ID B7QFI7_IXOSC Unreviewed; 363 AA.
AC B7QFI7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 08-NOV-2023, entry version 75.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN Name=8040490 {ECO:0000313|EnsemblMetazoa:ISCW021899-PA};
GN ORFNames=IscW_ISCW021899 {ECO:0000313|EMBL:EEC17609.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC17609.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC17609.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW021899-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW021899-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC {ECO:0000256|ARBA:ARBA00006222}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABJB010058502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010457476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010491297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS926118; EEC17609.1; -; Genomic_DNA.
DR RefSeq; XP_002414301.1; XM_002414256.1.
DR AlphaFoldDB; B7QFI7; -.
DR STRING; 6945.B7QFI7; -.
DR PaxDb; 6945-B7QFI7; -.
DR EnsemblMetazoa; ISCW021899-RA; ISCW021899-PA; ISCW021899.
DR GeneID; 8040490; -.
DR KEGG; isc:IscW_ISCW021899; -.
DR VEuPathDB; VectorBase:ISCI021899; -.
DR VEuPathDB; VectorBase:ISCP_015061; -.
DR VEuPathDB; VectorBase:ISCW021899; -.
DR HOGENOM; CLU_046495_0_0_1; -.
DR InParanoid; B7QFI7; -.
DR OMA; CINLEME; -.
DR OrthoDB; 297041at2759; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW Cell cycle {ECO:0000313|EMBL:EEC17609.1};
KW Cell division {ECO:0000313|EMBL:EEC17609.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7QFI7};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555}.
FT DOMAIN 1..122
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 110..278
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 282..363
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..106
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 42613 MW; 3DD012CD06959CFD CRC64;
MVDYSKWKTI EVSDDEDDTH PNIDTPSLFR WRHQARVERM AELEREKEEF MKRKAKNDAL
LLEARKKLEG KTGEALESAK REVAKLEKKD REFRKEKESL DKKEKLTPWN VDTISKEGFT
KTILNKPEPR KEEVLSEEDR ERKQKQFVTD NEPLLKQLGM LQKYDDSRRF LMEHPHLACE
ATANYLVMWC MRLEMDDKHE LMEHVAHQCI CIQYVLELAK QLEVDPRSCI SSFFTRIQTA
DQQYKDAFED ELRGFKERIR LRAQEKLEEA VKEMEEKERE ERLGPGGLDP VEVFETLPEV
LQKCFESRDL DMLKEAIAAM PEEEARYHMK RCVDSGLWVP DAKTAATGDA RPEDGGEDAA
KAE
//
