ID A0A1D6HH03_MAIZE Unreviewed; 1045 AA.
AC A0A1D6HH03;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
DE Flags: Fragment;
GN ORFNames=ZEAMMB73_Zm00001d017720 {ECO:0000313|EMBL:AQK73825.1};
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:AQK73825.1};
RN [1] {ECO:0000313|EMBL:AQK73825.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK73825.1};
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; CM000781; AQK73825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6HH03; -.
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 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|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 Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT NON_TER 1045
FT /evidence="ECO:0000313|EMBL:AQK73825.1"
SQ SEQUENCE 1045 AA; 119311 MW; 187E2AC31891AD3A CRC64;
MYQKKTQLEH ILLRPDTYIG SVEKHTQALW IYEDGAMVNR SVTYVPGLYK IFDEILVNAA
DNKQRDPKMD ALRVEIDVDS CCISVYNNGD GIPVEVHQEE GVYVPEMILG HLLTSSNYND
NEKKTTGGRN GYGAKLTNIF STEFVIETAD GRRQKKYKQV FYENMGKKSE PQITKCKQGE
NWTRVTFKPD LAKFNMTHLE DDVVALMRKR VVDMAGTLGK TVKVELDGQR VPIKSFCDYV
DLYMKSANCD RPDNFKRIYE QVNDRWEVCV SQSEGQFQQV SFVNRIATIR GGSHVDYVTN
QIANHVVAIV NKKNKNANMK LHNVKSHLWV FVNALIDNPA FDSQTKETLT TRQGSFGSKC
ELSSDFLKKV EKSGVIENVL SWADFKLSKE LKKTDGSKKS RISGIPKLED ANEAGGKDSD
KCTLILTEGD SAKALAMSGI AVVGRDYYGV FPLRGKLLNV REANHKQIMD NAEIQHIKQI
LGLQHGKQYE STKGLRYGHL MIMTDQDHDG SHIKGLLINF IHSFWPSLLK VPSFLVEFIT
PIIKATRGQT TKSFYTMPEY EEWRKNLGAS ASSWTIKYYK GLGTSTAKEG RKYFEDIIDH
KKDFVWVDDQ DGNHIELAFS KKRIADRKQW LTNFQPGTYI DQREKQVKYS DFINKELILF
SMADLQRSIP SMVDGLKPGQ RKILFCSFKR NFVKEAKVAQ FSGYVSEHSA YHHGEQSLAS
TIIGMAQNFV GSNNINLMSP NGQFGTRAQG GKDAASPRYI FTKLSNITRS IFPKDDDILL
NYLNEDGQSI EPTWYMPILP MVLVNGSEGI GTGWSTYIPN YNPRDIVANV RRLLNEESTV
PMHPWYRGFK GSIEKTVNTK VAGSTYTVTG IIEVVDNTTL RITELPIRRW TQDYKDFLES
LAPDPKNKDK VTFIEDVTSQ GDNEDVYIQL KLSEANVNVA KEEGLVKKFK LTTTIGTTNM
HLFDSDGKIR KYDTPEQILE EFFQLRLEFY CKRKEALLKN IKLDLKKLEN KVRFIRCVVD
NEIIVNNRKR ADLFLELRHK NFDPF
//
