ID A0A103XYG1_CYNCS Unreviewed; 329 AA.
AC A0A103XYG1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Heat shock protein Hsp90 {ECO:0000313|EMBL:KVH99260.1};
GN ORFNames=Ccrd_022520 {ECO:0000313|EMBL:KVH99260.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH99260.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH99260.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH99260.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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:KVH99260.1}.
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DR EMBL; LEKV01003629; KVH99260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XYG1; -.
DR STRING; 59895.A0A103XYG1; -.
DR EnsemblPlants; KVH99260; KVH99260; Ccrd_022520.
DR Gramene; KVH99260; KVH99260; Ccrd_022520.
DR OMA; FHLEDEY; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR PANTHER; PTHR11528:SF138; HEAT SHOCK COGNATE PROTEIN 80; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW Stress response {ECO:0000313|EMBL:KVH99260.1}.
FT DOMAIN 27..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 303..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 36653 MW; 8847A5AD2B5058AD CRC64;
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELVSNAS DALDKIRFES LTDKSKLDSQ
PELFIHIIPD KTNNTLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
FGVGFYSAYL VAEKVIVTTK HNDDEQYVWE SQAGGSFTIT RDSGEPLGRG TKITLFLKED
QLEYLEERRL KDLIKKHSEF ISEYGWTANM ERIMKAQALR DSSMAGYMSS KKTMEINPEN
PIMEELRKRA DADKNDKSVK DLVLLLFETS LLTSGFSLDE PNTFGNRIHR MLKLGLSIDE
DAGGEGDADI PALEEADIDA EGSKMEEVD
//
