TOP2A_CHICK
ID TOP2A_CHICK Reviewed; 1553 AA.
AC O42130;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=DNA topoisomerase 2-alpha;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II, alpha isozyme;
GN Name=TOP2A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11453553; DOI=10.1007/s004120100140;
RA Niimi A., Suka N., Harata M., Kikuchi A., Mizuno S.;
RT "Co-localization of chicken DNA topoisomerase IIalpha, but not beta, with
RT sites of DNA replication and possible involvement of a C-terminal region of
RT alpha through its binding to PCNA.";
RL Chromosoma 110:102-114(2001).
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 (By similarity). May
CC play a role in the regulation of circadian rhythm (By similarity).
CC {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:Q01320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11388}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11388}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus
CC {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P11388}.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; AB007445; BAA22539.2; -; mRNA.
DR RefSeq; NP_990122.1; NM_204791.1.
DR AlphaFoldDB; O42130; -.
DR SMR; O42130; -.
DR STRING; 9031.ENSGALP00000039270; -.
DR PaxDb; O42130; -.
DR PRIDE; O42130; -.
DR GeneID; 395570; -.
DR KEGG; gga:395570; -.
DR CTD; 7153; -.
DR VEuPathDB; HostDB:geneid_395570; -.
DR eggNOG; KOG0355; Eukaryota.
DR InParanoid; O42130; -.
DR OrthoDB; 117851at2759; -.
DR PhylomeDB; O42130; -.
DR PRO; PR:O42130; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005694; C:chromosome; IDA:AgBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; ISS:AgBase.
DR GO; GO:0000792; C:heterochromatin; IDA:AgBase.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:AgBase.
DR GO; GO:0030332; F:cyclin binding; IPI:AgBase.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030263; P:apoptotic chromosome condensation; ISS:AgBase.
DR GO; GO:0051301; P:cell division; IDA:AgBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:AgBase.
DR GO; GO:0007059; P:chromosome segregation; ISS:AgBase.
DR GO; GO:0006266; P:DNA ligation; ISS:AgBase.
DR GO; GO:0006260; P:DNA replication; IDA:AgBase.
DR GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR GO; GO:1905463; P:negative regulation of DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:AgBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR012542; DTHCT.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
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 SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Biological rhythms; Cytoplasm; DNA-binding; Isomerase;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..1553
FT /note="DNA topoisomerase 2-alpha"
FT /id="PRO_0000145367"
FT DOMAIN 456..573
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..345
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 991..1000
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1095..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 806
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 149..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 162..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 377..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 544
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 490
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 493
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 662
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 663
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 724
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 758
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 764
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 805
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 857
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 932
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
SQ SEQUENCE 1553 AA; 174993 MW; 3322CE95238F71B2 CRC64;
MELLDSPAPL RPLHDNPRLP KADGAQKRLS VERIYQKKTQ LEHILLRPDT YIGSVETVTQ
QMWVFDEDVG LNCRDVTFVP GLYKIFDEIL VNAADNKQRD KSMSCIKVTI DPENNTISVW
NNGKGIPVVE HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT GGRNGYGAKL CNIFSTKFTV
ETACREYKKL FKQTWTDNMG KAGEMTLKHF DGEDYTCVTF QPDLSKFKMT ILDKDIVALM
SRRAYDIAGS TKDVKVFLNG KRLPVKGFRS YVDLYLKDKV DETGNALKVI HEEVNSRWEV
CLTLSEKGFQ QVSFVNSIAT TKGGRHVDYV ADQIVTKLID VVKKKNKNGV GVKPFQVKNH
MWIFVNSLIE NPTFDSQTKE NMTLQAKSFG STCKLSEKFI KGAVGCGIVE SILNWVKFKA
QTQLNKKCSA VKHTKIKGVP KLDDANDAGS KNSIDCTLIL TEGDSAKTLA VSGLGVVGRD
KYGVFPLRGK MLNVREASHK QIMENAEINN IIKIVGLQYK KNYEDRESLK SLRYGKIMIM
TDQDQDGSHI KGLLINFIHH NWPSLLRHNF LEEFITPIIK VSKNKEEIPF YSIPEFEEWK
SSTQNYNSWK IKYYKGLGTS TSKEAKEYFA DMARHRIGFK YSGPEDDAAI TLAFSKKKVE
ERKEWLTNFM EDRRQRNVHG LPEDYLYGKD TNYLTYNDFI NKELVLFSNS DNERSIPSLV
DGLKPGQRKV LFTCFKRNDK REVKGAQLAG SVAEMSSYHH GEASLMMTII NLAQNFVGSN
NLNLLQPIGQ FGTRLHGGKD SASPRYIFTM LSPLARLLFP PVDDNVLRFL YDDNQRVEPE
WYMPIIPMVL INGAEGIGTG WSCKIPNFDI RETVNNIRCL LDGKEPLPML PSYKNFKGTI
DELGPNQYVI SGEVSILDST TIEITELPVR TWTQTYKEQV LEPMLNGTEK TPPLITDYKE
YHTDTTVKFV VKMSEEKLAE AEAVGLHKVF KLQTNLTCNS MVLFDHVGFL KKYESPQDIL
KEFFELRLRY YGLRKEWLIG MLGAESAKLN NQARFILEKI DGKIVIENKP KKELIQVLIQ
RGYESDPVKA WKELQNKEEE EGDESGEESA AATGPDFNYL LNMPLWYLTK EKKDELCKQR
DNKDKELEDL KHKSPSDLWK EDLAAFVEEL DAVEAKQMQD EMAGITGKPL KVKGGKQGGK
QKVTKAQLAE VMPSPHGIRV VPRVTAEMKA EAEKRIKKKI KSEKNESDEK QEGNSSGDKE
PSSLKQRLAQ KRKAEQGTKR QTTLPFKPIK KMKRNPWSDS ESDSESDDFE VPSKRERVVR
QAAAKIKPMV NSDSDADLTS SDEDSEYQEN SEGNTDSDTT SKKKPPKAKA VPKEKKGKAP
KEKPLPDAVP VRVQNVAAES ASQDPAAPPV SVPRAQAVPK KPAAAKKGST AKDNQPSIMD
ILTKKKAAPK APRRAQREES PPSEATAAVA KKPGPPRGRK ATKRLTSSSD SDSDFGSRPS
KSVAAKKSKR DDDDSYSIDL TADSPAAAAP RTRPGRLKKP VQYLESSDED DMF
