ID A0A395GLZ2_9EURO Unreviewed; 198 AA.
AC A0A395GLZ2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=HSP20-like chaperone {ECO:0000313|EMBL:RAK95043.1};
GN ORFNames=BO80DRAFT_430223 {ECO:0000313|EMBL:RAK95043.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK95043.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK95043.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK95043.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733}.
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; KZ824506; RAK95043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GLZ2; -.
DR STRING; 1448316.A0A395GLZ2; -.
DR VEuPathDB; FungiDB:BO80DRAFT_430223; -.
DR OrthoDB; 782824at2759; -.
DR Proteomes; UP000249402; 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:UP000249402}.
FT DOMAIN 6..104
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 161..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 198 AA; 21927 MW; 1BAD859665752ADD CRC64;
MPELPQVHPE VTWAQRSSAS DAERNYLYVN IKAADVARTS ATLDIKPTSV TFTGDSKKGV
KYHVSLELYA EIDPENSKVN HSDREVELVL RKKELKEEFW PRLLKTTQKI HFLKTDFDKW
VDEDEQDEVT EDDYANNFGG FEGLGGEGGL SNIDFSKLGA GLGGEAGAGG EEEDDEDMPE
LEEAEGEGAQ ASKIQEVS
//
