ID A0A1Y1ZMM1_9PLEO Unreviewed; 703 AA.
AC A0A1Y1ZMM1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Hsp90 protein-domain-containing protein {ECO:0000313|EMBL:ORY11492.1};
GN ORFNames=BCR34DRAFT_484054 {ECO:0000313|EMBL:ORY11492.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY11492.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORY11492.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY11492.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY11492.1}.
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DR EMBL; MCFA01000060; ORY11492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1ZMM1; -.
DR STRING; 1231657.A0A1Y1ZMM1; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000193144; 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; PF13589; HATPase_c_3; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000193144}.
FT DOMAIN 26..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 214..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..547
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 228..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 80344 MW; 71DF7B460E73FBE5 CRC64;
MSAETFEFQA EISQLLGLII NTVYSNKEIF LRELISNASD ALDKIRYEAL SDPSKLDSGK
DLRIDIIPDK EGKTLTIRDT GIGMTKADLI NNLGTIARSG TKQFMEALTA GADISMIGQF
GVGFYSAYLV ADRVTVISKN NDDEQYIWES SAGGTFKIIE DTEGEQIGRG TKIILHLKDE
QMDYLNESKI KEVVKKHSEF ISYPIYLHVL KESEKEVEDE DAEETKDDDD EKKPKVEEVD
DEEEVKKDRK TKKVKESKIE EEELNKTKPI WTRNPQDITQ EEYASFYKSL SNDWEDHLAV
KHFSVEGQLE FRAILFVPKR APFDLFETKK TKNNIKLYVR RVFITDDATD LIPEWLSFVK
GVVDSEDLPL NLSRETLQQN KIMKVIRKNI VKKTLELFNE IAEDREQFDK FYSAFSKNIK
LGIHEDSQNR QSLAKLLRFN STKSGDETTS LTDYITRMPE HQKQMYYITG ESLKAVQKSP
FLDSLREKGF EVLFLVDPID EYAMTQLKEF DGKKLVDITK DFELEESEEE KKQREAEEKE
YEGLAKSLKN VLGERVEKVV VSHKLIGSPC AIRTGQFGWS ANMERIMKAQ ALRDTSMSSY
MSSKKTFEIS PKSPIIKELK RKVEADGEED RTVKSITLLL FETSLLVSGF TIDEPVQYAE
RIHKLVSLGL NVDEEVETEQ EAKAEEAAAP AEAAGESAME EVD
//
