ID A0A094KM43_9PEZI Unreviewed; 1665 AA.
AC A0A094KM43;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=V502_02616 {ECO:0000313|EMBL:KFZ22903.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ22903.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ22903.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
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:KFZ22903.1}.
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DR EMBL; JPKE01000996; KFZ22903.1; -; Genomic_DNA.
DR STRING; 1420915.A0A094KM43; -.
DR HOGENOM; CLU_001935_2_0_1; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000029308; 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:UP000029308};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 570..686
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1495
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; 185399 MW; CC90D2883641879A CRC64;
MDDSVMDDYD DYGDSDNFSP VPVVKPKPKP KAAAPKKAPA AKSAAKPKAA PKKLSQTTLK
TKSVPSKRPK PDSDNEDAPE DDGAALEDDT MLSNTPPSAK KQKKAPAAKK AAGKPLETIE
NESMNLDGPT EAKPKSGSTT DRYQKLTPLQ HVLKRPDTYI GSVERTEQQM WVFNSQTEQM
ETRKVQYVPG LYKIFDEILV NAADNKQNDS NMKALKVTVD REKGEISVEN DGRGIPIEIH
NKEKIYIPEM IFGHLLTSSN YDDEESKTTG GRNGYGAKLC NIFSTSFTLE TQDSKNGRRY
KQTWTDNMSN MGKAKITANK SADFTRITFT PDWKKFQMDG IDDDFEGLVK RRVYDLAGTV
KGVSVYLNGT KIKVNSFKKY IEMYAKAINA ERGLQDAEVK TSVIVDDDDS HKRWEIGFAV
SDGSFQQVSF VNSVATTSGG 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
RHKQERNWKH KYYKGLGTST TQDAQVYFTK LDEHLKEFEP IKREEEDLFD LAFSKKRADH
RKQWLGNFIP GTFLDHSSSK ISYDDFVNRE LILFSMADNM RSIPSVIDGL KPGQRKVIYS
AFTRNITSDM KVVELAGYCS GLTAYQHGEQ SLQGTIIGLA QDFVGSNNVN CLEPSGNFGS
RLAGGSDAAS PRYIYTRLSP FARRVFSPLD EANLEYNTDD DRRIEPKVYC PVVPMVLING
AEGIGTGWST SIPNYHPEDV VTNLKRRMGR LDSSEEQPFE TMTPWFRGWK GVVEEAGPDR
FRADGRITEG PGDNEVEITE LPIRVWTDDF KGKLEEVIKG EKVTSFIKDY KEFNDHDNVH
FVVQMDPSQM KVALTEGLEE KFKLQKTIAT SNLVAFDLQG RIRKYSKVEE ILEEFYVHRL
AMYTKRKEHW LDIFGKEYRK LSNQARFVLE IIDNKLVVSK KTKPKLVAEL RSKKYEPFPK
VKDAKKAGEA DDVVENDEEV PDNEEGGARD YDYLLGLPIW SLTQERVDKL KKQMVDKKAE
LDDLEALSEK DLWCRDLDAF LEVWHAALEE DSQVKKNIRS LGRRASKKLG VGKNGKLSSK
IKKDEEYAPT KKAAKSLKAN PAKGVVQVKP TETAKKRFED MFSANPKKAK AQTLGSDGAE
EMSGLSDDDF AAVSAAPAPA ASRSKRAAAA KPKNWVVEDD ESESDDDKML GDVGAMVKGI
GAESDTATNN GRLSLFAMSR PDSSSGKAAA ASSRPKPAAK SKVVDLSDDD ETNYEMLAKS
SPQKAQAPQP LDRDLDSFLS DDDSLPVIVS KATATKPAPK AKAVPAPKPK KAPVVKKAPV
KASEPAPKPP GLSPAAKAYA AKQAKVKITS KAAAKDDSED DLAMSDAEDV NDDVTESPVR
PAARGRPARA AVVKAKSKKP VYADSDEDEE ESVVEEDSYD FDESD
//
