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Protein

Hybrid signal transduction histidine kinase A

Gene

dhkA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.1 Publication

GO - Molecular functioni

  • ATP binding Source: dictyBase
  • phosphorelay sensor kinase activity Source: dictyBase
  • transmembrane receptor histidine kinase activity Source: dictyBase

GO - Biological processi

  • cAMP-mediated signaling Source: dictyBase
  • cytokinin-activated signaling pathway Source: UniProtKB-KW
  • negative regulation of cyclic-nucleotide phosphodiesterase activity Source: dictyBase
  • peptidyl-histidine phosphorylation Source: GOC
  • protein autophosphorylation Source: dictyBase
  • protein phosphorylation Source: dictyBase
  • signal transduction by protein phosphorylation Source: GOC
  • sorocarp development Source: dictyBase
  • sorocarp morphogenesis Source: dictyBase
  • sorocarp stalk development Source: dictyBase
  • sporulation resulting in formation of a cellular spore Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase

Keywords - Biological processi

Cytokinin signaling pathway, Differentiation, Sporulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hybrid signal transduction histidine kinase A (EC:2.7.13.3)
Gene namesi
Name:dhkA
ORF Names:DDB_G0280961
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0280961. dhkA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei772 – 79221HelicalSequence analysisAdd
BLAST
Transmembranei1098 – 111821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: dictyBase
  • external side of plasma membrane Source: dictyBase
  • integral component of plasma membrane Source: dictyBase
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1396 – 13961H → Q: Impaired function. Normal function; when associated with N-2076. 1 Publication
Mutagenesisi2076 – 20761D → N: Impaired function. Normal function; when associated with Q-1396. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21502150Hybrid signal transduction histidine kinase APRO_0000328204Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1396 – 13961Phosphohistidine; by autocatalysisPROSITE-ProRule annotation
Modified residuei2076 – 207614-aspartylphosphatePROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ54U87.

Expressioni

Developmental stagei

Expressed from 8 hours following initiation of development, prior to the appearance of mound tips. Subsequently persists throughout development.1 Publication

Interactioni

Subunit structurei

Interacts with SDF-2, an acbA peptide involved in sporulation.1 Publication

Protein-protein interaction databases

STRINGi44689.DDB0215354.

Structurei

3D structure databases

ProteinModelPortaliQ54U87.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini838 – 1082245CHASEPROSITE-ProRule annotationAdd
BLAST
Domaini1235 – 131783PASAdd
BLAST
Domaini1321 – 137656PACAdd
BLAST
Domaini1393 – 1620228Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini2026 – 2146121Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1139 – 116426Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 6634Poly-GlnAdd
BLAST
Compositional biasi75 – 817Poly-Gln
Compositional biasi105 – 14541Poly-AsnAdd
BLAST
Compositional biasi200 – 2045Poly-Asn
Compositional biasi212 – 24332Poly-AsnAdd
BLAST
Compositional biasi305 – 31713Poly-AsnAdd
BLAST
Compositional biasi412 – 43625Poly-AsnAdd
BLAST
Compositional biasi472 – 4754Poly-Asn
Compositional biasi478 – 4847Poly-Asn
Compositional biasi525 – 5284Poly-Asn
Compositional biasi539 – 5424Poly-Asn
Compositional biasi565 – 57713Poly-AsnAdd
BLAST
Compositional biasi588 – 60013Poly-AsnAdd
BLAST
Compositional biasi657 – 67519Poly-AsnAdd
BLAST
Compositional biasi678 – 72750Poly-AsnAdd
BLAST
Compositional biasi1249 – 12535Poly-Gly
Compositional biasi1715 – 173319Poly-AsnAdd
BLAST
Compositional biasi1866 – 187611Poly-GlyAdd
BLAST
Compositional biasi1889 – 18924Poly-Asn
Compositional biasi1936 – 19394Poly-Gln
Compositional biasi1942 – 19487Poly-Gln
Compositional biasi1989 – 19924Poly-Asn

