YAKA_DICDI
ID YAKA_DICDI Reviewed; 1458 AA.
AC Q54QV3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable serine/threonine-protein kinase yakA;
DE EC=2.7.12.1;
GN Name=yakA; Synonyms=dagB; ORFNames=DDB_G0283605;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
RP DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=9584128; DOI=10.1242/dev.125.12.2291;
RA Souza G.M., Lu S., Kuspa A.;
RT "YakA, a protein kinase required for the transition from growth to
RT development in Dictyostelium.";
RL Development 125:2291-2302(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10375515; DOI=10.1242/dev.126.14.3263;
RA Souza G.M., da Silva A.M., Kuspa A.;
RT "Starvation promotes Dictyostelium development by relieving PufA inhibition
RT of PKA translation through the YakA kinase pathway.";
RL Development 126:3263-3274(1999).
RN [4]
RP MUTAGENESIS OF PRO-375, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=11410593; DOI=10.1074/jbc.m103365200;
RA van Es S., Weening K.E., Devreotes P.N.;
RT "The protein kinase YakA regulates G-protein-linked signaling responses
RT during growth and development of Dictyostelium.";
RL J. Biol. Chem. 276:30761-30765(2001).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12134067; DOI=10.1091/mbc.01-11-0555;
RA Taminato A., Bagattini R., Gorjao R., Chen G., Kuspa A., Souza G.M.;
RT "Role for YakA, cAMP, and protein kinase A in regulation of stress
RT responses of Dictyostelium discoideum cells.";
RL Mol. Biol. Cell 13:2266-2275(2002).
CC -!- FUNCTION: General sensor of environmental conditions, such as heat
CC stress, effecting changes through pkaC. Essential for survival to
CC nitrosoative and oxidative stresses. Required for cell cycle control,
CC not only at the onset but also during development (aggregation process
CC and postaggregative development). {ECO:0000269|PubMed:10375515,
CC ECO:0000269|PubMed:11410593, ECO:0000269|PubMed:12134067,
CC ECO:0000269|PubMed:9584128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11410593}.
CC -!- DEVELOPMENTAL STAGE: Expressed during growth-to-development stages with
CC increase in cell density. {ECO:0000269|PubMed:9584128}.
CC -!- DISRUPTION PHENOTYPE: Null cells fail to enter development, express low
CC levels of cAMP receptors, are smaller than wild-type cells, are
CC hypersensitive to nitrosoative/oxidative stress, and display slow
CC growth on bacterial lawns. {ECO:0000269|PubMed:10375515,
CC ECO:0000269|PubMed:11410593, ECO:0000269|PubMed:12134067}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000056; EAL65569.1; -; Genomic_DNA.
DR RefSeq; XP_638920.1; XM_633828.1.
DR AlphaFoldDB; Q54QV3; -.
DR SMR; Q54QV3; -.
DR STRING; 44689.DDB0191191; -.
DR PaxDb; Q54QV3; -.
DR EnsemblProtists; EAL65569; EAL65569; DDB_G0283605.
DR GeneID; 8624159; -.
DR KEGG; ddi:DDB_G0283605; -.
DR dictyBase; DDB_G0283605; yakA.
DR eggNOG; KOG0667; Eukaryota.
DR HOGENOM; CLU_250928_0_0_1; -.
DR InParanoid; Q54QV3; -.
DR OMA; ICRIIDM; -.
DR Reactome; R-DDI-3899300; SUMOylation of transcription cofactors.
DR PRO; PR:Q54QV3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; TAS:dictyBase.
DR GO; GO:0006935; P:chemotaxis; TAS:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR GO; GO:0051409; P:response to nitrosative stress; IMP:dictyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:dictyBase.
DR GO; GO:0010225; P:response to UV-C; IDA:dictyBase.
