ID A0A067GZ61_CITSI Unreviewed; 818 AA.
AC A0A067GZ61;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN ORFNames=CISIN_1g003458mg {ECO:0000313|EMBL:KDO84884.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO84884.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO84884.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK784874; KDO84884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067GZ61; -.
DR STRING; 2711.A0A067GZ61; -.
DR PaxDb; 2711-XP_006473673-1; -.
DR eggNOG; KOG0020; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; 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; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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:SF97; ENDOPLASMIN; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..818
FT /note="Histidine kinase/HSP90-like ATPase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001638288"
FT DOMAIN 100..257
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 293..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..795
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 93869 MW; F34A97131EF0EFB4 CRC64;
MRKWTIPSIL LLLFLVALIP DQGRNIQAKA EDESDKLVDP PKVEEKLGAV PNGLSTDSDV
AKREAESISK RSLRNNAEKF EFQAEVSRLM DIIINSLYSN KDIFLRELIS NASDALDKIR
FLSLTDKEVL GEGDNTKLEI QIKLDKEKKI LSIRDRGIGM TKEDLIKNLG TIAKSGTSAF
VEKMQTSGDL NLIGQFGVGF YSVYLVADYV EVISKHNDDK QYVWESKADG AFAISEDTWN
EPLGRGTEIR LHLRDEAGEY LEESKLKELV KKYSEFINFP IYIWASKEVD VDVPTDEDDS
SDEEEKAEKE EETEKSESES EDEDEDSEKK PKTKTVKETT FEWELLNDVK AIWLRNPKEV
TEEEYAKFYH SLVKDFSDEK PLAWSHFNAE GDVEFKAVLF VPPKAPHDLY ESYYNTNKAN
LKLYVRRVFI SDEFDELLPK YLNFLKGLVD SDTLPLNVSR EMLQQHSSLK TIKKKLIRKA
LDMIRKIAEE DPDESTGKDK KDVEKFSDDD DKKGQYTKFW NEFGKSIKLG IIEDAANRNR
LAKLLRFEST KSDGKLTSLD QYISRMKAGQ KDIFYITGAN KEQLEKSPFL ERLKKKNYEV
IFFTDPVDEY LMQYLMDYED KKFQNVSKEG LKLGKDTKDK ELKESFKELT KWWKGALASE
NVDDVKVSNR LDNTPCVVVT SKYGWSANME RIMQSQTLSD ASKQAYMRGK RVLEINPRHP
IIKELRERVV KDPEDAGVQQ TAQLIYQTAL MESGFSLNDP KDFASRIYST VKSSLNISPD
AAVEEEDDVE ETDADTEMKE SSAAKEDVDT EYSGKDEL
//