Q54U87 (DHKA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hybrid signal transduction histidine kinase A
EC=2.7.13.3

Gene names

Name:	dhkA
ORF Names:	DDB_G0280961

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	2150 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a receptor histidine kinase for the cytokinin SDF-2 in a signal transduction pathway that regulates prestalk gene expression and controls terminal differentiation of prespore cells. Binding of SDF-2 to this protein inhibits phosphorelay and induces rapid sporulation. 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. Ref.3 Ref.4
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Ref.3
Subunit structure	Interacts with SDF-2, an acbA peptide involved in sporulation. Ref.3
Subcellular location	Cell membrane; Multi-pass membrane protein Potential Ref.3.
Developmental stage	Expressed from 8 hours following initiation of development, prior to the appearance of mound tips. Subsequently persists throughout development. Ref.1
Sequence similarities	Contains 1 CHASE domain. Contains 1 histidine kinase domain. Contains 1 PAC (PAS-associated C-terminal) domain. Contains 1 PAS (PER-ARNT-SIM) domain. Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	Cytokinin signaling pathway Differentiation Sporulation
Cellular component	Cell membrane Membrane
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cAMP-mediated signaling Inferred from mutant phenotype. Source: dictyBase cytokinin mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cyclic-nucleotide phosphodiesterase activity Traceable author statement. Source: dictyBase peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro sorocarp stalk development Inferred from mutant phenotype Ref.1. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype Ref.1. Source: dictyBase
Cellular component	external side of plasma membrane Traceable author statement Ref.4. Source: dictyBase integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular Inferred from sequence or structural similarity Ref.1. Source: GOC
Molecular function	ATP binding Traceable author statement. Source: dictyBase transmembrane receptor histidine kinase activity Inferred from genetic interaction Ref.4. Source: dictyBase two-component response regulator activity Inferred from sequence or structural similarity Ref.1. Source: dictyBase two-component sensor activity Inferred from sequence or structural similarity Ref.1. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2150	2150	Hybrid signal transduction histidine kinase A		PRO_0000328204
Regions
	Transmembrane	772 – 792	21	Helical; Potential
	Transmembrane	1098 – 1118	21	Helical; Potential
	Domain	838 – 1082	245	CHASE
	Domain	1235 – 1317	83	PAS
	Domain	1321 – 1376	56	PAC
	Domain	1393 – 1620	228	Histidine kinase
	Domain	2026 – 2146	121	Response regulatory
	Coiled coil	1139 – 1164	26	Potential
	Compositional bias	33 – 66	34	Poly-Gln
	Compositional bias	75 – 81	7	Poly-Gln
	Compositional bias	105 – 145	41	Poly-Asn
	Compositional bias	200 – 204	5	Poly-Asn
	Compositional bias	212 – 243	32	Poly-Asn
	Compositional bias	305 – 317	13	Poly-Asn
	Compositional bias	412 – 436	25	Poly-Asn
	Compositional bias	472 – 475	4	Poly-Asn
	Compositional bias	478 – 484	7	Poly-Asn
	Compositional bias	525 – 528	4	Poly-Asn
	Compositional bias	539 – 542	4	Poly-Asn
	Compositional bias	565 – 577	13	Poly-Asn
	Compositional bias	588 – 600	13	Poly-Asn
	Compositional bias	657 – 675	19	Poly-Asn
