ID   A0A3Q3CW45_HAPBU        Unreviewed;       472 AA.
AC   A0A3Q3CW45;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Heat shock protein HSP 90-alpha 1 {ECO:0000313|Ensembl:ENSHBUP00000032088.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000032088.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000032088.1}
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}.
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DR   AlphaFoldDB; A0A3Q3CW45; -.
DR   Ensembl; ENSHBUT00000024691.1; ENSHBUP00000032088.1; ENSHBUG00000022200.1.
DR   GeneTree; ENSGT01020000230401; -.
DR   Proteomes; UP000264840; Unplaced.
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; 3.40.50.11260; -; 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   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; 2.
DR   PIRSF; PIRSF002583; Hsp90; 3.
DR   PRINTS; PR00775; HEATSHOCK90.
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; 2.
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:UP000264840}.
FT   REGION          146..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  53936 MW;  49A51C1FE39DA4C7 CRC64;
     MPESSAHIME EEVETFAFQA EIAQLMSLII NTFYSNKEIF LRELISNSSD ALDKIRYESL
     TDPTKLESCK DLKIEIRPDL HARTLTLLDT GIGMTKADLI NNLGTIAKSG TKAFMEALQA
     GADISMIGQF GVGFYSAYLV EKTREKEVDL EEGEKEEEVE KEAAEDKDKP KIEDVGSDED
     EDTKDGKNKR KKKVKEKYID AQELNKTKPI WTRNPDDITN EEYGEFYKSL TNDWEDHLAV
     KDYVSRMKDN QKHIYYITGE TKDQVANSAF VERLRKAGLE VIYMIEPIDE YCVQQLKEYD
     GKNLVSVTKE GLELPEDEEE KKKQEELKTK FEDLCKIMKD ILDKKIEKVV VSNRLVASPC
     CIVTSTYGWT ANMERIMKSQ ALRDNSTLGY MTAKKHLEIN PSHPIIETLR EKAEADKNDK
     AVKDLVILLF ETALLSSGFT LEDPQTHANR IYRMIKLGLG MYVFSFKHSG SS
//