ID A0A1R1YG78_9FUNG Unreviewed; 697 AA.
AC A0A1R1YG78;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Heat shock protein HSP 90-alpha 1 {ECO:0000313|EMBL:OMJ25917.1};
GN ORFNames=AYI70_g576 {ECO:0000313|EMBL:OMJ25917.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ25917.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ25917.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ25917.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMJ25917.1}.
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DR EMBL; LSSN01000093; OMJ25917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1YG78; -.
DR STRING; 133412.A0A1R1YG78; -.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF02518; HATPase_c; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW Stress response {ECO:0000313|EMBL:OMJ25917.1}.
FT DOMAIN 28..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 220..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..697
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 79889 MW; B5F63FC805DA1E11 CRC64;
MTNQPETFAF QAEISQLMSL IINTFYSNKE IFLRELISNA SDAIDKIRYE SLTNPSVLDT
EKDLYIQLSV DKVNNILTIR DSGIGMTKAD LVNNLGTIAK SGTKTFMEAL SQGADISMIG
QFGVGFYSAY LVADKVVVVT KNNDDEQYIW ESAAGGSFTI TLDESGERIG RGTEIRLHLK
EDQLEYLDEK KIKEVVKKHS EFISYPIRLL VEKEVETEVP VEKEESADGE SKIEEVEDED
GEKKETTKKI KELKIETEEL NKTKPLWTRN PDDITPEEYN TFYKALTNDW EDPLSLKHFS
VEGQLEFRAI LYIPSRAPFD LFETKKKRNN IKLYVRRVFI MDDCEELIPE WLSFVKGVVD
SEDLPLNISR EILQQNKILK VIKKNIVKKC LEMFTEISED KDSFTKFYEA FSKNIKLGIH
EDTQNRSKLA ELLRYSSSKS VDEPTSLKDY VTRMPENQKD IYYITGESKK AVMESPFLET
LKAKNFEVLF MVDPIDEYCV QQLREYDGKK LVSVTKEGLE FEESEEEKAK NEQIKKEFEP
LCAEIKEILG DQVEKVVVSN RISDSPCVLV TGQFGWTANM ERIMKAQALR DSSMSSYMMS
KKTMEINPHH KIIVALKERL EKDKSDKTIK DLALLMFDAA LLSSGFTLDN PSSFSNRIYR
MINHGLGHDD DEVEVDDVTA DAPALEEVTE SNMEEVD
//