	Compositional bias	678 – 727	50	Poly-Asn
	Compositional bias	1249 – 1253	5	Poly-Gly
	Compositional bias	1715 – 1733	19	Poly-Asn
	Compositional bias	1866 – 1876	11	Poly-Gly
	Compositional bias	1889 – 1892	4	Poly-Asn
	Compositional bias	1936 – 1939	4	Poly-Gln
	Compositional bias	1942 – 1948	7	Poly-Gln
	Compositional bias	1989 – 1992	4	Poly-Asn
Amino acid modifications
	Modified residue	1396	1	Phosphohistidine; by autocatalysis By similarity
	Modified residue	2076	1	4-aspartylphosphate By similarity
Experimental info
	Mutagenesis	1396	1	H → Q: Impaired function. Normal function; when associated with N-2076. Ref.3
	Mutagenesis	2076	1	D → N: Impaired function. Normal function; when associated with Q-1396. Ref.3
	Sequence conflict	1319	1	S → A in AAC47300. Ref.1
	Sequence conflict	1509	1	L → R in AAC47300. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q54U87 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 1FDA618EE9B3DBCA	FASTA	2,150	239,636
	10 20 30 40 50 60 MELKTFKDLN DDIIGDTSPV INTGDQPNPL RTQQQQLQQQ QQQQQQQQQQ QQQQQQQQQQ 70 80 90 100 110 120 QQQQQQHHIP QQLYQKQQQQ QHSHSYGNHS FIHNVSPTSP SYDINNNNNN NNNNNNNNNN 130 140 150 160 170 180 NNNNNNNSNN NNNNNNNNKN NYNNNYYYSP IENSNISKSL EESVLNQFPH NFNLNSSNNN 190 200 210 220 230 240 YLNNSSSLHN INQSVNSLSN NNNNQTNQQP INNNNNNNNN NNNNNSNNSN NSNNNNNGNN 250 260 270 280 290 300 NNNITDSPTK SKRHSTYETN IGSHQRRKSI QSLIANSAIH SFSKLKNKPL SSSTPSTVNT 310 320 330 340 350 360 CGAVNNNSNN NNNNNNNSTG SLGAIPMDRS FDGNINTITE ESTGGNNSPR SNCGSNCGSN 370 380 390 400 410 420 GGIPLSPRNL SSLNSGVNVS PRNIHLNNLN NNSSNLPPLS PRHINFHINV SNLNNNNNNN 430 440 450 460 470 480 INPNNNPNNS NNSNNNVSPR NNNHNISPRG SNISPRSNNG GSTTISPRNI SNNNNIINNI 490 500 510 520 530 540 NNNNILTPPR NSPRLENVNP TNSPRLLATS LNSTLPIVSS LTSSNNNNQS NNNTNPSINN 550 560 570 580 590 600 NNGRNGHCIQ TISEEILGNK PVVYNNGNNN NNNNTNNSTT SNNNITTNNN NNNNNNINNN 610 620 630 640 650 660 VLSTPRKRTK GNHSKTNSLQ DFETSSMNGG DDSISGAGSG GSLRRRNKDD NDENDGNSNN 670 680 690 700 710 720 TNSNNSNNNN NNNNNSSNNN NNNSNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN 730 740 750 760 770 780 NNNNNNNYHN GATMMMSHNH QSIGMSSSPK KNNFKPFSRN CSLMGMGRRA WAIILGLFIV 790 800 810 820 830 840 GSSISILATL VLRYSEENSI ADDFARVARD RFTMLRIEFN NRLYITQTLS LLLSVFPSTS 850 860 870 880 890 900 EDQFVPFSKL WSDNAEGLEG IMWAPRVSNL DRYTWEIEHS VKIREIVTNP NNSSDMRDVP 910 920 930 940 950 960 AAAASDYYPI LFSEPQSSND HFKGYNIYSD MWRRPSLNKT RDTGEKVSVA SPYINKLANV 970 980 990 1000 1010 1020 PKNSRSNVLL YIYQAVYTYG KVLSTVEDRR HEVIGFASCR FFISRMVSAS LQRLTEEDSL 1030 1040 1050 1060 1070 1080 DLYVFDLDST PIGELIYYRA SNAGNDDGSS PTNIMNGKML EDRSDMIYYN TMNVGGRNWM 1090 1100 1110 1120 1130 1140 IALRPSRKFT NKHYTFYPYA IGGVCMLLSA LVSFWFAVNT KHNIKLSATN EDLHKEIYNR 1150 1160 1170 1180 1190 1200 KLAEKALAES QERLELAMEG SEDAVWDWKV NTGELHISSR WFQILKAHDT SYQSRTLYEE 1210 1220 1230 1240 1250 1260 LKSSSTNNLN FKGDSKNGGS NNGTFNLFKN GKVDSSSPQS ITNVNTTNGG GGGELRKSNS 1270 1280 1290 1300 1310 1320 GYLYNDELFS PIILEEMVSS PNTHQLAIWN MKFLAELIHP DDKQKFISEI KKTITRETSI 1330 1340 1350 1360 1370 1380 MEIECRMRKK YGGYLYIIMR GKVVSNETSF KDNSLRMAGT LRDMTSRKDM QRLILEKEAA 1390 1400 1410 1420 1430 1440 EEANKAKSAF VATVSHEVRT PLSGVIGVSD LLLETNLSEE QRDYVQTIQK SSQALLTIIN 1450 1460 1470 1480 1490 1500 DILDYSKLES RQLKMETLPF SIIETCQAVI HMLSVAANDD VDILLRVPPN VPRIIFGDAM 1510 1520 1530 1540 1550 1560 RMRQVLLNLL SNAIKFTSRG HVLTDISVDD SIPPTNTEEE IIHLCITIED TGIGIPQSLF 1570 1580 1590 1600 1610 1620 DSIFEPFSQA DNSTTRKYGG TGLGLSITKR LIEEVMGGTI QVSSIVGQGS