DHKI_DICDI
ID DHKI_DICDI Reviewed; 1736 AA.
AC Q86AT9; Q557P4; Q95PH7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Hybrid signal transduction histidine kinase I;
DE EC=2.7.13.3;
GN Name=dhkI-1; ORFNames=DDB_G0273475;
GN and
GN Name=dhkI-2; ORFNames=DDB_G0295835;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
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: 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 -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AF362371; AAK54090.1; -; Genomic_DNA.
DR EMBL; AAFI02000010; EAL70692.1; -; Genomic_DNA.
DR RefSeq; XP_644590.1; XM_639498.1.
DR AlphaFoldDB; Q86AT9; -.
DR STRING; 44689.DDB0231984; -.
DR PaxDb; Q86AT9; -.
DR EnsemblProtists; EAL70692; EAL70692; DDB_G0273475.
DR GeneID; 8618954; -.
DR KEGG; ddi:DDB_G0273475; -.
DR dictyBase; DDB_G0273475; dhkI-1.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_239956_0_0_1; -.
DR InParanoid; Q86AT9; -.
DR OMA; FWISSTE; -.
DR PRO; PR:Q86AT9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0030587; P: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; IPR000700; PAS-assoc_C.
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; 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; 2.
DR SUPFAM; SSF55874; SSF55874; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transducer; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..1736
FT /note="Hybrid signal transduction histidine kinase I"
FT /id="PRO_0000328339"
FT DOMAIN 234..286
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 287..358
FT /note="PAS"
FT DOMAIN 556..908
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1551..1674
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 143..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1695..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..787
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 559
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1605
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 1559
FT /note="T -> P (in Ref. 1; AAK54090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1736 AA; 191865 MW; 8DEDD5BB99744798 CRC64;
MIYLKILEKL NQAIWLFDIN KRVLIWGNQS CKKYKNIESI TSLFNNSNLI NDIRNGKSKH
EHIDIIESNE NGEILKQMIF KYSSIHISDM DARQLYLDTS INLLVNQDSH YLDYEGKRIF
ILVEAIEEIK FIQSPLSSSI ENHNINNNQN NQNSVNINSS NKGQYNRPEP SNMGSWEWNV
QNDTTKASNQ FYKIIGIEND FNKKLNFNDF INKLGIQEIQ PIINNCIESN SSSFEYPLRI
NRKNDNLVRY IQLKGEIIKK DDKVFKVLGV CHDFSEIQEA KDKLEEESKF VEALIGCLKA
GIVACNSNGD LTHFNKSAQD LHGLELNDKT DRKQLLDQIL KCYRSPYEQI NLEKSGTPII
RALSGEFIND QEIIITPTSN QQQSSLSKSN RPRSQSNCSN GNKSQNRLSK NYSTTTTTTN
NNNNNNNNNN NNNNNNNNNN SISQQQQTQV STQQTQQQQN TTNGIGGATT STTAAAATIT
SPQQIPIATK IPTKINDNEF LVLASGQEIV SKDGKTIGAF VALHDITERK RNEVILKNAT
EEAQRANQLK GEFLANISHE LLSPMNSIIG MVGLCLDVAP RNLKEMLNDV VESSKILLDL
LHQILDFTTL ESNSLAVRPF PFKLRDTFNQ LFKVFYTRII EKKISLTFSI DPNIADDFYG
DQNRLKQILS NLIDNAIKFS NSSNINNSIS IIVEQLTHNQ FKKYKDSFRS NSKTHSRLNS
HDDYSIDGDY DDQDNNDSYF GRDINVSDNE SAVGGFSELD EKDNSDDDDE NDDENDETDE
NDDDTDDDTS SNTSRNNISN NLLFHNNTSG GGGGGINKRE KFKKKDREGF VNLKFSIKDR
GIGVPEDKHD FIFDRFFQVD GSYSRVQGGV GLGLSICKKL IEFFGGAIWF ESEASQGSTF
HFILSIKSVE APSPKSPSLQ SSNGSINSTT KLFESSRLKN EIYIPSLPNV QTKKVKKDSN
DNGNNDSTNY GISLSNSMNN ININGSTLNN NNSINNNNNS NDNGPLTSRT PSNSYYNFIA
SLNNTSLKSS SHNTLSSSPT GFNGISNLNI SGLNNLSNLS NNPNNLNNII GNTNGNNNTN
GNNNSGISLN NSNNNIQTPN GLNNSRGSSL ISTPSTKNVK KQHSCPMDLI QRIHSICTPR
GPISKECGLN NLPAYSPPKS PGRSLSHGGK NYSNLISTPR GGVGYSSPPI NSSSSSGGGS
STNGSNSGNS SANNSTPSSS SLSSTPLTSS NTPSPVSISS NNVNNNNQQQ QTQPILSPIL
PLKDNSIDIS DLNNINSLTP NSSNSTSTNV TQSSSNIINN GNSITIINNN PVTPNGKKIV
IVPLLSLQSA SSPKQSQRGY SPKQQYSPKQ YSPKQQYSPK QYSPKQQQQQ QQQQQQLEQL
SGRMSPHKSN LSSTNLHHIH HHHIHQQQSQ QHNNTTVHSN NLILNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNTTNTSN NHTSDPSKSS NSTPETSPPI SSPRSNNNNN CSLTTIVGVT
TPPQPSSTIT TPQFQSPPIL SGNSGNINLL SSNGTSSGGI EISGSQMIPQ KVLVAEDNTM
NQKLIKTLLT KRGFDITIAK DGKQALDFYH ESKNKSILYD CILMDIQMPI LSGLEATCAI
REIEANEGGH IPIIAVTAHA MKGDKEKFLE SGVDDYVTKP INPKLLYEVI NTQICKYIEE
NRSSSTINEN KNTINNNNNN TNNNNNNNNS SNPVNNNNSN SIDATQQELN NEKIRI
