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Database: UniProt
Entry: G8JNI4_ERECY
LinkDB: G8JNI4_ERECY
Original site: G8JNI4_ERECY 
ID   G8JNI4_ERECY            Unreviewed;       712 AA.
AC   G8JNI4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN   OrderedLocusNames=Ecym_2148 {ECO:0000313|EMBL:AET37900.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS   NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET37900.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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; CP002498; AET37900.1; -; Genomic_DNA.
DR   RefSeq; XP_003644717.1; XM_003644669.1.
DR   AlphaFoldDB; G8JNI4; -.
DR   STRING; 931890.G8JNI4; -.
DR   GeneID; 11470521; -.
DR   KEGG; erc:Ecym_2148; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   InParanoid; G8JNI4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000006790; Chromosome 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006790}.
FT   DOMAIN          27..165
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          219..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  81300 MW;  6B4F3090A54C340A CRC64;
     MSNQETYEFQ AEITQLMSLI INTVYSNKEI FLRELISNAS DALDKIRYQS LSDSKVLESE
     PEMFIRITPK PEDKVLELRD SGIGMTKAEL INNLGTIAKS GTKAFMEALS AGADVSMIGQ
     FGVGFYSLFL VADRVQVISK HNDDEQYVWE SNAGGSFTVT LDTTNEKIGR GTILRLFLKE
     DQLEYLEEKK IKEVVKRHSE FVAYPIQLLV SKEIEKEVPV AEDEAEEKKE GEEEAEDKKP
     KLEEVDEDDA GEEKKPKTEK VKETVKELEE LNKTKPLWTR NPSEVSQEEY NAFYKSISND
     WEDPLAVKHF SVEGQLEFRA ILFIPKRAPF DLFESKKKKN NIKLYVRRVF ITDEAEDLIP
     EWLSFVKGVV DSEDLPLNLS REMLQQNKIM KVIKKNIVKK LIEAFNEIGE DAEQFEKFYS
     AFAKNIKLGI HEDSQNRASL AKLLRYNSTK SVDEQTSLSD YVTRMPEHQK NIYFITGESI
     KAVEKSPFLE ALKAKNFEVL FLVDPIDEYA FQQLKEFEGK QLVDITKDFE LEETDEEKAQ
     REQEIKEFEP LTTALKEVLG EQVEKVVVSY KLVDAPAAIR TGQFGWSANM ERIMKAQALR
     DSTMSSYMAS KKTFEISPKS AIIKELKKRV EESGAQDRTV KDLTTLLYET ALLTSGFTLE
     EPATFANRIN RLISLGLNID EEPEQVTEVS SDATATAPVE EVVPETEMEE VD
//
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