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Database: UniProt
Entry: M3HRI2_CANMX
LinkDB: M3HRI2_CANMX
Original site: M3HRI2_CANMX 
ID   M3HRI2_CANMX            Unreviewed;       221 AA.
AC   M3HRI2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-MAY-2023, entry version 29.
DE   SubName: Full=Co-chaperone protein, putative {ECO:0000313|EMBL:EMG50117.1};
GN   ORFNames=G210_4868 {ECO:0000313|EMBL:EMG50117.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG50117.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG50117.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) 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:EMG50117.1}.
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DR   EMBL; AOGT01000367; EMG50117.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3HRI2; -.
DR   STRING; 1245528.M3HRI2; -.
DR   eggNOG; KOG3158; Eukaryota.
DR   HOGENOM; CLU_078883_0_0_1; -.
DR   OMA; KMHFLKT; -.
DR   OrthoDB; 782824at2759; -.
DR   Proteomes; UP000011777; 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:UP000011777}.
FT   DOMAIN          5..104
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          124..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..221
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   221 AA;  23467 MW;  30F843B2FEB7DDEF CRC64;
     MSTTTHTPTV LWAQRSSETD AAKNIIYLTI QLLDPVDLKL DLKPDHLSLT AKSSDAEAIN
     YDLNIDFFKE VDPDQSKINT ENGSHIFIIL RKKEKQEEYW PRLTKEKLKY HYIKTDFDKW
     VDEDEQDEAK DDPEDFAGAG PGGFGAGGPG GPGGAGGFDF AQMLSSMGGA GGAGGLGGAG
     GPDLSALASQ LGQAGGFANP GADGEEDGEE EGEEEGEEAK P
//
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