ID A0A1E4SCB0_9ASCO Unreviewed; 702 AA.
AC A0A1E4SCB0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=HSP90-domain-containing protein {ECO:0000313|EMBL:ODV77150.1};
GN ORFNames=CANTADRAFT_23973 {ECO:0000313|EMBL:ODV77150.1};
OS Suhomyces tanzawaensis NRRL Y-17324.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Suhomyces.
OX NCBI_TaxID=984487 {ECO:0000313|EMBL:ODV77150.1, ECO:0000313|Proteomes:UP000094285};
RN [1] {ECO:0000313|Proteomes:UP000094285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17324 {ECO:0000313|Proteomes:UP000094285};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV453916; ODV77150.1; -; Genomic_DNA.
DR RefSeq; XP_020062272.1; XM_020207026.1.
DR AlphaFoldDB; A0A1E4SCB0; -.
DR STRING; 984487.A0A1E4SCB0; -.
DR GeneID; 30981163; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000094285; 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; PF02518; HATPase_c; 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:UP000094285}.
FT DOMAIN 29..167
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 217..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 80097 MW; 7E8EC0B748E4B160 CRC64;
MSDAKAETHE FTAEISQLMS LIINTVYSNK EIFLRELISN ASDAIDKIRY EALSDPSKLE
TEPELFIRIT PKPEEKVLEI RDSGIGMTKA DLVKNLGTIA KSGTKSFMEA LSAGADVSMI
GQFGVGFYSL FLVADHVQVI SKHNDDEQYI WESNAGGKFT VTLDETNERL GRGTVLRLFL
KEDQLEYLEE KRIKEVVKKH SEFVSYPIQL VVTKDVEKEV PAEDEEEEAK EGDDKKAKLE
EVEDEDSEKP KTKKITEKVT ENEELNKTKP LWTRNPSDVT QEEYNAFYKS ISNDWEDPLA
VKHFSVEGQL EFRAILFVPK RAPFDAFESK KKKNNIKLYV RRVFITDEAD ELIPEWLGFV
KGVVDSVDLP LNLSREMLQQ NKILKVIKKN IVKKLIETFN EIAEDQEQFE KFYTAFSKNI
KLGVHEDQQN RNALSKLLRY YSTKSTEEYT SLSDYVTRMP EHQKNIYYIT GESIKAVEKS
PFLDALKAKK FEVLFLVDPI DEYAMTQLKE FEDKKLVDIT KDFDLEETEE EKAEREKEIA
EFEPLTKALK EVLGEQVEKV VVSHKLVDAP AAIRTGQFGW SANMERIMKA QALRDTTMSS
YMSSKKTFEI SPKSPIIKEL KKKVEADGAE DKTVKDLTTL LYETALLTSG FSLDEPSSFA
GRINRLISLG LNIDEEEEVE AEIGTTTSST EPAVESAMEE VD
//
