ID D0V3X9_HALDH Unreviewed; 728 AA.
AC D0V3X9;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ACX94847.1};
OS Haliotis discus hannai (Japanese abalone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX NCBI_TaxID=42344 {ECO:0000313|EMBL:ACX94847.1};
RN [1] {ECO:0000313|EMBL:ACX94847.1}
RP NUCLEOTIDE SEQUENCE.
RA Wu C.L., Zhang W.B., Mai K.S.;
RT "Molecular cloning, characterization and expression analysis of heat shock
RT protein 90 gene from abalone (Haliotis discus hannai Ino) in response to
RT dietary selenium, iron and zinc.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACX94847.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21044885; DOI=10.1016/j.fsi.2010.10.019;
RA Zhang W., Wu C., Mai K., Chen Q., Xu W.;
RT "Molecular cloning, characterization and expression analysis of heat shock
RT protein 90 from Pacific abalone, Haliotis discus hannai Ino in response to
RT dietary selenium.";
RL Fish Shellfish Immunol. 30:280-286(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; GU014545; ACX94847.1; -; mRNA.
DR AlphaFoldDB; D0V3X9; -.
DR SMR; D0V3X9; -.
DR GO; GO:0005737; C:cytoplasm; 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: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.
DR PROSITE; PS00298; HSP90; 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:ACX94847.1}.
FT DOMAIN 37..191
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 222..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..728
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 84134 MW; 19D6D76B2371CC3E CRC64;
MPEPQEAQME EAEVETFAFQ AEIAQLMSLI INTFYSNKEI FLRELISNSS DALDKIRYES
LTDPSKLDAC KDLQIRIVPD KENKTLVIQD SGIGMTKADL VNNLGTIAKS GTKAFMEALQ
AGADISMIGQ FGVGFYSAYL VAERAVVESK HNDDEQYIWE SSAGGSFTIK NSNDPTLPRG
TRITLYMKED QVEYLEERRV KEIVKKHSQF IGYPIKLMVE KERDKEVSDD EEEEEKKEDE
EKKEDEENEE KPKVEDLDED EDEDKNKDKK KKKKIKEKYT EDEELNKTKP LWTRNADDIT
QEEYAEFYKS LTNDWEDHLA VKHFSVEGQL EFRALLFLPK RAPFDMFENK KKKNNIKLYV
RRVFIMDNCE DLIPEYLNFV RGVVDSEDLP LNISREMLQQ SKILKVIRKN LVKKCMELFD
DIMEDKDNFK KFYDQFSKNL KLGIHEDSTN RKKLSELLRY YTSQSGDEVT SLKDYVSRMK
ENQKSIYYIT GESKDSVQNS AFVERVKKRG FEVIYMTDPI DEYCVQQLKE YDGKTLVCVT
KEGLELPEDE EEKKKLEESK AQFEGLCKVM KEILDKKVEK VVVSNRLVTS PCCIVTSQYG
WSANMERIMK AQALRDTSTM GYMAAKKHLE INPDHPIVKT LKEKADADKN DKAVKDLCML
LFETSLLASG FSLEDPTSHA NRIHRMIKLG LGIDEDDIPT EPTAESATDE MPPLEGDEDD
ASRMEEVD
//
