ID A0A087YF12_POEFO Unreviewed; 1520 AA.
AC A0A087YF12;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016615.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016615.2}
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 EMBL; AYCK01000756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01000757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01000758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01000759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000016615; -.
DR Ensembl; ENSPFOT00000016637.2; ENSPFOP00000016615.2; ENSPFOG00000016534.2.
DR eggNOG; KOG0355; Eukaryota.
DR GeneTree; ENSGT00940000157539; -.
DR OMA; QEMGYDS; -.
DR Proteomes; UP000028760; 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: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; 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: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; 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 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:UP000028760};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 395..512
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1031..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 171420 MW; 14B0ADE66DAFC5F3 CRC64;
MWVYDEGVGL NCRDVTFVPG LYKIFDEILV NAADNKQRDK SMSCIRVNID VENNTISVWN
NGKGIPVVEH KVEKVYVPAL IFGQLLTSSN YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE
TACKESKKVF KQTWYDNMGR AGDASIKPFE GEEYTCITFR PDLAKFKMSI LDKDTVALMT
RRAYDIAGSS KGVKVFFNSK RLPVSGFRSY VDMYVKDKVD ELGSPLSVVH EVVNERWEVC
LTMSEKGFQQ VSFVNSIATT KGGRHIDYVA DQVVGKLIEV VKKKNKAGVT VKPFQVKNHM
WLFVNCLIEN PTFDSQTKEN MTLQQKKFGS TCPLGDKFIK QATGCGIVES IMNWVKFKAQ
SQLNKKCSAV KHTKIKGVPK LDDANDAGGK NSIGCTLILT EGDSAKTLAV SGLGVVGRDR
FGVFPLRGKM LNVREASHKQ IMENAEINNI IKILGLQYKK NYSDPESLKT LRYGKIMIMT
DQDQDGSHIK GLLINFIHHN WPSLLHHNFL EEFITPIIKV SFKKSQLSFY SIPEFNAWKE
SQPNHRSWKI KYYKGLGTST SQEAKEYFLD MQRHRIPFKY SGPADDEAIT LAFSKKKVDE
RKEWLTNFMN NRRQRREHNL PEDYLYGQST KSLSYNDFVN KELVLFSNSD NERSIPCLVD
GLKPGQRKVL YCCFKRNDKR EVKVAQLAGS VAEMSAYHHG EVSLMMTIVG LAQNFVGSNN
MNLLQPLGQF GTRLHGGKDS ASPRYIFTML SPLARLVFPA VDDNLLKYNY DDNQRVEPEW
YIPIIPTVLI NGSEGIGTGW ASKIPNYDIR EIISNIHRML NGQEPLPMLP NYKNFRGTIE
QVMDNQYMNS GEVAIIDSTT IEISELPVKT WTQAYKENVL EPMLNGTEKV PPLITDYKDY
HTDTTVRFVI KMSEEKLREA EAAGLHKVFK LQSPLTCNSM VLFDHVGSLK KYESVQDILK
DFFELRMKYY VLRKDWLAGM LGAESAKLSN QARFILEKIQ GTLVIENKPK KELIRMLQKM
GYDSDPVKAW KQAQEKNEEL EDEEEEGAEK EDDSGPDYNY LLSMPMWFLT KEKKEELCRQ
RDAKMTELNT LKKKSPEDLW REDLAAFSEE LERIEAKEKE SDGIPVKGAG KGKAVKVKKE
TLPTPQGRRV VPRITSTMKA EANRKADLKK GEGRRGRKVK TEDVVMQMEF DEEVENVEPE
EMGLASRLAK KAKPEPKQRA TSKVVKQTTL QFKPVAKKSK KNPWSDDESE GSSGSDMEAE
EAAAPRDRIE RKTKAPVKYS LSDSEDEFDD WGKKSSPKRK SVISDEDSSF ALGPSTASDS
DVDSPPPPPK APEPAKKTVK SKTTVKKTET KSSVSSDDAA PASKPPAQRK PKETAAKKAP
AKKPTASKKK ASDEKQPSIL DALSKPKVSS KTAPKKIPTF GSSDSEDEGT VPAKKQSKAA
VKRKQVISDE SDSSSDDLMS RLKAKPQAAV KKSKKWMEDD MFQFSDQEEA ALVAVAPRDK
PSRARKPVTY NMDSDSDEDF
//
