TOP2_DICDI
ID TOP2_DICDI Reviewed; 1521 AA.
AC Q55BP5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
GN Name=top2; Synonyms=topB; ORFNames=DDB_G0270418;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks (By similarity). {ECO:0000250}.
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}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72559.1; -; Genomic_DNA.
DR RefSeq; XP_646786.1; XM_641694.1.
DR AlphaFoldDB; Q55BP5; -.
DR SMR; Q55BP5; -.
DR STRING; 44689.DDB0231510; -.
DR PaxDb; Q55BP5; -.
DR EnsemblProtists; EAL72559; EAL72559; DDB_G0270418.
DR GeneID; 8617759; -.
DR KEGG; ddi:DDB_G0270418; -.
DR dictyBase; DDB_G0270418; top2.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_1_1; -.
DR InParanoid; Q55BP5; -.
DR OMA; TWTQDFK; -.
DR PhylomeDB; Q55BP5; -.
DR Reactome; R-DDI-4615885; SUMOylation of DNA replication proteins.
DR PRO; PR:Q55BP5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005694; C:chromosome; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; ISS:dictyBase.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; ISS:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; ISS:dictyBase.
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; 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; 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; 2.
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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Topoisomerase.
FT CHAIN 1..1521
FT /note="Probable DNA topoisomerase 2"
FT /id="PRO_0000330609"
FT DOMAIN 527..640
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..414
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1007..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1094
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1192..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 861
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 220..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 446..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 533
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 609
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 609
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 561
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 564
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 728
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 729
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 779
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 813
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 819
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 860
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 912
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 992
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1521 AA; 171162 MW; E7E2E6E51E13BCF1 CRC64;
MSDSENDYSD ESSGSEYESP VKKGKSAPKK PAAAGSKKKA SATRKPAAKK ATTTTTSTTK
KSTTSKKSES DNDDFSGDDK SSSSDNENVF KNIASSAKKG KSIEEIYQKK ELLDQILLRP
DTYIGSTERQ EEELWVWEDK RMVHRKVSFV PGIYKIFDEI LVNAADNKQR EGNMKFIKVV
IDREKGFISV TNDGAGIPIQ VHSEHKIYIP ELIFGNLLTS SHYDDSEKRL TGGRNGFGAK
LANIFSTKFI VECADSKSKK LYKQTFTNNM RSKEDPKITS YQNKTDYTKI TFYPELDRFG
MVEFDDDLVA LLSKRVYDIA GCNPTLKVSL NDEELGIRSF EKYINLYFPD EENAPKVYYE
KVSDRWELAV TLSKESQFNQ VSFVNSICTV KGGTHVTHAL SNIVTAIQEQ VNKKNKGSAD
IKPAFIKNHL SVFVNCLIEN PHFDSQTKET LTSKISSFGS RCEPSEKFIK RVLDSKSGIV
ASILEFAQFK DQSALKRSTS SGGKKGKVSI PKLDDANLAG GTKSEDCTLI LTEGDSAKSL
ATAGISVVGK DHYGAFPLKG KLLNVRDQST KVINNDEINN IVTILGLKYG KVYETLSDLR
YGHLMIMTDQ DHDGSHIKGL IINMVHHFWP TLLRMPGFLV EFITPIVKVF KNNQKPISFY
TMPEFLKWRE TNDKGWDVKY YKGLGTSTPG EGKEYFSDLE RHKIDFEWDE GANDNIELAF
SKSRADDRKK WMAEHIEGTF LEQFGVKKLT YSDFINKELV LFSIADCERS IPNIVDGLKT
SHRKTLYSCF KRNLKKEIKV AQLIGYVSEH SAYHHGEASL YSTIVGMAQE FVGSNNINLL
NPAGSYGTRI AGGKDCSSAR YIHTRLNDIA RAVYHADDDP ILSCVVDDGK KVQPKFYIPV
IPMILVNGCV GIGTGWSSTI PNYNPRDLIQ NMRLAIDGKP LKPIKPWYRG FLGSIEANQG
SKVQGGQYLS KGIWKKLSDN RFEITELPIG FWTQDYRELL DELETPGTRK KKKEEKEKKA
ASRKGTKAKP TTTKRSKRVD DDDDNEKVTE ATVKSYTNYS SESTIHFIID TIQPVDEINI
EKVFKLVSTI NETNMVVFDE EGRIQRFATT TALQEHFFPL RIKHYQMRKD FLSERLSEEY
SRLSNKARFI LAVVNKELVI SNVKKVDLIN KLKEMKFDRI INKNSNKSAR DKIKKKKNAF
DEEDAAISSD EEKDGAQEEQ DDDTKGYDYL LSLPLWSLTL ERVKKLIEER DSKKKEWDIL
LSTPIQEIYK RDLDALEKAL DDQDAYDESL KNQTESLKKR TKTKALPRAK KISAKVVKDT
KEAPLTKLVK PTVKIPTTTD SNVSGSKRKK SDDTTSTSTS TTTSSNTKPI ESFFAKEDKK
PTPAVKKSTL VSLDSDSDFD DDVVVSSKPK APPKKTSKVI ELSDESDQES DQESDQGSDP
ESPPKRSKAP PKKPTTIATK KATTSKSKVI DDKSSDDEVI KAPTNRPTRS RVPPPKSLSF
LDSDSDDDDL YDNEESSSDS D
