ID A1C4S0_ASPCL Unreviewed; 703 AA.
AC A1C4S0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Molecular chaperone Mod-E/Hsp90 {ECO:0000313|EMBL:EAW14688.1};
GN ORFNames=ACLA_000990 {ECO:0000313|EMBL:EAW14688.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14688.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14688.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027004; EAW14688.1; -; Genomic_DNA.
DR RefSeq; XP_001276114.1; XM_001276113.1.
DR AlphaFoldDB; A1C4S0; -.
DR STRING; 344612.A1C4S0; -.
DR EnsemblFungi; EAW14688; EAW14688; ACLA_000990.
DR GeneID; 4708584; -.
DR KEGG; act:ACLA_000990; -.
DR VEuPathDB; FungiDB:ACLA_000990; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000006701; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 26..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 214..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 520..554
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 228..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 80188 MW; 83FADD429BC2AEB1 CRC64;
MSSETFEFQA EISQLLSLII NTVYSNKEIF LRELISNASD ALDKIRYQSL SDPSKLDSGK
DLRIDIIPDK ENKTLTIRDT GIGMTKADLI NNLGTIARSG TKQFMEALSA GADISMIGQF
GVGFYSAYLV ADRVTVISKN NDDEQYVWES AAGGTFTLTQ DTEGEQLGRG TKIILHLKDE
QTDYLNEARI KEVVRKHSEF ISYPIYLHVL KETEKEVPDE EAEETKEEEG DEKKPKIEEV
DEEEEKKEKK TKTIKESKIE EEELNKTKPI WTRNPADITQ EEYAAFYKSL SNDWEDHLAV
KHFSVEGQLE FRAILYVPKR APFDLFETKK TKNNIKLYVR RVFITDDATD LIPEWLSFIK
GVVDSEDLPL NLSRETLQQN KIMKVIKKNI VKKTLELFNE IAEDREQFDK FYAAFNKNIK
LGIHEDAQNR QTLAKLLRYQ STKSGDEATS LADYVTRMPE HQKQIYYITG ESIKAVAKSP
FLDSLKQKNF EVLFLVDPID EYAFTQLKEF DGKKLVDITK DFELEETDEE KAEREKEEKE
FEDLAKALKN ILGDKVEKVV VSHKLVGSPC AIRTGQFGWS ANMERIMKAQ ALRDTSMSSY
MSSKKTFEIS PKSSIIKELK KKVEADGEND RTVKSITQLL FETSLLVSGF TIDEPASFAE
RIHKLVSLGL NIDEETETSE EKATEDAAPV EATTGESAME EVD
//
