ID A0A099Z0W1_TINGU Unreviewed; 1623 AA.
AC A0A099Z0W1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
DE Flags: Fragment;
GN ORFNames=N309_05738 {ECO:0000313|EMBL:KGL74390.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL74390.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL74390.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL74390.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL886993; KGL74390.1; -; Genomic_DNA.
DR STRING; 94827.A0A099Z0W1; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
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; 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; 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:UP000053641};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 477..594
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1391
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL74390.1"
FT NON_TER 1623
FT /evidence="ECO:0000313|EMBL:KGL74390.1"
SQ SEQUENCE 1623 AA; 183855 MW; 883BBEEC92730B7F CRC64;
TLFDNQINAS KKEESESINK NETSKKLSVE RVYQKKTQLE HILLRPDTYI GSVEPLTQLM
WVYDEDVGMN CREVTFVPGL YKIFDEILVN AADNKQRDKN MTCIKISIDP ESNIISIWNN
GKGIPVVEHK VEKVYVPALI FGQLLTSSNY DDDEKKVTGK TIYHVLFVQL TSGRNGYGAK
LCNIFSTKFT VETACKEYKH SFKQTWMNNM MKTSEPKIKH FDGDDYTCIT FQPDLSKFKM
EKLDKDIVSL MTRRAYDLAG SCKGVKVMLN GKKLPVNGFR SYVDLYVKDK LDETGVALKV
IHEVVNERWD VCLTLSEKGF QQISFVNSIA TTKGGRHVDY VVDQVVGKLI EVVKKKNKAG
VSVKPFQAIN CFLCFQQVKN HIWVFVNCLI ENPSFDSQTK ENMTLQPKSF GSKCQLSEKF
FKAASNCGII ESILNWVKFK AQTQLNKKCS SVKHSKIKGI PKLDDANDAG GKHSLDCTLI
LTEGDSAKSL AVSGLGVIGR DRYGVFPLRG KILNVREASH KQIMENAEIN NIIKIVGLQY
KKSYEDPESL KSLRYGKIMI MTDQDQDGSH IKGLLINFIH HNWPSLLKHG FLEEFITPIV
KASKNKQELS FYSIPEFDEW KKHMENHKAW KIKYYKGLGT STAKEAKEYF ADMERHRILF
RYAGPEDDAA ITLAFSKKKI DDRKEWLTNF MEDRRQRRLH GLPEQFLYGT ATKHLTYNDF
INKELILFSN SDNERSIPSL VDGLKPGQRK VLFTCFKRND KREVKVAQLA GSVAEMSAYH
HGEQALMMTI VNLAQNFVGS NNVNLLQPIG QFGTRLHGGK DAASPRYIFT MLSPLARLLF
PSVDDNLLKF LYDDNQRVEP EWYIPIIPMV LVNGAEGIGT GWACKLPNYD TREIVNNVRR
MLDGLDPHPM LPNYKNFKGT IQELGQNQYV VSGEIFVVDR NTVEITELPV RTWTQVYKEQ
VLEPMLNGTE KTPALISDYK EYHTDTTVKF VVKMTEEKLA QAEAAGLHKV FKLQTSLTCN
SMVLFDHMGC LKKYETVQDI LKEFFDLRLH YYSLRKEWLV GMLGAESTKL NNQARFILEK
IQGKITIENR SKRDLIQMLV QRGYESDPVK AWKEAQEKAA EEEEPQNAND DASSASGSTS
GPDFNYILNM SLWSLTKEKV EELIKNRDSK ERELNNLKRK SPSDLWKEDL AAFVEELEVV
EAQEREDVLA GMVGKPIKGK VGKPKVKKLQ LEETMPSPFG RRIVPQITSA MKADASRKLL
KKKKGDTDSL AIKVEFEEEF GGVPAEGAGE DSLNTSVSAT KTPKPKREKK EPGTRVRRTP
SSTKSGAKKV KKRNPWSDDE SKSESDLEEN EPVIIPRDSL LRRAAAERPK YTFDFSEEED
EADDDDDANN NNDLEELKVK ASPVVNDRDD EFVPSDSIDK DEYDFSPAKS KPSPEKPSQD
KKNQDFGNIF SFPSYSQKTD DDTTKLDSDE DDSAPVFSPS FAPKPSEKNP SKTVATKKAK
LDVPPKPKRA PKAKKMEPVN SDSDSEFGLP KKTAAPKGKG RGAKKRKASG SENEGEYNPG
KKTPKSTPSK KAKKAAFDQD SDVEIFQSGF ASETAPKPRT GRARKEVKYF AESDEDDDFD
MFN
//
