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Database: UniProt
Entry: A0A1D6Q7T3_MAIZE
LinkDB: A0A1D6Q7T3_MAIZE
Original site: A0A1D6Q7T3_MAIZE 
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
//
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