DHKE_DICDI
ID DHKE_DICDI Reviewed; 1699 AA.
AC Q55E44; Q95PH3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Hybrid signal transduction histidine kinase E;
DE EC=2.7.13.3;
GN Name=dhkE; ORFNames=DDB_G0269204;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX4;
RA Anjard C., Loomis W.F.;
RT "The histidine kinases of Dictyostelium.";
RL (In) Inouye M., Dutta R. (eds.);
RL Histidine kinases in signal transduction, pp.1-1, Academic press, San Diego
RL (2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: May act in a signal transduction pathway. This protein
CC undergoes an ATP-dependent autophosphorylation at a conserved histidine
CC residue in the kinase core, and a phosphoryl group is then transferred
CC to a conserved aspartate residue in the receiver domain (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AF362375; AAK54094.2; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71952.1; -; Genomic_DNA.
DR RefSeq; XP_645937.1; XM_640845.1.
DR AlphaFoldDB; Q55E44; -.
DR SMR; Q55E44; -.
DR STRING; 44689.DDB0191265; -.
DR PaxDb; Q55E44; -.
DR EnsemblProtists; EAL71952; EAL71952; DDB_G0269204.
DR GeneID; 8616881; -.
DR KEGG; ddi:DDB_G0269204; -.
DR dictyBase; DDB_G0269204; dhkE.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_240946_0_0_1; -.
DR InParanoid; Q55E44; -.
DR OMA; IYRRCCI; -.
DR PRO; PR:Q55E44; -.
DR Proteomes; UP000002195; Chromosome 1.
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 GO; GO:0099139; P:cheating during chimeric sorocarp development; IMP:dictyBase.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 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 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; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transducer; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..1699
FT /note="Hybrid signal transduction histidine kinase E"
FT /id="PRO_0000328271"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 678..950
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1575..1695
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 681
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1625
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 665
FT /note="A -> T (in Ref. 1; AAK54094)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="T -> P (in Ref. 1; AAK54094)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="S -> T (in Ref. 1; AAK54094)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="Q -> P (in Ref. 1; AAK54094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1699 AA; 191750 MW; ED9704160973EAE2 CRC64;
MDKLKINNNL SPPSSPSSST TTPNLSSTNL ENNLNSNINN NINNFNLNNS TNTFNNSNNI
IINNNNNNNN NNNNNNNNNN NNSNNNNNNI NNNNPNVNSP NEVILNNNFL KQNKKGFFKR
NKKMIEIFLP PKFKSPIYRR CCILLGECGV YVFIYMFFLI FLRSFYPIFI CGIVSMIVLY
IVSTKTTKYK LVALIYIFVQ SILNFTFFLQ ITNNFNNNTV NINNTDDYSN EVIEFSKLNF
LFIMNLILSL ISIQIFFPKF TFSITLTCSL NIFNIIIHLI SIYSLNTKKL IVFQNLIVPI
TVSFLLSFYS YILSIDNQEI EAKEKRFRNI FDTSSEALVI HKNGLIIDVN STFEKIFQIK
QSDLINGTIW EYLPELESFF QNTNGNSKYT NQSLQQQLQQ QQQQQQQLYN TITNGGNNKQ
TSTTSANSTP RYNNYNNNNI NSNNLNNLNV FNNLNNLNNL NNNNNNHHIH KVSRSNTGLS
DSSSIFDDSD SVDFFSMKNI NKCPIVLDTV GITPCGSEFC AQVKIERKKD MLIGSGTSSF
NLLNNNNNNN NNNNNNNNNN NNNNNNNNNS NNNNNNNSNN NNNNNNINNN ISNNIINNNN
NNNNSGIITN LSQQSNNLST TNLNTSSKII NHKHKNSKQD FDVMSIVDIS AKKKLMIADQ
ALRRAEELNQ AKINFLTTVS HEVRTPINGI LASVEILDGS QLDVTQRDFL SCIKQSADYL
LDLITDILDF SKIEAGKFEL DRVEFNLITM LEESINIVYR TAQERGIEVL TFIDPDVPII
LIGDPYRVKQ CVLNFLSNAI KFTHKGQVMV KVSIVDQINN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNKI VGFSNNNNNN NNNNNNGNNG ILNFKLSFSV EDSGVGIKEE VLDCLFTPFH
QLGGSPRKYL GTGLGLSISK KLTTLMGGEI GVKSVYGVGS AFSFTSILST TSTTPISLQS
LGSSLSIALN NLSPTIPKIS GFIYDDNIHT SNSLFNFLKL MNINLKIINP IINNNNNNNN
NNNNNNNNNN NNNNNNNNNN NDNNNNNNNN NDNNIDQQQL KFEFENEIDK YCNVEDDNNN
VILIITNQLS NDNLNYFKDK INQLNNSIYW FVLCDNGLKA IDPFYYGIVK KPNNLLNLVD
TVFKVYNCQL PQDLYQLLTN GSKDDYKNYL KYRNVVIKKI TEDNEKKQQQ QQQQQQQMGD
TLSSTKSPQY TNLPPLDISS SSNGSLNKSN RSNLLRKSSS VYSDHVAITR GMVQVNRSPR
PSTPPPLFNL KGNNSNPNST ELNSTNSVNG NPNNDSTLET IEPLNISETV GDLCSSGSVI
NNSNFIINNN FLTSSPYGSC LTPNSGTTSP SIPININNND NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNSFKKLEPD NFSPPPSILI NDNNIIPALN VTTPITISTS TSSSSSLLIN
NEINNKSTTS KRPSFIPPLD IQSKKLIINT ADENHKNNCI IDFEQIFGQD GKQQPQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQKLNIGN QQQQQILSSP RLQSQLLSNC
DSLGNTPPVT PHRRNALIVD DTELNRKVLA QLLRRMDWSV SFAENGIEAL KEITSERCFD
IIFMDCQMPI LDGFETTKLL RLRELENNWK PLNIVALSAD SSSSFGQVCF DCGMNGYLGK
PITLITLKDT LLKWGGYRD
