ID A0A060XPW0_ONCMY Unreviewed; 725 AA.
AC A0A060XPW0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN ORFNames=GSONMT00026598001 {ECO:0000313|EMBL:CDQ81678.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ81678.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ81678.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ81678.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; FR905814; CDQ81678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060XPW0; -.
DR SMR; A0A060XPW0; -.
DR STRING; 8022.A0A060XPW0; -.
DR PaxDb; 8022-A0A060XPW0; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
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:UP000193380}.
FT DOMAIN 36..190
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 226..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..725
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 83437 MW; DA5064E2B3B557ED CRC64;
MPEIASHTME EEVETFAFQA EIAQLMSLII NTFYSNKEIF LRELISNSSD ALDKIRYESL
TDPTKLDSCK DLKIEVTPDL RTRTLTLVDT GIGMTKADLI NNLGTIAKSG TKAFMEALQA
GADISMIGQF GVGFYSAYLV AERVTVITKH NDDEQYIWES AAGGSFTVKV DTGESIGRGT
KVILHMKEDQ FEYCEEKRVK EVVKKHSQFI GYPITLYVEK SREKEVDLEE GEKDEEADKD
AAAEDKDKPK IEDVGSDEDE DTKDSKNKRK KKVKEKYIDA EELNKTKPIW TRNPDDITNE
EYGEFYKSLT NDWEDHLAIK HFSVEGQLEF RALLFVPRRA SFDLFENKKK KNNIKLYVRR
VFIMDNCDEL MPEYLNFIKG VVDSEDLPLN ISREMLQQSK ILKVIRKNLV KKCIELFIEL
SEDKDNYKKF YEQFSKNIKL GIHEDSQNRK KLSDMLRYYT SNSGDEMVSL KDYVSRMKDT
QKHIYYITGE TKEQVANSSF VERLRKAGLE VIYMIEPIDE YCVQQLKEYD GKNLVSVTKE
GLELPEDEDE KKKQEELNSK FENLCKIMKD ILDKKIEKVS VSNRLVSSPC CIVTSTYGWT
ANMERIMKSQ ALRDNSTMGY MTAKKHLEIN PTHPIVETLR EKAEADKNDK AVKDLVILLF
ETALMSSGFT LDDPQTHANR IYRMIKLGLG IDDDDSAVED ILQPSEDDMP VLEGDDDTSR
MEEVD
//
