ID A0A2V1AP36_9ASCO Unreviewed; 707 AA.
AC A0A2V1AP36;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Hsp82-like protein {ECO:0000313|EMBL:PVH19316.1};
GN ORFNames=CXQ85_001622 {ECO:0000313|EMBL:PVH19316.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH19316.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH19316.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH19316.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-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:PVH19316.1}.
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DR EMBL; PKFO01000001; PVH19316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AP36; -.
DR STRING; 45357.A0A2V1AP36; -.
DR EnsemblFungi; CXQ85_001622-t46_1; CXQ85_001622-t46_1-p1; CXQ85_001622.
DR VEuPathDB; FungiDB:CXQ85_001622; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000244309; 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:UP000244309}.
FT DOMAIN 28..166
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 216..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 81181 MW; 036DDA5AD9FFDFE7 CRC64;
MSEKVETHEF TAEISQLMSL IINTVYSNKE IFLRELISNA SDALDKIRYQ ALSEPSQLET
EPELFIRLTP KPEGKVLEIR DSGIGMTKTD LINNLGTIAK SGTKAFMEAL SAGADVSMIG
QFGVGFYSLF LVADHVQVIS KHNDDEQYVW ESNAGGKFTI TLDETNERIK RGTIIRLFLK
EDQLEYLEEK RIKEVVKRHS EFVSYPVQLV VRKEVEKEVP ADDEESKDEE KKEDEDDKKP
KLEEVDDEEE KKEKTKTVKE EVTETEELNK TKPLWTRNPN DVSKEEYNAF YKSISNDWED
PLAVKHFSVE GQLEFKAILF VPKRAPFDAF ESKKKKNNIK LYVRRVFITD DAEELIPEWL
SFVKGVVDSE DLPLNLSREM LQQNKIMKVI RKNIVKKLIE TFNEIAEDSE QFEKFYTAFS
KNIKLGIHED QQNRPALAKL LRYYSTKSTE EYTSLSDYVT RMPEHQKNIY YITGESIKSV
EKSPFLDALK AKSFEVLFLV DPIDEYAMTQ LKEFEDKKLV DITKDFELEE SEEEKKQREK
EVEEFEPLTK SLKEILGDQV EKVVVSHKLV DAPAAIRTGQ FGWSANMERI MKAQALRDTT
MSSYMSSKKT FEISPKSPII KELRKKVDAD GAEDKTVKDL TTLLYETALL TSGFSLEEPS
SFAHRINRLI SLGLNIEDDE PETAEVGTTA TASTEEPAVE SAMEEVD
//
