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
//