ID A0A165E0R8_9BASI Unreviewed; 528 AA.
AC A0A165E0R8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=HSP90-domain-containing protein {ECO:0000313|EMBL:KZT53875.1};
GN ORFNames=CALCODRAFT_485967 {ECO:0000313|EMBL:KZT53875.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT53875.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT53875.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT53875.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; KV424026; KZT53875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165E0R8; -.
DR STRING; 1353952.A0A165E0R8; -.
DR InParanoid; A0A165E0R8; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 Gene3D; 3.30.230.80; -; 2.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
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; PF00183; HSP90; 2.
DR PIRSF; PIRSF002583; Hsp90; 3.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT REGION 374..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 61598 MW; 5E548D39AD101F9A CRC64;
MPDEPGEVVR KAAVVDWEVA KITQEEYNAF YKSLTNDWEA PLAVQQSSIE GQLEFKAILF
IPKRAPFALS ETKKKRNNIK LYIRRVFIMD DYKDIMPEYL NFVRGIVDSE DFPLNISRET
LQQIKTLQAI HKNLNPKFMD LFSEIAEGKD MSSIRRVLSL GRGTNMERIM KGQRLPILLP
LTKRARFDVF ETKKKRNNIK LYYLNFVKGI VDSEDFPLNI SRETLQQNKI LKVIRKNLVK
KCMDLFNEKA QDKDNFAKFY EAFPKNLKIG IHEDSQNRSK LAEFLRFYST NSGEEMTSFK
DYIIRMTEGP KSIYYLTGES LAATRDGPFL EDLRKKGFEV ILLGDPIDEY AVTQLKEFEG
KKLVRVSKEG LELEETEAEK KEREEEAERE EEAEREEEAK REEEAKREEE AKREEEAKQF
DDLDKSIKEA LGDNVEKVVV SNRIVDSACV LVTWPMSLEL KERAWGKEWD DMVKEVDDLC
KSIKDALGDK IENVVSAKTL NVKEKEEPEK AKLEKEKLEK EIEEMKEE
//
