ID A0A367YJY6_9ASCO Unreviewed; 786 AA.
AC A0A367YJY6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:RCK65341.1};
GN Name=HSP90 {ECO:0000313|EMBL:RCK65341.1};
GN ORFNames=Cantr_01263 {ECO:0000313|EMBL:RCK65341.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK65341.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK65341.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK65341.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RCK65341.1}.
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DR EMBL; QLNQ01000020; RCK65341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YJY6; -.
DR SMR; A0A367YJY6; -.
DR STRING; 5486.A0A367YJY6; -.
DR Proteomes; UP000253472; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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; -; 2.
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 Gene3D; 3.90.530.10; XPA C-terminal domain; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
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 InterPro; IPR022656; XPA_C.
DR InterPro; IPR037129; XPA_sf.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR Pfam; PF05181; XPA_C; 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; SSF46955; Putative DNA-binding 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472};
KW Stress response {ECO:0000313|EMBL:RCK65341.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 184..317
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 90642 MW; 0816392B832EF519 CRC64;
MAKLQLQPTE TAKPKDQPRP RRPNFNLHLY VNKITLNIER VEEGAPYERV ATAMDLRGLL
LTEPELADKD LLKRIEKPNP HGYSNMQLFV RFQVEEYAWK KWGGPEQLDQ EWERREVNKA
KRKERTEEYT RKLRDGKSLG EKHEHDWSSP VAIDKNTIKR RCIDCGIETE EVLMSLIINT
VYSNKEIFLR ELISNASDAL DKIRYQALSD PSQLESEPEL FIRIIPHKEQ KVLEIRDSGI
GMTKADLVNN LGTIAKSGTK SFMEALSAGA DVSMIGQFGV GFYSLFLVAD HFTVTLDETN
ERLGRGTMLR LFLKEDQLEY LEEKRIKEVV KKHSEFVAYP IQLVVTKEVE KEIPEDETLA
EDEDKATEDD DKKPKLEETV KEEVTETEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW
EDPLAVKHFS VEAPFDAFES KKKKNNIKLY VRRVFITDDA EELIPEWLSF IKGVILKVIR
KNIVKKMIET FVELSENSTE YEQFYTAFSK NIKLGIHEDA QNRQALAKLL RYYSTKSTEE
MTSLSDYVTR MQPHQKNIYY ITGESIKAVE KSPFLDALKA KNFEVLFMVD PIDEYAMTQL
KEFEDKKLVD ITKDFDLEET DEEKSAREQE IKEFEPLTKA LKDILATKSK TAIRTGQFGW
SANMERIMKA QALRDTTMSS YMSSKKTFEI SPKSPIIKEL RKKVEEDGAE DKTVKDLTTL
LFDTALLTSG FTLDEPSNFA HRINRLIALG LNIDDDTEET AIEPESTTTA TTTEEPAAES
AMEEVD
//
