Q95PI2 (DHKC_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	dhkC
ORF Names:	DDB_G0274191

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1225 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts in a signal transduction pathway that regulates the slug versus culmination choice. Believed to be the first component of a phosphorelay that couples the sensing of ammonia to the modulation of PKA activity and hence activates culmination and spore germination. Ammonium transporters amtA and amtC are thought to respectively activate and inhibit dhkC phosphorelay. This protein probably undergoes an ATP-dependent autophosphorylation at conserved His residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. Ref.5 Ref.6
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Developmental stage	Expressed at low levels during growth and development, with a peak during early aggregation (8 h). Mounds display weak expression within the upper regions and very strong expression at the perimeter of basal cells in contact with the substrate. Expression becomes tip-specific during first finger formation. Ref.5
Sequence similarities	Contains 1 histidine kinase domain. Contains 2 response regulatory domains.
Sequence caution	The sequence AAB84206.1 differs from that shown. Reason: Frameshift at positions 945 and 991.

Ontologies

Keywords
Biological process	Two-component regulatory system
Cellular component	Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transducer Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
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 spore germination Inferred from mutant phenotype Ref.1. Source: dictyBase
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW receptor 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 – 1225	1225	Hybrid signal transduction histidine kinase C		PRO_0000328269
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Domain	426 – 653	228	Histidine kinase
	Domain	669 – 784	116	Response regulatory 1
	Domain	1078 – 1200	123	Response regulatory 2
	Compositional bias	53 – 65	13	Poly-Asn
	Compositional bias	101 – 122	22	Poly-Asn
	Compositional bias	199 – 202	4	Poly-Asn
	Compositional bias	234 – 243	10	Poly-Asn
	Compositional bias	317 – 329	13	Poly-Ser
	Compositional bias	380 – 388	9	Poly-Ser
	Compositional bias	802 – 821	20	Poly-Asn
	Compositional bias	844 – 847	4	Poly-Asn
	Compositional bias	894 – 936	43	Poly-Gln
	Compositional bias	1028 – 1036	9	Poly-Asn
Amino acid modifications
	Modified residue	429	1	Phosphohistidine; by autocatalysis By similarity
	Modified residue	721	1	4-aspartylphosphate By similarity
	Modified residue	1127	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q95PI2 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 4BB546254BF7EF16	FASTA	1,225	137,347
	10 20 30 40 50 60 MIVEVELGFL LSTLFFTIIS IILFYFFINN KNNLIDQCQE VTKLNNKDNK IVNNNNNNYN 70 80 90 100 110 120 NNNFNKIEEI NDDKNKEIIK LINNSNNKNL KIKIQEIDSG NNNNNNNNNN NNNNNNLNKN 130 140 150 160 170 180 SNEIFRNFKI FSGSLLVIDQ DLNIISSSES VRDIFSNIND INGVNQQVIG SLQNYSFINL 190 200 210 220 230 240 VHQKDKDRVS TFLKLKFKNN NNIKHQQFSE DIINEKDELK EIQIEDNKEL IIINNNNNNN 250 260 270 280 290 300 NDNVLKFGNN NSNNSSIILF QGVYHLNNTD LSKPFNLQVS ILPFISENYI VLSLKDLSPP 310 320 330 340 350 360 PLRLLLNKTS SALSPRSLSS SSSSSPSSSN NNGNTNNSGS LSPRSSNSNG SAVSPRNVSS 370 380 390 400 410 420 NSMSPRGQNS DRSISSPRGS SSSSSSSSNE LAISPRNSNG TISSPRTSNL SIESVLNNKS 430 440 450 460 470 480 IDMISHLSHE LRTPIHSVIA SIQLFRSTIL TVTQNEYLSI IDTSANTLLE LVSNVLDYKR 490 500 510 520 530 540 IRSGKLTLNN VDFNLCHVIE DVCAMVSPQA QAKSLQIASF IFIHCPLSFY GDPIRLRQVL 550 560 570 580 590 600 LNLIGNGLKY TNKGQVCISV EPEQVNEHCM YLHFQVKDSG IGIKEENMSK LFAGFSQVNN 610 620 630 640 650 660 GGTTQEALGS GLGLAISKDL VELMGGKIWC SSNATQNNGE AGCTFHFVIP LETNPKQLPC 670 680 690 700 