KFKCIIPFLL 1630 1640 1650 1660 1670 1680 PNTSPSDLNL ISPSSLPKPF INRSPKSTYS FTDKKNSVPS TPIPSGDILI NKVCLLICRD 1690 1700 1710 1720 1730 1740 TVTELVFKEQ LEWLGMIVKQ VPRNVIDSIK NTILNNNNNN NNNNNNNNNN SNNSSSIISP 1750 1760 1770 1780 1790 1800 SSLDYSDENE HLDLVLIDLE ILTEHLKIPS NVPIIFITPT KFNISKHNGI LNKWITKSPN 1810 1820 1830 1840 1850 1860 QRVELIRRPA ITDKLIPIIS KCIKSQVQFT SGSSQLQSQQ ANLQQQLLHQ QLCNNGQTLN 1870 1880 1890 1900 1910 1920 NNYNSGGIGG GGGGGGSNTM NGSSGNLSNN NNFGQTPLSS GLVLLVHTGR TPPLFNNNGN 1930 1940 1950 1960 1970 1980 SIIPPLELAV DHHGNQQQQL YQQQQQQQNN SSGNFQQFYQ QQNNNSNNSF TPTLPNENSN 1990 2000 2010 2020 2030 2040 NSIMNNSLNN NNTTPSNVTP TLFTSSPLDL QGRDTPVLQP PAYRKKALIV EDNELNRKVL 2050 2060 2070 2080 2090 2100 AQLFKKIDWT ISFAENGREA LKEITGERCF DIVFMDCQMP VLDGFQTTKI IRSKERENNW 2110 2120 2130 2140 2150 KRMNIVALSA GSSSSFVQDC LDSGMDSFMG KPITLATLKD ALAKWGGYNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A two-component histidine kinase gene that functions in Dictyostelium development." Wang N., Shaulsky G., Escalante R., Loomis W.F. EMBO J. 15:3890-3898(1996) [PubMed: 8670894] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS, CHARACTERIZATION, DEVELOPMENTAL STAGE. 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.
[3]	"SDF-2 induction of terminal differentiation in Dictyostelium discoideum is mediated by the membrane-spanning sensor kinase DhkA." Wang N., Soderbom F., Anjard C., Shaulsky G., Loomis W.F. Mol. Cell. Biol. 19:4750-4756(1999) [PubMed: 10373524] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-1396 AND ASP-2076, INTERACTION WITH SDF-2, SUBCELLULAR LOCATION.
[4]	"Peptide signaling during terminal differentiation of Dictyostelium." Anjard C., Loomis W.F. Proc. Natl. Acad. Sci. U.S.A. 102:7607-7611(2005) [PubMed: 15897458] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U42597 mRNA. Translation: AAC47300.1. AAFI02000040 Genomic DNA. Translation: EAL66777.1.
PIR	S71629.
RefSeq	XP_640889.1. XM_635797.1.
3D structure databases
HSSP	HSSP built from PDB template 2C2A based on UniProtKB Q9WZV7.
ProteinModelPortal	Q54U87.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0215354; DDB0215354; DDB_G0280961.
GeneID	8622946.
GenomeReviews	Gene locus dhkA in contig CM000152_GR.
KEGG	ddi:DDB_G0280961.
Organism-specific databases
dictyBase	DDB_G0280961. dhkA.
Phylogenomic databases
eggNOG	KOG0519.
GeneTree	EPrGT00060000009498.
Family and domain databases
InterPro	IPR003594. ATPase-like_ATP-bd. IPR006189. CHASE. IPR011006. CheY-like_superfamily. IPR001610. PAC. IPR013655. PAS_fold_3. IPR004358. Sig_transdc_His_kin-like_C. IPR003661. Sig_transdc_His_kin_sub1_dim/P. IPR005467. Sig_transdc_His_kinase_core. IPR009082. Sig_transdc_His_kinase_dimeric. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
Pfam	PF03924. CHASE. 1 hit. PF02518. HATPase_c. 1 hit. PF00512. HisKA. 1 hit. PF08447. PAS_3. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
SMART	SM01079. CHASE. 1 hit. SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. SM00086. PAC. 1 hit. SM00448. REC. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF52172. CheY_like. 1 hit. SSF47384. His_kin_homodim. 1 hit.
PROSITE	PS50839. CHASE. 1 hit. PS50109. HIS_KIN. 1 hit. PS50113. PAC. False negative. PS50112. PAS. False negative. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHKA_DICDI

Accession

Primary (citable) accession number: Q54U87
Secondary accession number(s): Q23863

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)