DOKA_DICDI
ID DOKA_DICDI Reviewed; 1671 AA.
AC Q869S5; Q23901; Q554Z4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Hybrid signal transduction protein dokA;
GN Name=dokA; ORFNames=DDB_G0274101;
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], CHARACTERIZATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=AX2;
RX PubMed=8670893; DOI=10.1002/j.1460-2075.1996.tb00762.x;
RA Schuster S.C., Noegel A.A., Oehme F., Gerisch G., Simon M.I.;
RT "The hybrid histidine kinase DokA is part of the osmotic response system of
RT Dictyostelium.";
RL EMBO J. 15:3880-3889(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11060029; DOI=10.1093/emboj/19.21.5782;
RA Ott A., Oehme F., Keller H., Schuster S.C.;
RT "Osmotic stress response in Dictyostelium is mediated by cAMP.";
RL EMBO J. 19:5782-5792(2000).
RN [5]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF GLY-1206 AND GLY-1208.
RX PubMed=11299049; DOI=10.1186/1471-2091-2-2;
RA Oehme F., Schuster S.C.;
RT "Osmotic stress-dependent serine phosphorylation of the histidine kinase
RT homologue DokA.";
RL BMC Biochem. 2:2-2(2001).
CC -!- FUNCTION: Part of the osmoregulatory pathway which leads to the
CC increase of intracellular cAMP concentration in response to
CC hyperosmotic stress. Thought to negatively regulate the rdeA-regA
CC pathway by acting as a phosphatase towards the HPt protein rdeA. Has
CC probably no histidine kinase activity. {ECO:0000269|PubMed:11060029,
CC ECO:0000269|PubMed:11299049}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during the late culmination
CC stage. {ECO:0000269|PubMed:8670893}.
CC -!- PTM: Under osmotic stress conditions, this protein undergoes
CC phosphorylation at a serine residue in the kinase core, which is not
CC due to an autophosphorylation of dokA. This is in contrast to the
CC classic two-component paradigm, which predicts only histidine and
CC aspartate phosphorylation. {ECO:0000269|PubMed:11299049}.
CC -!- DISRUPTION PHENOTYPE: Elevated levels of cAMP.
CC {ECO:0000269|PubMed:11060029}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65612.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X96869; CAA65612.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AAFI02000012; EAL69943.1; -; Genomic_DNA.
DR PIR; S71628; S71628.
DR RefSeq; XP_644179.1; XM_639087.1.
DR AlphaFoldDB; Q869S5; -.
DR SMR; Q869S5; -.
DR STRING; 44689.DDB0185194; -.
DR PaxDb; Q869S5; -.
DR PRIDE; Q869S5; -.
DR EnsemblProtists; EAL69943; EAL69943; DDB_G0274101.
DR GeneID; 8619608; -.
DR KEGG; ddi:DDB_G0274101; -.
DR dictyBase; DDB_G0274101; dokA.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_241803_0_0_1; -.
DR InParanoid; Q869S5; -.
DR OMA; MTANDSK; -.
DR PRO; PR:Q869S5; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; ISS:dictyBase.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:dictyBase.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; ISS:dictyBase.
DR GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IMP:dictyBase.
DR GO; GO:0000160; P:phosphorelay signal transduction system; ISS:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_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; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..1671
FT /note="Hybrid signal transduction protein dokA"
FT /id="PRO_0000339235"
FT DOMAIN 1050..1276
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1519..1633
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1206
FT /note="G->A: Phosphorylation is not affected."
FT /evidence="ECO:0000269|PubMed:11299049"
FT MUTAGEN 1208
FT /note="G->A: Phosphorylation is not affected."
