ID A0A3Q3FLJ7_9LABR Unreviewed; 1440 AA.
AC A0A3Q3FLJ7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000020364.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000020364.1}
RP IDENTIFICATION.
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 -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR STRING; 56723.ENSLBEP00000020364; -.
DR Ensembl; ENSLBET00000021472.1; ENSLBEP00000020364.1; ENSLBEG00000015255.1.
DR GeneTree; ENSGT00940000157539; -.
DR InParanoid; A0A3Q3FLJ7; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
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:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF61; DNA TOPOISOMERASE 2-ALPHA; 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; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000261660};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 443..560
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1081..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1122..1172
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1348..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 163563 MW; F92985AFE125762E CRC64;
LEGREGGLEK IINQLSVERI YQKKTQLEHI LLRPDSYIGS VEPVTQQMWV YDEEEAELNC
RDVTFVPGLY KIFDEILVNA ADNKQRDKRM SCIKINIDVE NNTISVWNNG KGIPVVLHQV
EKVFVPALIF GQLLTSSNYD DDQKKVTGGR NGYGAKLCNI FSTKFTVETA CKESKRNFKQ
TWYDNMARTE EPKITPFGKE EFTCITFKPD LPKFKMTILD KDTVALMTRR AYDIAGASKG
VCVYFNGKKL PITGFRNYVD MYLKDKVDEV GNPLSVVHEV VNERWEVCLT MSEKGFNQVS
FVNSIATTKG GRHVDYVGDQ VVSKIVEIVK KKNKAGVAVK PFQVKNHMWL FVNCLIENPT
FDSQTKENMT LQQKTFGSTC PLSEKFMKQA TSCGIVESIM NWVKFKAQSQ LNKKCSAVKH
TRVKGVPKLD DANEAGGKNS IGCTLILTEG DSAKTLAVSG LGVVGRDRYG VFPLRGKMLN
VREASLKQIM ENAEINNVIK ILGLQYKKNY SDPESLKSLR YGKLMIMTDQ DQDGSHIKGL
LINFIHHNWP SLLRHNFLEE FITPIIKVTF KKTHMSFYSI PEFDEWKATV SNIKSWKIKY
YKGLGTSTSQ EAKEYFSDME RHRIPFKYGG PEDDEAITLA FSKKKVDERK EWLTNFMVNR
RQRREHNLPE DYLYGQSTSS LSYNDFVNKE LVLFSNSDNE RSIPCLVDGL KPGQRKVLMC
CFKRNDKREV KVAQLAGSVA EMSAYHHGEV SLMMTIVGLA QNFVGSNNLN LLQPMGQFGT
RLHGGKDSAS PRYIFTMLSP LARLVFPSLD DNLLKYNYDD NQRVEPEWYL PIIPMVLVNG
AEGIGTGWAS KVPNFNIREI VNNIHRMLNG EEPLPMLPSY KGFKGTIEQL VDNQNLISGE
VSIIDSTTIE ISELPVKSWT QAYKENVLEP MLNGTDKVPA LITDYKEYHT DTTVRFVVKM
SEEKLMEAEA AGLHKVFKLQ TMLTCNSMVL FDHVGSLNKF ESVQDILKIF FELRLKYYVL
RKDWLAGMLG AENAKLSNQA RFILEKIEGT LVIENKAKKE LIRMLQEMGY DSDPVKSWKQ
AQEKHVEEID NDEEEAGQED TSGPDYNYLL SMPMWFLTKE KKEELCKQRD AKMTELNTLK
QKTPADLWKE DLAAFSEELE RLEQKEKDID NMPVTKVVSG KGKGRAVKVK NETLPTPHGR
RVVPRITSIM KAEANKKSKD VVMKMEFEDN AENEENAVPT EKIGLAARLS KKTKTQAKEK
GETSKTNRQS TLQFKPVIKK NPWSDDDQMD VMSDSELQTE EVVAPRVRVD RKSKGMPEDV
PDNSLNPYYF CPILCITTVQ PSILDALSKP KPSSNTSTKK IPSFGSSDSE EEIKVTKTKP
ALKRKQNVSD DSDSSSDDLM SRLKAKTTAA GKVCFDNDFR HAFYPISPPI PFQAWCSLVL
//
