ID A0A3Q2I7B7_HORSE Unreviewed; 1578 AA.
AC A0A3Q2I7B7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=TOP2B {ECO:0000313|Ensembl:ENSECAP00000043845.2,
GN ECO:0000313|VGNC:VGNC:50517};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000043845.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000043845.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000043845.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000043845.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000043845.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Key decatenating enzyme that alters DNA topology by binding
CC to two double-stranded DNA molecules, generating a double-stranded
CC break in one of the strands, passing the intact strand through the
CC broken strand, and religating the broken strand.
CC {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|RuleBase:RU362094};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU362094};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR STRING; 9796.ENSECAP00000043845; -.
DR PaxDb; 9796-ENSECAP00000043845; -.
DR Ensembl; ENSECAT00000041409.2; ENSECAP00000043845.2; ENSECAG00000005608.3.
DR VGNC; VGNC:50517; TOP2B.
DR GeneTree; ENSGT00940000157921; -.
DR InParanoid; A0A3Q2I7B7; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000002281; Chromosome 16.
DR Bgee; ENSECAG00000005608; Expressed in endometrium and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2I7B7; baseline.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
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; IPR012542; DTHCT.
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:SF36; DNA TOPOISOMERASE 2-BETA; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF08070; DTHCT; 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; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 468..585
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1102..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1578 AA; 178242 MW; 694E36EB056D098E CRC64;
MAKAGGGGAG AGGNGALTWV NNAARKEELE TANKNDPSKK LSVERVYQKK TQLEHILLRP
DTYIGSVEPL TQLMWVYDED VGMNCREVTF VPGLYKIFDE ILVNAADNKQ RDKNMTCIKV
SIDPESNIIS IWNNGKGIPV VEHKVEKVYV PALIFGQLLT SSNYDDDEKK VTGGRNGYGA
KLCNIFSTKF TVETACKEYK HSFKQTWMNN MMKTSEAKIK HFDGEDYTCI TFQPDLSKFK
MEKLDKDIVA LMTRRAYDLA GSCKGVKVMF NGKKLPVNGF RSYVDLYVKD KLDETGVALK
VIHELANERW DVCLTLSEKG FQQISFVNSI ATTKGGRHVD YVVDQVVSKL IEVVKKKNKA
GVSVKPFQVK NHIWVFINCL IENPTFDSQT KENMTLQPKS FGSKCQLSEK FFKAASNCGI
VESILNWVKF KAQTQLNKKC SSVKYSKIKG IPKLDDANDA GGKHSLECTL ILTEGDSAKS
LAVSGLGVIG RDRYGVFPLR GKILNVREAS HKQIMENAEI NNIIKIVGLQ YKKSYDDAES
LKTLRYGKIM IMTDQDQDGS HIKGLLINFI HHNWPSLLKH GFLEEFITPI VKASKNKQEL
SFYSIPEFDE WKKHIENQKA WKIKYYKGLG TSTAKEAKEY FADMERHRIL FRYAGPEDDA
AITLAFSKKK IDDRKEWLTN FMEDRRQRRL HGLPEQFLYG TATKHLTYND FINKELILFS
NSDNERSIPS LVDGFKPGQR KVLFTCFKRN DKREVKVAQL AGSVAEMSAY HHGEQALMMT
IVNLAQNFVG SNNINLLQPI GQFGTRLHGG KDAASPRYIF TMLSSLARLL FPAVDDNLLK
FLYDDNQRVE PEWYIPIIPM VLINGAEGIG TGWACKLPNY DAREIVNNVR RMLEGLDPHP
MLPNYKNFKG TIQELGQNQY AVSGEIFVVD RNTVEITELP VRTWTQVYKE QVLEPMLNGT
DKTPALISDY KEYHTDTTVK FVVKMTEEKL AQAEAAGLHK VFKLQTTLTC NSMVLFDHMG
CLKKYETVQD ILKEFFDLRL SYYGLRKEWL VGMLGAESTK LNNQARFILE KIQGKITIEN
RSKKDLIQML VQRGYESDPV KAWKEAQEKA AEEEETQNQH DDSSSDSGTP SGPDFNYILN
MSLWSLTKEK VEELIKQRDA KGREVNDLKR KSPSDLWKED LAAFVEELDK VEAQEREDIL
AGMAGKAIKG KVGKPKVKKL QLEETMPSPY GRRVVPEITA MKADASKKLL KKKKGDLDTT
AVKVEFDEEF SGTPVESTGE EALIPPTSIN KGPKPKREKK EPGTRVRKTP TSSGKSSAKK
VKKRNPWSDD ESKSESDLEE TEPVVIPRDS LLRRAAAERP KYTFDFSEEE EEDADDDDDN
NDLEELKVKA SPITNDGEDE FVPSDGLDKD EYTFSPGKSK AIPEKSSHDK KTQDFGNLFS
FPSYSQKSED GKPSSDTTPK PKRTPKAKKV ETVNSDSDSE FGIPKKTTTP KGKGRGAKKR
KASGSENEGD YNPGRKTSKP ASKKPKKTSF DQDSDVDIFP SDFTSEPPSL PRTGRARKEV
KYFAESDEEE DVDFAMFN
//
