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
//