DHKG_DICDI
ID DHKG_DICDI Reviewed; 3432 AA.
AC Q54Q69; Q95PH9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Hybrid signal transduction histidine kinase G;
DE Includes:
DE RecName: Full=Histidine kinase dhkG;
DE EC=2.7.13.3;
DE Includes:
DE RecName: Full=Probable serine/threonine-protein kinase dhkG;
DE EC=2.7.11.1;
GN Name=dhkG; ORFNames=DDB_G0284045;
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: 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: Atypical domain architecture: contains STYKc/AAA module and
CC histidine kinase/receiver module.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF362369; AAK54088.2; -; Genomic_DNA.
DR EMBL; AAFI02000063; EAL65363.1; -; Genomic_DNA.
DR RefSeq; XP_638728.1; XM_633636.1.
DR STRING; 44689.DDB0191388; -.
DR PaxDb; Q54Q69; -.
DR EnsemblProtists; EAL65363; EAL65363; DDB_G0284045.
DR GeneID; 8624398; -.
DR KEGG; ddi:DDB_G0284045; -.
DR dictyBase; DDB_G0284045; dhkG.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_224929_0_0_1; -.
DR InParanoid; Q54Q69; -.
DR OMA; CAISPNA; -.
DR PhylomeDB; Q54Q69; -.
DR PRO; PR:Q54Q69; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; IEA:UniProt.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Multifunctional enzyme; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW TPR repeat; Transducer; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Tyrosine-protein kinase.
FT CHAIN 1..3432
FT /note="Hybrid signal transduction histidine kinase G"
FT /id="PRO_0000328337"
FT TRANSMEM 1567..1587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1599..1619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 263..792
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 1965..1998
FT /note="TPR"
FT DOMAIN 2215..2465
FT /note="GAF"
FT DOMAIN 2491..2769
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 3305..3424
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 44..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..1121
FT /note="AAA"
FT REGION 1040..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2071..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2299..2349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2637..2673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2785..2815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2917..3030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3134..3160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3247..3281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2650..2670
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 585
FT /note="Proton acceptor; for protein kinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 269..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 871..878
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2494
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 3356
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 1335
FT /note="Y -> N (in Ref. 1; AAK54088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3432 AA; 383457 MW; DA45965835CEB03A CRC64;
MNYSWIHEYY LGTCIQEEKV FSIYSASTSN NSFSFPSIPT TTTHFSNSVL NQTTTTTTTT
TTTTTTTNTP PPPPQSQLQA QLQSQSQQNN QHHRPLSPNG GFFSITNSSS ISDQDLRSRL
KLYDDQPQQQ QQQQASNKSK LSQKQTSQLN ISGNNSGNST PPLPTISNSN NSINFIHSPP
PTPPLLKTPI LSSHNHNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNHNIN
TIDIDLVSPP PPLLLPSGSL SPLSFKHGYN SGLGGNFCSN SIANGIHLGK KPSEFQSHNN
NVLLKILNYK YPPIEISTIF QREYFILSYL NDLDGTLKLI KTQSEYGNIV ALIFEENGYK
