ID W5MZM5_LEPOC Unreviewed; 349 AA.
AC W5MZM5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Hsp90 co-chaperone Cdc37-like 1 {ECO:0000256|ARBA:ARBA00040086};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013834.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000013834.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Co-chaperone that binds to numerous proteins and promotes
CC their interaction with Hsp70 and Hsp90.
CC {ECO:0000256|ARBA:ARBA00037145}.
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; AHAT01017150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MZM5; -.
DR Ensembl; ENSLOCT00000013863.1; ENSLOCP00000013834.1; ENSLOCG00000011249.1.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_046495_1_0_1; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000011249; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 6.10.140.250; -; 1.
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 PANTHER; PTHR12800; CDC37-RELATED; 1.
DR PANTHER; PTHR12800:SF2; HSP90 CO-CHAPERONE CDC37-LIKE 1; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 114..267
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 270..343
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
SQ SEQUENCE 349 AA; 39934 MW; 40132FB5AF98B905 CRC64;
MEWFGSGSPG FSREKDETCC QTIKRDVGAA SVESLCRSQQ QCVKDSIVGS WQLAEAQDRL
CGLELHGSES AEQERARAQA SSAELFQTER EWRHKESLLG SEDRKSPVLC NTYSRDVFNK
SIINVQNGNK EANDDLSQTF IQKYEHQLRH YGMLRRWDDS QRFLSDHTHL ICEETANYLV
LWCFRLSAEE KEALMEQVAH QAVAMQFILE MASTNKEDPR GCFRKFFQKA KEGQEGYVNI
FTAELEAFKQ RVREYTMKCK SETFTAPELQ NTPTVSLLDP KEVLESLPPD LKRGFQLQDM
QILQNVLGNM NPQVAEYYVK RCLDAGLWVS SANGTKGEAT EDTRTMETS
//