710 720 PIQNFNGLSV LVVDKNPYIQ TVLCQYLEGW NCQVIKSSDI KEASNKLKDL RREQIEVVMI 730 740 750 760 770 780 DIDNIDFRDF IQFKDAFNRL EFGRIGLITM SSDRSMVNEM GFGTSKLTKP FRQSHLVACL 790 800 810 820 830 840 LASMPEHSSS TTNCFSNIVG MNSNINNNNN INNNSNNNNN NMQTHNSNSV YGNGNYGNCT 850 860 870 880 890 900 PFSNNNNRIH MMSSGDKPSI NNRRMSISLG KIPTFNSGGS NSPRSKKLFE EVLQQQQLQQ 910 920 930 940 950 960 QLQQQLQQQQ QLQQQQQQQQ QQQQQQQQQL QQQQQQLNTI DDDSNNYCNT TGTMDSIDEI 970 980 990 1000 1010 1020 NKNNYSDSES DELNDDQAPI IAPVQQLSFG RVTRRHSIDI IMFENSRELS ELRNLEDSTR 1030 1040 1050 1060 1070 1080 YLSPRSMNNN NGNNDNGING GSGNSLFGSS IKEEIGGTSD TSSLAQSPNS LSPRAPTKIM 1090 1100 1110 1120 1130 1140 ILDDNPVSLK LMQRILESRG FECYPFDCSE KAVAQLDQVN PAIIFMDCEM PKMNGFECTQ 1150 1160 1170 1180 1190 1200 LIRKREQESL CLLKDRKIII ALTAHINPEI QVKCFDAGMN DFISKPFKPQ CLELILRKWE 1210 1220 DCISNNQLNY NNSLINNQTT IQEQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The histidine kinase dhkC regulates the choice between migrating slugs and terminal differentiation in Dictyostelium discoideum." Singleton C.K., Zinda M.J., Mykytka B., Yang P. Dev. Biol. 203:345-357(1998) [PubMed: 9808785] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]	"The histidine kinases of Dictyostelium." Anjard C., Loomis W.F. (In) Inouye M., Dutta R. (eds.); HISTIDINE KINASES IN SIGNAL TRASNDUCTION, pp.1-1, Academic press, San Diego (2001) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AX4.
[3]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed: 12097910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[4]	"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.
[5]	"Ammonium transporter C of Dictyostelium discoideum is required for correct prestalk gene expression and for regulating the choice between slug migration and culmination." Kirsten J.H., Xiong Y., Dunbar A.J., Rai M., Singleton C.K. Dev. Biol. 287:146-156(2005) [PubMed: 16188250] [Abstract] Cited for: FUNCTION, MUTAGENESIS, DEVELOPMENTAL STAGE, PHOSPHORELAY INHIBITION BY AMTC.
[6]	"Function of ammonium transporter A in the initiation of culmination of development in Dictyostelium discoideum." Singleton C.K., Kirsten J.H., Dinsmore C.J. Eukaryot. Cell 5:991-996(2006) [PubMed: 16835443] [Abstract] Cited for: FUNCTION, PHOSPHORELAY ACTIVATION BY AMTA.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF029726 mRNA. Translation: AAB84206.1. Frameshift. AF361474 Genomic DNA. Translation: AAK50004.1. AAFI02000012 Genomic DNA. Translation: EAL69988.1.
PIR	T09057.
RefSeq	XP_644273.1. XM_639181.1.
3D structure databases
HSSP	HSSP built from PDB template 2C2A based on UniProtKB Q9WZV7.
ProteinModelPortal	Q95PI2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0185038; DDB0185038; DDB_G0274191.
GeneID	8619701.
GenomeReviews	Gene locus dhkC in contig CM000151_GR.
KEGG	ddi:DDB_G0274191.
Organism-specific databases
dictyBase	DDB_G0274191. dhkC.
Phylogenomic databases
eggNOG	KOG0519.
GeneTree	EPrGT00050000000304.
OMA	ASANTDY.
ProtClustDB	CLSZ2846868.
Family and domain databases
InterPro	IPR003594. ATPase-like_ATP-bd. IPR011006. CheY-like_superfamily. 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	PF02518. HATPase_c. 1 hit. PF00512. HisKA. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
SMART	SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. SM00448. REC. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF52172. CheY_like. 2 hits. SSF47384. His_kin_homodim. 1 hit.
PROSITE	PS50109. HIS_KIN. 1 hit. PS50110. RESPONSE_REGULATORY. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHKC_DICDI

Accession

Primary (citable) accession number: Q95PI2
Secondary accession number(s): O15784, Q554Q0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	December 1, 2001
Last modified:	September 21, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)