Reviewed, UniProtKB/Swiss-Prot Q54Q69 (DHKG_DICDI)

Names and origin

Protein names

Recommended name:
    Hybrid signal transduction histidine kinase G
Including the following 2 domains:
    1- Recommended name:
            Histidine kinase dhkG
              EC=2.7.13.3
    2- Recommended name:
            Probable serine/threonine-protein kinase dhkG
              EC=2.7.11.1

Gene names

Name:	dhkG
ORF Names:	DDB_G0284045

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	3432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Acts as a receptor histidine kinase for a signal transduction pathway. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain By similarity.
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Domain	Atypical domain architecture: contains STYKc/AAA module and histidine kinase/receiver module.
Post-translational modification	Activation probably requires transfer of a phosphate group between a histidine in the kinase core (transmitter) domain and an aspartate of the receiver domain By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 GAF domain. Contains 1 histidine kinase domain. Contains 1 protein kinase domain. Contains 1 response regulatory domain. Contains 1 TPR repeat.

Ontologies

Keywords
Biological process	Two-component regulatory system
Cellular component	Membrane
Domain	TPR repeat Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transducer Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW two-component response regulator activity Inferred from electronic annotation. Source: InterPro two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3432	3432	Hybrid signal transduction histidine kinase G		PRO_0000328337
Regions
	Transmembrane	1567 – 1587	21	Potential
	Transmembrane	1599 – 1619	21	Potential
	Domain	263 – 792	530	Protein kinase
	Repeat	1965 – 1998	34	TPR
	Domain	2215 – 2465	251	GAF
	Domain	2491 – 2769	279	Histidine kinase
	Domain	3305 – 3424	120	Response regulatory
	Nucleotide binding	269 – 277	9	ATP By similarity
	Nucleotide binding	871 – 878	8	ATP Potential
	Region	863 – 1121	259	AAA
	Compositional bias	40 – 43	4	Poly-Thr
	Compositional bias	53 – 69	17	Poly-Thr
	Compositional bias	70 – 74	5	Poly-Pro
	Compositional bias	126 – 134	9	Poly-Gln
	Compositional bias	195 – 240	46	Poly-Asn
	Compositional bias	395 – 406	12	Poly-Asn
	Compositional bias	409 – 419	11	Poly-Asn
	Compositional bias	476 – 479	4	Poly-Ser
	Compositional bias	497 – 508	12	Poly-Asn
	Compositional bias	510 – 524	15	Poly-Gly
	Compositional bias	630 – 634	5	Poly-Asn
	Compositional bias	653 – 657	5	Poly-Asn
	Compositional bias	800 – 816	17	Poly-Asn
	Compositional bias	1030 – 1041	12	Poly-Asn
	Compositional bias	1045 – 1052	8	Poly-Asn
	Compositional bias	1055 – 1079	25	Poly-Asn
	Compositional bias	1270 – 1288	19	Poly-Asn
