DHKK_DICDI
ID DHKK_DICDI Reviewed; 1213 AA.
AC Q86CZ2; Q54Y10; Q95PH2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Hybrid signal transduction histidine kinase K;
DE EC=2.7.13.3;
DE AltName: Full=Protein sombrero;
GN Name=dhkK; Synonyms=smbA; ORFNames=DDB_G0277887;
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].
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 [MRNA], CHARACTERIZATION, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=AX2;
RX PubMed=16473345; DOI=10.1016/j.ydbio.2006.01.010;
RA Thomason P.A., Sawai S., Stock J.B., Cox E.C.;
RT "The histidine kinase homologue DhkK/Sombrero controls morphogenesis in
RT Dictyostelium.";
RL Dev. Biol. 292:358-370(2006).
RN [3]
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).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=16765443; DOI=10.1016/j.plasmid.2006.04.001;
RA Thomason P.A., Brazill D.T., Cox E.C.;
RT "A series of Dictyostelium expression vectors for recombination cloning.";
RL Plasmid 56:145-152(2006).
CC -!- FUNCTION: Involved in a signal transduction pathway that regulates
CC morphogenesis and controls entry into the culmination stage. May act
CC via the regA pathway, being activated by a morphogenesis-stimulated
CC ligand, reducing phosphodiesterase regA levels and allowing cAMP level
CC to rise to promote the culmination stage. This protein probably
CC undergoes an ATP-dependent autophosphorylation at a conserved histidine
CC residue in the kinase core, and a phosphoryl group is then transferred
CC to a conserved aspartate residue in the receiver domain.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: First expressed prior to the start of aggregation,
CC becoming concentrated in the slug anterior. Later is expressed in the
CC maturing spore head of the fruiting body. {ECO:0000269|PubMed:16473345,
CC ECO:0000269|PubMed:16765443}.
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}.
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DR EMBL; AF362376; AAK54095.1; -; Genomic_DNA.
DR EMBL; AY263399; AAP20874.1; -; Genomic_DNA.
DR EMBL; AAFI02000023; EAL68116.1; -; Genomic_DNA.
DR RefSeq; XP_642392.1; XM_637300.1.
DR AlphaFoldDB; Q86CZ2; -.
DR SMR; Q86CZ2; -.
DR STRING; 44689.DDB0214934; -.
DR PaxDb; Q86CZ2; -.
DR EnsemblProtists; EAL68116; EAL68116; DDB_G0277887.
DR GeneID; 8621597; -.
DR KEGG; ddi:DDB_G0277887; -.
DR dictyBase; DDB_G0277887; dhkK.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_269528_0_0_1; -.
DR InParanoid; Q86CZ2; -.
DR OMA; CSKTIRE; -.
DR PRO; PR:Q86CZ2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..1213
FT /note="Hybrid signal transduction histidine kinase K"
FT /id="PRO_0000328272"
FT TRANSMEM 600..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 822..1052
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1076..1199
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 825
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1125
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 253
FT /note="N -> T (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="V -> A (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="S -> F (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="I -> F (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
FT CONFLICT 509..510
FT /note="QQ -> HL (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="L -> V (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="T -> P (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="I -> P (in Ref. 1; AAK54095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1213 AA; 137716 MW; 69B171E952D02195 CRC64;
MIELNNHSKI NKNENNTNTR NNSSNNNNNN NNINKTNTNK YFEYNQNSII YSSIPNSFLS
HHPNSVGSQC LSLNSFLPPK PPILLSIFNS DTIGNNNNNN YSSSSSRNNS SGCSSSNNNN
NNNNNNNNNN NNNNNNNNNN CNIEQYKNNQ KQPKQQQQQK DQTIATQHRI SLSSSSSSSS
LSSSSSSSSV KQSFQIVKRL FGSLSEYMFP QKDEILYETD PYYLYQDDTQ SNDSNEFYDD
TDIGSDIDEA NLNNTYNIQN CNKTLYNKQQ QQAHFVNMNK NVNSNNGTGN SNQSNNVNKN
QQNNNNNNNN NSHNNNNGNQ NSSSSSSNSG ASGSGGNGNN NNNNNNNNNN NNNNNNNSNS
NSNNNSKSNN NNKKEGKDGA TMNGSHPLIP FRKKPAQVPS PCFRMNSPNS DNDQYLDQLA
LENSSKKSLV VYNTDNLDQW KHSHLNENFD ILQNDLIDIQ QQQQQQQQQD NTLQYSSPIN
KRQEQEQQHI PFQFTTEQQQ QLQQQQQQQQ QNKTKQHPIL LQRQQQQKQK QQQQQQIQQE
QIGNNNSNNN NNINNNNNIN NNYNNVNDLM NKFEIDQKQH DSQQNLVEEK RTPSFHEHNI
IFNSFNFICS IVLDGSNIKS TEKYKAKLII GFCFTILSFI PSWIIFFWLS GINKPAVMAI
IAMPMSISSL VILKRTGSIH YPCHILCFTL CFALTINSYY TGGHQSTIRL LMSTVPIISA
LVLGRKASIQ WSLMVLSIYL LFFVANLYGH EYVQGIPSII IRSHMNFIID VTIIIMTLIF
TLCYQYFIDE AHRETKLKNA QLTIAKDAAI EAYQARQEFL ATMSHEIRTP LNGLIGMATL
LRDSHNLPPE EKTMAKAVKS CGDILLRLVN DILDLSKLEA NQMGLEHIPF RMRELTQQIC
HVLSGQANEK NIHLSCEVSD KIPSILLGDS GRILQILMNL TGNALKFTQS GYVKIIIDLI
EEESELVSLK KGEYNISFRV KDTGIGVPVE SHQKIFEAFV QADPSDSRKY GGSGLGLYLC
AKLVRLMKGE IGVYNNPDCD GSTFWFILPL EEGTDQSMQQ MNNGARHKAF PQDCVKVLIA
EDNIINQRVA VKFLEKIGIK AEVAGNGNEV LEILERQHYD LIFMDFQMPI LDGLRCSKTI
REFEQNHKWN RICPSIFICG LTANTMSTDK KRCFDHGMNH FISKPFQLEQ LRSAIEMAIE
HKQRNLMNLN IRN