DR GO; GO:0007165; P:signal transduction; TAS:dictyBase.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1458
FT /note="Probable serine/threonine-protein kinase yakA"
FT /id="PRO_0000362075"
FT DOMAIN 205..548
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 32..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..643
FT /evidence="ECO:0000255"
FT COILED 878..927
FT /evidence="ECO:0000255"
FT COILED 1346..1383
FT /evidence="ECO:0000255"
FT COILED 1409..1442
FT /evidence="ECO:0000255"
FT COMPBIAS 32..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 211..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 375
FT /note="P->S: Causes a temperature-sensitive phenotype,
FT which fails to develop at restrictive temperature."
FT /evidence="ECO:0000269|PubMed:11410593"
SQ SEQUENCE 1458 AA; 166973 MW; 656073216ADF46EF CRC64;
MGSTTQMSDY LVSTTTTSSA SSMVTMTSQI ENNSLNSNDN TNTTNNNNNN NNNNNNNNNN
NNNNNNNNNI NNNNNNGGMV GVNHKTHKKT ASIGGGKNRA ILHDFTFSYF IPNQNRSEDN
SNENELGLNN HNVQHQGPII HLTKNLLHFY KKCNSNFNYI SSLNPRRVLT HPSEPLSNDG
YDNVNSDYIV YVNDIITNNE SGQKYKVLDS LGQGTFGQVV KCKNCDTDEL VAIKILKNKQ
AYFQQGRLEI QTLKSLNDQH DPEDKNHILR LLDSFIHKMH LCIVFELLSV NLFELIKQNN
FRGLSTNLIK VFLIQILDAL IVLANANIIH CDLKPENILL QNVNSPAIKI IDFGSACYEK
STLYTYIQSR HYRSPEVLVG TVYCASIDMW SLGCISAELF LGLPLFPGNS EYNQISRIVE
MRGIFPSDLL DKGKSSTRYF HRHLGSNSDD NNNNNNNNNG KPYYYTLKSE EDYQRDSKTT
LLPSKKYFNY KTLPEIIQNY GFKKSMSPQD IEKEKQHRIV FTDFINGLLQ LDPNERWSPM
QAKEHPFITG QPYNGPFIPD PSKKRHFTYS QPKQIPQHSM LNGNQILNQH QLFQQLQQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQHNQF QQQQQQQQQQ QQSSSQQHIQ IQPLQLFSTP
YTSTNNTPNL SSSNSGSSLN NLKKLNLPPF KQQQQQQFST SQNSDSFNFP NESFSPRGIY
IPSSASNIQQ QQQPININNN QNGVGSQVSQ LALGQSPSLF GTPTNIYPPY SSMYNNSPVA
TPNSLSFYGS SWGSDSSSIS LNPSTPTQKQ MFQQQQYSNN NNNNNNNNNN NSNNNNGNNT
NNINSNNNNN NVNRRNRSKS DIPSDSFSSS EGMDPQFNLY QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQLQYQQQ FQTLQDLNIE GEKPPIYPNS PHRKRSHSGY LDQYANGYNS
QQTNNTQQQQ QQQQQQQQQQ QQQQQQQQHP SFFSTRMHLD HFNGGSRYRS QSYGDQQFQQ
QQYKQQQKNL HHQQQQQQRF MQVGSPPTSH LSPPIPQSPL MMSQPLHQTY IPQQQQQQQQ
QQQQSQPTPF TPQMISQEPI SPALMGDASS IWNPSPTEEL LFTIDLPNQQ NTPHLTPSNS
STNLLGKSAS SPLKNSSGGA IPPTPTIPIN MEEINNGFSK FHFNDQPSWN SNGNSPWMIQ
QQQQHQQGFN GNSESMYNDD LIGFSPYNNY SNDYRPQLFN KQSPPSSYNS NKSFYGGSGG
GGNNNNNNNS RPTNQNFSNS LLPSQQQNVI FPQNSPPSSY NSSNSLSKSG GNTVKNNSNT
GGRPRGDSMK QRFNSTNNLL SGGSYQYQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQYK
KDTPSLMMSP PMNGLKTSSE IGIPSEEIRY QYQQQQLQQQ FQQQQQQQQQ QQIQQQLQQQ
QAPPQNRKQV VIGSYRET
