ID A0A3B4Z181_SERLL Unreviewed; 1484 AA.
AC A0A3B4Z181;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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 Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000028804.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000028804.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSSLDT00000029651.1; ENSSLDP00000028804.1; ENSSLDG00000021789.1.
DR GeneTree; ENSGT00940000157539; -.
DR Proteomes; UP000261360; Unplaced.
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 GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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: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; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
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 Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 439..556
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1072..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1484 AA; 167703 MW; 9DD45B7985529E34 CRC64;
SCCTKQPLQT QTFFENKPVE KTKKDPKRLS VERIYQKKTQ LEHILLRPDS YIGSVEPVTQ
QMWVYDEDVG LNCRDVMFVP GLYKIFDEIL VNAADNKQRD KIINNNVQLG IPVVQHKVEK
VYVPALIFGQ LLTSSNYDDE EKKVTGGRNG YGAKLCNIFS TKFTVETACK ESKKTFKQTW
YDNMGRTGDA AIKSFDGEEF TCITFRPDLP KFKMSTLDKD TLALMTRRAY DIAGATKGVR
VLYGLNHITG FRSYVDMFVK DKVDELGDTL TVVHETVNER WEVCLTMSEK GFQQVSFVNS
IATTKGGRHV DYVADQVVGK LIEVVKKKNK AGVAVKPFQV KNHMWLFVNC LVENPTFDSQ
TKENMTLQQK NFGSTCLLSD KFIKQATSCG IVESIMNWVK FKAQTQLNKK CSAVKHTKIK
GVPKLDDAND AGGKNSIGCT LILTEGDSAK TLAVSGLGVV GRDRYGVFPL RGKMLNVREA
SHKQIMENAE INNIIKILGL QYKKNYTDPE SLKSLRYGKI MIMTDQDQDG SHIKGLLINF
IHHNWPSLLR HNFLEEFITP IIKASHKKTQ MSFYSIPEFS AWKESQSNHK SWKVKYYKGL
GTSTSQEAKE YFSDMQRHRI PFKYAGPEDD EAITLAFSKK KVEERKEWLT NFMTNRRQRR
EHNLPEEYLY GQSTKSLSYN DFVNKELVLF SNSDNERSIP CLVDGLKPGQ RKVLFCCFKR
NDKREVKVAQ LAGSVAEMSA YHHGEVSLMM TIVGLAQNFV GSNNLNLLQP LGQFGTRLHG
GKDSASPRYI FTMLSPLTRL LFPPTDDNLL KYNYDDNQRV EPEWYMPIIP TVLVNGAEGI
GTGWASKIPN YDIREIISNI HRMLNGEEPL PMLPNYKGFR GTIEQVMDNQ FMNSGEIAII
NSTTIEISEL PVKSWTQTYK ENVLEPMLNG TEKVPPLITD YKEYHTDTTV RFVVKMTEEK
LREAEAAGLH KVFKLQSPLT CNSMVLFDHV GSLKKYESVQ DILRDFFELR MRYYVLRKDW
LVGMLGAESA KLTNQARFIL EKIEGTLVIE NKPKKELIRM LQSMGYDSDP VKAWKQAQEK
EEMEEQEEEE GTEKEDTSGP DYNYLLSMPM WFLTKEKKEE LCKQRDTKMT ELNTLKKKNP
EDLWREDLAA FSEELECTEA KEKETATMPV GKGAGKGKKA MKMKEETLPT PQGRRVVPRV
TSTMKAEANR KADKKGDGKR GKKIKVSSKT GTQTTLQFKP ATKKPKKSPW SDDEPDNLSD
SEMEAEEAFA PRERVERKTK AAVKYSLSDS EDDFDDWVNK DAPKQKAVIS DDDTSFAPEP
STMADSDMDS PAPPPKAPVQ RKTKEAAPKK AAAAKKPPAP KKKAADVKQP SILDALYKAK
PSSNTASKKV PSFDSSDSEG EAKPAPAKAK AKAKPALKRK QAVSDDSDCS SDNLMSRIRG
KVTAGGKVSD EEAAAPVAVA PRDKPSRSRK PVTYNLDSDS DEDF
//
