ID   A0A3Q2CEU8_CYPVA        Unreviewed;       724 AA.
AC   A0A3Q2CEU8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Heat shock protein HSP 90-alpha 1 {ECO:0000313|Ensembl:ENSCVAP00000003477.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000003477.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000003477.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_015254225.1; XM_015398739.1.
DR   AlphaFoldDB; A0A3Q2CEU8; -.
DR   STRING; 28743.ENSCVAP00000003477; -.
DR   Ensembl; ENSCVAT00000009982.1; ENSCVAP00000003477.1; ENSCVAG00000004674.1.
DR   GeneID; 107100299; -.
DR   KEGG; cvg:107100299; -.
DR   GeneTree; ENSGT01020000230401; -.
DR   OMA; MSTEMET; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
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   GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR   GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
DR   GO; GO:0048769; P:sarcomerogenesis; IEA:Ensembl.
DR   GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IEA:Ensembl.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; IEA:Ensembl.
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:SF122; HEAT SHOCK PROTEIN HSP 90-ALPHA 1; 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:UP000265020}.
FT   DOMAIN          36..190
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          225..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..724
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  83383 MW;  82420FF0D17FB396 CRC64;
     MPENAGHVME EEVETFAFQA EIAQLMSLII NTFYSNKEIF LRELISNSSD ALDKIRYESL
     TDPSRLESCK ELKIEIRPDL HARTLTITDT GIGMTKADLI NNLGTIAKSG TKAFMEALQA
     GADISMIGQF GVGFYSAYLV AEKVTVITKH NDDEQYVWES AAGGSFTVKP DNGEPLGRGT
     KVILHLKEDQ TEYCEEKRVK EVVKKHSQFI GYPITLFVEK TREKEVDLEE GEKEEEVEKD
     AAENKDKPKI EDVGSDEDED SKDGKNKRKK KVKEKYIDAQ ELNKTKPIWT RNPDDITNEE
     YGEFYKSLTN DWEDHQAVKH FSVEGQLEFR ALLFVPRRAA FDLFENKRKR NNIKLYVRRV
     FIMDNCEELI PEYLNFIKGV VDSEDLPLNI SREMLQQSKI LKVIRKNLVK KCLELFTEMS
     EDKENYKKFY EQFSKNIKLG IHEDSQNRKK LSDLLRYYTS ASGDEMVSLK DYVSRMKDNQ
     KHIYYITGET KDQVANSAFV ERLRKAGLEV IYMIEPIDEY CVQQLKEYDG KNLVSVTKEG
     LELPEDDEEK KKHEELKNRF ENLCKIMKDI LDKKIEKVTV SNRLVASPCC IVTSTYGWTA
     NMERIMKSQA LRDNSTMGYM TAKKHLEINP LHPIIETLRE KAEADKNDKA VKDLVILLFE
     TALLSSGFTL EDPQTHANRI YRMIKLGLGI DDDDSAVEDL IQPADEDMPV LEGDDDTSRM
     EEVD
//