ID A0A1B8G1C1_9PEZI Unreviewed; 703 AA.
AC A0A1B8G1C1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:OBT89643.1};
GN ORFNames=VE02_01855 {ECO:0000313|EMBL:OBT89643.1};
OS Pseudogymnoascus sp. 03VT05.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT89643.1};
RN [1] {ECO:0000313|EMBL:OBT89643.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03VT05 {ECO:0000313|EMBL:OBT89643.1};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; KV459367; OBT89643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8G1C1; -.
DR Proteomes; UP000091872; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 26..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 212..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 79591 MW; 4FC1ED1370AFA3EB CRC64;
MVAETFEFQA EISQLLGLII NTVYSNKEIF LREIISNGSD ALDKIRYESL ADPSKLDTGK
DLRIDIIPDK VNKTLTIQDS GIGMTKADLV NNLGTIARSG TKQFMEALTA GADVSMIGQF
GVGFYSAYLV ADRVTVISKN NDDEQYIWES AAGGTFTLTQ DTEGEPIGRG TKIILHLKDE
QTEYLNEAKI KEVVKKHSEF ISYPIYLHVE KETETEVPDE EAEESKEEEG DDKKPKIEEV
DDEEDEKKEK KTKKVKETKI EEEELNKQKP IWTRNPSDIS PEEYGAFYKS LSNDWEDHLA
VKHFSVEGQL EFKAILFVPK RAPFDLFETK KTKNNIKLYV RRVFITDDAT DLIPEWLSFV
KGVVDSEDLP LNLSRETLQQ NKIMKVIKKN IVKKTLELFQ EIAEDKEQFD KFYSAFGKNI
KLGVHEDAQN RGALAKLLRY NSTKTGEDDQ TSFADYITRM GEHQKNIYYI TGESLKAVQK
SPFLDSLKAK NFEVLFLVDP IDEYAMTQLK EFDGKKLVDI TKDFELEETD EEKAEREAEE
KEYESTAKAL KNILGDKVEK VVVSHKLVGA PCAIRTGQFG WSANMERIMK AQALRDTSMS
SYMSSKKTFE ISPKSPIIKE LRKKIEADGE NDRTVKSITQ LLFETSLLVS GFTIEEPAGF
ADRIHKLVSL GLQVDEEPEV EGEAATEAGA TDAPVESAME EVD
//
