ID A0A397FXR3_9EURO Unreviewed; 205 AA.
AC A0A397FXR3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=CS domain-containing protein {ECO:0000259|PROSITE:PS51203};
GN ORFNames=CDV56_100618 {ECO:0000313|EMBL:RHZ43455.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ43455.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ43455.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ43455.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733}.
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:RHZ43455.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NKHU02000413; RHZ43455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397FXR3; -.
DR STRING; 41047.A0A397FXR3; -.
DR VEuPathDB; FungiDB:CDV56_100618; -.
DR OrthoDB; 782824at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR CDD; cd06465; p23_hB-ind1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932:SF1; CO-CHAPERONE PROTEIN DAF-41; 1.
DR PANTHER; PTHR22932; TELOMERASE-BINDING PROTEIN P23 HSP90 CO-CHAPERONE; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT DOMAIN 6..104
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 22693 MW; CBDDBD898E2BC6FF CRC64;
MPETPQLTPE VTWAQRSSSS DPERNYLYVN IKTPDVAKSA ADLKITANNV SFTGESKKGV
KYHVSLDLYA EIDPENSKVN HTDREVELVL RKKELKEEYW PRLVKDTQKL HFLKTDFDKW
VDEDEQDEAG DDDYANNFGG FEGLDQGGLG NIDFSKLGAD LGGGAEGAEG AEVVEGEESD
EEMPELEGDS KAEGEAKSSK IQEVS
//