ID S9PY72_SCHOY Unreviewed; 464 AA.
AC S9PY72;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN ORFNames=SOCG_03246 {ECO:0000313|EMBL:EPX74031.1};
OS Schizosaccharomyces octosporus (strain yFS286) (Fission yeast)
OS (Octosporomyces octosporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=483514 {ECO:0000313|EMBL:EPX74031.1};
RN [1] {ECO:0000313|EMBL:EPX74031.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX74031.1};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [2] {ECO:0000313|EMBL:EPX74031.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX74031.1};
RG The Broad Institute Genome Sequencing Platform;
RA Nusbaum C., Russ C., Rhind N., Niki H., Allshire R., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Birren B.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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; KE503206; EPX74031.1; -; Genomic_DNA.
DR RefSeq; XP_013017188.1; XM_013161734.1.
DR AlphaFoldDB; S9PY72; -.
DR EnsemblFungi; EPX74031; EPX74031; SOCG_03246.
DR GeneID; 25032218; -.
DR VEuPathDB; FungiDB:SOCG_03246; -.
DR eggNOG; KOG2260; Eukaryota.
DR HOGENOM; CLU_033261_0_0_1; -.
DR OMA; ITTKDHQ; -.
DR OrthoDB; 1329460at2759; -.
DR Proteomes; UP000016088; Unassembled WGS sequence.
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}.
FT DOMAIN 2..181
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 180..365
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 380..460
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 182..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 52984 MW; F5EB68C8A6406DBE CRC64;
MAIDYSKWDK LELSDDSDIE VHPNVDKKSF IRWRQRDIHE KRSIRKQKME DIKSALTMNE
KLKDRISQMY SYLQKDSPSE PLPYLSSFLQ SKREEDSEQA IEGGMSYHQM LVALLDTIKK
AIEEEKNTSL GLTEQYIKHL QSHEKRLDNL MVNAKKEYDE LESESKKYIT SEDLHIGFDS
THVQKKEEEQ QKKKKQKESV QVIESLNDPS PFAQHENASQ AQSSSVAGKP EEEDSDSDSI
SMSTDGKKFS QIAFGDYSAS ESFLKDHLHI LAQESESDSI LLEAFNAELE GKPWLAKQYV
HQALLINYCR QLGPSGITIF FQRVQDPNHQ ARRLFLEDVQ NTYSRIHERS HAMANEQAQN
GEGVEQIQLC SVDPNTKLSI IIPEKDAVEP ELKAARMTFE SFPPNLQRAL ETNNLDKINS
VLGKMSVEDA EEVVEKLSST GMLSIEEGII DTTKGETIPQ PINE
//