ID A0A022R8V3_ERYGU Unreviewed; 818 AA.
AC A0A022R8V3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN ORFNames=MIMGU_mgv1a001447mg {ECO:0000313|EMBL:EYU36792.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU36792.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU36792.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI630592; EYU36792.1; -; Genomic_DNA.
DR RefSeq; XP_012839184.1; XM_012983730.1.
DR AlphaFoldDB; A0A022R8V3; -.
DR STRING; 4155.A0A022R8V3; -.
DR GeneID; 105959588; -.
DR KEGG; egt:105959588; -.
DR eggNOG; KOG0020; Eukaryota.
DR OMA; EDEIRWW; -.
DR OrthoDB; 547579at2759; -.
DR PhylomeDB; A0A022R8V3; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
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; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; 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: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:UP000030748};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..818
FT /note="Histidine kinase/HSP90-like ATPase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001504890"
FT DOMAIN 100..257
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 291..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..322
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..795
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 94057 MW; FD041970D649E96A CRC64;
MRKWTIPSVL FLLCLLFLLP DQGRKIHANA EADSDVPLDP PKVEEKIGAV PHGLSTDSEV
VKREAESMSR KTLRASAQKF EFQAEVSRLM DIIINSLYSN KDIFLRELIS NASDALDKIR
FLSLTDKEVL GEGDNTKLEI QIKLDKENKI LSIRDRGVGM TKEDLIKNLG TIARSGTSAF
VEKMQTSGDL NLIGQFGVGF YSVYLVADYV EVISKHNDDK QHVWESKADG AFAISEDEWN
EPLGRGTEIR LHLRDEAQEY LDEYKLKELV KKYSEFINFP IHLWASKEVD EEVPADEDES
NDDDDDTAES KSSEEEEEEE DKGEDEKKPK TKTIKKTTYE WELLNDVKAI WLRSPKEVTD
EEYTKFYHSL AKDFADEKPL SWSHFNAEGD VEFKALLFVP PKAPHDLYES YYNSNKSNLK
LFVRRVFISD EFDELLPKYL NFLKGLVDSD TLPLNVSREM LQHHSSLKTI KKKLIRKALD
MIRKLAEEDP DESNDKSKKD VEESGDNNEK KGQYAKFWNE FGKSIKLGII EDATNRNRLA
KLLRFETTKS DGKLTSLDQY ISRMKSGQKD IFYITGTSKE QLEKSPFLER LTKKNYEVIF
FTDPVDEYLM QYLTEYEDTK FQNVSKEGLK IEKDSKDKEL KESFKELTKW WKGALASHNV
DDVKISNRLA DSPCVVVTSK YGWTSNMERI MQSQTLSDAN KQAYMRGKRV LEINPRHPII
KELRDRVVKD SEDESVKQTA QLIYQTALME SGFMLSDPQD FASRIYSSVK NSLKISPDAT
VEEEDDMEEA ETVSSAEETE STTKTEEALV DDDVNDEL
//
