ID A0A091E108_FUKDA Unreviewed; 806 AA.
AC A0A091E108;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Heat shock protein HSP 90-beta {ECO:0000256|ARBA:ARBA00041115};
GN ORFNames=H920_02412 {ECO:0000313|EMBL:KFO36200.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO36200.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO36200.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO36200.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Dynein axonemal particle
CC {ECO:0000256|ARBA:ARBA00024190}. Melanosome
CC {ECO:0000256|ARBA:ARBA00004223}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; KN121537; KFO36200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091E108; -.
DR STRING; 885580.ENSFDAP00000009995; -.
DR eggNOG; KOG0019; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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:SF79; HEAT SHOCK PROTEIN HSP 90-BETA-RELATED; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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:UP000028990};
KW Stress response {ECO:0000313|EMBL:KFO36200.1}.
FT DOMAIN 117..271
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 91893 MW; A4AE2E0F880692B2 CRC64;
MMLLSAWDGN KKSTQGPLKT ADFSQGAEKG AQSRKAKARL CSLDSATDRA GQGRTIGPGV
VAATPQYCGT GKEQVHPSRA EQMPEEVHHG EEEVETFAFQ AEIAQLMSLI INTFYSNKEI
FLRELISNAS DALDKIRYES LTDPSKLDSG KELKIDIIPN PQERTLTLVD TGIGMTKADL
INNLGTIAKS GTKAFMEALQ AGADISMIGQ FGVGFYSAYL VAEKVVVITK HNDDEQYAWE
SSAGGSFTVR ADHGEPIGRG TKVILHLKED QTEYLEERRV KEVVKKHSQF IGYPITLYLE
KEREKEISDD EAEEEKGEKE EEDKDDEEKP KIEDVGSDEE DDTGKDKKKK TKKIKEKYID
HEELNKTKPI WTRNPDDITQ EEYGEFYKSL TNDWEDHLAV KHFSVEGQLE FRALLFIPRR
APFDLFENKK KKNNIKLYVR RVFIMDSCDE LIPEYLNFIR GVVDSEDLPL NISREMLQQS
KILKVIRKNI VKKCLELFSE LAEDKENYKK FYEAFSKNLK LGIHEDSTNR RRLSELLRYH
TSQSGDEMTS LSEYVSRMKE TQKSIYYITG ESKEQVANSA FVERVRKRGF EVVYMTEPID
EYCVQQLKEF DGKSLVSVTK EGLELPEDEE EKKKMEESKA KFENLCKLMK EILDKKVEKV
TISNRLVSSP CCIVTSTYGW TANMERIMKA QALRDNSTMG YMMAKKHLEI NPDHPIVETL
RQKAEADKND KAVKDLVVLL FETALLSSGF SLEDPQTHSN RIYRMIKLGL GIDEDEVTAE
EPSATVPDEI PPLEGDEDAS RMEEVD
//
