ID   A0A0G4FB63_VITBC        Unreviewed;       793 AA.
AC   A0A0G4FB63;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEM09884.1};
GN   ORFNames=Vbra_14835 {ECO:0000313|EMBL:CEM09884.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM09884.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM09884.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CDMY01000396; CEM09884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4FB63; -.
DR   STRING; 1169540.A0A0G4FB63; -.
DR   VEuPathDB; CryptoDB:Vbra_14835; -.
DR   InParanoid; A0A0G4FB63; -.
DR   OMA; EINPNHY; -.
DR   OrthoDB; 1067at2759; -.
DR   PhylomeDB; A0A0G4FB63; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
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; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11528:SF41; HEAT SHOCK PROTEIN 90-6, MITOCHONDRIAL; 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:UP000041254};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..793
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005189029"
FT   REGION          747..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..793
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  89178 MW;  B579992820D4EA65 CRC64;
     MAPVSWMLVI SALALTTEGI NGFSVRREPA FVMHSGRVTS TNGRSSSAVH QPRQHIRPST
     TRLRMSTAVA EAPQAEAPET EETETYAFQA EVSRVMDIIV NSLYTDKDVF LRELVSNAAD
     ACDKRKLLMM KEGVYNGEGG VKIKADKEQK VLVVEDAGIG MNKTELVNNL GTIAQSGTAK
     FLQQVAEGSV ESSLIGQFGV GFYSSFLVAD KVEVVSKRFG DKQHRWCSVP GGTFTVGPDN
     SEEIEGSGTR IILHLKEDCD EYLEDYKIKE LLRKYSEFIQ FPISVWSEKV DYERVPDPDA
     PSKPGETPKM KTVTKRYFEW ERVNTQPPIW RRNPADLVDD DYNEFYKSTF KAYDDPLGYI
     HFKVEGQVEF SSVLFIPGSI PWELTRNMFD DDSRGIRLYV KRVFINDKFQ EAIPRWLTFI
     RGVVDSEDLP LNVGREILQK SKMLTIINKR ITNKAIDMIR KIRDKGGDQW NKFWENFGKY
     LKVGVVEDRD NQEIIASLLQ FWSSSSGTER IDLDGYIERM KPNQTAIYYI AAESRKAAEE
     SPALEKLRKL KYEVLYLTEP LDEFCMQSLG INKFRGKEVI DVTKEDLKLA EPEAETPDQI
     EKRKTKRIEM EGMCTWLQDF FGSKKVQRAV VSDRLTESPA VLVQGEFGMS PTMQRYIRQQ
     AAAQGLSENE MYGMSMNQAV LEINPDHPII EQLNDMVKKD KNAKANKEVA TLIYDVACLQ
     GGYNVEDPGS FAKRITSMMA REASAYMTTA SSPPAPAAAP EPSASASAQP PSPASPPSLP
     EQSQPISPDA PPS
//