ID   K5VKN9_PHACS            Unreviewed;       506 AA.
AC   K5VKN9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN   ORFNames=PHACADRAFT_262403 {ECO:0000313|EMBL:EKM51968.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM51968.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM51968.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51968.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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; JH930476; EKM51968.1; -; Genomic_DNA.
DR   RefSeq; XP_007399759.1; XM_007399697.1.
DR   AlphaFoldDB; K5VKN9; -.
DR   STRING; 650164.K5VKN9; -.
DR   GeneID; 18918271; -.
DR   KEGG; pco:PHACADRAFT_262403; -.
DR   HOGENOM; CLU_033261_0_0_1; -.
DR   InParanoid; K5VKN9; -.
DR   OrthoDB; 1329460at2759; -.
DR   Proteomes; UP000008370; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT   DOMAIN          2..183
FT                   /note="Cdc37 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01071"
FT   DOMAIN          186..367
FT                   /note="Cdc37 Hsp90 binding"
FT                   /evidence="ECO:0000259|SMART:SM01070"
FT   DOMAIN          383..502
FT                   /note="Cdc37 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01069"
FT   REGION          467..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          139..166
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        480..506
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  56464 MW;  17827FBFE0A6E212 CRC64;
     MPLNYSKWDN LELSDDSDIE GHPNIDKKSL IRWKQRDIHE KREMRRMHIA QLEADIACNE
     VLEPRLHQIT ADVEAKGPAE FSSLVERFKT NPSPEKPPTN APQQKTYDEM LLALMLKVWE
     EAKKEGVEKD DPKLSEALAK GLKKHIEELG KHQEKLKQEL AQEEVEQKKK ITSDDIHEAW
     ESHYVSPKPA PPPVKNAIAS GSGSTNKVAT TEFEVLNPKG VTTGQETFAG SSSKADPLDE
     SAELPELTLS LEAFSRLPLG GYEQSWEFIK QHRDVIVPGA SDALLVAAFT AQSEGKAKYA
     KQCVHQSLLL QYCDKLGKDG VSIFFRRMMS GDPRASAVFE KDIEDTYAHL CERVRISKAE
     TEAAAEQEQI QLVPENPGQS ISFNVPDGPP PERIQLEGEG LEGVNPEDVR RALQMRWDVF
     QGFAPAFQDA LRSQSLDQVN KVLGNMKVED AEQVVNMLDV AGILNFSEHG VRDDTGKAND
     DGDGDEDGEG EEEEEEEEQG DEQDVD
//