	Compositional bias	1345 – 1357	13	Poly-Asn
	Compositional bias	1793 – 1819	27	Poly-Asn
	Compositional bias	1902 – 1910	9	Poly-Asn
	Compositional bias	1927 – 1932	6	Poly-Asn
	Compositional bias	2074 – 2089	16	Poly-Asn
	Compositional bias	2116 – 2131	16	Poly-Asn
	Compositional bias	2136 – 2140	5	Poly-Ser
	Compositional bias	2285 – 2296	12	Poly-Asn
	Compositional bias	2301 – 2313	13	Poly-Asn
	Compositional bias	2319 – 2348	30	Poly-Asn
	Compositional bias	2648 – 2658	11	Poly-Asp
	Compositional bias	2787 – 2818	32	Poly-Asn
	Compositional bias	2958 – 3006	49	Poly-Asn
	Compositional bias	3131 – 3145	15	Poly-Asn
	Compositional bias	3225 – 3234	10	Poly-Thr
	Compositional bias	3253 – 3275	23	Poly-Ser
	Compositional bias	3276 – 3286	11	Poly-Thr
Sites
	Active site	585	1	Proton acceptor; for protein kinase activity By similarity
	Binding site	305	1	ATP By similarity
Amino acid modifications
	Modified residue	2494	1	Phosphohistidine; by autocatalysis By similarity
	Modified residue	3356	1	4-aspartylphosphate By similarity
Experimental info
	Sequence conflict	1335	1	Y → N in AAK54088. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q54Q69-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: DA45965835CEB03A	FASTA	3,432	383,457
	10 20 30 40 50 60 MNYSWIHEYY LGTCIQEEKV FSIYSASTSN NSFSFPSIPT TTTHFSNSVL NQTTTTTTTT 70 80 90 100 110 120 TTTTTTTNTP PPPPQSQLQA QLQSQSQQNN QHHRPLSPNG GFFSITNSSS ISDQDLRSRL 130 140 150 160 170 180 KLYDDQPQQQ QQQQASNKSK LSQKQTSQLN ISGNNSGNST PPLPTISNSN NSINFIHSPP 190 200 210 220 230 240 PTPPLLKTPI LSSHNHNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNHNIN 250 260 270 280 290 300 TIDIDLVSPP PPLLLPSGSL SPLSFKHGYN SGLGGNFCSN SIANGIHLGK KPSEFQSHNN 310 320 330 340 350 360 NVLLKILNYK YPPIEISTIF QREYFILSYL NDLDGTLKLI KTQSEYGNIV ALIFEENGYK 370 380 390 400 410 420 SLTSYYNVLS LLNGVGGCAS FTNYNLNYNI NNSLNNLNNN NNNNNNSYNN NYNNNNNNNG 430 440 450 460 470 480 QVTSPILNNT ELSQSSASAF KPFQLNSSTN STGSPLIITS QPMPFQLNSN SNTTASSSSP 490 500 510 520 530 540 ITHSNLNTAI TSTTTSNSNS NNNSNNNNSG GGGGGGGGGG GGGGTKINNK RRASLTPTST 550 560 570 580 590 600 PLSASPLLFN TKKYADIDIN TFLSIAIQLT TILESIHGKG CIHRDIRPNN IYINSECKVK 610 620 630 640 650 660 LANFQFSIFK KTSSFLKKSK FQQQHQQSEN NNNNTLDSDI TMIDNIDLTN SYNNNNNSST 670 680 690 700 710 720 NNIFFNFNND YDEESINELF KSYPDLSRFS TSTYYYISPE DTGRTIHPVD EKSDLYSLGV 730 740 750 760 770 780 TFFELLTGRL PFQSSDLSEL IHSHLAKKPP LVIDLNQNVP LILSNIVNKL LQKSPDDRYQ 790 800 810 820 830 840 SAYGLKKDLE MFKLQLSIIN NNNNNNNNNN NNNNNNLSNQ QITDFKLGAY DVLNRPYISN 850 860 870 880 890 900 ELYSRKKELN SILTTIKRVS KGGKEFIIVS GLSGVGKTSL INQACKKSNT KVRFICGKFD 910 920 930 940 950 960 QFNKSPYSAI IEALSQLVNL ILSLSPLELE FYKDRLLRTL GSNISVITEV IPKLCLIVGT 970 980 990 1000 1010 1020 HYKVLPLPSS ESQNRFDLAF KDFLRVFAEE GNPLVLFLDD FQRADPSSYR LIKLLMESNN 