ID M3HRN4_CANMX Unreviewed; 418 AA.
AC M3HRN4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 03-MAY-2023, entry version 35.
DE SubName: Full=Hsp90 co-chaperone, putative (Cell division control protein, putative) {ECO:0000313|EMBL:EMG50192.1};
GN ORFNames=G210_4782 {ECO:0000313|EMBL:EMG50192.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG50192.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG50192.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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}.
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:EMG50192.1}.
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DR EMBL; AOGT01000345; EMG50192.1; -; Genomic_DNA.
DR AlphaFoldDB; M3HRN4; -.
DR STRING; 1245528.M3HRN4; -.
DR eggNOG; KOG2260; Eukaryota.
DR HOGENOM; CLU_033261_0_0_1; -.
DR OMA; ITTKDHQ; -.
DR OrthoDB; 1329460at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.610; Cdc37, Hsp90 binding domain; 1.
DR InterPro; IPR004918; Cdc37.
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; PF08565; CDC37_M; 1.
DR Pfam; PF03234; CDC37_N; 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 Cell cycle {ECO:0000313|EMBL:EMG50192.1};
KW Cell division {ECO:0000313|EMBL:EMG50192.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT DOMAIN 2..201
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 204..384
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT REGION 200..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 48071 MW; A67D6AC4AB47DDFC CRC64;
MPIDYSKWDK IEISDDSDIE VHPNVDKNSF IRWKQRDIHE KRFQRNIEIK SILVQLTTYE
KINQRVDYLL EKLGAKEIVD NSLVMSALNS KFDRNDKFDY EKLIQGEGSN LRKGLKDLHF
EKEEIENTPP YNEMVEDLFT QIKDDHPATK TDGDKLIGFL KEHRAKIDDV LANQTKKLDD
LLYQKSQLIV SDDLHTGFDR SFLNKDKPQQ EEEEQKVAPA PSKKTTVTTT ETINSPKTVE
ETPSVQDMMD ELTLLPATEQ FAEIPINDYS KASDFLIKHP SICTEQQKDA LMMSAFDHQL
SGDSEKARHV IFQALLLQYI AQLSGSSTDK ARVINTVRLF FSKISDKSSP AHNAFMDEVK
KTADHIKARC EIIKQERELS NEGEDGDEEE ALIQLRALDD KTELVIFKSL SKSSRLMK
//
