ID M7TM08_BOTF1 Unreviewed; 701 AA.
AC M7TM08;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Putative heat shock protein 90 protein {ECO:0000313|EMBL:EMR84551.1};
GN ORFNames=BcDW1_6780 {ECO:0000313|EMBL:EMR84551.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR84551.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; KB707943; EMR84551.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TM08; -.
DR SMR; M7TM08; -.
DR STRING; 1290391.M7TM08; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Stress response {ECO:0000313|EMBL:EMR84551.1}.
FT DOMAIN 26..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 212..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 79537 MW; 7760F20B28BF96CD CRC64;
MAGETFEFQA EISQLLSLII NTVYSNKEIF LRELVSNCSD ALDKIRYEAL SDSSKLDSGK
DLRIDIIPDK ENKTLTIRDT GIGMTKADLV NNLGTIARSG TKQFMEALTA GADISMIGQF
GVGFYSAYLV ADRVTVVSKN NDDEQYIWES SAGGTFTLTQ DSEGEQLGRG TKIILHLKDE
QMDYLNESKI KEVIKKHSEF ISYPIYLHVS KETETEVPDE EAEETKEEDE EKKAKIEEVD
DEEEAKKPKT KKVKETKIEE EELNKQKPIW TRNPSDITAE EYGSFYKSLS NDWEDHLAVK
HFSVEGQLEF RAILFVPKRA PFDLFETKKT KNNIKLYVRR VFITDDATDL IPEWLSFVKG
VVDSEDLPLN LSRETLQQNK IMKVIKKNIV KKVLELFQEI SEDKEQFDKF YAAFAKNIKL
GIHEDSQNRA ALAKLLRFSS TKSGDDITSL SDYVTRMPEH QKNLYYITGE SLKAVQKSPF
LDSLKAKNFE VLFLVDPIDE YAMTQLKEFE GKKLVDITKD FDLEETDEEK KTREEEEKEF
EGLAKALKNV LGENVEKVVV SHKLVNAPCA IRTGQFGWSA NMERIMKAQA LRDTSMSSYM
SSKKTFEISP KSPIIKELKK KVEADGENDR TVKSITQLLF ETSLLVSGFT IEEPAGFAER
IHKLVSLGLN VEEDAETTEE AAATTEATSD APVESAMEEV D
//
