ID E4UPJ5_ARTGP Unreviewed; 703 AA.
AC E4UPJ5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:EFQ99870.1};
GN ORFNames=MGYG_02882 {ECO:0000313|EMBL:EFQ99870.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; DS989823; EFQ99870.1; -; Genomic_DNA.
DR RefSeq; XP_003175353.1; XM_003175305.1.
DR AlphaFoldDB; E4UPJ5; -.
DR STRING; 535722.E4UPJ5; -.
DR GeneID; 10030661; -.
DR VEuPathDB; FungiDB:MGYG_02882; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; E4UPJ5; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UP000002669};
KW Stress response {ECO:0000313|EMBL:EFQ99870.1}.
FT DOMAIN 25..180
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 213..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 79928 MW; A6A54E897572A72C CRC64;
MSETFEFQAE ISQLLSLIIN TVYSNKEIFL RELISNASDA LDKIRYESLS DPSKLDSNKD
LRIDIIPDKE NKTLTIRDTG IGFTKADLVN NLGTIARSGT KQFMEALTAG ADISMIGQFG
VGFYSAYLVA DKVTVVSKHN DDEQYIWESS AGGTFTLTQD TEGEPLGRGS KIILHLKDEQ
TEYLTESKVK EVVKKHSEFI SYPIYLHVLK ETEKEVPDED AEEVTEAEEG DDKKPKVEEV
DDEEEDKEKK KKTKTVKESS IEEEELNKTK PIWTRNPADI TQEEYASFYK TLSNDWEDHL
AVKHFSVEGQ LEFRAVLFVP KRPPFDLFES KKTKNNIKLY VRRVFITDDA TDLIPEWLSF
VKGVVDSEDL PLNLSRETLQ QNKIMKVIKK NIVKKTLELF NEIAEDREQF DKFYSAFSKN
IKLGIHEDSQ NRATLAKLLR FNSTKSGDEI TSLTDYVTRM QPHQKQMYYI TGESIKAVQK
SPFLDSLKEK DFEVLYLVDP IDEYAMTQLK EFDGKKLVDI TKDFELEETD EEKTAREAEE
KEFEGLAKSL KNVLGDAVEK VVVSHKLVGA PCAIRTGQFG WSANMERIMK AQALRDTSMS
SYMASKKTFE ISPKSPIIKE LKKKVETDGE NDRNVKSITQ LLYETSLLVS GFTIEEPAAF
AERIHKLVSL GLDVEEEETP EEKADTEEAA AEPAAASAME EVD
//
