ID A0A061H3A3_9BASI Unreviewed; 505 AA.
AC A0A061H3A3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN ORFNames=PFL1_05195 {ECO:0000313|EMBL:EPQ27272.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27272.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ27272.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27272.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC {ECO:0000256|ARBA:ARBA00006222}.
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DR EMBL; KE361640; EPQ27272.1; -; Genomic_DNA.
DR RefSeq; XP_007880915.1; XM_007882724.1.
DR AlphaFoldDB; A0A061H3A3; -.
DR GeneID; 19319292; -.
DR KEGG; pfp:PFL1_05195; -.
DR eggNOG; KOG2260; Eukaryota.
DR HOGENOM; CLU_033261_0_0_1; -.
DR OrthoDB; 1329460at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR Gene3D; 1.20.58.610; Cdc37, Hsp90 binding domain; 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; CDC37-RELATED; 1.
DR PANTHER; PTHR12800:SF4; HSP90 CO-CHAPERONE CDC37; 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.
DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT DOMAIN 4..184
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 187..394
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 411..505
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 38..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 55701 MW; FF417FF9583B970D CRC64;
MVGKLNYSKW DNLELSDDSD IEVHPNIDKK SFVRWKQQDI HQKREQRKQE IQQLKAESET
NEQLKPRVDE ILKQTKSEGP AYYSREVSRL SAGRQERGNK DGPNGPTIDD MILSLLLQIN
QEPSVKGKEP SDPALIEGLA AQLEHHSSQL TKRQQQIKDE LAKMEAEDAK KITSDGIREG
WSSGHVSKAE PEPAPKPKPA KPAKSSKVTS IETLNSPSAA GSSSQAQAAD SDAEETDDEE
DVPEVSTSMR QFANLPSTIP SSLDLSASSL PSSFNPAKNL NEGAFEVALK FLAAHKELLR
EDSGTTDALL VEAFQAEMRG ESAYARRCTE KGLMIQYCNK LGKDGVALFF RKMSSGDGRA
SVVYLNDVLQ TYTRIRDRSK ALSESSASGG GGEGEEQIQL VAEDPSTVIS FEVPDGPAPE
HIQLEGEGTE GMDLDRVREF LDRRWQIFCG FDAEMQEALK TKELDKVNRV LGKMKCEEAE
KVVGLLDEAG ILNFSSSEVK DETGR
//
