ID A0A1U8M665_GOSHI Unreviewed; 1462 AA.
AC A0A1U8M665;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=LOC107934399 {ECO:0000313|RefSeq:XP_016722312.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016722312.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016722312.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016722312.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR RefSeq; XP_016722312.1; XM_016866823.1.
DR STRING; 3635.A0A1U8M665; -.
DR PaxDb; 3635-A0A1U8M665; -.
DR GeneID; 107934399; -.
DR KEGG; ghi:107934399; -.
DR OMA; NESMDYN; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000189702; Unplaced.
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 Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 447..561
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1156..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1462 AA; 164972 MW; 485D0DCBBC790B38 CRC64;
MVADSKLPLQ SSNNVNTKAS KTIEETYQKK TQLEHILLRP DTYIGSIEQH TQRLWVYEND
EMVHRDIKYV PGLYKIFDEI LVNAADNKQR DPSMDSIKVV IDAEQNLISV YNNGDGVPVE
IHQEEKVYVP ELIFGHLLTS SNYDDNVKKT TGGRNGYGAK LTNIFSTEFV IETADGKRQK
KYKQVFKNNM GNKTEPLITK CKEGENWTKV TFKPDLAKFN MTHLEDDVVA LMRKRVFDLA
GCLGKTVKVE LNGKRIAVKS FLDYVNLYLS AASKNKSEPL PRISEKVNAR WEVCVSLSEG
QFQQVSFVNS IATIKGGTHV DYVTNQISNY VMNAVNKKNK NANVKAHNVK NHLWVFVNAL
IDNPAFDSQT KETLTLRQSS FGSKCELPED FLKKVAKSGV VDNLLQWAEF KHSKDLKKTD
GTKSGSIRGI PKLDDANEAG GRNSDKCTLI LTEGDSAKSL AVAGLSVVGR NHYGVYPLRG
KLLNVREASH KQLMENAEIQ NLKRILGLQQ NKEYTDVKSL RYGHLMIMTD QDHDGSHIKG
LLINFIHSFW PSLLKVKSFM VEFITPIVKA TRKVNKQEEE LCFYTMPEYQ AWKESLGTNA
KSWRIKYYKG LGTSTGPEGK KYFKDIDKHM KEFVWEGDMD GDAIELAFSK KKIEARKNWL
RQFEPGTHLD HNEKLINYSD FINKELILFS MADLQRSIPS MVDGLKPGQR KILFCAFKRN
FVHEAKVSQF SGYVSEHSAY HHGEQSLCST IVGMAQDFVG SNNINLLRPG GQFGTRNQGG
KDAASARYIF TNLTTITRYL FRKDDDGLLN YLNEDGQSIE PSWYVPIIPM VLVNGSEGIG
TGWSSYIPNY NPRDIVANVR RLLNGEPMEP MHPWYRGFKG TIEKTASKES GVTYTISGIV
EEVDETTLKI TELPLRRWTQ DYKEFLESVI TANDSFIKEF KQYSDDRTVH FEVFMTEENM
MLAKQEGLMK KFKLTTTVST SNMHLFDSRG MIKKYDTPEE ILDEFYHLRL EFYEKRRKHM
LDTLELELLK MDNKVRFILD VVKGNIIVNN RKRADLFLEL QEKGFTPFPK KTKAVEVAVA
GDIDHEGEPE LSPEATRASD YDYLLSMAIG TLTLEKVQEL CSDRDKLEHE VEELRKHTPK
SLWLKDLEEL EKQLDEQDQA DLEAEEENSK NRAKGGVAGK KARRPVAPKN PKKVNKKDDP
QVSEASEISS TTAMEAEKAP AVVKPKGRAG AKKKTKKQDD SDDDDDDDDD FDIPDLRERL
AKHNIDSSPD HSADMETEMF QEPAGKKGPA KRAAATKKNP VISLSESIGE INISDGELEV
VEPAPAATKK GGRKPAAPKA SKPPAAAKKR GPAAGKQQKL LTQMLKPAAE AEGSGISPEK
KVRKMRASPF NKKSGSVLGK TSSSSLSSMP EIDSDEDEEV AVVVEPRARP QRANRTKTTY
VVSDSETEEE VNDDSDFEED ED
//