TOP2B_CHICK
ID TOP2B_CHICK Reviewed; 1627 AA.
AC O42131;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DNA topoisomerase 2-beta;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II, beta isozyme;
GN Name=TOP2B;
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], AND SUBCELLULAR LOCATION.
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. Plays a role in B-cell
CC differentiation. {ECO:0000250|UniProtKB:Q64511}.
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:Q02880}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q02880}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q02880}. Nucleus {ECO:0000269|PubMed:11453553}.
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; AB007446; BAA22540.1; -; mRNA.
DR RefSeq; NP_990413.1; NM_205082.1.
DR AlphaFoldDB; O42131; -.
DR SMR; O42131; -.
DR STRING; 9031.ENSGALP00000018410; -.
DR PaxDb; O42131; -.
DR PRIDE; O42131; -.
DR GeneID; 395966; -.
DR KEGG; gga:395966; -.
DR CTD; 7155; -.
DR VEuPathDB; HostDB:geneid_395966; -.
DR eggNOG; KOG0355; Eukaryota.
DR InParanoid; O42131; -.
DR PhylomeDB; O42131; -.
DR PRO; PR:O42131; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003916; F:DNA topoisomerase activity; ISS:UniProtKB.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
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; IPR028467; Top2b.
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 PANTHER; PTHR10169:SF36; PTHR10169:SF36; 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 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; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Topoisomerase.
FT CHAIN 1..1627
FT /note="DNA topoisomerase 2-beta"
FT /id="PRO_0000145371"
FT DOMAIN 481..598
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 368..370
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 1016..1025
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 1115..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 831
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 174..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 402..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 487
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 567
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 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 569
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 515
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 518
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 687
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 688
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 749
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 783
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 830
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 882
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 957
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
SQ SEQUENCE 1627 AA; 183246 MW; 8B651D10A2CAD34B CRC64;
MAKSGGGGGG GGGGGGGGGG SGGLTCVTLF DNQINASKKE ESESVNKNDT SKKMSVERVY
QKKTQLEHIL LRPDTYIGSV EPLTQLMWVY DEDVGMNCRE VTFVPGLYKI FDEILVNAAD
NKQRDKNMTC IKISIDPESN IISIWNNGKG IPVVEHKVEK VYVPALIFGQ LLTSSNYDDD
EKKVTGGRNG YGAKLCNIFS TKFTVETACK EYKHSFKQTW MNNMMKTSEP KIKHFEGDDY
TCITFQPDLS KFKMENLDKD IVSLMTRRAY DLAGSCKGVK VMLNGKKLPV NGFRSYVDLY
VKDKLDETGV ALKVIHEVVN ERWDVCLTLS EKGFQQISFV NSIATTKGGR HVDYVVDQVV
GKLIEVVKKK NKAGVSVKPF QVKNHIWVFV NCLIENPSFD SQTKENMTLQ PKSFGSKCQL
SEKFFKAASN CGIIESILNW VKFKAQTQLN KKCSSVKHSK IKGIPKLDDA NDAGGKHSLD
CTLILTEGDS AKSLAVSGLG VIGRDRYGVF PLRGKILNVR EASHKQIMEN AEINNIIKIV
GLQYKKSYED PESLKSLRYG KIMIMTDQDQ DGSHIKGLLI NFIHHNWPSL LKHGFLEEFI
TPIVKASKNK QELSFYSIPE FDEWKKHMEN HKAWKIKYYK GLGTSTAKEA KEYFADMERH
RILFRYAGPE DDAAITLAFS KKKIDDRKEW LTNFMEDRRQ RRLHGLPEQF LYGTATKHLT
YNDFINKELI LFSNSDNERS IPSLVDGLKP GQRKVLFTCF KRNDKREVKV AQLAGSVAEM
SAYHHGEQAL MMTIVNLAQN FVGSNNVNLL QPIGQFGTRL HGGKDAASPR YIFTMLSPLA
RLLFPSVDDN LLKFLYDDNQ RVEPEWYIPI IPMVLVNGAE GIGTGWACKL PNYDTREIVN
NVRRMLDGLD PHPMLPNYKN FRGTIQELGQ NQYVVSGEIF VVDRNTVEIT ELPVRTWTQV
YKEQVLEPML NGTEKTPALI SDYKEYHTDT TVKFVVKMTE EKLAQAEAAG LHKVFKLQTS
LTCNSMVLFD HMGCLKKYET VQDILKEFFD LRLHYYSLRK EWLVGMLGAE STKLNNQARF
ILEKIQGKIT IENRSKRDLI QMLVQRGYES DPVKAWKEAQ EKAAEEEDPQ NANDDASSAS
GSTSGPDFNY ILNMSLWSLT KEKVEELIKH RDSKERELND LKRKSASDLW KEDLAAFVEE
LEKVEAQERE DVLAGMVGKP IKGKVGKPKM KKLQLEETMP SPFGRRIVPQ ITSAMKADAS
RKLLKKKKGD ADSVAIKMEF DEEFGGVQAE GGGDDTVNTA ASGTKTPKLK REKKEPGTRV
RRAPSSTKSS AKKVKKRNPW SDDESKSESD LEESEPVIIP RDSLLRRAAA DRAKYTFDFS
KEEDDAHDDD DANNNNDLDE LKVKASPVIN DREDEFVPSD SVEKDEYDFS PVKSKPSPEK
MSQEKKNQDF GNIFSFPSYS QKTDDDTTKL DSDEEDSTPV FSSPFAPKQT EKMLSKTVAA
KKAKVDVPPK PKRAPKAKKM ETVNSDSDSE FGIPKKTAAP KGKGRGAKKR KTSGSENEGE
YNPGKKAPKS TPCKKSKKAA FDQDSDVEIF QSGFASETAP KPRTGRARKE VKYFAESDED
DDFDMFN
