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Database: UniProt
Entry: J9HY07_9SPIT
LinkDB: J9HY07_9SPIT
Original site: J9HY07_9SPIT 
ID   J9HY07_9SPIT            Unreviewed;       700 AA.
AC   J9HY07;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:EJY69804.1};
GN   ORFNames=OXYTRI_09455 {ECO:0000313|EMBL:EJY69804.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY69804.1};
RN   [1] {ECO:0000313|EMBL:EJY69804.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY69804.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY69804.1}.
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DR   EMBL; AMCR01017572; EJY69804.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9HY07; -.
DR   EnsemblProtists; EJY69804; EJY69804; OXYTRI_09455.
DR   OrthoDB; 547579at2759; -.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Stress response {ECO:0000313|EMBL:EJY69804.1}.
FT   DOMAIN          26..164
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          212..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          517..544
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        230..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  81009 MW;  46325278DF73647A CRC64;
     MSEEVFAFNA DIQQLMSLII NTFYSNKEIF LRELISNASD ALDKIRYRSI TEPEHLETEP
     NLGIKIIPDK SNNTLTVWDS GIGMTKAELI NNLGTIAKSG TKAFMEAISA GADISMIGQF
     GVGFYSAYLV AERVTVITKS NDDEQFRWES NAGGTFTVVK DEGERITRGT KIILHMKEDQ
     MENLEERKLK DLVKKHSEFI GFPIELYVEK SQDKEVTESD DEEDAKKDEE DKKDDEPKIE
     EEEKKKEKKM KKIKEVTHEY EQLNKTKPIW MRKPEDITKD EYSSFYKGLS NDWEDHLAVK
     HFSVEGQLEF KALLFVPKRA PFDLFETKKK KNNIKLYVRR VFIMDDCDEL IPEWLGFVKG
     VVDSEDLPLN ISRETLQQNK ILKVIKKNIV KKCLEMFAEV QENQEDYKKF YEQFSKNLKL
     GIHEDSTNRT KIADLLRFHT SKTGDDLISF KEYIQRMKEG QKDIFYITGE SRAAVSNSPF
     LEALKKRGYE VLYLVDPIDE YMVQQLKDYD GKKLKSCTKE GLDLEETEEE KKHQEEEKAR
     FETLCKLMKD VLGDKVEKVV VSTRIDESPC VLVTGEHGWT ANMERIMKAQ ALRDSSMTSY
     MISKKTMEIN PRNPIIQELR NKAEVDQSDK TVKDLVWLLF DTSLLTSGFS LDEANTFASR
     IHRMIKLGLS IFEDDKQEDD DLPPLQESDA PADNKMEEVD
//
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