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
//