FT /evidence="ECO:0000269|PubMed:11299049"
SQ SEQUENCE 1671 AA; 186136 MW; ED349E0613B43345 CRC64;
MSSPHIELHS QRTLSPQPSS NNFELTGNKS CALSASLNGS IDDLNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNDGDKNDK KLLIITNAPT PPLTPPQPTK TQQTLLELNQ
KFQEQQQQQQ QQQQLQKQNK QQQSQKQQEE PPSSQQEEPP LSQQQQEQEQ EQEQEQEQEE
QSKQKIEGKG GGGEEEECEG GGGGEGEGEE QFKEGDEEEH EGIEIDPNLP TTGYTGKRRS
SLQINEASPK LIQTPSVDRT LCILDSLPCP IFQIGIIENT ENGNITLTGF ANERLTTLLS
CSSNLLVDSL KSIPSPHYNT VPSLESCNSI PINNLAPGLL PNTDPTKILD PYISLYNKKQ
LKERYSNNNN NTNTNNNNNN NNNNNNNNNN NNNNNNNDTT TTTTTTTTTT TTTTTTTTTT
TTNESDNNNN NNNNNNNNNN NNNNNNNNNE EIKQNTKEGE EILHESTNST GTGNSISRPN
SILQCILDSF HEQKTITEKV LLSNFLIRQQ YKSRATIKPF PDGCICIFEY IENINLNYQQ
PPTSLNDRIN STNKLTNEME LLSLSPDSNH QHVQKLHNHN HNHHNHNHNN TTQRASSTDS
PFIHSVSANS LSSMSSNSSV TSACASLSSN SSSNSNNNSN NASSSNCSSN ANSNNTNSSS
SNCCCCCNNN NNNNTSSTSS TISSASSTKS KSYLHQQHKN SKVYSTLLNS FENLSFLLKS
TPIIIWRADH NGEMVFFKKS DEIPIDEKKV VGNNFQDFLQ WVPQTYRTNF QEMFQNSLKC
GKIFEFLFWF QTPQNYVQLF KIAGYPIFHI DGKDCIASKR YLIGWLGVTY NYLINDGAEI
SIKGSANLDS MYEKFKIIYE MPNIERTKLT NNGISSGGDI TNANNNGGSS ESSNKILEKK
KHLISEAEKE CFLKCKETYN ILFKLSLLGV MFSTFKGIIL DANDMLLQTI GYTRGDLENG
KIDWMLLTPP EHFEISARAL QELKAKRWCQ PIEKAYIHKS GKRVPVLITS AMIDGSTEQC
ITFVFDLSRY RQAEMAAIEA TRLKTQFITN ISHELRTPCH GIVGMSQLLL DSQLTNTQRD
NIDSIKRSTD SLISLINDIL DFSKLEYGKV TLENESFELL PMIEEVLDSQ ATAANRKGID
LIFVMGRDYP VPPVIFGDRN SLKKVLLNLV GNAVKFTETG FVLLEISTDY ESGDQISLRF
TVKDSGIGIP ENKIEQIFVP FGQIDGSFSR KYGGSGLGLS FCKELVALMG GYIRVESGDQ
EGGKGTTFWF AIKVSISSPS YLPNSVPAAN QFFYPEYRPS HYNNVIGNGD SPKNVLIIES
NQMVIMSIQS ILLSMKCECI SASKAITALD LLESSKSTEN QIDIIVCSDK STFVQQILDY
VTTEKVILYG VDPNSKYNEN SKVYSYLVTP ITHSKLISSI LLSKNLKSKN SFLTTTNNTN
NTNNTNNIEN KSSIDSPLSI TSTSSSIITP ILTSNNLDLN NNNNNNNNSI LVSNNGGVDG
GNNVPSTLTT IQQSQPKKYI LVAEDNDINI KVVVRQLEKL GYTAIVGING LKALEIIGSF
PICLILLDCQ MPQMDGFTCS TILRQIEPTG QRIPIIAMTA NDSKDRCFEV GMDDYLSKPV
RVDRLQKTLS DWIKTDENGN PTNSYNFYPL SYSLVYNNFI DTQLKKEKND D
