
THLDPNITEI PISDFINKEL ILFSMSDNIR SIPSVLDGLK PGQRKVLYGC IKKRLTSEIK
VAQLAGYVSE NTGYHHGEQS LVQTIIGLAQ NFVGSNNINI LKPNGSFGSR AAGGKDFSAA
RYIFTELNEI TRRIFNPLDD PLYTYVQDDE QTVEPEWYLP VLPMILVNGA EGIGTGWSTN
IPSYNPKDLI SNIRKMLDGE EPESMIPWYR GWTGDVELNA PQKYRVTGRI EQVDDNTVEI
TEIPIKTWTN NVKEFLLAGF GNEKTQPWIK DMEEHHTTSI RFVVKLSDAE MQKSLRVGLL
ERFKLIGSIS TANMIAFDEH GRIKKYNDTL EILKDFYYVR LEYYQKRKDF MIDNLQNELS
LIGERARFVK LIIDKQISVA NKRKKDLFKI LEDHKFIKFT KNGKPMTTST PSASIVEDGE
EAEEEEEADS SSGYNYLLSM AIWSLTREHF ERLLKQRDEK EKELEILLSK SAKDLWRADL
IDFETEYDKF LIRDEQERES LASGKSKKPT KRRIKAATKS EPPAKKIKTE SKVKKESTPS
TKSSTPATKT TTTAEAAPKK KTDDILSFFS PTGSKTKKST TDAGSAANPI SIFSDDDDDD
GLFVNDSSST VKKEPKSRSK SSTPQPAVEK PKKTTKAKPS ILDELDDLEI DANFETSDEP
TGRRKRGTTR TAKKPIIIDS EDEEDDDMIV DDDDDEDDDG SFIDEDD
//
