ID A0A0G4FK69_VITBC Unreviewed; 723 AA.
AC A0A0G4FK69;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Vbra_9248 {ECO:0000313|EMBL:CEM13956.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM13956.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM13956.1, 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 -!- 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; CDMY01000450; CEM13956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4FK69; -.
DR STRING; 1169540.A0A0G4FK69; -.
DR VEuPathDB; CryptoDB:Vbra_9248; -.
DR InParanoid; A0A0G4FK69; -.
DR OMA; DHTQQNE; -.
DR OrthoDB; 5485387at2759; -.
DR PhylomeDB; A0A0G4FK69; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
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; 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.
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}.
FT REGION 506..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 80982 MW; 0977A651FFBFEFDA CRC64;
MEFRAETQKL LHIVTHSLYT DKEVFIRELI SNASDALEKL RFLQVSGQAP SVPEEEGALR
IVISADPAAK TFTIEDSGVG MTREDCIDNL GTIAKSGSRK FIEEANKAAS GGESERAQAL
IGQFGVGFYS SFIVSDKVEV FTRHFDADKG ASAWHWTSDG LGSFNIRECP LDEAPARGSR
IVCHLKPDCL EFANPQNCKT KAEHFSSFIS FPLYLKEGTD ETRLNPQEAL WLKSSVSEEE
HKEFLRFLGN TTYGEPLYTL RFNTDAPLSI KSLFYIPEDA PVRIFQKQTD REVSVALHSR
RVLVQKSASR VIPRWLGFIR GVIDCEDLPL NISRENMQDT RLMEKLSYAV VRRILKFFDE
ESQRDGKKFL QFYHKFSSYL KEGLLEDMGQ QETSTGGTGG AHKNQLVKLL RYECSQKPPK
EYISLEEYVK SMKAKQENIY YMCATNRQTA LASPYMEQFL QKDRNVLLMY DEIDEFVAMN
LQNYDGKKLV AVDSPEDDFE PLLEEEQEAE ADEETKAEDK KDVERPALSS EQQSQLEGYI
KGVLGNRVTA IKFSSRLTKS PAVVTGFLSS TMRKMMKSMM KGSEEGPSNL ANLPVTLELN
PGHELTTSLY HLQTSQPDIA QMLTEQLYDN ACIAAGILDE PKTMLDRLNN LLQVTASYAY
YSSSSPGVNQ PPPTDAPEDR AATSDPPPPS EETPSSSSGR AASSESFDTM QEEPTGKTAE
AKA
//