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Database: UniProt
Entry: A0A1Y1UDG9_9TREE
LinkDB: A0A1Y1UDG9_9TREE
Original site: A0A1Y1UDG9_9TREE 
ID   A0A1Y1UDG9_9TREE        Unreviewed;       700 AA.
AC   A0A1Y1UDG9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative cytoplasmic chaperone {ECO:0000313|EMBL:ORX36090.1};
GN   ORFNames=BD324DRAFT_581403 {ECO:0000313|EMBL:ORX36090.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX36090.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX36090.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX36090.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA   Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA   Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA   Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA   Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) 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:ORX36090.1}.
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DR   EMBL; NBSH01000009; ORX36090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1UDG9; -.
DR   STRING; 4999.A0A1Y1UDG9; -.
DR   InParanoid; A0A1Y1UDG9; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000193218; Unassembled WGS sequence.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193218}.
FT   DOMAIN          28..166
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          216..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  79795 MW;  32D792644E5F4248 CRC64;
     MSGQTETFGF QAEISQLLDL IINTFYSNKE IFLREIISNS SDALDKIRYA ALTDPSQLES
     EKDLYIRIIP NKEEGTLTIR DTGIGMTKAD LVNNLGTIAK SGTKAFMEAL SSGADISMIG
     QFGVGFYSSY LVAEKVQVTT KHNDDEQYIW ESAAGGTFTI TEDVDGPRLG RGTSMKLFIK
     DDLKEYLEEK RIRDIVKKHS EFISYPIQLV VTKETEKEVE EEEEVKEGDS KIEEVEDEDS
     SKKTKKTKKV KETTTENEEL NKQKPIWTRN PADVNQEEYA SFYKSISNDW EEHLAVKHFS
     VEGQLEFKAM LFIPKRAPFD LFETKKKRHN IKLYVRRVFI SEDNEELMPE YLNFVVGVVD
     SEDLPLNISR ETLQQNKILK VIRKNLVKKT LELISEIAED KENFDKFYSA FAKNLKLGIH
     EDSTNRSKLA EFLRFHSTKS VDEMTSFKDY ITRMPEVQKS IYYLTGESLE AVKDSPFLEA
     LKKKNFEVLL LVDPIDEYAV TQLREFDGKK LVCVSKEGLE LEETPEEKEE REKDEKEFAE
     LCTAVKENLG DKVEKVVVSN RITESPCVLV TGQFGWSSNM ERIMKAQALR DSSMSSYMAS
     KKTMELNPHH PIIKVLKTRI AEDKTDKTVK DLTFLLYETA LLTSGFTLAQ PQDFANRINR
     MIALGLSIDQ DEIAAPAASS SKDEDMPALE EAGGSMEEVD
//
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