ID A0A3M9Y5Z9_9PEZI Unreviewed; 1744 AA.
AC A0A3M9Y5Z9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=TOP2 {ECO:0000313|EMBL:RNJ55186.1};
GN ORFNames=D7B24_008882 {ECO:0000313|EMBL:RNJ55186.1};
OS Verticillium nonalfalfae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ55186.1, ECO:0000313|Proteomes:UP000267145};
RN [1] {ECO:0000313|EMBL:RNJ55186.1, ECO:0000313|Proteomes:UP000267145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ55186.1,
RC ECO:0000313|Proteomes:UP000267145};
RA Stajich J.E., Kasson M.T.;
RT "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL Submitted (OCT-2018) 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:RNJ55186.1}.
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DR EMBL; RBVV01000083; RNJ55186.1; -; Genomic_DNA.
DR STRING; 1051616.A0A3M9Y5Z9; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000267145; 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; 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 Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 557..675
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1744
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1744 AA; 194518 MW; 58D04503534D8985 CRC64;
MDFSDESMFS AQEESDAFSP EPKPKAAKAP AKKAPAAKKP AAKKLTQTTL KTAAAPKKRP
VSFSDDEASG LSNTPPSSKK LKKAPAASKS SGNPLAEIEN DSMALDEPSA PAPAVKGTKK
TVEETYQKLT QLEHIVKRPD TYIGSVERTE MPMWVYNKET QLMEFRKVTT VPGLYKIFDE
ILVNAADIKV RREESGEEPV THIKVNIDRE AGQISIENNG KGIPVEMHKQ HGIYVPEMIF
GHLLTGSNYD DDEKKTTGGR NGYGAKLCNV FSTEFTVECQ DSANGKRYKQ TWTDNMSKMG
KAKITSSKSS DFVRITFKPD FKRFSMEGID DDLEALLYRR VYDMAGTIKG IKVHLNGTVV
KPSAFKGYSE MYAKAIAKER ASEEGGEPKV TVEMDKNDNP RWDVGFTVSD GSFQHISFVN
NIATTSGGTH VNYVADQIVQ YLTKYLDKKK KGHALKPQHI RNHIFVFINC RIENPSFNSQ
TKEQMTTKIS SFGSKCVLSE AFLKKVAASD AIQNIMSFAE KKADKMMAKS DGNRRSRINN
AKLVDANLAG TKRGHECTLI LTEGDSAKSL AVAGRAILDP DRIGVFPLRG KMLNVRDASI
EQITKNQEIQ NIKQFLGLKH KQNYTDTKGL RYGHLMIMAD QDHDGSHIKG LLINFLQVQY
PSLLQIPDFF REFITPIVKV WQGKNPKNPQ KLQAFFTQPQ YEEWKEAHKN EISRWEYKYY
KGLGTSSNED AQVYFTNLDD HLKEFDTMQS SEADLFDLAF SKKKADARKE WLGNFVPGTY
LDHSTKSITY DDFVNRELIL FSMADNMRSI PSVLDGLKPG QRKVMFACFK RNLIKDQKVV
ELAGYVSEKA AYHHGEMSLQ QTIIGLAQNF VGSNNVNCLE PSGNFGSRLA GGSDAASPRY
IHTRLSPFAR KIFSVLDEPN LEVQMEDGKP IEPKVYAPII PMVLCNGADG IGTGWSTSIP
NYHPMEIVRA IKRRMGRLDS DDTEGKPFET MMPWFRGWKG TPEPAEKDRY KFNGIYETDD
KTGEIIIKEL PIRMWTDDFK AKLEEVISGA KGPAWIKDYK EFNDHKNVNF VIQLDEKHYK
DIHKTHEGIM DRFKLNKQVA TSNLVAFDST GRIRKYEKVE DILEEFYVYR LDMYSARKKH
WLGVYHSDYR KLKNQARFIQ EIIDGELIVS KKRKPVLVQE LRDRKYEAFP KNDGKKQATT
EEEDMDASDN EDDSVGGAAD YDYLLSLPIW SLTLERLERL NSAIMKKKGE HDALLARSEK
DLWCQDLDEF AEEWEAQLEM DDKIQSKINR MGRRRSRKIG AGGGKVSRNK ADDDFEPERK
RAAPKAKAAA KPVPAAKRFQ EQFDRKLEIA KAESPVDAFS DDDFAILAKP KAAPKTAPKA
KEPVLKAEES DDDTATAALA RKSSVPASRP KPKAKETLPK FADSSDFSDG DLTSMSAKKK
KPTASVEPEA EPVMGGRTKR AAAAKARPVF DLSESDASDN DFGDVGDIGQ MVHGYKPTTT
DPSKELKNGR LSLHGMNRPE SSHGAREAAL PKLKSKPSRH ILDDDSHDET NYEALAVRSS
PHKPVASKDD DLEEFLSDDS LPARKPSKAS SSSREPVPPP ALEVKKARGR PAGMKNKQKD
DAATAKAPAA KAKAKAAPKT APKAAPKAAA KPLPLSPAAK AYSASKEAKK PAKKTVFSDD
DDDSDDMMVD ADDAEPSSPP PRPAARGRPG RAAAKKKPTY IIDDDEESSV AMDEPQDDGF
SDSD
//
