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Database: UniProt
Entry: C1DYQ7_MICCC
LinkDB: C1DYQ7_MICCC
Original site: C1DYQ7_MICCC 
ID   C1DYQ7_MICCC            Unreviewed;       700 AA.
AC   C1DYQ7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN   ORFNames=MICPUN_106749 {ECO:0000313|EMBL:ACO60985.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO60985.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO60985.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CP001323; ACO60985.1; -; Genomic_DNA.
DR   RefSeq; XP_002499727.1; XM_002499681.1.
DR   AlphaFoldDB; C1DYQ7; -.
DR   STRING; 296587.C1DYQ7; -.
DR   GeneID; 8241403; -.
DR   KEGG; mis:MICPUN_106749; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   InParanoid; C1DYQ7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000002009; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; 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; 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:SF34; HEAT SHOCK PROTEIN 83; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   DOMAIN          28..182
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          214..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  80294 MW;  4D5F2D3C8B09238D CRC64;
     MAEETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNS SDALDKIRFE GLTDKSRLEA
     QPELFIHIVP DKTNNTLTII DSGIGMTKAD LVNNLGTIAR SGTKAFMEAL TAGADISMIG
     QFGVGFYSAY LVAEKVIVYT KHNDDEQYRW ESQAGGSFTV TKDNSEPMGR GTKMVLHLKD
     DQLEYLEERR LKDLVKKHSE FISYPISLWT EKTTEKEVSD DEAEEDDAAE EEGKITEIKD
     EDEKKEKKKK TVKEVSHEWA LMNKQKPIWM RAPEEISKDE YSAFYKSLTN DWEEQLAVKH
     FAVEGQLEFK SVLFVPKRAP FDMFDGKKKA NNIKLYVRRV FIMDNCEDII PEFLSFVKGI
     VDSEDLPLNI SREMLQQNKI LKVIKKNIVK KCLEMFNEIA ENKDDYTKFY EAFGKNLKLG
     IHEDAQNRSK LAELLRYHST KSGEEMTSLK DYVTRMKENQ KDIYYITGES RKAVENSPFI
     EKLKKRGLEV LFMVDPIDEY AVQQLKEYDG KKLVCCTKEG LQLDETEEEK AKKEEVKAQY
     EALCRLMKDI LGDKVEKVLV SDRVVDSPCV LVTGEYGWSA NMERIMKAQA LRDNSMSGYM
     ASKKTLEINP DNAIMQELRK RADADKSDKT VKDLVLLLFE TALLTSGFSL EEPNTFGGRI
     HRMIKLGLSI DDDIGLDDDD HDLPPLEEDV DEGSRMEEVD
//
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