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Database: UniProt
Entry: A0A2T7DU23_9POAL
LinkDB: A0A2T7DU23_9POAL
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ID   A0A2T7DU23_9POAL        Unreviewed;       806 AA.
AC   A0A2T7DU23;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN   ORFNames=GQ55_4G012300 {ECO:0000313|EMBL:PUZ59080.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ59080.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ59080.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CM009752; PUZ59080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7DU23; -.
DR   STRING; 1504633.A0A2T7DU23; -.
DR   EnsemblPlants; PUZ59080; PUZ59080; GQ55_4G012300.
DR   Gramene; PUZ59080; PUZ59080; GQ55_4G012300.
DR   Proteomes; UP000244336; Chromosome 4.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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; 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:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 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:UP000244336};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..806
FT                   /note="Histidine kinase/HSP90-like ATPase domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015625283"
FT   DOMAIN          100..257
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          292..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..317
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..806
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  92619 MW;  F981C0B5E0347E50 CRC64;
     MRKWALSSAL LLLFLLTTLP GPAKKLQVNA EESSDDLANP PKVEEKIGAV PHGLSTDSEV
     AQREAESISR KTLRSSAEKF EFQAEVSRLM DIIINSLYSN KDIFLRELIS NASDALDKIR
     FLSLTDKEVL GEGDTAKLEI QIKLDKEKKI LSIRDRGIGM TKEDLIKNLG TIAKSGTSAF
     VEKMQSGGDL NLIGQFGVGF YSVYLVADYV EVVSKHNDDK QYVWESKADG SFAISEDTWN
     EPLGRGTEIR LHLRDEAKEY LEEDKLKDLV KRYSEFINFP IYLWSTKEVD VEVPADEEET
     SEEEESTPET TEEEETEESE EKKPKTKTIK ETTSEWELLN DVKAVWLRSP KEVTDEEYSK
     FYHSLAKDFG DDKPMAWSHF TAEGDVEFKA LLFVPPKAPH DLYESYYNNN KSNLKLYVRR
     VFISDEFDDL LPKYLNFLKG IVDSDTLPLN VSREMLQQHS SLKTIKKKLI RKALDMIRKI
     AEEDPDEYSN KDKTDEEKSE MEEKKGQYAK FWNEFGKSIK LGIIEDATNR NRLAKLLRFE
     STKSDGKLAS LDEYISRMKP GQKDIFYITG SSKEQLEKSP FLERLTKKNY EVIFFTDPVD
     EYLMQYLMDY EDKKFQNVSK EGLKLGKDSK LKDLKESFKE LTDWWKKALE SENVDSVKIS
     NRLHNTPCVV VTSKYGWSAN MEKIMQAQTL SDSSKQAYMR GKRVLEINPR HPIIKELRDK
     VAQDSESEGL KQTARLVYQT ALMESGFNLP DPKEFASSIY KSVQKSLDLS PDATVEEEDE
     AEEQPEVEEK ESAKEESEPS YDKDEL
//
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