ID G2X7V2_VERDV Unreviewed; 375 AA.
AC G2X7V2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-MAY-2023, entry version 44.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN ORFNames=VDAG_06560 {ECO:0000313|EMBL:EGY15070.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY15070.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS572706; EGY15070.1; -; Genomic_DNA.
DR RefSeq; XP_009657233.1; XM_009658938.1.
DR AlphaFoldDB; G2X7V2; -.
DR STRING; 498257.G2X7V2; -.
DR EnsemblFungi; EGY15070; EGY15070; VDAG_06560.
DR GeneID; 20708023; -.
DR KEGG; vda:VDAG_06560; -.
DR eggNOG; KOG2260; Eukaryota.
DR HOGENOM; CLU_033261_0_0_1; -.
DR InParanoid; G2X7V2; -.
DR OMA; CINLEME; -.
DR OrthoDB; 1329460at2759; -.
DR Proteomes; UP000001611; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0031072; F:heat shock protein binding; IEA:EnsemblFungi.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:EnsemblFungi.
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:UP000001611}.
FT DOMAIN 2..188
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 96..254
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 271..368
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 97..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 41732 MW; 7C7C4ADDD98EE1DD CRC64;
MPVDYSKWDA LELSDDSDIE VHPNVDKRSF IRAKQNQIHQ ERQQRKHQIE TLKYERVINE
GLMRRISALL SALKAHAAVA ETRNPGEVAF QAVLESAGRP EDDQPPPRPA GVHTESEPLP
SYSKMMATLL DQPSPAAQLF AQIRANDYAA SLSFLSKHPE ILTERETDGL LVMAFDAALE
RKDDWSRQCV HQALLLQYCR ALGKDGVAMF FKRITTKGHQ AQEVFYKDVT DTYARIRTRA
REIVAERAKE PAEGVEQIQL HAVEPGTEIK IRIPPADSEE VEVKEACLIF ESFSDEFRKA
LETGSLDKVN HVLGNMTVEA AEDVVAKLGD AGILSLEERI IDATTEEGRK ALKEMEAAQT
GTGAGSESGY APDPE
//