PAKD_DICDI
ID PAKD_DICDI Reviewed; 1678 AA.
AC Q55DD4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serine/threonine-protein kinase pakD {ECO:0000250|UniProtKB:Q869N2};
DE EC=2.7.11.1;
GN Name=pakD {ECO:0000312|EMBL:EAL72198.1}; ORFNames=DDB_G0269696;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL72198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL72198.1};
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).
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000250|UniProtKB:Q869N2}.
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DR EMBL; AAFI02000005; EAL72198.1; -; Genomic_DNA.
DR RefSeq; XP_646197.1; XM_641105.1.
DR AlphaFoldDB; Q55DD4; -.
DR SMR; Q55DD4; -.
DR STRING; 44689.DDB0229968; -.
DR PaxDb; Q55DD4; -.
DR PRIDE; Q55DD4; -.
DR EnsemblProtists; EAL72198; EAL72198; DDB_G0269696.
DR GeneID; 8617150; -.
DR KEGG; ddi:DDB_G0269696; -.
DR dictyBase; DDB_G0269696; pakD.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_241590_0_0_1; -.
DR InParanoid; Q55DD4; -.
DR OMA; FHHVYNE; -.
DR Reactome; R-DDI-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-DDI-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DDI-5627123; RHO GTPases activate PAKs.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR Reactome; R-DDI-9013420; RHOU GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR PRO; PR:Q55DD4; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0001931; C:uropod; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045499; F:chemorepellent activity; IMP:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0030041; P:actin filament polymerization; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; IMP:dictyBase.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:dictyBase.
DR GO; GO:0110094; P:polyphosphate-mediated signaling; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1678
FT /note="Serine/threonine-protein kinase pakD"
FT /id="PRO_0000363949"
FT DOMAIN 82..189
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1202..1215
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 1376..1647
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 1141..1197
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 512..542
FT /evidence="ECO:0000255"
FT COILED 570..628
FT /evidence="ECO:0000255"
FT COILED 752..862
FT /evidence="ECO:0000255"
FT COILED 1269..1309
FT /evidence="ECO:0000255"
FT COMPBIAS 450..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1515
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1382..1390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1678 AA; 190772 MW; 67F77AE2AF468FF7 CRC64;
MSRLQPQQQQ RGRSSSFKDN FQIQKPLQSL TPSEQQQQQQ QQQQQQQQQQ QQQQQQQQQN
NANNNNNNNN NKFNNQYIQQ MKNVENDIKK WIGEKCSSSL SDDFLEKDLM ESLCTGTILC
VLINMIKQGT IQKIHLQPNY LQRVENIRNY LRACWLFGLH SKYFFPSSYL LSMTIENNDN
SNSSKTTTNN NNNNNNNNNN NNNNNNNNNN NNNNRAIITS PNKNGGVNTM IVNLEYKEKI
MINLTELCKI SLKIKNFGSF LQLSSSSSST PPPPINNNNN NNNNNNNNNN NNNDLLISNN
SSNISSPNSF SDSPMGFSSS INSSSNNSNL NTPNNYNNTN NNNNNNNNNN NNNNNNINNL
TPQMIISSPT STSSTPPLPP CANNINNNNL KKRTKIPKNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNKI IIKRDCKKVY RKRKSSNCDN DDNGSNSDSD SSDSSDSSDS DSDSLLSSDG
TPIILSQSSN PESVSFKSFI KEILHLKNII SKQDKTITSQ KQTIETLEKD LEFQKQLTKK
LLSSPIDLSN FIETSSDPNG AIPVSIQAFT RQIQQIQTLQ QQNLSLETEL SKTNEHLSTN
IRKNSKLENE VLSIETELLN LRMKYANTLS SSNSNGNNNS NNNSLGCNNS INGSSSGGGG
NNSSTSKGTL SRTISQPFPL RKSISHSNII TSPVNSHQQQ QQQNQLSQSQ TTSPKNTSAS
YNNGILSKSS IVSNTNTNST YKFGSSTGIL KVSATLQQKQ QQQQQQQNQQ QQQNQQQQQQ
NQQQQNQQQQ NQQKQNQQQQ NQQQQQQQQQ QQQQNQQQQQ QQQQQQQQQQ QQQNQQQQQN
NQLSQSQQLQ QQQNQQINNL IDSPLIISNS SNQQIESESI ESDSDYDKDM VDFGKKIVSA
LISSSNHVEM SEIYKMNDIL TNETSRRQIC IVLEEETKIN QLKLPMNENS FEVTLYLVNT
ILQCIHEAPS KDYFSLKLIM ESSRILNRKK VNGSCEFIQE FIKDHPTWKD IKFWEEQYWD
ELIIKHQQFS GSGSSSSSNT GGSIVTTMTT TTTVTSAITS SSSTTSDDFD VDYTELVNTL
LISYVYNLAS WGLSKSDVKE FTISMSKKSF LKSNELEKLI EQVTSTVELS FTSDHNVCKG
PHSFVLKSFR IISECNYCRQ YIWGVRGIVA REAFECVGCK YKTHKKCLKE ASEKTFCSSP
NVGAPFNVKH EMHVGLAIQG LPSGWRTLLL QSGFQDYEIQ QHQEDVLDVL EFHHVYNEKQ
QNSIKLLTNN SNNNNNNNNS NNNLQQQQQQ NQQLKQKLNI TNNQQNNTII NINITSPSIS
VNNNTYNNNN NNNNNNEINP SSPNNNNNYY DSLLEIEEPS FTLKDLVSLE NPIDLYKVRE
VVGGGSTGKV YVGENSITGE KVAIKKMKVD NNNIKNIINE ISTMKNSKHK NVIKYVSSHL
VINHIWLIME YMSYGSLTDL ISNCINIQCN GNNQQQQQQQ QQQQTYFIES HIAYICQQVL
QGMDYIHKGH RTHRDIKSDN ILLGKDGSVK IADFGFVANL TRKKLQRNSV VGTPYFMAPE
LIRGNQYNHK VDIWSLGILA RELSEGEPPY AKYPPVRALF LLTLEGVPDF KEPNKWSSDF
IEFVNLCLNL DDKRRPDAHY LLRHPFLKKA CSSREFADKV EEIYNTRKNQ FSDINFNF
