CDC37_CANAL
ID CDC37_CANAL Reviewed; 508 AA.
AC Q8X1E6; A0A1D8PPZ3; Q5AC19;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Hsp90 co-chaperone Cdc37;
DE AltName: Full=Cell division control protein 37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
GN Name=CDC37; OrderedLocusNames=CAALFM_C602610CA; ORFNames=CaO19.5531;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RA Ni J., Chen J.;
RT "A Cdc37 homolog in Candida albicans interacting with Crk1 kinase domain.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC their interaction with the Hsp90 complex, resulting in stabilization
CC and promotion of their activity. {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with Hsp90. Interacts with a number of kinases
CC such as crk1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; AF397024; AAL56555.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30194.1; -; Genomic_DNA.
DR RefSeq; XP_719095.1; XM_714002.1.
DR AlphaFoldDB; Q8X1E6; -.
DR IntAct; Q8X1E6; 2.
DR MINT; Q8X1E6; -.
DR STRING; 237561.Q8X1E6; -.
DR PRIDE; Q8X1E6; -.
DR GeneID; 3639210; -.
DR KEGG; cal:CAALFM_C602610CA; -.
DR CGD; CAL0000192456; CDC37.
DR VEuPathDB; FungiDB:C6_02610C_A; -.
DR eggNOG; KOG2260; Eukaryota.
DR HOGENOM; CLU_033261_1_0_1; -.
DR InParanoid; Q8X1E6; -.
DR OrthoDB; 786744at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IGI:CGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:EnsemblFungi.
DR GO; GO:0030474; P:spindle pole body duplication; IEA:EnsemblFungi.
DR Gene3D; 1.20.58.610; -; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR InterPro; IPR013855; Cdc37_N_dom.
DR PANTHER; PTHR12800; PTHR12800; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR Pfam; PF03234; CDC37_N; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SMART; SM01071; CDC37_N; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..508
FT /note="Hsp90 co-chaperone Cdc37"
FT /id="PRO_0000195065"
FT REGION 201..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 58564 MW; 89E4EDDEBF322868 CRC64;
MPIDYSKWDK IEISDDSDVE VHPNVDKQSF IRWKQRDIHE KRMQRNIEIK SILIQLTMYA
KLNERVDYLL EKLTSTELLD SEKVMSKLNS EFDPQEKFDY DKLIKDKGST LRKGLKDLKF
DREEIENTPC YNEMIEDLFV QIKDDHPETK TDGDKLIEYL KEHRNRIDDV LSKQTIKLDD
LLYQKAQLIV SDDLHTGFDR SFLNKDKPEE KEENQDKPKA PEAKKTTVTT TETINSPKPV
EENTDKEILD ELEILPATKE FAKIPSDNLS KAAEFLIKHP SICTEQQKDA LIMTAFDLQL
ENKSDEAKHI VHQSLLLQYV GQLSDNGKAA PANVINAIKL FFSKIAAESS PAKHAFLEDV
NQTFNHIKGR CEIIKEEQKQ NAANKEGTGE EEEEEALIQL KALDDNTELS VNIPQEGTKE
YEIFTTKLPI EFQNAIKTES IDEVNKEFAK LKIEDAERIL EIFNECGVIG ISGYIEDEKE
FEELKKEYAH ETANQEEDQS ASVEDTVD