1030 1040 1050 1060 1070 1080 STSNNSTFLN CNGNNNNNNN NFSINNNNNN NNGCNNNNNN NNNNINNNNN NNNNNNINNS 1090 1100 1110 1120 1130 1140 GGSLNYLLVI GAFRENEPNF ELDFGDLSNF ITMKIVLKNL DLKYVNLMVS TTLHASPQET 1150 1160 1170 1180 1190 1200 LSLSQVVLSK THGNAFFVIL FLRTLFDESL VYFSTTTDKW CWNIEKIQKR EFTDNVVEFM 1210 1220 1230 1240 1250 1260 VENLKQLDKQ AQRVLHLASC IGNSFDLDML AFVAELSPEQ CLKIMAEIIS RDLIVITQQP 1270 1280 1290 1300 1310 1320 TTTTNNNTTN NTNNNNTNNN NNNTNGNNSD INQTNLIRYH FVHDRIQQAA FNLVLLKDEK 1330 1340 1350 1360 1370 1380 KQIHLNIGRI LYKKYYVQSN NNSSNNNNNN NNNNNINIFE ILNQYNFGIE LIKDQDERLN 1390 1400 1410 1420 1430 1440 LSKLNFEAGC KANSSTAFNY GNQYFQIALN LLFGESEQGE DDDLVWNEHY QMLFNIYLEK 1450 1460 1470 1480 1490 1500 SQSEFMVGNC QESDRLLEKA LQRAKKDEHI GEVTARRVKQ YTLQLRFDDC IEMSIEFLKR 1510 1520 1530 1540 1550 1560 QGIFLDINLS MDTLTKDYQK FKNRLNGQPI STIMNKLVGG GGGGSGSSNN SNNGSVVSPL 1570 1580 1590 1600 1610 1620 VDCCLRVMVI MMPSLYLNNL NVLTLLLMKF VEYTLENGIS SWSSTAFAMF GMVVSIGHFC 1630 1640 1650 1660 1670 1680 DYSVGYQFGQ YAMSLKEKYS EQPGTKGMVT LLYSGYIHHL GNHLSTSIPI VKQAFLESIE 1690 1700 1710 1720 1730 1740 YGDFGCACYA SVNLILHRIL LGLPLDETYQ LSKQYSNYIE QYYFKPMYQI VVSLQNFILE 1750 1760 1770 1780 1790 1800 LTGTDLLPEQ QQPQQQTPNN SNSSCGSNCS SGGNSNNSNL NCSSGSSFAS GSNYNNININ 1810 1820 1830 1840 1850 1860 NNNNNNNNNN NNNNNNNYNA EWDIEEFEND LLSTPDVHCP IAYHFISKCQ TCYLFGDFES 1870 1880 1890 1900 1910 1920 AWQAVLRGEN SIIGIFAHTH LFSVLYLFKS LIIMKNLGNQ HNNNNNNNSN HIYKTYGIEN 1930 1940 1950 1960 1970 1980 ENNNDSNNNN YNFKIYSLEE EIKMAKDCIE KLESYSEQSY ENFSSQLMLA KAEFERINGN 1990 2000 2010 2020 2030 2040 FEQAMEYFSE AISLAQQFKY QQYEALANEL SSRMYIQIKK FAVAKAYLIE SHQCYKSWGA 2050 2060 2070 2080 2090 2100 LRKANQLELE FPNLLNFNRL NVQTKRSKRF EYSNNNNNNN SNNNNNNANQ SQASISLSSS 2110 2120 2130 2140 2150 2160 TSFNSKIIGN SSNSSNNNFN NNNNNNNNNN NLMAISSSSS ICSSGSGSYG SSNGISGTTQ 2170 2180 2190 2200 2210 2220 LNSNYNSNFF EPSLSIRRRS QDGTVSTKNL SRYPVDAVDL CSVIKVSHSL AEEIYFDRLL 2230 2240 2250 2260 2270 2280 KRLMKVVIKN AGASRGFLLL IEDKITKELF INPTSKTNIT LLGDLSVAAS ALVNNEKVIV 2290 2300 2310 2320 2330 2340 EVFINNNINN NNININSSGY NNTNKNDNNN NNNYSPAYNN NNNNNNNNNN NNNNNNNNNN 2350 2360 2370 2380 2390 2400 NNNNNNNNKK QINEIIKNDS FNEEDGTWNM CLSMINYVKR TLTPLLITNA IQDNTFSEDP 2410 2420 2430 2440 2450 2460 YVKKRNPKSI LVLPIVYQGN LVSILYLENN FSTGIFSNEK LEILNLISSQ IAISFSNARL 2470 2480 2490 2500 2510 2520 FIKVNQLANQ AFLAKEEAEK ANKAKSDFIS NMSHEMRTPL NHIIGSIELL KSYNHLFNSD 2530 2540 2550 2560 2570 2580 QKELLDISAK SSESLLFMVN NILDLSKVEQ GKTKLNLTNF NLVSFLEDSI CAISPNAHLK 2590 2600 2610 2620 2630 2640 GVYIALFINP CLSKIPVIGD INILRQVIVN LLTNAIKFTE SGQVYIKLNL SINNNPTTTN 2650 2660 2670 2680 2690 2700 NKKQLNTDND GDDDDDDDNE NLDENNEDTS IDLDDNGKVI YQKNPKSNQC YIVNIEVVDS 2710 2720 2730 2740 2750 2760 GIGIKNEDFG KLFQRFSQIE CGSNRAYDGT GLGLSIVKDL VCNLMKGDIG