ID   A0A3B5AUQ6_9TELE        Unreviewed;       696 AA.
AC   A0A3B5AUQ6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Heat shock protein 90 alpha family class B member 1 {ECO:0000313|Ensembl:ENSSPAP00000021554.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000021554.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000021554.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Dynein axonemal particle
CC       {ECO:0000256|ARBA:ARBA00024190}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   AlphaFoldDB; A0A3B5AUQ6; -.
DR   STRING; 144197.ENSSPAP00000021554; -.
DR   Ensembl; ENSSPAT00000021891.1; ENSSPAP00000021554.1; ENSSPAG00000016242.1.
DR   GeneTree; ENSGT01020000230401; -.
DR   Proteomes; UP000261400; 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   GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR   GO; GO:0050900; P:leukocyte migration; 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; 2.
DR   HAMAP; MF_00505; HSP90; 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:SF79; HEAT SHOCK PROTEIN HSP 90-BETA-RELATED; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 2.
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; 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}.
FT   REGION          192..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..696
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  80157 MW;  0D596F44288BDE33 CRC64;
     MPEEMHQEEE AETFAFQAEI AQLMSLIINT FYSNKEIFLR ELISNASDAL DKIRYESLTD
     PSKLDSDLIN NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN
     DDEQYAWESS AGGSFTVKVD NGEPIGRGTK IILYLKEDQT EYIEEKRVKE IVKKHSQFIG
     YPITLFVEKE RDKEISDDEA EEEKAEKEEK EEGEDKPKIE DVGSDDEEDS KDKDKKKKKK
     IKEKYIDQEE LNKTKPIWTR NPDDITNEEY GEFYKSLTND WEDHLAVKHF SVEGQLEFRA
     LLFIPRRAPF DLFENKKKKN NIKLYVRRVF IMDNCEELIP EYLNFVRGVV DSEDLPLNIS
     REMLQQSKIL KVIRKNIVKK CLELFAELAE DKDNYKKFYE AFSKNIKLGI HEDSQNRKKL
     SELLRYHSSQ SGDETTSLTE YLTRMKENQK SIYYITGESK DQVANSAFVE RVRKRGFEVL
     YMTEPIDEYC VQQLKEFDGK SLVSVTKEGL ELPEDEEEKK KMEEDKAKFE SLCKLMKEIL
     DKKVEKVTVS NRLVSSPCCI VTSTYGWTAN MERIMKAQAL RDNSTMGYMM AKKHLEINPD
     HPIVETLRQK AEADKNDKAV KDLVILLFET ALLSSGFSLD DPQTHSNRIY RMIKLGLGID
     DDDVATEETT TAAVPDEIPP LEGDGDDDAS RMEEVD
//