ID A0A401GLS6_9APHY Unreviewed; 507 AA.
AC A0A401GLS6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN ORFNames=SCP_0501690 {ECO:0000313|EMBL:GBE83122.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE83122.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE83122.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC {ECO:0000256|ARBA:ARBA00006222}.
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:GBE83122.1}.
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DR EMBL; BFAD01000005; GBE83122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401GLS6; -.
DR STRING; 139825.A0A401GLS6; -.
DR InParanoid; A0A401GLS6; -.
DR OrthoDB; 1329460at2759; -.
DR Proteomes; UP000287166; 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:UP000287166}.
FT DOMAIN 24..205
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 214..387
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 401..507
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 200..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 56589 MW; 04FE10077C79098A CRC64;
MIREPSDFRL DVSLLARSPL VQMPLNYSKW DALELSDDSD IEGHPNVDKR SLIRWKQRDI
HEKREERKHR IALLEADIAC NAVLQPRLRT IADEVASKGP AHFSALVERF KTEPSPERPP
TNAPEQQTYD EMLLNLMLTI WEEVKKAGID KDDARLGELL VQGLEKHFVQ MGEHQGKQKQ
ELAQLQEDNK RKITSDDIHV GFDSHYVPPK PEPSPIKGAI EPSKPKKTTE YEVLNPKGVE
GTTTTSVPAA SSSSSVASDD ELPELTPSLE QFSHLPLRGY QQSWDFIRSH RDVYVAGASD
ALLVAAFKAQ NDGKAVYAQQ CVHQSLLIQY CEKLGPDGVT LFFRKMVVAD PRASSVFEND
VAQTYAHLAE RVRISKAEEA AVAGEEQIQL VAENPSQSIS FNIPDGPPPE HLQLEGPGFE
DVNIEDVRKA LQMRWDVFQG FSEAMQEALK SQELDKVNKV LGSMSVKEAE DVVQLLDLGG
ILNFSSGGIR DETGEEGEGV EEQEVEQ
//
