ID A0A1D6Q7T3_MAIZE Unreviewed; 1477 AA.
AC A0A1D6Q7T3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=ZEAMMB73_Zm00001d051542 {ECO:0000313|EMBL:AQK54496.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK54496.1};
RN [1] {ECO:0000313|EMBL:AQK54496.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK54496.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR EMBL; CM000780; AQK54496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6Q7T3; -.
DR SMR; A0A1D6Q7T3; -.
DR IntAct; A0A1D6Q7T3; 42.
DR STRING; 4577.A0A1D6Q7T3; -.
DR PaxDb; 4577-GRMZM2G121210_P01; -.
DR InParanoid; A0A1D6Q7T3; -.
DR ExpressionAtlas; A0A1D6Q7T3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
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; 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|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|RuleBase:RU362094};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT REGION 1075..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1477 AA; 165578 MW; 22F3A7F4F1DE3029 CRC64;
MTGPLHSSSG HNAAAGGGGK TIEEMYQKKT QLEHILLRPD TYIGSVEKHT QTLWVYEDGA
MVNRSVTYVP GLYKIFDEIL VNAADNKQRD PKMDALRVEI DVDGCSISVY NNGDGIPVEV
HQEEGVYVPE MIFGHLLTSS NYNDNEKKTT GGRNGYGAKL TNIFSTEFVI ETADGRRQKK
YKQVFSENMG KKSEPQITKC KQGENWTRVT FKPDLAKFNM IHLEDDVVAL MRKRVVDMAG
TLGKTVKVEL DGHRVPIKSF CDYVDLYMKS ANCDRPDNFK KSVLALIYEQ VNDRWEVCVS
QSEGQFQQVS FVNRIATIRG GTHVDYVTNQ IATHVMAFVN KKNKNANMKL HNVKSHLWVF
VNALIDNPAF DSQTKETLTT RQGSFGSKCE LSSDFLKKVE KSSVIDNVLS WADFKLSKEL
KKTDGSKKSR ISGIPKLEDA NEAGGKDSHK CTLILTEGDS AKALAMSGIA VVGRDYYGVF
PLRGKLLNVR EANHKQIMDN AEIQNIKQIL GLQHGKQYDS TKGLRYGHLM IMTDQDHDGS
HIKGLLINFI HSFWPSLLKV PSFLVEFITP IIKATRGQTT KSFYTLPEYE EWRNNLGASA
SSWTIKYYKG LGTSTAKEGR KYFEDITEHK KDFLWVDDQD GNHIELAFSK KRIADRKQWL
TNFQPGTYID QRDKHVKYSD FINKELILFS MADLQRSIPS MVDGLKPGQR KILFCSFKRN
FVKEAKVAQF SGYVSEHSAY HHGEQSLAGT IIGMAQNFVG SNNINLMYPS GQFGTRAQGG
KDAASPRYIF TKLSHITRSI FPKDDDILLN YLNEDGQSIE PTWYMPILPM VLVNGSEGIG
TGWSTYIPNY NPRDILANLR RLLNGESTVP MHPWYRGFKG SIEKTVNTKV AGSTYTVTGI
IEVLDNTTLR ITELPIRRWT QDYKDYLESL APDTKNKDKV PFIEDVTCQG DNEDVYIQFT
LSEKNMNIAM EEGLVKKFKL TTTIGTSNMH LFDSDGKIRK YDTPEQILEE FCHLRLEFYC
KRKEALLKSI KLDLKKLENK VRFIRCVVDN EIIVNNRKRA DLFLELRQKN FDPFPKKKKR
AEPAAVGALE EEENEESPEA AGAEPSDYEY LLSMSIGTLT LEKIQELNAE KQKLVDDVEE
LENMSPKSLW LKDLDAFEKE LDVLDQMDLA EELQREKRIN AGKKGGSKAA PKKPRKKAAS
KKLDSDTEDD DFEPAVAKRG AQPKKTSSKA NDSASEDGDY VAAENQKKQS KKASAHVDEE
VDMPSLKDRL AAFNISDSSP DHSAMETEVT ELTEQQNENK ATEGASKRGG RKKASSSLAT
IPSDVDEEVL EVQAQKKGRG RKPAAVVKPK APAAARKRAP AQGKVTQKKI DEMLKATEDN
NTSASSPEKK VRKMRSSPFN KKSGSILQRG STASASSGTT VEASPPSGSS AEPVGAAQPR
RTARATKKPI YISDSDPEDE VELIDDSDFD ADGDSDE
//