ID B5Y5R0_PHATC Unreviewed; 750 AA.
AC B5Y5R0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Heat shock protein 90 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHATR_18793 {ECO:0000313|EMBL:ACI65978.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000313|EMBL:ACI65978.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:ACI65978.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:ACI65978.1,
RC ECO:0000313|Proteomes:UP000000759};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2] {ECO:0000313|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; CP001142; ACI65978.1; -; Genomic_DNA.
DR RefSeq; XP_002186508.1; XM_002186472.1.
DR AlphaFoldDB; B5Y5R0; -.
DR STRING; 556484.B5Y5R0; -.
DR PaxDb; 2850-Phatr18793; -.
DR EnsemblProtists; Phatr3_J18793.t1; Phatr3_J18793.p1; Phatr3_J18793.
DR GeneID; 7204126; -.
DR KEGG; pti:PHATR_18793; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_3_1_1; -.
DR InParanoid; B5Y5R0; -.
DR OMA; DHTQQNE; -.
DR OrthoDB; 5485387at2759; -.
DR Proteomes; UP000000759; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; 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:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 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:UP000000759}.
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 84459 MW; A0FB92600C43F305 CRC64;
MTTPLSSRLL AALRASRPAS RRSALRSTQI GACMLPRNSP HRGFRTSTQA MAEGISQSTE
RPAATSTADV KDKPPAPDVR VQASEPEKQP EMLEFQAETR QLLDIVTNSL YTDKEVFLRE
LVSNASDSLE KLRHLQATNA MIVDPDLALE IRIELDEVTS TISITDTGIG MTRDDMIQNL
GTIARSGSKQ FVKELERQAS GSIPDPARGI IGKFGVGFYS SFMVGEKVEV RSRSAQHDDE
PSRVWTSEGQ GAYSITDLPE DVRQQRGSSV VIHLKEKHWD FVDESRIEGI LKRYSNFVNF
PIYLNGNRVN TLEAIWTKEP KEVEEEAYSA FYKYIANAID EPLDVYHFRA DAPLDVKALF
FIPSFHSEKF GMERMEPGVS LYSRKVLIES KSKDILPEWL RFIKGIVDSE DLPLAISREK
PQDSALIAKL RKTLTRKFIA HLTKMAKKDR PKFLDEFYRE YSFFLKEGIC QEYEFQEHLA
KLLFFETSRS TDADMVSFDE YVGRMRPEQK EIYYLMAPSR EAAINSPYLE TFEKAGVEVL
FLFSTIDDFV MANLELYEGR KLVSVEKSDI DLKDLMDADA DKADEGEEIF TADKELSATE
QVEFCNWFKT ELGSKKISSC TVTARLSSSP AIVTDSESGA MRRMMRLVDT SEGSRDSVPL
PKQHVEINPK HPVIVGIHDL ITKEPTLARV LAEQVYDNCL VAAGLLDDSR SMLPRLNDIL
VCVVNGAKAK HGSGSKEIVE PEVVAKTDNE
//