SLTSYYNVLS LLNGVGGCAS FTNYNLNYNI NNSLNNLNNN NNNNNNSYNN NYNNNNNNNG
QVTSPILNNT ELSQSSASAF KPFQLNSSTN STGSPLIITS QPMPFQLNSN SNTTASSSSP
ITHSNLNTAI TSTTTSNSNS NNNSNNNNSG GGGGGGGGGG GGGGTKINNK RRASLTPTST
PLSASPLLFN TKKYADIDIN TFLSIAIQLT TILESIHGKG CIHRDIRPNN IYINSECKVK
LANFQFSIFK KTSSFLKKSK FQQQHQQSEN NNNNTLDSDI TMIDNIDLTN SYNNNNNSST
NNIFFNFNND YDEESINELF KSYPDLSRFS TSTYYYISPE DTGRTIHPVD EKSDLYSLGV
TFFELLTGRL PFQSSDLSEL IHSHLAKKPP LVIDLNQNVP LILSNIVNKL LQKSPDDRYQ
SAYGLKKDLE MFKLQLSIIN NNNNNNNNNN NNNNNNLSNQ QITDFKLGAY DVLNRPYISN
ELYSRKKELN SILTTIKRVS KGGKEFIIVS GLSGVGKTSL INQACKKSNT KVRFICGKFD
QFNKSPYSAI IEALSQLVNL ILSLSPLELE FYKDRLLRTL GSNISVITEV IPKLCLIVGT
HYKVLPLPSS ESQNRFDLAF KDFLRVFAEE GNPLVLFLDD FQRADPSSYR LIKLLMESNN
STSNNSTFLN CNGNNNNNNN NFSINNNNNN NNGCNNNNNN NNNNINNNNN NNNNNNINNS
GGSLNYLLVI GAFRENEPNF ELDFGDLSNF ITMKIVLKNL DLKYVNLMVS TTLHASPQET
LSLSQVVLSK THGNAFFVIL FLRTLFDESL VYFSTTTDKW CWNIEKIQKR EFTDNVVEFM
VENLKQLDKQ AQRVLHLASC IGNSFDLDML AFVAELSPEQ CLKIMAEIIS RDLIVITQQP
TTTTNNNTTN NTNNNNTNNN NNNTNGNNSD INQTNLIRYH FVHDRIQQAA FNLVLLKDEK
KQIHLNIGRI LYKKYYVQSN NNSSNNNNNN NNNNNINIFE ILNQYNFGIE LIKDQDERLN
LSKLNFEAGC KANSSTAFNY GNQYFQIALN LLFGESEQGE DDDLVWNEHY QMLFNIYLEK
SQSEFMVGNC QESDRLLEKA LQRAKKDEHI GEVTARRVKQ YTLQLRFDDC IEMSIEFLKR
QGIFLDINLS MDTLTKDYQK FKNRLNGQPI STIMNKLVGG GGGGSGSSNN SNNGSVVSPL
VDCCLRVMVI MMPSLYLNNL NVLTLLLMKF VEYTLENGIS SWSSTAFAMF GMVVSIGHFC
DYSVGYQFGQ YAMSLKEKYS EQPGTKGMVT LLYSGYIHHL GNHLSTSIPI VKQAFLESIE
YGDFGCACYA SVNLILHRIL LGLPLDETYQ LSKQYSNYIE QYYFKPMYQI VVSLQNFILE
LTGTDLLPEQ QQPQQQTPNN SNSSCGSNCS SGGNSNNSNL NCSSGSSFAS GSNYNNININ
NNNNNNNNNN NNNNNNNYNA EWDIEEFEND LLSTPDVHCP IAYHFISKCQ TCYLFGDFES
AWQAVLRGEN SIIGIFAHTH LFSVLYLFKS LIIMKNLGNQ HNNNNNNNSN HIYKTYGIEN
ENNNDSNNNN YNFKIYSLEE EIKMAKDCIE KLESYSEQSY ENFSSQLMLA KAEFERINGN
FEQAMEYFSE AISLAQQFKY QQYEALANEL SSRMYIQIKK FAVAKAYLIE SHQCYKSWGA
LRKANQLELE FPNLLNFNRL NVQTKRSKRF EYSNNNNNNN SNNNNNNANQ SQASISLSSS
TSFNSKIIGN SSNSSNNNFN NNNNNNNNNN NLMAISSSSS ICSSGSGSYG SSNGISGTTQ
LNSNYNSNFF EPSLSIRRRS QDGTVSTKNL SRYPVDAVDL CSVIKVSHSL AEEIYFDRLL
KRLMKVVIKN AGASRGFLLL IEDKITKELF INPTSKTNIT LLGDLSVAAS ALVNNEKVIV
EVFINNNINN NNININSSGY NNTNKNDNNN NNNYSPAYNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNKK QINEIIKNDS FNEEDGTWNM CLSMINYVKR TLTPLLITNA IQDNTFSEDP
YVKKRNPKSI LVLPIVYQGN LVSILYLENN FSTGIFSNEK LEILNLISSQ IAISFSNARL
FIKVNQLANQ AFLAKEEAEK ANKAKSDFIS NMSHEMRTPL NHIIGSIELL KSYNHLFNSD
QKELLDISAK SSESLLFMVN NILDLSKVEQ GKTKLNLTNF NLVSFLEDSI CAISPNAHLK
GVYIALFINP CLSKIPVIGD INILRQVIVN LLTNAIKFTE SGQVYIKLNL SINNNPTTTN
NKKQLNTDND GDDDDDDDNE NLDENNEDTS IDLDDNGKVI YQKNPKSNQC YIVNIEVVDS
GIGIKNEDFG KLFQRFSQIE CGSNRAYDGT GLGLSIVKDL VCNLMKGDIG VKSKVGVGST
FHFCVELGKS FDESMSNKYH LPLELLNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNINCS
NGGSVNINSS GNSVFSCSSS NSGTRVTILE ENKIICDQLS MLCVSNGLND LTVLNDIFSL
ELLADCLDCY KPPIQSPRFG STSSSLVLLS PRSTLNLSPK IISPRPYPNN QNNFLSSSPQ
MLSPLPNSPL SSSQQHQNNN NINNNNINNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNGVGL SINLSNLNNH NHNNSHNNNS QQIQYQNSKE IFIIGLPFSY NEDKILTLVE
NIKSLTYSAS FNKRGNISIS SNVNKVEFIL VTHILLSANS REILNNSNIY IVNRPIKMKT
LHKTFLKIFE NNNNNNINNI NNNNNKSNSP IPEDSKHSQY KYQKQLSESN ICYTKKPISP
SPSSATVILE QQQDHNLQSP TAITTNLISE EYDHFDSNST PPPNTATTTT TTTTLANSAL
ANSTLANSIS TTSHSSTSTS SSSSSSSSSS SSLSSTTTIT TTTTTTSNLD KMLIDKKITS
TQELKILIVE DNEMNANIMF KMLAKLGIQC EPHLALNGLE GVKKAKNEEY DLIIMDIQMP
VMCGLTATSL IRKHEGTKKR TPIVAITASA MNGEMSKALA AGCDDYLSKP LQLKDLRYVI
NRYGPITLEY NS
