ID F6SX68_XENTR Unreviewed; 702 AA.
AC F6SX68; B5DFP8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Heat shock protein HSP 90-alpha {ECO:0000256|ARBA:ARBA00039928};
GN Name=hsp90aa1.1 {ECO:0000313|EMBL:AAI69144.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI69144.1};
RN [1] {ECO:0000313|EMBL:AAI69144.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=TGA IC {ECO:0000313|EMBL:AAI69144.1};
RC TISSUE=Testes {ECO:0000313|EMBL:AAI69144.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2008) 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; BC169144; AAI69144.1; -; mRNA.
DR AlphaFoldDB; F6SX68; -.
DR AGR; Xenbase:XB-GENE-495303; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR PhylomeDB; F6SX68; -.
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}.
FT DOMAIN 41..195
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 228..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 81401 MW; A1CD830E417684D7 CRC64;
MPEEVQTTTQ DQQMEEDVET FAFQAEIAQL MSLIINTFYS NKEIFLRELI SNSSDALDKI
RYESLTDPSK LDSGKELKIY LIPNKQDRTL TIIDTGIGMT KADLINNLGT IAKSGTKAFM
EALQAGADIS MIGQFGVGFY SAYLVAEKVT VITKHNDDEQ YAWESSAGGS FTVKVDNGEP
LGRGTKVILY LKEDQSEYFE EKRIKETVKK HSQFIGYPIT LFVEKERDKE ISDDEAEEEK
EEKKEEAKDE EKPEIEDVGS DEEDDKKEGD KKKKKKIKEK YIDQEELNKT KPIWTRNPDD
ITNEEYGEFY KSLTNDWEDH LAVKHFSVEG QLEFRALLFV PRRAPFDLFE NRKKKNNIKL
YVRRVFIMDN CEELIPEYLN FIRGVVDSED LPLNISREML QQSKILKVIR KNLVKKCLEL
FTELSEDKEN YKKFYEQFSK NIKLGIHEDS QNRNKLSELL RYYTSASGDE MVSLKDYCTR
MKESQKHIYY ITGETKEQVA HSAFVERLRK HGLEVIYMIE PIDEYCVQQL KEFEGKTLVS
VTKEGLELPE DEEEKKKQEE KKSKFENLCK IMKDILEKKV EKVVVSNRLV TSPCCIVTST
YGWTANMERI MKAQALRDNS TMGYMAAKKH LEINPDHSII ETLRQKADSD KNDKSVKDLV
ILLFETALLS SGFSLEDPQT HANRIYRMIK LGLGIDEDEW AP
//
