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Database: UniProt
Entry: C1D0Y9_DEIDV
LinkDB: C1D0Y9_DEIDV
Original site: C1D0Y9_DEIDV 
ID   C1D0Y9_DEIDV            Unreviewed;       774 AA.
AC   C1D0Y9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   SubName: Full=Putative histidine kinase, classic {ECO:0000313|EMBL:ACO45513.1};
GN   OrderedLocusNames=Deide_06600 {ECO:0000313|EMBL:ACO45513.1};
OS   Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO45513.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO45513.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCD115 / DSM 17065 / LMG 22923
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P.,
RA   Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P.,
RA   Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S.,
RA   Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of
RT   Sahara bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC         Evidence={ECO:0000256|SAAS:SAAS01126420};
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DR   EMBL; CP001114; ACO45513.1; -; Genomic_DNA.
DR   STRING; 546414.Deide_06600; -.
DR   PaxDb; C1D0Y9; -.
DR   EnsemblBacteria; ACO45513; ACO45513; Deide_06600.
DR   KEGG; ddr:Deide_06600; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   OMA; MEEIEGC; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 2.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002208};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:ACO45513.1};
KW   Membrane {ECO:0000256|SAAS:SAAS00925724, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00926038,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00926160,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     15     33       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    189    207       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      213    265       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      270    322       PAS. {ECO:0000259|PROSITE:PS50112}.
FT   DOMAIN      349    401       PAC. {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      402    449       PAS. {ECO:0000259|PROSITE:PS50112}.
FT   DOMAIN      467    518       PAC. {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      536    750       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
SQ   SEQUENCE   774 AA;  84847 MW;  77CB5BB40D7794AE CRC64;
     MQKPPLQPYI LTYQLGSWLF LLAVAIAVAL GMHRLEQNTR ANMQAQSELV ALQSVSAALV
     DQQAGVRGYV LTGEDRYLEV YQRGLAALPQ HFGTLRTLAG SEAPAVRQAR LDVLRDLERL
     HKQWLDTAAT PGVAETRLGN SSPAVQIVRA GEGTGLMDEM RALLDEQRNT VGARQATLNQ
     TTLATLQQVR WLTLGGLMLA LLVSILVTTR ATRTVAKGLR SVSDAARRIT DGQLDERVPL
     GPVQEGALLG VAFNELTDQL RRQESQQERS STRNRLILEA VGDGVISTDM HGRGTFANPA
     ALSMTGYALP DIIGQDIHER LHHAREDGKA YPALECPACR AVEDGKAPAL AAATFWRQDG
     SSFPVEYVVI PIRGEDGVVE GSIISFRDVT ERRAAHRTLL LREALLQAVT ANLPVVLFAL
     DRSGEFTLVE GQQLTDLGFG SEKLVGQNLH ARPNNLEMTD HFEAALRGEE PQFTVDVDGK
     TLDVWLTPLA NKDNGVSYVI GAAVDVTERL RTELELREAN RNLLESNTEF EQIAHVISHD
     LQAPLQAVIS STEQLKGQLD GQLDAQSKTY VGHIADGAHR MKRMIDDLLM YARVDRGERE
     LQDVPLENVL QGVQHTLVDT LTASEAVLTH DPLPAVRGDL TELTALLQHL IENAVKYRAP
     DRTPTIHVGA TLEGTGWHFT VSDNGLGIDT QDFARIFKVF QRLHHQDTVE GTGVGLAMCR
     KIVERAGGRM WVESVRGSGS SFHFTLPKGS TDLGPEDKVR ALIEQAVKGL YKDK
//
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