TOP2_PENCH
ID TOP2_PENCH Reviewed; 1587 AA.
AC Q9Y8G8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
GN Name=TOP2;
OS Penicillium chrysogenum (Penicillium notatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kim K., Akashi T., Mizuguchi I., Ozeki M., Kanbe T., Kikuchi A.;
RT "Type II DNA topoisomerase of Penicillium chrysogenum.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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.
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.
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; AB029613; BAA82356.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y8G8; -.
DR SMR; Q9Y8G8; -.
DR PRIDE; Q9Y8G8; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR SMART; SM00387; HATPase_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; Phosphoprotein; Topoisomerase.
FT CHAIN 1..1587
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145384"
FT DOMAIN 492..606
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..386
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 381..383
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 461..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1025
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 1204..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 833
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 183..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 196..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 415..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 498
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 575
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 575
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 577
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 526
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 529
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 701
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 702
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 751
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 785
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 791
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 832
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 884
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 959
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
SQ SEQUENCE 1587 AA; 178761 MW; E3A992F63474BD64 CRC64;
MSDADPFDMS DDDDNSVLSH TPPKKQKKAP TTKKGGSKPL ADVENESFMD GIEESNNQDK
DTNVSEKYQK LTQLEHIIKR PDTYVGSTER TTQHMWVYSS ESEGMEYREV SYVPGLYKIF
DEIVVNAADN KQNDKNMDEI RVTIDRESGE ISVWNNGRGI PIEMHSKEKM YVPELIFGHL
LTSSNYDDTQ MKVTGGRNGF GAKLCNVFST EFTIETQDSR QKKKYKQTWT ENMTKMGKAK
ITDAKGADYT KVTFKPDYAK FGMTGMDDDF EALVKRRVYD LAGTAKVAVK LNGSRIPIRN
FKMYMEMYTK AIRRERGDMG PAGKNEIITC SPDPRWEVGF AVSDGAFQQV SFVNSIAITS
GGTHVNYIAD QICSKLAEQV KKKNKNGATL KPAQIRNHIF IFVNALIVNP AFTSQTKEQL
TTKQSQFGSK CVLEEDFYKK ILKTEVMTNI LHFAQQKADQ MLKKTDGGRR SRMNNPKLTD
ANKAGTKEGH HCTLILTEGD SAKGLAMAGR AVVGPDLFGV FPLRGKLLNV RDASFDQIAK
NQEIQNIKNF IGLQHKKEYT DTRGLRYGHL MITTDQDHDG SHIKGLLINF LQAQFPSLLK
IPEFLIEFIT PIVKVWKGDP KNPTKQRSFF TMPEYEAWKE EHGHERGWEH KYYKGLGTST
TEDAQIYFRD LDRHLKEFHT MQDNEVELIE LAFSKKKADE RKGNVRQFRP GTFLDHSVDK
ITYTDFINKE LILFSMADNI RSIPSVVDGL KPGQRKVLYT CFRRNLKKDM KVVELAGHVS
GTTAYQHGEG SLQQTIVGLA QTFVGSNNVN CLEPSGNFGS RLQGGADCAS ARYIYTRLWP
FARRVFHNHD DPLLTYNEDD GAKIEQEVYV PVVPMILING ADGIGTGWSS STPNYNPEDI
VENLKRMMDG EPLKPMQPWF RGFTGEVTAV GQDRFKFSGI IKETGDKEVE ITELPIRTWT
QDFKDKLEDI IKAEKTPSFI KDYKDYNTHT KVHFVIQMDE KHMKTAIAEG LEEKFKLSKT
MTTTNLVAFD PERITKYASV EDIMKEFYAV RLKYYERRKQ YQLSEMQKEL DKLSNQARFV
QMIIDGKLVI SKKKKAVLVA ELKEKDFKPF PKVKEAVKAG ETEPVVEEEE DSESGDTEVL
SNSYDYLLGM PIWSLTQERV EKLRRQIGDK ELEIDTLIKL SKEDIWKRDL EDFINEWRFQ
NDEEARRQRK VANMGRRTSS KLMTTGRGGG AAARKRKAAL GDDPDDEDFA APKSKKSAAA
KKTESKGGGL LSFLGKSSAK PKPSPADGGD SDDDFDMEIM PKKSRGAPKS EPKADPKPKD
EDEDIVMEDS DIEEIIPKKS RGSSKPSVKP ESEDGQAKIA EAPKRGRAAA KPKPKPKSED
EEDELDDDDF MEITKAEAAK PSAQPARSGR KTTKYAELSD SDSDNGDDLL GDVSKMVKGI
GSTNGASTSD SRLLFSERSR PGSSAGLKTT ASKASKPSEF DADETDYSKL VPSNTPRRSL
QVKPKDAKVS DDNEPEDDDD EPVKPAAKGK AAAKGKSTAA AANQLLQRLV VGRRKMLPKP
PPRLPCPLPQ RRTHRSNPRP RRPRRRS
