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Database: UniProt
Entry: A0A1U8M665_GOSHI
LinkDB: A0A1U8M665_GOSHI
Original site: A0A1U8M665_GOSHI 
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
//
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