VKSKVGVGST 2770 2780 2790 2800 2810 2820 FHFCVELGKS FDESMSNKYH LPLELLNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNINCS 2830 2840 2850 2860 2870 2880 NGGSVNINSS GNSVFSCSSS NSGTRVTILE ENKIICDQLS MLCVSNGLND LTVLNDIFSL 2890 2900 2910 2920 2930 2940 ELLADCLDCY KPPIQSPRFG STSSSLVLLS PRSTLNLSPK IISPRPYPNN QNNFLSSSPQ 2950 2960 2970 2980 2990 3000 MLSPLPNSPL SSSQQHQNNN NINNNNINNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN 3010 3020 3030 3040 3050 3060 NNNNNNGVGL SINLSNLNNH NHNNSHNNNS QQIQYQNSKE IFIIGLPFSY NEDKILTLVE 3070 3080 3090 3100 3110 3120 NIKSLTYSAS FNKRGNISIS SNVNKVEFIL VTHILLSANS REILNNSNIY IVNRPIKMKT 3130 3140 3150 3160 3170 3180 LHKTFLKIFE NNNNNNINNI NNNNNKSNSP IPEDSKHSQY KYQKQLSESN ICYTKKPISP 3190 3200 3210 3220 3230 3240 SPSSATVILE QQQDHNLQSP TAITTNLISE EYDHFDSNST PPPNTATTTT TTTTLANSAL 3250 3260 3270 3280 3290 3300 ANSTLANSIS TTSHSSTSTS SSSSSSSSSS SSLSSTTTIT TTTTTTSNLD KMLIDKKITS 3310 3320 3330 3340 3350 3360 TQELKILIVE DNEMNANIMF KMLAKLGIQC EPHLALNGLE GVKKAKNEEY DLIIMDIQMP 3370 3380 3390 3400 3410 3420 VMCGLTATSL IRKHEGTKKR TPIVAITASA MNGEMSKALA AGCDDYLSKP LQLKDLRYVI 3430 NRYGPITLEY NS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The histidine kinases of Dictyostelium." Anjard C., Loomis W.F. (In) Inouye M., Dutta R. (eds.); Histidine kinases in signal transduction, pp.1-1, Academic press, San Diego (2001) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AX4.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF362369 Genomic DNA. Translation: AAK54088.2. AAFI02000063 Genomic DNA. Translation: EAL65363.1.
RefSeq	XP_638728.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3390285.
KEGG	ddi:DDB_0191388.
Organism-specific databases
dictyBase	DDB_G0284045. dhkG.
Enzyme and pathway databases
BRENDA	2.7.13.3. 424.
Family and domain databases
InterPro	IPR003594. ATP_bd_ATPase. IPR003593. ATPase_AAA+_core. IPR003018. GAF. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR004358. Sig_transdc_His_kin-like_C. IPR003661. Sig_transdc_His_kin_sub1_dim/P. IPR005467. Sig_transdc_His_kinase_core. IPR001789. Sig_transdc_resp-reg_receiver. IPR008266. Tyr_pkinase_AS. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
Pfam	PF02518. HATPase_c. 1 hit. PF00512. HisKA. 1 hit. PF00069. Pkinase. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
ProDom	PD000001. Prot_kinase. 2 hits. PD000039. Response_reg. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00382. AAA. 1 hit. SM00065. GAF. 1 hit. SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. SM00448. REC. 1 hit. [Graphical view]
PROSITE	PS50109. HIS_KIN. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHKG_DICDI

Accession

Primary (citable) accession number: Q54Q69
Secondary accession number(s): Q95PH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)