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Database: UniProt
Entry: A0A0D3CLH8_BRAOL
LinkDB: A0A0D3CLH8_BRAOL
Original site: A0A0D3CLH8_BRAOL 
ID   A0A0D3CLH8_BRAOL        Unreviewed;       730 AA.
AC   A0A0D3CLH8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 39.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|RuleBase:RU362094};
DE            EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN   Name=106296101 {ECO:0000313|EnsemblPlants:Bo5g137640.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g137640.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo5g137640.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo5g137640.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC       circular double-stranded DNA in an ATP-dependent manner.
CC       {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|RuleBase:RU362094};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU362094};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU362094};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis.
CC       {ECO:0000256|RuleBase:RU362094}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708, ECO:0000256|RuleBase:RU362094}.
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DR   RefSeq; XP_013587612.1; XM_013732158.1.
DR   AlphaFoldDB; A0A0D3CLH8; -.
DR   STRING; 109376.A0A0D3CLH8; -.
DR   EnsemblPlants; Bo5g137640.1; Bo5g137640.1; Bo5g137640.
DR   GeneID; 106296101; -.
DR   Gramene; Bo5g137640.1; Bo5g137640.1; Bo5g137640.
DR   KEGG; boe:106296101; -.
DR   eggNOG; KOG0355; Eukaryota.
DR   HOGENOM; CLU_006146_4_1_1; -.
DR   OMA; KIAYAWT; -.
DR   OrthoDB; 231762at2759; -.
DR   Proteomes; UP000032141; Chromosome C5.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd16928; HATPase_GyrB-like; 1.
DR   CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   CDD; cd03366; TOPRIM_TopoIIA_GyrB; 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   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR011557; GyrB.
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; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034160; TOPRIM_GyrB.
DR   NCBIfam; TIGR01059; gyrB; 1.
DR   PANTHER; PTHR45866:SF7; DNA GYRASE SUBUNIT B, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 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};
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   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU362094};
KW   Transit peptide {ECO:0000256|RuleBase:RU362094}.
FT   DOMAIN          511..618
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   730 AA;  81002 MW;  E546BE7EE20BDA6D CRC64;
     MALLQRPAPY LHFYFRLMAS RSRLFSHSLC PSLHRHSSSL SSSTPRIKFQ LAKVLSQRLV
     IRNAVSPRSF MSSTMDTDAL HESSTSKDYS SEHIQVLEGL DPVRKRPGMY IGSTGSRGLH
     HLVYEILDNA IDEAQAGFAS KIDVVLHADG SVSISDDGRG IPTDLHPATR KSSLETVLTV
     LHAGGKFGGK SSGYSVSGGL HGVGLSVVNA LSEALEVIVR RDGMEFQHKY SRGKPITTLT
     CHVLPPESRG TQGTCIRFWP DKEVFTTAIQ FDHNTIAGRI RELAFLNPKV TISLKKEDDD
     PERDLYSEYF YAGGLTEYVS WLNTDKKPLH DVLGFRKEIN GTTVDVALQW CSDAYSDTML
     GYANSIRTID GGTHIEGVKA SLTRTLNSLA KKLKVIKEKD ISLSGEHVRE GLTCIVSVKV
     PDPEFEGQTK TRLGNPEVRK IVDQSLQEYL TEYLELHPDV LESIISKSLN AYKAALAAKR
     ARELVRSKSI LKSSSLPGKL ADCSSTDPAE SEIFIVEGDS AGGSAKQGRD RRFQAILPLR
     GKILNIERKD EAAMYKNEEI QNLILGLGLG VKGEDFNMEN LRYHKIIILT DADVDGAHIR
     TLLLTFFFRY QRALFDAGCI YVGVPPLFKV ERGKQAHYCY DEAALKQVIA SFPGNASYNI
     QRFKGLGEMM PEQLWETTMN PDTRILKQLV VDDAAETNVV FSSLMGARVD VRKELIKSAA
     TRMNLENLDI
//
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