ID S8CRG0_9LAMI Unreviewed; 815 AA.
AC S8CRG0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN ORFNames=M569_05408 {ECO:0000313|EMBL:EPS69355.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS69355.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS69355.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(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}.
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:EPS69355.1}.
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DR EMBL; AUSU01002158; EPS69355.1; -; Genomic_DNA.
DR AlphaFoldDB; S8CRG0; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000015453; 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; 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:UP000015453};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..815
FT /note="Histidine kinase/HSP90-like ATPase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004549686"
FT DOMAIN 100..257
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..815
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 801..815
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 93194 MW; 6073B82D9E5423E6 CRC64;
MRKWTVTSIL LLLCILLVLP DQGRKARVNA ESEKDAATGP PKVEEKIGGI PSGLSTDSEV
VKREAESISG RNLRAEAEKF QFQAEVSRLM DIIINSLYSN KDIFLRELIS NASDALDKIR
FLSLTDKEVL GEGENAKLDI QIKLDKDKKI LSLRDRGIGM TKEDLIKNLG TIAKSGTSAF
VEKMQTSGDL NLIGQFGVGF YSVYLVADYV EVISKHNDDK QHVWESKADG AFAVSEDTWN
EPLGRGTEIR LHLRDEAQEY LDEYKLKELV KKYSEFINFP IYLWASKEVD EEVPADEDED
EEAPESKSPE EEDEEEEEDA EKEEEKPKTK TIKKTTYEWE LLNDMKAIWL RNPKEVSDEE
YAKFYHSLAK DLSEDNPLAW SHFTAEGDVE FKAVLFVPPK APHDLYESYY NSKKSNFKLY
VRRVFISDEF DELLPKYLNF LLGLVDSDTL PLNVSREMLQ QHSSLKTIKK KLIRKALDMI
RKLADEDPDE SHGDKKGSTS DSEEEKKDKK GQYTKFWNEF GKSIKLGIIE DATNRNRLAK
LLRFETTKSD GKLTSLDQYI SRMKSGQKDI FYITGTTKEQ LEKSPFLERL VKKNYEVILF
TDPVDEYLMQ YLMDYEDKKF QNVSKEGLKL GKDSKDSKEV KESFKELTKW WKGALASDNV
DDVKISSRLS DSPCVVVTSK YGWSANMERI MQSQTLSDSN KQSSYMRGKR VLEINPRHPI
IKELRDRVAL NPEDEGVKQT AQLMYQTALM ESGFVLNDPK DFASRIYGSV KNSLNISPDA
TVEEEEEAEE TTTTTATTTA DDVNDDDDEG VKDEL
//