Sequence similaritiesi

Contains 1 CHASE domain.PROSITE-ProRule annotation
Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.Curated
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0519. Eukaryota.
ENOG410XNMH. LUCA.
InParanoidiQ54U87.
OMAiKERENNW.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR006189. CHASE_dom.
IPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR001610. PAC.
IPR000014. PAS.
IPR013655. PAS_fold_3.
IPR004358. Sig_transdc_His_kin-like_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF03924. CHASE. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF08447. PAS_3. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM01079. CHASE. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00086. PAC. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50839. CHASE. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q54U87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELKTFKDLN DDIIGDTSPV INTGDQPNPL RTQQQQLQQQ QQQQQQQQQQ
60 70 80 90 100
QQQQQQQQQQ QQQQQQHHIP QQLYQKQQQQ QHSHSYGNHS FIHNVSPTSP
110 120 130 140 150
SYDINNNNNN NNNNNNNNNN NNNNNNNSNN NNNNNNNNKN NYNNNYYYSP
160 170 180 190 200
IENSNISKSL EESVLNQFPH NFNLNSSNNN YLNNSSSLHN INQSVNSLSN
210 220 230 240 250
NNNNQTNQQP INNNNNNNNN NNNNNSNNSN NSNNNNNGNN NNNITDSPTK
260 270 280 290 300
SKRHSTYETN IGSHQRRKSI QSLIANSAIH SFSKLKNKPL SSSTPSTVNT
310 320 330 340 350
CGAVNNNSNN NNNNNNNSTG SLGAIPMDRS FDGNINTITE ESTGGNNSPR
360 370 380 390 400
SNCGSNCGSN GGIPLSPRNL SSLNSGVNVS PRNIHLNNLN NNSSNLPPLS
410 420 430 440 450
PRHINFHINV SNLNNNNNNN INPNNNPNNS NNSNNNVSPR NNNHNISPRG
460 470 480 490 500
SNISPRSNNG GSTTISPRNI SNNNNIINNI NNNNILTPPR NSPRLENVNP
510 520 530 540 550
TNSPRLLATS LNSTLPIVSS LTSSNNNNQS NNNTNPSINN NNGRNGHCIQ
560 570 580 590 600
TISEEILGNK PVVYNNGNNN NNNNTNNSTT SNNNITTNNN NNNNNNINNN
610 620 630 640 650
VLSTPRKRTK GNHSKTNSLQ DFETSSMNGG DDSISGAGSG GSLRRRNKDD
660 670 680 690 700
NDENDGNSNN TNSNNSNNNN NNNNNSSNNN NNNSNNNNNN NNNNNNNNNN
710 720 730 740 750
NNNNNNNNNN NNNNNNNNNN NNNNNNNYHN GATMMMSHNH QSIGMSSSPK
760 770 780 790 800
KNNFKPFSRN CSLMGMGRRA WAIILGLFIV GSSISILATL VLRYSEENSI
810 820 830 840 850
ADDFARVARD RFTMLRIEFN NRLYITQTLS LLLSVFPSTS EDQFVPFSKL
860 870 880 890 900
WSDNAEGLEG IMWAPRVSNL DRYTWEIEHS VKIREIVTNP NNSSDMRDVP
910 920 930 940 950
AAAASDYYPI LFSEPQSSND HFKGYNIYSD MWRRPSLNKT RDTGEKVSVA
960 970 980 990 1000
SPYINKLANV PKNSRSNVLL YIYQAVYTYG KVLSTVEDRR HEVIGFASCR
1010 1020 1030 1040 1050
FFISRMVSAS LQRLTEEDSL DLYVFDLDST PIGELIYYRA SNAGNDDGSS
1060 1070 1080 1090 1100
PTNIMNGKML EDRSDMIYYN TMNVGGRNWM IALRPSRKFT NKHYTFYPYA
1110 1120 1130 1140 1150
IGGVCMLLSA LVSFWFAVNT KHNIKLSATN EDLHKEIYNR KLAEKALAES
1160 1170 1180 1190 1200
QERLELAMEG SEDAVWDWKV NTGELHISSR WFQILKAHDT SYQSRTLYEE
1210 1220 1230 1240 1250
LKSSSTNNLN FKGDSKNGGS NNGTFNLFKN GKVDSSSPQS ITNVNTTNGG
1260 1270 1280 1290 1300
GGGELRKSNS GYLYNDELFS PIILEEMVSS PNTHQLAIWN MKFLAELIHP
1310 1320 1330 1340 1350
DDKQKFISEI KKTITRETSI MEIECRMRKK YGGYLYIIMR GKVVSNETSF
1360 1370 1380 1390 1400
KDNSLRMAGT LRDMTSRKDM QRLILEKEAA EEANKAKSAF VATVSHEVRT
1410 1420 1430 1440 1450
PLSGVIGVSD LLLETNLSEE QRDYVQTIQK SSQALLTIIN DILDYSKLES
1460 1470 1480 1490 1500
RQLKMETLPF SIIETCQAVI HMLSVAANDD VDILLRVPPN VPRIIFGDAM
1510 1520 1530 1540 1550
RMRQVLLNLL SNAIKFTSRG HVLTDISVDD SIPPTNTEEE IIHLCITIED
1560 1570 1580 1590 1600
TGIGIPQSLF DSIFEPFSQA DNSTTRKYGG TGLGLSITKR LIEEVMGGTI
1610 1620 1630 1640 1650
QVSSIVGQGS KFKCIIPFLL PNTSPSDLNL ISPSSLPKPF INRSPKSTYS
1660 1670 1680 1690 1700
FTDKKNSVPS TPIPSGDILI NKVCLLICRD TVTELVFKEQ LEWLGMIVKQ
1710 1720 1730 1740 1750
VPRNVIDSIK NTILNNNNNN NNNNNNNNNN SNNSSSIISP SSLDYSDENE
1760 1770 1780 1790 1800
HLDLVLIDLE ILTEHLKIPS NVPIIFITPT KFNISKHNGI LNKWITKSPN
1810 1820 1830 1840 1850
QRVELIRRPA ITDKLIPIIS KCIKSQVQFT SGSSQLQSQQ ANLQQQLLHQ
1860 1870 1880 1890 1900
QLCNNGQTLN NNYNSGGIGG GGGGGGSNTM NGSSGNLSNN NNFGQTPLSS
1910 1920 1930 1940 1950
GLVLLVHTGR TPPLFNNNGN SIIPPLELAV DHHGNQQQQL YQQQQQQQNN
1960 1970 1980 1990 2000
SSGNFQQFYQ QQNNNSNNSF TPTLPNENSN NSIMNNSLNN NNTTPSNVTP
2010 2020 2030 2040 2050
TLFTSSPLDL QGRDTPVLQP PAYRKKALIV EDNELNRKVL AQLFKKIDWT
2060 2070 2080 2090 2100
ISFAENGREA LKEITGERCF DIVFMDCQMP VLDGFQTTKI IRSKERENNW
2110 2120 2130 2140 2150
KRMNIVALSA GSSSSFVQDC LDSGMDSFMG KPITLATLKD ALAKWGGYNN
Length:2,150
Mass (Da):239,636
Last modified:May 24, 2005 - v1
Checksum:i1FDA618EE9B3DBCA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1319 – 13191S → A in AAC47300 (PubMed:8670894).Curated
Sequence conflicti1509 – 15091L → R in AAC47300 (PubMed:8670894).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42597 mRNA. Translation: AAC47300.1.
AAFI02000040 Genomic DNA. Translation: EAL66777.1.
PIRiS71629.
RefSeqiXP_640889.1. XM_635797.1.

