ID A0A2U4CFF7_TURTR Unreviewed; 1618 AA.
AC A0A2U4CFF7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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|RefSeq:XP_019804177.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019804177.1};
RN [1] {ECO:0000313|RefSeq:XP_019804177.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019804177.1};
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_019804177.1; XM_019948618.2.
DR GeneID; 101333334; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000245320; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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 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:UP000245320};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 472..589
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1106..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1618 AA; 182126 MW; 9614BE53CC1A8A84 CRC64;
MAKAGGGGGG SGAGAGGLGA LTWVNNAAKK EESETANKND SSKKLSVERV YQKKTQLEHI
LLRPDTYIGS VEPLTQLMWV YDEDVGMNCR EVTFVPGLYK IFDEILVNAA DNKQRDKNMT
CIKVSIDPES NIISIWNNGK GIPVVEHKVE KVYVPALIFG QLLTSSNYDD DEKKVTGGRN
GYGAKLCNIF STKFTVETAC KEYKHSFKQT WMNNMMKTSE AKIKHFDGED YTCITFQPDL
SKFKMEKLDK DIVALMTRRA YDLAGSCKGV KVMFNGKKLP VNGFRSYVDL YVKDKLDETG
VALKVIHELA NERWDVCLTL SEKGFQQISF VNSIATTKGG RHVDYVVDQV VGKLIEVVKK
KNKAGVSVKP FQVKNHIWVF INCLIENPSF DSQTKENMTL QPKSFGSKCQ LSEKFFKAAS
NCGIVESILN WVKFKAQTQL NKKCSSVKYS KIKGIPKLDD ANDAGGRHSL ECTLILTEGD
SAKSLAVSGL GVIGRDRYGV FPLRGKILNV REASHKQIME NAEINNIIKI VGLQYKKSYD
DAESLKTLRY GKIMIMTDQD QDGSHIKGLL INFIHHNWPS LLKHGFLEEF ITPIVKASKN
KQELSFYSIP EFDEWKKHIE NQKAWKIKYY KGLGTSTAKE AKEYFADMER HRILFRYAGP
EDDAAITLAF SKKKIDDRKE WLTNFMEDRR QRRLHGLPEQ FLYGTATKHL TYNDFINKEL
ILFSNSDNER SIPSLVDGFK PGQRKVLFTC FKRNDKREVK VAQLAGSVAE MSAYHHGEQA
LMMTIVNLAQ NFVGSNNINL LQPIGQFGTR LHGGKDAASP RYIFTMLSSL ARLLFPAVDD
NLLKFLYDDN QRVEPEWYIP IIPMVLINGA EGIGTGWACK LPNYDAREIV NNVRRMLEGL
DPHPMLPNYK NFKGTIQELG QNQYAVSGEI FVVDRNTVEI TELPVRTWTQ VYKEQVLEPM
LNGTDKTPAL ISDYKEYHTD TTVKFVVKMT EEKLAQAEAA GLHKVFKLQT TLTCNSMVLF
DHMGCLKKYE TVQDILKEFF DLRLSYYGLR KEWLVGMLGA ESTKLNNQAR FILEKIQGKI
TIENRSKKDL IQMLVQRGYE SDPVKAWKEA QEKAAEEEET QNQHDDSSSD SGTPSGPDFN
YILNMSLWSL TKEKVEELIK QRDAKGREVN DLKRKSPSDL WKEDLAAFVE ELDKVEVQER
EDLLAGMAGK AIKGKVGKPK VKKLQLEETM PSPFGRRIVP EITAMKADAS KKLLKKKKGD
LDTTAVKVEF DEEFSGAQVE GAGEEALIPS APINKGPKPK REKKEPGTRV RKAPTSSGKP
SAKKVKKRNP WSDDESKSES DLEETEPVVI PRDSLLRRAA AERPKYTFDF SEEEDDDADD
DDDNNDLEEL KVKASPITND GEDEFVPSDG LDKDEYTFSP GKSKASPEKS SHDKGQDYGN
LFSFPSYSQK SEDDSAKFDS NEEDSASVFS PSFGLKQTEK VPSKTVAAKK GKPSLDTAPK
PKRTPKQKKV ETVNSDSDSE FGVPKKTTAP KGKGRGAKKR KASGSENEGD YNPGRKTSRT
TSKKPKKTSF DQDSDVDIFP SDFTSEPPSL PRTGRARKEV KYFAESDEED DVDFAMFN
//
