ID G5E707_LOXAF Unreviewed; 1604 AA.
AC G5E707;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ENSLAFP00000013292.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000013292.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000013292.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013292.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000013292.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013292.3};
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; 9785.ENSLAFP00000013292; -.
DR Ensembl; ENSLAFT00000015847.3; ENSLAFP00000013292.3; ENSLAFG00000015837.3.
DR eggNOG; KOG0355; Eukaryota.
DR GeneTree; ENSGT00940000157921; -.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; G5E707; -.
DR OMA; TWTQDFK; -.
DR TreeFam; TF105282; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
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:0003682; F:chromatin binding; IEA:Ensembl.
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:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:Ensembl.
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:UP000007646};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 467..584
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1103..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1604 AA; 181019 MW; D40CEB8FB5F7C18F CRC64;
IGNLSLGSSS AASVTLFDQN NAAKKEELET ANRNDSSKKL SVERVYQKKT QLEHILLRPD
TYIGSVEPLT QLMWVYDDDV GMNCREVTFV PGLYKIFDEI LVNAADNKQR DKNMTCIKVS
IDPESNIISI WNNGKGIPVV EHKVEKVFVP ALIFGQLLTS SNYDDEEKKV TGGRNGYGAK
LCNIFSTKFT VETACKEYKH SFKQTWMNNM MKTSEAKIKH FDGEDYTCIT FQPDLSKFKM
EKLDKDIVAL MTRRAYDLAG SCKGVKVMFN GKKLPVNGFR SYVDLYVKDK LDETGVALKV
IHELANERWD VCLTLSEKGF QQISFVNSIA TTKGGRHVDY VVDQVVGKLI EVVKKKNKAG
VSVKPFQVKN HIWVFINCLI ENPTFDSQTK ENMTLQPKSF GSKCQLSEKF IKAASNCGIV
ESILNWVKFK AQTQLNKKCS SVKYSKIKGI PKLDDANDAG GKHSLDCTLI LTEGDSAKSL
AVSGLGVIGR DRYGVFPLRG KILNVREASH KQIMENAEIN NIIKIVGLQY KKSYDDAESL
KTLRYGKIMI MTDQDQDGSH IKGLLINFIH HNWPSLLKHG FLEEFITPIV KASKNKQELS
FYSIPEFDEW KKHIENQKAW KIKYYKGLGT STAKEAKEYF ADMERHRILF RYAGPEDDAA
ITLAFSKKKI DDRKEWLTNF MEDRRQRRLH GLPEQFLYGT ATKHLTYNDF INKELILFSN
SDNERSIPSL VDEIGFKPGQ RKVLYTCFKR NDKREVKVAQ LAGSVAEMSA YHHGEQALMM
TIVNLAQNFV GSNNINLLQP IGQFGTRLHG GKDAASPRYI FTMLSSLARL LFPAMDDNLL
KFLYDDNQRV EPEWYIPIIP MVLINGAEGI GTGWACKLPN YDAREIVNNV RRMLDGLDPH
PMLPNYKNFK GTIQELGQNQ YAVSGEIFVV DRNTVEITEL PVRTWTQVYK EQVLEPMLNG
TDKTPALISD YKEYHTDTTV KFVVKMTEEK LAQAEAAGLH KVFKLQTTLT CNSMVLFDHM
GCLKKYETVQ DILKEFFDLR LSYYGLRKEW LVGMLGAESS KLNNQARFIL EKIQGKITIE
NRSKRDLIQM LVQRGYESDP VKAWKEAQEK AAEEEDTQNQ HDDSSSDSGT PAGPDFNYLL
NMSLWSLTKE KVEELIKQRD TKGREVSDVK RKSPSDLWRE DLAAFIEELD KVEAQEREDI
LAGMSGKAIK GKVGKPKVKK LQLEETMPSP YGRRIVPEIT AMKADASKKL LKKKKGDLDT
TAVKVEFDEE FSGTPVEGTG EEALTPSAPI NKGPKPKREK KEPGTRVRRT PASAGKSNTK
KVKKRNPWSD DESKSESDLE ETEPVVIPRD SLLRRAAAER PKYTFDFSEE LEELKVKASP
ITNDGEDEFV PSDGLDKDEY TFSPGKPKAT PEKPSHDKKS QDFGNLFSFP SYSQKSEDDS
AKFDSNEEDS ASVFSPSFGL KQTDKVPSKT AAAKKGKPSS DITPKPKRTP KQKKVETVNS
DSDSEFGVPK KTAAPKGKGR GAKKRKASGS ENEGDYNPGR KTSKTTASKK PKKSSFDQDS
DVDIFPSDFA SEPPSLPRAG RARKEVKYFA ESDEEEDVDF AMFN
//