Genome annotation databases

EnsemblProtistsiDDB0215354; DDB0215354; DDB_G0280961.
GeneIDi8622946.
KEGGiddi:DDB_G0280961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42597 mRNA. Translation: AAC47300.1.
AAFI02000040 Genomic DNA. Translation: EAL66777.1.
PIRiS71629.
RefSeqiXP_640889.1. XM_635797.1.

3D structure databases

ProteinModelPortaliQ54U87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0215354.

Proteomic databases

PaxDbiQ54U87.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0215354; DDB0215354; DDB_G0280961.
GeneIDi8622946.
KEGGiddi:DDB_G0280961.

Organism-specific databases

dictyBaseiDDB_G0280961. dhkA.

Phylogenomic databases

eggNOGiKOG0519. Eukaryota.
ENOG410XNMH. LUCA.
InParanoidiQ54U87.
OMAiKERENNW.

Miscellaneous databases

PROiQ54U87.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR006189. CHASE_dom.
IPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR001610. PAC.
IPR000014. PAS.
IPR013655. PAS_fold_3.
IPR004358. Sig_transdc_His_kin-like_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF03924. CHASE. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF08447. PAS_3. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM01079. CHASE. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00086. PAC. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50839. CHASE. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiDHKA_DICDI
AccessioniPrimary (citable) accession number: Q54U87
Secondary accession number(s): Q23863
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: January 20, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.