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Database: UniProt
Entry: I1JEL6_SOYBN
LinkDB: I1JEL6_SOYBN
Original site: I1JEL6_SOYBN 
ID   I1JEL6_SOYBN            Unreviewed;       794 AA.
AC   I1JEL6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN   ORFNames=GLYMA_02G124500 {ECO:0000313|EMBL:KRH71021.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH71021};
RN   [1] {ECO:0000313|EMBL:KRH71021.1, ECO:0000313|EnsemblPlants:KRH71021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH71021};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH71021.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH71021}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH71021};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH71021.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH71021.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; CM000835; KRH71021.1; -; Genomic_DNA.
DR   RefSeq; XP_003518802.1; XM_003518754.3.
DR   AlphaFoldDB; I1JEL6; -.
DR   SMR; I1JEL6; -.
DR   STRING; 3847.I1JEL6; -.
DR   PaxDb; 3847-GLYMA02G13790-1; -.
DR   EnsemblPlants; KRH71021; KRH71021; GLYMA_02G124500.
DR   Gramene; KRH71021; KRH71021; GLYMA_02G124500.
DR   eggNOG; KOG0019; Eukaryota.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   InParanoid; I1JEL6; -.
DR   OMA; QYSEFVH; -.
DR   Proteomes; UP000008827; Chromosome 2.
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:UP000008827}.
FT   DOMAIN          104..266
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          302..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  90092 MW;  BF5E811AC02996EE CRC64;
     MAPVLSRTMA TASLASLPPS SPFARTSLLR SAFLPPQIGL GRNCFSPAAG LRWTQQRREG
     RRGGLTVRCE AAVAEKDEAT GEKFEYQAEV SRLLDLIVHS LYSHKEVFLR ELVSNASDAL
     DKLRFLSVTE PSLLGDAGDL EIRIKSDPDN GTITITDTGI GMTKEELIDC LGTIAQSGTS
     KFLKALKENK DLGADNGLIG QFGVGFYSAF LVAERVVVST KSPRSDKQYV WEAEADSSSY
     VIKEETDPEK VLRRGTQITL YLREDDKYEF SEPSRIQGLV KNYSQFVSFP IYTWQEKSRT
     VEVEEEEEPK EGEEPKEEGE KKKVKKTKTE KYWDWELANE TKPIWMRNPK EVEKEEYNEF
     YKKTFSEFLE PLAHTHFTTE GEVEFRSILY VPGMGPLNNE EVVNPKTKNI RLYVKRVFIS
     DDFDGELFPR YLSFVKGVVD SDDLPLNVSR EILQESRIVR IMRKRLVRKA FDMIQDLAES
     ENKEDYKKFW ENFGRFIKLG CIEDTGNHKR ITPLLRFYTS KSEEELKSLD DYVENMGENQ
     KAIFYLATDS LKSAKTAPFL EKLVQKDIEV LYLVEPIDEV AIQNLQTYKE KKFVDISKED
     LELGDEDEVK ERENKQEYNL LCDWIKQQLG DKVAKVQISN RLSSSPCVLV SGKFGWSANM
     ERLMKAQALG DTASLEFMRG RRILEINADH PIIKDLSAAC KNAPDSSEAK RAVDLLYDTA
     LISSGFSPDS PAELGNKIYE MMALALGGRW GRSEEEEGDA SVEAADSSTS EESSEPEVYE
     PSEVIAESDP WTTD
//
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