ID   A0A2Z3JGK0_9DEIO        Unreviewed;       878 AA.
AC   A0A2Z3JGK0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DKM44_14525 {ECO:0000313|EMBL:AWN24293.1};
OS   Deinococcus irradiatisoli.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2202254 {ECO:0000313|EMBL:AWN24293.1, ECO:0000313|Proteomes:UP000245368};
RN   [1] {ECO:0000313|EMBL:AWN24293.1, ECO:0000313|Proteomes:UP000245368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17bor-2 {ECO:0000313|EMBL:AWN24293.1,
RC   ECO:0000313|Proteomes:UP000245368};
RA   Srinivasan S.;
RT   "Complete Genome Sequence of Deinococcus sp. strain 17bor-2.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP029494; AWN24293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z3JGK0; -.
DR   KEGG; dez:DKM44_14525; -.
DR   OrthoDB; 53662at2; -.
DR   Proteomes; UP000245368; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 3.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AWN24293.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245368};
KW   Transferase {ECO:0000313|EMBL:AWN24293.1}.
FT   DOMAIN          11..84
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          87..139
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          664..877
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   878 AA;  97266 MW;  9CFE1C3319493A9C CRC64;
     MLTHQHVPFP DVQLLSQALA ASVNSVVLVD VRQPDQPIVY ANPAFERLSG YPASEILGHN
     CRFLQGPERD QPARFALQQA VEHGQSTTTI LRNYRRDGSL FYNELTISPI HDAAGTVTHF
     VGFQNDVTER QQAAELMIHS QTLVQALAAV RTQESVFDLI LRDGLEALGG IGGAVLLMHE
     GALRVAARHG PVEASVWQDG DLEGHRPSPD ALRTNTPLFF SHHGELTAAY PELEACTGGV
     APVASAVLPM VEDGRPLGTI VLDFREPHDF TPDEVHFLLT LAAQCALALD RAQLAENLEQ
     QVENRTAELE AFVRFTELAD GEMDMLALAQ RAVEVLGVLF PGCSNGYYVL EDGRWKVKIY
     TEDLEAEPAL LASLKAGLPL STPIFAQPVQ TGEPAFVDAW DAEKEQVAES ESYQAVALYP
     LGVDGTVRAM FALGLKDTPH WTDHHKAVFR SVGRSLVLAL ERTQAARRLE EQNAELHAQT
     LVLEGVAELT RDLTLPGGPH QLIGQVMDLV LSLLPSGYAS FWEVRDGLWR LITQRGDVGR
     PGWQAARERG FPVGHFPTLD RPWQTRQPYF QGHYDPVHDA VPDLMDHLLS IASLPVMVQG
     EMLGVFGVGL FGHRPWNVAD QALLITAVQS LGLALERAEQ ARQLTDQRDM LKASNEELEA
     FTYSVSHDLR TPVRHIISFG NLLRRTMTAP LDEKTERYFK VIEEAALHLN RLIDGMLELS
     RASRQPLRLE TVDLDRVVEA VRQEVMVGAQ HQVTWQVSLL PQVTGDATLI RQVVTALLEN
     AVKYSRTREE ALIEVWAEER GQTWALFVRD NGVGFDPRYK DKLFSMFQRL HRQEEFEGAG
     VSLANARRIV ARHGGLMTGE GQLNGGATFG FILPKSVP
//