DHKH_DICDI
ID DHKH_DICDI Reviewed; 1378 AA.
AC Q54W36; Q95PH8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Hybrid signal transduction histidine kinase H;
DE EC=2.7.13.3;
GN Name=dhkH; ORFNames=DDB_G0279913;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-1378.
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).
CC -!- FUNCTION: Acts as a receptor histidine kinase for a signal transduction
CC pathway. This protein undergoes an ATP-dependent autophosphorylation at
CC a conserved histidine residue in the kinase core, and a phosphoryl
CC group is then transferred to a conserved aspartate residue in the
CC receiver domain (By 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 -!- PTM: Activation probably requires transfer of a phosphate group between
CC a histidine in the kinase core (transmitter) domain and an aspartate of
CC the receiver domain. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK54089.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AAFI02000035; EAL67428.1; -; Genomic_DNA.
DR EMBL; AF362370; AAK54089.2; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_641414.1; XM_636322.1.
DR AlphaFoldDB; Q54W36; -.
DR SMR; Q54W36; -.
DR STRING; 44689.DDB0219944; -.
DR PaxDb; Q54W36; -.
DR EnsemblProtists; EAL67428; EAL67428; DDB_G0279913.
DR GeneID; 8622297; -.
DR KEGG; ddi:DDB_G0279913; -.
DR dictyBase; DDB_G0279913; dhkH.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_255816_0_0_1; -.
DR InParanoid; Q54W36; -.
DR OMA; QTMSHEM; -.
DR PRO; PR:Q54W36; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
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; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transducer; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..1378
FT /note="Hybrid signal transduction histidine kinase H"
FT /id="PRO_0000328338"
FT DOMAIN 243..314
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 498..805
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1244..1364
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 294..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 212..242
FT /evidence="ECO:0000255"
FT COMPBIAS 663..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..716
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 501
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1297
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 685
FT /note="N -> T (in Ref. 2; AAK54089)"
FT /evidence="ECO:0000305"
FT CONFLICT 699..700
FT /note="Missing (in Ref. 2; AAK54089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1339
FT /note="L -> F (in Ref. 2; AAK54089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1367
FT /note="R -> G (in Ref. 2; AAK54089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1378 AA; 156521 MW; EECF8D05DA08DC79 CRC64;
MNIGDDKSEV DVIIDSSSIT LNNNESSNNN TNIGDVLKFE SGLYNSFECE LINQVFNSVP
IMMGVCDLYD NSNSDFQIQD SQNYDFKFVI SNRCSYDNLH MFLDKGKGLD GHYSAKELHL
PAYFITLWIE NMLRSLRKKK SVKFMYPRYV DNGETPSSDD FYSQKIVWKK STMCFMGQVL
VPLDDINSNS NNNSNQKQTA CRFFFTSEEV TKEKFKKEEL INDFKSRLET LENKIDQRVD
ERIETRFKYV LESIPQMVWV TDNHGKIEFV NRQWKDYLGI DHSGQYLNWG SISYQQHNNN
NNNNNNNNNN NNNNNNNNSN NKSPIINSPN TTSPTNTQID FDSQWHYSLK EMKRFEMEIL
LQSMSGEYRW FLVRAEPYIE PNLGHPSSPL PSIISACVDN CDIMTDDNSS GILINNNNNI
QQPYLNNDNI SGDNVNNTPT CIDNNNNNID GSNNSVNSTG TEQLDIKWIG TCTDVNDQKT
AQDRIENAEK SKALFLQTMS HEMRTPLAGI MGINSWLSTS SPQLTSEQLD GCHTIDMCAE
ALLVLINNIL DLSKLEENKI ILEETEFYPT KIVEDSVDIL SSQAEQKKLD IIFQLKYNCL
SKVVGDFYRI RQVLTNLISN SVKFTPANGQ IIVGCEIYHE TTPSTRKRSS LDSIEITIPC
NHNNSNNSNN NHNHNNNNNN NNHLNCSGSF NNNGFNHGHH HHHHHHHHHH HHHDKHCDQK
IIVPGKYGKL LFWVIDNGIG IPEEGREKLF QTFSQYDAST TRKYGGSGLG LAISKRLTQL
LGGDIWFESQ KGKGSSFHFL VEVFFPDYPT IYNQQLQQQQ QQPNLPHQFN IGTSAPQPID
SILTSYSSNN SNNNINNNNI TTSVISQSPI VDKSNLCTYI FLLSTNQVLV NSLSQWINEW
IGNATNNNNS NNDNNNNNTT STTTTTTTTT ATINTNINQQ VKILYDIDSI EQISNSAIQS
GKRLDFLFLI EDTFWNNYSD KISNSQEIIE SLINQNYQQQ QQQQQEQRQQ HNIKNVILSF
SNSAQIYGNS IILKKPIKYS PLKDCIYTNL LYFKSIYSVN SFDVIIATQM SSSVSPSSLS
SSPSIQGLTN SSLSINNINI SGNNSNNNIN NNNNNSGSST PKKLKKSNSD QSIHFSPSLT
SSSLPSLDLN NNNNINNNNN INNNNNINNN NNNNNNNNNN NNNNNNNLNH YNSDSILSSD
LSPQQHQYHH PNPLLANYQK KRRNSVVNDT DIPLEMTGIR YPLKIMVAED SLVNQKVACR
FLTKLGYKKE EIIFVVNGQQ AIDHIENVEM VDVILMDMQM PEVDGCEATT RIRMRYPTTG
PHIIGLTANA FNEDKDKCLL SGMCHYLAKP VKMDILAVEL KRAWLIRNKF RVCLCAVL
