ID F0ZJX8_DICPU Unreviewed; 1225 AA.
AC F0ZJX8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN Name=DHKH {ECO:0000313|EMBL:EGC35772.1};
GN ORFNames=DICPUDRAFT_151857 {ECO:0000313|EMBL:EGC35772.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC35772.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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DR EMBL; GL871048; EGC35772.1; -; Genomic_DNA.
DR RefSeq; XP_003287724.1; XM_003287676.1.
DR AlphaFoldDB; F0ZJX8; -.
DR STRING; 5786.F0ZJX8; -.
DR EnsemblProtists; EGC35772; EGC35772; DICPUDRAFT_151857.
DR GeneID; 10500836; -.
DR KEGG; dpp:DICPUDRAFT_151857; -.
DR eggNOG; KOG0519; Eukaryota.
DR InParanoid; F0ZJX8; -.
DR OMA; QTMSHEM; -.
DR OrthoDB; 10685at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
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; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
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; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT DOMAIN 237..274
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 418..667
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1093..1213
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 292..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..235
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1057..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1146
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1225 AA; 139246 MW; 58DDAFDBC29B3309 CRC64;
MSESSPFTED SENSTKIFQD LLFQSFNNTN NNTTNDNNKS NILLKKYKFL NGGYNNYETD
LIIKVFNSVP IMMGVCDLYD NSNSNFQIQD SQNYDFKFVV SNKCSVDALY MFLGEDQGLD
GLFSVKELNL PTYFTTLWIE NMLRSLRKKK IVKFMYPRYI DNGEAPSSDD FYSQKIVWKK
SSMCYLGPGE DGSSKRFFFT SEEVTKEKFK KEELINDFKN RLETLEHKID QRVDERIETR
FKYVLESIPQ MVWVTDNHGK IEFVNRQWKD YLGIDHAGQY LNWGSISYQQ NKHLQQQQQK
SGSSTTPKIN SPNGQIDFDS QWHYSLKEMK RFEMEILLQS ISGEYRWFLV RAEPYIEPKP
SNTSSTPSIH SINFSDIDQG NTSLDIKWIG TCTDVNDQKT AQDRIENAEK SKAIFLQTMS
HEMRTPLAGI MGINSWLCTS SPQLSGEQLD GCHTIEMCAE ALLVLINNIL DLSKLEENKI
ILEETEFYPS KIVEDSVDIL SSQAEQKRLD IIFQLKYKSL PKVVGDFYRI RQVLTNLISN
SVKFTPPGGQ VTVGCEVYQE TGTTTRKRSS LDSIEITSHD QKIVVPGKYG KLLFWVIDNG
IGIPEEGREK LFQTFSQYDA STTRKYGGSG LGLAISKRLT QLLGGDIWFE SQKGKGSSFH
FLVEVFFPDY QTIQQSSLQP QFNITNQLTS NDSSTSGTNN ISSSTSASTA TTTASTNNNI
DIASLCSKII ILSTNKNLVD SLSQWIGDWS NSTNVDLLYD VESIEEISRI ALINNKRLDF
LFLIEDSYWI HYSDTISNVQ ETIESLVSQQ QVQMQIDQTK QTTEQHLQKH QYQHQQLIVP
IIASGTTTTT TTTTTTTTIS TPPTNNNTTN NNTNNINNNN NNQTTTTPPL HNIKNVFLSF
SVPYYNSSTL KKPIKYTPLK DCIFSNLLYF KSLYSNLLKK SFIVFFTKLA FTFIITDHSG
LTVSSTHTEV NAKKIKSNSD QLANFSPVLT PIPPCLNLNS SNINTANMQI EPIAETPNHN
HDNDINQQHS PQLHLLPQQQ HSPQNNSQPL IINNHIINQD GSNSNTNQKK RRNSVVSDTD
IPIEMTAVRY PLKIMVAEDS QVNQIVASRF LTKLGYKKEE IVFVVNGQQA IDYIDNIEMV
DVILMDMQMP ELDGCEATSR IRIKYPTTGP HIIGLTAFCF NEDKDKCLLS GMCHYLSKPV
KLDVLAVELK RAWLIRNNLR VCGCC
//
