DHKL_DICDI
ID DHKL_DICDI Reviewed; 1709 AA.
AC Q54RP6; Q95PH5; Q9GTU0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Hybrid signal transduction histidine kinase L;
DE EC=2.7.13.3;
GN Name=dhkL; ORFNames=DDB_G0282927;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1562-1709.
RC STRAIN=AX2;
RX PubMed=11060029; DOI=10.1093/emboj/19.21.5782;
RA Ott A., Oehme F., Keller H., Schuster S.C.;
RT "Osmotic stress response in Dictyostelium is mediated by cAMP.";
RL EMBO J. 19:5782-5792(2000).
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 -!- DOMAIN: Atypical domain architecture: contains 2 receiver domains.
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}.
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DR EMBL; AF362373; AAK54092.2; -; Genomic_DNA.
DR EMBL; AAFI02000049; EAL65907.1; -; Genomic_DNA.
DR EMBL; AF258796; AAG00916.1; -; Genomic_DNA.
DR RefSeq; XP_639305.1; XM_634213.1.
DR AlphaFoldDB; Q54RP6; -.
DR SMR; Q54RP6; -.
DR STRING; 44689.DDB0191389; -.
DR PaxDb; Q54RP6; -.
DR EnsemblProtists; EAL65907; EAL65907; DDB_G0282927.
DR GeneID; 8623876; -.
DR KEGG; ddi:DDB_G0282927; -.
DR dictyBase; DDB_G0282927; dhkL.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_240641_0_0_1; -.
DR InParanoid; Q54RP6; -.
DR OMA; SWTIGES; -.
DR PRO; PR:Q54RP6; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IEP:dictyBase.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; PF13426; PAS_9; 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; 2.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 3.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..1709
FT /note="Hybrid signal transduction histidine kinase L"
FT /id="PRO_0000328369"
FT DOMAIN 700..771
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 770..822
FT /note="PAC"
FT DOMAIN 837..1059
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1312..1492
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1570..1692
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 52..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1219
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 840
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1366
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 1622
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 2
FT /note="E -> Q (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 6..7
FT /note="RD -> TH (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="N -> Y (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="L -> W (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="C -> G (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="L -> V (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="N -> T (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="A -> G (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
FT CONFLICT 701..702
FT /note="TR -> PG (in Ref. 1; AAK54092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1709 AA; 192704 MW; D64A78BBE43ABA12 CRC64;
MEGSKRDIIE NSNNGNNKGV VIEELGETYY TNSKPSTSAD CKYFRDSFEF GSNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNEE KSNNETEKTL ESNGDTTTTT TTNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNTNSS NDIYMNSPSS TLSSPGNAGN NLPIGCTKPN
VPKSPYSPSP PHLYKSNSTS YLKSSFFSGN GSSSSSSSTT TTNINSNNSN TNTYSTSTNV
KKNNSNTNSN TNNNTNGNTN TNSNSNKKNI NSNSSDNIII NDTADIMNRR RDRFKSFSWT
IGESNSNSKF SELSMISSKC KSIKSEFTPL FETLTVFDES DKIRHSLIQN HYKTLLIQNP
ASPNRTLLTN LLQRRGHNLT TCPIDINHVL QLLQKESFSL FIFDPNESII NNTSNSISSN
EPISLSSSSS YYNNNNSNNN SVNNNNNNNS GNSTNNNSPS SHTPNSPMIF QPIVSNICSN
SGGSGNNSPH HIDNNNNSNQ QQQQQQQQQQ QQQQHQHQQQ QQQSSSTTAT TNNSCTLNQQ
QQQQQQQQQQ QQQQQQQQQQ SQPTTPTQST QSPTTSISFS KKKNLTINTS FKTSPMSSPK
SFNKPSQSPQ NIFNNFSNTY NPNNIEFCKI LKSKLTEFET VIVLTESTDP SEFCQYIDAG
ATDYIPQPIS PILLDLRLTT CQKLVNNNLH LKKAESLKDA TRKMVTCIEN SPDCVEIWDP
SGHIQYLNLA FSEMTGFARW ELLGKEFSNL IDNTEIIPNM WATLTDKKTW NGFIRTRHNN
NTLIYFEASI SPVLDQFQQI LYYNCTKRDV TQKRIDEESK TLEQNKIIEK SRLRLSMMSH
DIRTPMSNII GMADLLLDTS LSQHQHHYLE IIKNSSNTLL TIINDILDIS KIEAGKLDID
YESFDFNATV SQVVESMAQR VQSKGLELLS YVDPKIPNIL IGPSSRLNQI LTNLLGNSLK
FTDKGEISIC CLLNDETDSE YEIKVDVRDT GIGIKKEALP LLFKAFTQAE GTITRQYGGS
GLGLAICKEL VHLAFNGEIS VESQYGHGST FTCILKFKKF LPSDSQNLLP ASSPLQQQQQ
QQQHQQQTQF HQHQQQTQFH QHQQQQLQHQ QHQQHQQLQQ QQQQQQQLQQ QLQQHQQHQL
QQRQHHQQQL QQQQHHHHQQ VHLQQQQQHE HDAQHNQHIQ QQQQQQQQQQ QQQQQHEHNN
NGHHNSHGHN HHGSHHNHNH QHNNNNNNIT INKLQHQEKK QKSNEQQLES ITENSFSPIV
EPMVISDPDT PEALNISQSP SPQSIHNGTT INQQPTSPLN TLGSKFDFSG AKMLFIERND
TSRGNLFKQL LAWNIQLELV EDGESGFRKW KQSIESNSPY SIIIMDLNTP GVDGASLPMR
IKKELELMQQ HLQQQQEQEQ QQQQEQQQSE LQKQPDVENK NSSQNNDNNN NNNKSNSSGG
NQCIYRSPII MLMPIQFLNS QLEDNLKDAG VCAILSKPIR MSQLADVFMM YLGPNSEHNN
NNNYNNNNGN GYLNGGGGGG GSVNGTGNGT LQVGMSNDGG NGCGVVSFWN KQRRASAEEQ
EQDPSKLLGK VLVVDDNHIN IQILSKMLQT VGCEVDSVLS GADALAKINQ SSGDSYDAIF
LDIQMPDMDG FQVSRKIRER EKKFSLPRVA IIATTANVFK EDQLKCFDAG MDDFISKPIK
RAEIKEIIKK YGKNGNHQSG SAYSLYKLS
