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Database: UniProt
Entry: A0A3Q3MBH5_9TELE
LinkDB: A0A3Q3MBH5_9TELE
Original site: A0A3Q3MBH5_9TELE 
ID   A0A3Q3MBH5_9TELE        Unreviewed;       724 AA.
AC   A0A3Q3MBH5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 {ECO:0000313|Ensembl:ENSMAMP00000020086.1};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000020086.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000020086.1}
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; A0A3Q3MBH5; -.
DR   Ensembl; ENSMAMT00000020618.2; ENSMAMP00000020086.1; ENSMAMG00000013506.2.
DR   GeneTree; ENSGT01020000230401; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000261640; 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; 3.30.230.80; -; 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:UP000261640}.
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          703..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;  83354 MW;  98B4F9FEF79CEFB9 CRC64;
     MPESAGHIME EETETFAFQA EIAQLMSLII NTFYSNKEIF LRELISNSSD ALDKIRYESL
     TDPSKLESCK DLKIEISPDL HARTLTIIDT GIGMTKADLI NNLGTIAKSG TKAFMEALQA
     GADISMIGQF GVGFYSAYLV AEKVTVVTKH NDDEQYMWES AAGGSFTVRP DNGEPIGRGT
     KVILHLKEDQ TEYCEEKRIK EVVKKHSQFI GYPITLYVEK TREKEVDLEE GEKEEEVERD
     AAENKDKPKI EDVGSDEDED TKDSKNKRKK KVKEKYIDAQ ELNKTKPIWT RNPDDITNEE
     YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFVPRRAA FDLFENKKRR NNIKLYVRRV
     FIMDNCEELI PEYLNFIKGV VDSEDLPLNI SREMLQQSKI LKVIRKNLVK KCLELFTELA
     EDKDNYKKYY EQFSKNIKLG IHEDSQNRKK LSELLRYYTS ASGDEMVSLK DYVSRMKDNQ
     KHIYYITGET KDQVANSAFV ERLRKAGLEV IYMIEPIDEY CVQQLKEFDG KTLVSVTKEG
     LELPEDEDEK KKQEELKNKF ENLCKIMKDI LDKKIEKVTV SNRLVSSPCC IVTSTYGWTA
     NMERIMKSQA LRDNSTMGYM TAKKHLEINP LHPIIETLRE KAEADKNDKA VKDLVVLLFE
     TSLLSSGFTL EDPQTHANRI YRMIKLGLGI DDDDSAVEDL IQPAEEDMPV LEGDDDTSRM
     EEVD
//
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