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Database: UniProt
Entry: A0A1V8USU2_9PEZI
LinkDB: A0A1V8USU2_9PEZI
Original site: A0A1V8USU2_9PEZI 
ID   A0A1V8USU2_9PEZI        Unreviewed;       706 AA.
AC   A0A1V8USU2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:OQO26775.1};
GN   ORFNames=B0A51_07379 {ECO:0000313|EMBL:OQO26775.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO26775.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
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:OQO26775.1}.
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DR   EMBL; NAEU01000195; OQO26775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8USU2; -.
DR   STRING; 1974281.A0A1V8USU2; -.
DR   Proteomes; UP000192386; 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:UP000192386};
KW   Stress response {ECO:0000313|EMBL:OQO26775.1}.
FT   DOMAIN          27..182
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          216..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   706 AA;  80038 MW;  0A72E3A3C9680544 CRC64;
     MSSEETFEFQ AEISQLLSLI INTVYSNKEI FLRELISNGS DALDKIRYEA LSDPSKLDSE
     KDLRLDIIPD KENKTLTLRD TGIGMTKADL VNNLGTIARS GTKQFMEALT AGADISMIGQ
     FGVGFYSAYL VADRVTVVSK HNDDEQYIWE SSAGGTFTLK HDTEGEQLGR GTKIILHMKD
     EQTDYLNEAK IKEVVKKHSE FISYPIYLHV LKETEKDVPD EDAEDVEEDE EKKPKVEEVD
     DDEEEGKEKP KKTKKIKESK IEEEELNKTK PIWTRNPSDI SAEEYGAFYK SLSNDWEDHL
     AVKHFSVEGQ LEFRAILFVP KRAPFDLFET KKTKNNIKLY VRRVFITDDA TDLIPEWLSF
     VKGVVDSEDL PLNLSRETLQ QNKIMKVIKK NIVKKTLELF AEIAEDKEQF DKFYTAFSKN
     IKLGVHEDAQ NRNALAKLLR YNTTTSGDDL TSLADYVTRM PEHQKQMYYI TGESKAAVEK
     SPFLDALKAK KFEVLFLNDP IDEYAFTQLK EFDGKKLVDI TKDFELEETD EEKKDRETEE
     KEFEGFAKSL KNVLGDKVEK VVVSQKLVNS PCAIRTGQFG WSANMERIMK AQALRDTSMS
     SYMSSKKTFE ISPKSPIIKE LKKKVEADGE SDRTVKSITT LLYETSLLVS GFTIDEPAAY
     AERIHKLVSL GLNVDEDVET AAEGEAADGE APAAEAAGES AMEEVD
//
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