ID A0A166HNL3_9AGAM Unreviewed; 818 AA.
AC A0A166HNL3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE SubName: Full=Heat shock protein Hsp90 {ECO:0000313|EMBL:KZT42906.1};
GN ORFNames=SISSUDRAFT_979285 {ECO:0000313|EMBL:KZT42906.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT42906.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT42906.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT42906.1,
RC ECO:0000313|Proteomes:UP000076798};
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; KV428010; KZT42906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166HNL3; -.
DR STRING; 1314776.A0A166HNL3; -.
DR Proteomes; UP000076798; 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 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 InterPro; IPR036890; HATPase_C_sf.
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:SF97; ENDOPLASMIN; 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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798};
KW Signal {ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000313|EMBL:KZT42906.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..818
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007874704"
FT REGION 259..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 91873 MW; E9BF3E9DD738AB6C CRC64;
MRYGWLLSFS LLAWRSFGQV PDSEVPKQKH DYQSDVARMR KIVVNSLYSN QCEHFVRELL
SNANDALEKL RIVSLTNKDI VDPSQPLNIT IRAVKDEEGT GGRLIITDTG IGMSPDDLTR
NLGTLAKSGT SEFLAKADSL DTSGGGNLIG QFGLGFYSSF LVADQVYVAS IPTKSETNPE
PAQYVFSSSA DDSSFEIYPD PRGNTLGHGT EITLVIRPDA SQFLNTDRLK ELVEKHSSFS
TAFPIYLLTQ VTEEVIDEDT LTEDEPSTAE EPSAPSEESV LDDDDDVVVE EVSEEEVPTK
EPKVTTVTVD KWAHLNEQPP LWMRDPKDVT NEQYIEFYKT TFKEDEAPLA WHHFQGESGD
GIHFKSIIYI PHELNPEFWS KSTSDNKGVR LMVKRVFITN DLGDDALPKW ASWLKVIVDA
DDLPLNVSRE TLQSTRFLKT LRSFVIKHLI KLMTRIAQDD PDKYVEIIKV YGNAIKLGAV
ESTKERNRLA VLARWPTNLR NFTSLDEYYV NRRQGQKQVF FHAGVGATTE NLAKSIFVEK
VHARGYEVFL LSEPLDEILF TNLGQWQDIR FQDVAKKGLE FGDEEEDLEA EKAKDEELAT
RFQPLVDWLK QETKDVVIDV TLSKRLVTSP CAIVADTYGY SANMERIMNA QNAKQAQGFL
HEMAKKQKFL EINPHSPLIE GLLRRVEQIA PEEGEEIDPD AEAELREVTS ILIDSALVRS
GFDVADPSVF FTRVDRVLRR SLGVSELAEA DIFIKPAPPI AKPYNAVEET ESETAPESEP
AEPEPVQEAE PAQPAESLSI ELESVEEIDI PLGGHDEL
//
