ID T1E691_CROHD Unreviewed; 728 AA.
AC T1E691;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Heat shock protein HSP 90-alpha {ECO:0000256|ARBA:ARBA00039928};
OS Crotalus horridus (Timber rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=35024 {ECO:0000313|EMBL:JAA96822.1};
RN [1] {ECO:0000313|EMBL:JAA96822.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAA96822.1};
RX PubMed=23758969; DOI=10.1186/1471-2164-14-394;
RA Rokyta D.R., Wray K.P., Margres M.J.;
RT "The genesis of an exceptionally lethal venom in the timber rattlesnake
RT (Crotalus horridus) revealed through comparative venom-gland
RT transcriptomics.";
RL BMC Genomics 14:394-394(2013).
RN [2] {ECO:0000313|EMBL:JAG44413.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type B {ECO:0000313|EMBL:JAG46613.1};
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAG44413.1};
RX PubMed=25727380; DOI=10.1016/j.toxicon.2015.02.015;
RA Rokyta D.R., Wray K.P., McGivern J.J., Margres M.J.;
RT "The transcriptomic and proteomic basis for the evolution of a novel venom
RT phenotype within the Timber Rattlesnake (Crotalus horridus).";
RL Toxicon 98:34-48(2015).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; GAAZ01001121; JAA96822.1; -; mRNA.
DR EMBL; GBKC01001657; JAG44413.1; -; Transcribed_RNA.
DR EMBL; GBKD01001005; JAG46613.1; -; Transcribed_RNA.
DR AlphaFoldDB; T1E691; -.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
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:0046677; P:response to antibiotic; ISS:AgBase.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0009408; P:response to heat; ISS:AgBase.
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:SF87; HEAT SHOCK PROTEIN HSP 90-ALPHA; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Stress response {ECO:0000313|EMBL:JAA96822.1}.
FT DOMAIN 39..193
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 225..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 84128 MW; B640AA1B04594D33 CRC64;
MPEEVQTQDQ PMEEEVETFA FQAEIAQLMS LIINTFYSNK EIFLRELISN SSDALDKIRY
ESLTDPSKLD SGKELKISLT PNKQDRTLTL VDTGIGMTKA DLINNLGTIA KSGTKAFMEA
LQAGADISMI GQFGVGFYSA YLVAEKVTVI AKHNDDEQYA WESSAGGSFT VRLDNGEPLG
RGTKVILHLK EDQTEYLEER RIKEIVKKHS QFIGYPITLF VEKERDKEVS DDEAEEKEEE
KEEKEEKPED KPEIEDVGSD EEEEKKDGDK KKKKKIREKY IDQEELNKTK PIWTRNPDDI
TNEEYGEFYK SLTNDWEDHL AVKHFSVEGQ LEFRALLFVP RRAPFDLFEN RKKKNNIKLY
VRRVFIMDNC EELIPEYLNF MRGVVDSEDL PLNISREMLQ QSKILKVIRK NLVKKCLELF
TELAEDKENY KKFYEQFSKN IKLGIHEDSQ NRKKLSELLR YYTSASGDEM VSLKDYCTRM
KENQKHVYYI TGETKDQVAN SAFVERLRKH GLEVIYMIEP IDEYCVQQLK EFEGKTLVSV
TKEGLELPED EEEKKKQEEK KAKFESLCKI MKDILEKKVE KVVVSNRLVT SPCCIVTSTY
GWTANMERIM KAQALRDNST MGYMAAKKHL EINPDHSIIE TLRQKAEADK NDKSVKDLVI
LLYETALLSS GFSLEDPQTH ANRIYRMIKL GLGIDEDDAT TEETSPAVTE EMPPLEGDDD
TSRMEEVD
//
