ID   G4TFY1_SERID            Unreviewed;       846 AA.
AC   G4TFY1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Related to HSP82-Heat shock protein {ECO:0000313|EMBL:CCA70224.1};
GN   ORFNames=PIIN_04163 {ECO:0000313|EMBL:CCA70224.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA70224.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA70224.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA70224.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA   Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA   Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT   the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
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:CCA70224.1}.
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DR   EMBL; CAFZ01000076; CCA70224.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4TFY1; -.
DR   STRING; 1109443.G4TFY1; -.
DR   eggNOG; KOG0020; Eukaryota.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   InParanoid; G4TFY1; -.
DR   OMA; QPPIWMR; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000007148; Unassembled WGS sequence.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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; 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:SF97; ENDOPLASMIN; 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   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:UP000007148};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Stress response {ECO:0000313|EMBL:CCA70224.1}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..846
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003468462"
FT   REGION          257..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   846 AA;  95407 MW;  1337BA776EF17121 CRC64;
     MKLLPSLLLA LSLFSGASFA QEPVATDSST KHEYQSDVAR LRKIVIESLY SHREVFLREL
     ISNANDAIEK LRLTALKDKT VWDGVAPLNI TLKLEKNEEG DGGRLIISDT GIGMSPKELT
     TNLGTLAKSG TSEFLAKADS NSGSSNGNLI GAFGLGFYSS FLVADKVYVA SLPPATEANP
     QPVQHVFSSS ADEPSFDVYP DPRGNTLGRG TEITLVLKKD ALEYLEEETV KSLITKHSGF
     ASSFPVYLFT KRIEEQPIPQ DELDQTTEEK KEKPKVDDDE VVVEDAKEEE PKENEVKTRQ
     VTVEEWVHLN DQPPLWTRDP KDVTDEEYKN FYKATFKQYQ DPILWHHFKG DSGPVSFRAL
     IYVPSTLPED FWQSPQTAQQ DTRLLVKRVL ITSEFGEHRL PKWISWAKVI IDADDLPLNV
     SRETLQSNRF LKQIKNIIIT RFIQVMQKTA EEDVEKYKEI LKVYNPILKL GVIETAAEGK
     TGNRDKLSSL LRFDTTLRTG ISLQDYVDNR KEGQNQIFFL ANIGQTTENM RHSVFVEKLI
     ARGYEVLLMT DTMDEIFVSN LRVWGNMRFQ DVAKKGLQYG DEDVEKEKKE LEKFKEDYKP
     LVNFFVKSTK DISRMAIVIS NRLVTSPCAI VVDSFGYSAN MEKLLTSHGK KTALQEYASK
     QKVLEINPRS PLIEGLLKRV MALPVEETER DKEEEAELRE VVQILIDGAL IRSGFEVMES
     NIFFERVDRA LRRSLGVSET AKVEVEVAPA PPKAETAPPE MDEVATNAAD FIEMQDFRAS
     LGPELDRTFG GPKLMKMDAN GPIETVPNQV AFDANDVRKR MESGEEVDIE GMVADAIKPK
     TEHTEL
//