ID L7P417_9EUGL Unreviewed; 635 AA.
AC L7P417;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:AFK26091.1};
DE Flags: Fragment;
GN Name=hsp90 {ECO:0000313|EMBL:AFK26091.1};
OS Monomorphina pseudopyrum.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Monomorphina.
OX NCBI_TaxID=565119 {ECO:0000313|EMBL:AFK26091.1};
RN [1] {ECO:0000313|EMBL:AFK26091.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCAC 0093 {ECO:0000313|EMBL:AFK26091.1};
RA Karnkowska-Ishikawa A., Watza D., Bennett M.S., Zakrys B., Triemer R.E.;
RT "Phylogenetic relationships and character evolution of photosynthetic
RT euglenoids (Euglenea) inferred from taxon-rich analyses of five genes.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity. This cycle
CC probably induces conformational changes in the client proteins, thereby
CC causing their activation. Interacts dynamically with various co-
CC chaperones that modulate its substrate recognition, ATPase cycle and
CC chaperone function. {ECO:0000256|ARBA:ARBA00037441}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; JQ398664; AFK26091.1; -; mRNA.
DR AlphaFoldDB; L7P417; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 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.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Stress response {ECO:0000313|EMBL:AFK26091.1}.
FT DOMAIN 1..155
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 186..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFK26091.1"
FT NON_TER 635
FT /evidence="ECO:0000313|EMBL:AFK26091.1"
SQ SEQUENCE 635 AA; 73456 MW; 921A86218293906A CRC64;
NKEIFLRELI SNASDALDKI RYQALTDKTI LDAEPNFFIH IIPDKANKTL TIHDSGIGMT
KADLINNLGT IARSGTKQFM ESLSAGADIS MIGQFGVGFY SAYLVAEKVV VVSKNQEDDC
YLWESAAGGT FTVTKCEDES LKRGTKMTLY LKEDQQEYLE ERRLKDLIKK HSEFIGFPIS
LQVEKTTEKE VTDDDEEEKK EEKKEGDDDE PKVEEVDEKD KDKKKKKKIK EVTVELELQN
KNKPIWTRDP KDITNEEYAS FYKAISNDWE DHLAVKHFSV EGQLEFRAIL FTPKRAPFDM
FETNKKKNNI KLYVRRVFIM DNCEDIIPEW LTFIKGIVDS EDLPLNISRQ QLQQNKILKV
IKKNVVKKVL EMFEELAENA DDYKKFYEQF GKNIKLGIHE DSQNRKKLAD LLRYPSTKSG
EEMTSLKDYV TRMKEGQKDI YYITGENKKQ LETSPFIESC KKRGYEVIFM TDPIDEYAMQ
QLKDYEDKKF VCLTKDGVKF EETEEEKKRK EEEKAAFENL TKLMKEILGD KVEKVLLSDR
IVNSPCVLVT GEYGWSANME RIMKAQALRD ASTSSYMVSK KTMELNPQHP IVKELKKKAD
EDKSDKTVKD LVWLLFDTAL LTSGFSLDDP AGYAE
//
