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Database: UniProt
Entry: A0A067GZ61_CITSI
LinkDB: A0A067GZ61_CITSI
Original site: A0A067GZ61_CITSI 
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}.
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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
//
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