ID A0A074W1C8_9PEZI Unreviewed; 701 AA.
AC A0A074W1C8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Molecular chaperone and allergen Mod-E/Hsp90/Hsp1 {ECO:0000313|EMBL:KEQ65359.1};
GN ORFNames=M437DRAFT_63976 {ECO:0000313|EMBL:KEQ65359.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ65359.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ65359.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ65359.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584827; KEQ65359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074W1C8; -.
DR STRING; 1043003.A0A074W1C8; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000030672; 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:UP000030672}.
FT DOMAIN 26..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 214..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..553
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 227..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 79820 MW; 9082370091FCE36B CRC64;
MAAETFEFQA EISQLLSLII NTVYSNKEIF LRELISNSSD ALDKIRYEAL SDPSKLDSGK
DLRIDIIPDK EAKTLTIRDT GIGMTKADLV NNLGTIARSG TKQFMEALTA GADISMIGQF
GVGFYSAYLV ADKVTVTSKN NDDEQYLWES SAGGTFTLTQ DTEGEQLGRG TKMVLHLKDE
QLDYLNEAKI KEVVKKHSEF ISYPIYLHVL KETEKEVPDE EAEEKTEEGD EKKPKVEEVD
DEDEKKEKKT KKVKESKIEE EELNKTKPIW TRNPADITQE EYGSFYKSLS NDWEDHLGVK
HFSVEGQLEF RAILFVPKRA PFDLFETKKT KNNIKLYVRR VFITDDATDL IPEWLSFVKG
VVDSEDLPLN LSRETLQQNK IMKVIKKNIV KKTLELFNEI AEDREQFDKF YTAFSKNLKL
GIHEDAQNRP QLAKLLRFNS TKSLDEVTSL QDYITRMPEH QKQMYYITGE SLKAVQKSPF
LDALKEKNFE VLFLVDPIDE YAFTQLKEFE GKKLVDITKD FELEETDEEK KKREEEEKEY
ESLAKSLKNV LGDKVEKVVV SHKLVGSPCA IRTGQFGWSA NMERIMKAQA LRDTSMSSYM
SSKKTFEISP ASPIIKELKK KVETDGENDR TVKSITQLLY ETSLLVSGFT IDEPAAYAER
IHKLVSLGLN VDEEAETSEE AASTEAPAAE AAGESAMEEV D
//
