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Database: UniProt
Entry: A0A2C9VQX8_MANES
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ID   A0A2C9VQX8_MANES        Unreviewed;       796 AA.
AC   A0A2C9VQX8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN   ORFNames=MANES_06G078500 {ECO:0000313|EMBL:OAY47426.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY47426.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY47426.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY47426.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CM004392; OAY47426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9VQX8; -.
DR   STRING; 3983.A0A2C9VQX8; -.
DR   EnsemblPlants; OAY47426; OAY47426; MANES_06G078500.
DR   Gramene; OAY47426; OAY47426; MANES_06G078500.
DR   OMA; QYSEFVH; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000091857; Chromosome lg6.
DR   GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 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   HAMAP; MF_00505; HSP90; 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   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11528:SF54; HEAT SHOCK PROTEIN 90-5, CHLOROPLASTIC; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; 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   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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:UP000091857}.
FT   DOMAIN          107..269
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          303..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   796 AA;  90333 MW;  F02CEA34506BA404 CRC64;
     MAPVLSRSLT AASLVSLPSS TPFSRKHLGS KSFALRSPFL PQNNGLKKGF SCTGLNWKLE
     RRNNRIAVRC EAAVAEKEAA DTSGEKFEYQ AEVSRLLDLI VHSLYSHKEV FLRELVSNAS
     DALDKLRFLS VTEPSLLGDA GDLEIRIKPD PDNGTITITD TGIGMTKEEL VDCLGTIAQS
     GTSKFLKALK ENKDHGADNG LIGQFGVGFY SAFLVAEKVV VSTKSPRSDK QYVWEAVADS
     SSYVIKEESD PEKLLRRGTQ ITLYLREDDK YEFSDPARIQ GLVKNYSQFV SFPIYTWQEK
     SRTVEVEEEE EPKEGEEAKP EDEKKKKTKT EKYWDWELAN ETKPIWMRNS KEVEKDEYHE
     FYKKTFNEFM DPIAYTHFTT EGEVEFRSVL YVPGMGPLNN EEVINPKTKN IRLYVKRVFI
     SDDFDGELFP RYLSFVKGVV DSDDLPLNVS REILQESRIV RIMRKRLVRK TFDMIQELSE
     SENKEDYKKF WENFGRFLKL GCIEDTGNHK RITPLLRFYT SKSEDELTTL DDYVENMGEN
     QKAIYYLATD SLKSAKSAPF LEKLVQKGIE VLYLIEPIDE VAIQNLQTYK EKKFVDISKE
     DLELGDEDEV KERETKQEFN LLCDWIKQQL GDKVAKVQVS KRLSSSPCVL VSGKFGWSAN
     MERLMKAQAL GDTSSLEFMR GRRILEINPD HPIIKDLSAA CKNAPDSGDA TRAVDLLYDT
     ALISSGFAPD SPAELGNKIY EMMAIALGGR WGRSEDDEAE TVDNNAAESV ANADEATETE
     VVEPSEVRAE SDPWND
//
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