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Database: UniProt
Entry: A0A3L6RJI2_PANMI
LinkDB: A0A3L6RJI2_PANMI
Original site: A0A3L6RJI2_PANMI 
ID   A0A3L6RJI2_PANMI        Unreviewed;       774 AA.
AC   A0A3L6RJI2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Heat shock protein 90-5, chloroplastic-like {ECO:0000313|EMBL:RLN04308.1};
GN   ORFNames=C2845_PM13G20870 {ECO:0000313|EMBL:RLN04308.1};
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN04308.1, ECO:0000313|Proteomes:UP000275267};
RN   [1] {ECO:0000313|Proteomes:UP000275267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA   Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA   Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA   Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT   "The genome of broomcorn millet.";
RL   Nat. Commun. 10:436-436(2019).
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:RLN04308.1}.
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DR   EMBL; PQIB02000008; RLN04308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6RJI2; -.
DR   STRING; 4540.A0A3L6RJI2; -.
DR   Proteomes; UP000275267; Chromosome 13.
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; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11528:SF135; OS08G0487800 PROTEIN; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 2.
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:UP000275267};
KW   Stress response {ECO:0000313|EMBL:RLN04308.1}.
FT   DOMAIN          100..262
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          731..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..774
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  87291 MW;  29240B7E17AE4507 CRC64;
     MAPALSGTLG ASSVAALRPC AARRAPSAAS SVAPRGSGAA RCPRGVRWEA ERSRGRLVRV
     RCDAAVTEKP AGEEAAEEKF EYQAEVSRLM DLIVHSLYSH KEVFLRELVS NASDALDKLR
     FLGVTDSSLL ADGGELEIRI KPDPDAGTIT ITDTGVGMTK DELKDCLGTI AQSGTSKFLK
     ALKENQDLGS DNGLIGQFGV GFYSAFLVAE KVVVSTKSPK SDKQYVWEAV ADSSSYVIKE
     ETDPEKMLTR GTQITLFLRP DDKYEFADPS RIQGLVKNYS QFVSFPIYTW QEKSRTVEGE
     KQKKKKTITE KYWDWELANE TKPIWMRNPK EIEKTEYNEF YKKTFNEFLD PLAHTHFTTE
     GEVEFRSVLY IPGMAPLSNE EIMNPKTKNI RLYVKRVFIS DDFDGELFPR YLSFVKGVVD
     SNDLPLNVSR EILQESRIVR IMRKRLVRKT FDMIEEIAEK EDKEDYKKFW ESFGKFIKLG
     CIEDTGNHKR LAPLLRFHSS KNEGDTISLD QYVENMPESQ KAIYYIATDS LQSAKTAPFL
     EKLVQKDIEV LYLIEPIDEV AIQNLQTYKE KKFVDISKED LELGDEEEEN KETKQEFTLL
     CDWVKQQLGD KVAKVQISKR LSSSPCVLVS GKFGWSANME RLMKAQTLGD TSSLEFMRGR
     RIFEINPDHP IIKDLNAACK NEPESTEAKR AVELLYEAAL ISSGYTPESP AELGGKIYEM
     MAIALGGRWG RSDTEEAEAT TSGEASAEAD SSESTETEVI EPSEVRPESD PWRD
//
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