ID A0A094HZN0_9PEZI Unreviewed; 1665 AA.
AC A0A094HZN0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635, ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|RuleBase:RU362094};
GN ORFNames=V501_00922 {ECO:0000313|EMBL:KFZ18919.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ18919.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ18919.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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. {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|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ18919.1}.
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DR EMBL; JPKD01000302; KFZ18919.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094HZN0; -.
DR HOGENOM; CLU_001935_2_0_1; -.
DR Proteomes; UP000029315; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
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; 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:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
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 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 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 570..686
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1665
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1665 AA; 185406 MW; A1895A84EAA58C0F CRC64;
MDDSVMDDYD DYGDSDNFSP VPVVKAKPKP KAAPKKAPAA KAAAKPKAAP KKLSQTTLKT
KSVPSKRPKP DSDDDEDAAE DGEAAIEDDT MLSNTPPSAK KQKKAPVAKK AAGKPLETIE
NESMNVDGPT ESKPKSGNST DRYQKLSPVQ HILTRPDTYI GSVERTEQQM WVFNSQTEQM
ESRKVEYIPG LYKIFDEILV NAADNKQNDA NMKALKVTVD REKGEISVEN DGRGIPIEIH
EKEKIYIPEM IFGHLLTSSN YDDEQSKTTG GRNGYGAKLC NIFSTSFTLE TQDSKNGKRY
KQVWTDNMSN MGKAKITANK SADFTRVTFT PDWKKFQMDG IDDDFEGLVK RRVYDLAGTV
KGVSVYLNGT KIKVNSFKKY IEMYAKAINS QRGIQDAEVK TTVIVDDDDS HKRWEIGFAV
SDGSFQQVSF VNSIATTTGG THVSYIADQI CQRLLDHVKK INKQGTALKT NQIRNHIFLF
VNCLIVNPAF TSQTKEQLTT KVSQFGSKCQ VTEEFLKKIV KTDAVANIMH FAQQKADQVL
SKSDGNRRSR MTNPKLVDAN LAGTRRGHEC TLILTEGDSA KALAVAGRAI LDPDRIGVFP
LRGKMLNVRD ASIDQISKNA EIQNIKQFLG LKHKQVYTDP QSQGLRYGHL MIMADQDHDG
SHIKGLLINF LHVAFPSLLK LPNFFQEFIT PIVKVWKGPN PKTAISRTFF TMPQYDEWRE
RHKHERSWKH KYYKGLGTST TQDAQVYFTK LDEHLKEFEP IKREEEDLFD LAFSKKRADH
RKQWLGNFVP GTFLDHSSSK ISYDDFVNRE LILFSMADNM RSIPSVIDGL KPGQRKVIYS
AFTRNITSDM KVVELAGYCS GLTAYQHGEQ SLQGTIIGLA QDFVGSNNVN CLEPSGNFGS
RLAGGSDAAS PRYIYTRLSP FARRVFSPLD EANLEYNTDD DRRIEPKVYC PIVPMVLING
AEGIGTGWST SIPNYHPEDI VTNLKRRMGR LDSSEEQPFE PMMPWFRGWK GVVEEAGPDR
FRADGRITEG PGDNEVEITE LPIRVWTDDF KGKLEEVIKG EKVTSFIKDY KEFNDHDNVH
FVVQMEASQM KAALTEGLEE KFKLQKTIAT SNLVAFDLEG RIRKYTKVEE ILEEFYVHRL
AMYTKRKQHW LDVFGKEYRK LSNQARFVLE IIDNKLVVSK KTKPKLVAEL RAKKYEPFPK
VKYAKKAGEA DDVVENDEEV PDDEEGGARD YDYLLGLPIW SLTQERVDKL KRQMVDKKAE
LDDLEALSEK DLWCRDLDAF LEVWHAALEE DTQVKKSIRS LGRRASKKLG VGKGGKLSTK
IKKDEEYMPT KKAAKPAKAN PAKGVVQVKP TETAKKRFED MFSAKPKKPK TQAHGSDGAE
EMSGLSDDDF AAVSAAPAPA ASRSKRAAAA KPKNWLVEDD DESESDDDKM LGDVGAMVKG
IGAESDTAAN NGRLSLFAMS RPGSSSGKAS SASSKAKPAA KSKVIDLSDD DETNYEMLAK
PSPQKAQAPQ PLDRDLDSFL SDDDSLPVVV KAAAAKPAPK AKAVPAPKPK KAPVVKKAPV
KAAEPAPKPP GLSPAAKAYA AKQAKVKVNS KAAVKDDSED DLAMSDAEDV EDDVTESPVR
PAARGRPARA AVVKAKSKKP VYADSDEEEE ESVVEEDSYD FDESD
//
