DRKD_DICDI
ID DRKD_DICDI Reviewed; 1288 AA.
AC Q54TM7; O15912;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable serine/threonine-protein kinase drkD;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like kinase D;
GN Name=drkD; Synonyms=rsc21; ORFNames=DDB_G0281557;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 104-618.
RC STRAIN=AX4;
RA Iranfar N., Loomis W.F.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000042; EAL66540.1; -; Genomic_DNA.
DR EMBL; U82512; AAB69632.1; -; mRNA.
DR RefSeq; XP_640564.1; XM_635472.1.
DR AlphaFoldDB; Q54TM7; -.
DR SMR; Q54TM7; -.
DR STRING; 44689.DDB0214883; -.
DR PaxDb; Q54TM7; -.
DR PRIDE; Q54TM7; -.
DR ABCD; Q54TM7; 2 sequenced antibodies.
DR EnsemblProtists; EAL66540; EAL66540; DDB_G0281557.
DR GeneID; 8623174; -.
DR KEGG; ddi:DDB_G0281557; -.
DR dictyBase; DDB_G0281557; drkD.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_262498_0_0_1; -.
DR InParanoid; Q54TM7; -.
DR OMA; PCIVTEY; -.
DR PhylomeDB; Q54TM7; -.
DR Reactome; R-DDI-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-DDI-170968; Frs2-mediated activation.
DR Reactome; R-DDI-3295583; TRP channels.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR Reactome; R-DDI-430116; GP1b-IX-V activation signalling.
DR Reactome; R-DDI-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-DDI-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-5675482; Regulation of necroptotic cell death.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR PRO; PR:Q54TM7; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0005524; F:ATP 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:0050829; P:defense response to Gram-negative bacterium; IMP:dictyBase.
DR GO; GO:2000146; P:negative regulation of cell motility; IMP:dictyBase.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; IMP:dictyBase.
DR GO; GO:0051593; P:response to folic acid; IMP:dictyBase.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Kinase; Leucine-rich repeat; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1288
FT /note="Probable serine/threonine-protein kinase drkD"
FT /id="PRO_0000354060"
FT REPEAT 400..421
FT /note="LRR 1"
FT REPEAT 423..444
FT /note="LRR 2"
FT REPEAT 446..468
FT /note="LRR 3"
FT REPEAT 469..490
FT /note="LRR 4"
FT REPEAT 492..513
FT /note="LRR 5"
FT REPEAT 517..538
FT /note="LRR 6"
FT REPEAT 540..561
FT /note="LRR 7"
FT DOMAIN 851..1104
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 221..248
FT /evidence="ECO:0000255"
FT COMPBIAS 1..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 974
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 857..865
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 878
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 232
FT /note="Q -> L (in Ref. 2; AAB69632)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="L -> F (in Ref. 2; AAB69632)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="L -> F (in Ref. 2; AAB69632)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="K -> Q (in Ref. 2; AAB69632)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="L -> F (in Ref. 2; AAB69632)"
FT /evidence="ECO:0000305"
FT CONFLICT 617..618
FT /note="KR -> NT (in Ref. 2; AAB69632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1288 AA; 147339 MW; B078BF437BBD4AB7 CRC64;
MEGSFQFNKS KQTNNNSSLD SNNIINDNIN NNLNFENNNN NNNNNNNNNN NNNNNNNNNN
TNNNNTTNDT SKTSANSTST EDDEEDILGN RKKDTTGSRV LPMDTSLTGA AEPSKKRKNT
QDDSEVEVQY HPQKRASFSL NISPTQLQND LSLNIFNVSN SNNNNNSNNN NNNNNNNNNN
NNKINNNSNL ILNSSVDSTT SSNNNNNKNS NDNQQPQQQP EEIEGELNRE RQERDKMLHE
EAEIEQYKYG DGEEGENYEI MVTPHHRTSF GHITSANSDE TTNNESGSPI NSRKMVTDEE
DPHSSHNEDH QSDQDNHGQF MNDEHQSTDD DQNKSDNEKE SESARNSGDL QQKVHNSKDE
STVSTPQHIF NNGNGEGEEE DDDDEEYDVP LRIQTVANNK STKLSLSNCW LKVIPTDVWS
ILELRDLDLS ANQLKKVSKS IGLLVHLKRL RLNHNQLTAL PKELYSLPRL TTLYLNNNNF
KVVPKEINRL TSLKTLDLSF NQITDISPQT NLHQMTNLVE LRLRYNQLSS LPQNMLESNH
LQVLWLEGNR LPLNKAILKK SPSEILSFLR GYKPPNKKVN DKVINKAHVN PALPPIDTAS
TIAVAQVFAQ KELDTKKRKK ENLDDFKKQH IETELKLKQL EEELQIANAK ATKFEEEASL
LQQQFNNPNT PTGPSLNLPS ILLNQPHLGW DQQQQQQQQQ SPNVSTPPIS TSPVLTGGQQ
VVNGISQISL LSPTQQINNP PSPVTQFNQA SPQHNNNQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QNGSPQQPHV NNNNNNNIQQ NKDHQFPVPT IPAKIIEVEK
PFEWEVPLSE IAIGARIGRG GYGQVFRGSW RGTEVAVKML FNDNVNLKLI SDLRKEVDLL
CKLRHPNIVL FMGACTEPSS PCIVTEYLSR GSLANILLDE SIEMDWGLRL QLGFDCARGM
TYLHSRNPII IHRDLKTDNL LVDDSWQVKV ADFGLATVKS HTFAKTMCGT TGWVAPEVLA
EEGYTEKADV YSYAIVLWEL LTRLIPYAGK NTMQVVRSID RGERLPMPAW CPPKYAALMN
RCWETDPTHR PSFPEILPIM EGMISEFQKE KKESIAQGRP IPYVGPPEKD PSNKQPPQNM
ATTIQQQLAQ QQPQQLLEQQ ILLQVQQQAQ LQHLQQQLEQ QQKLQQQLQQ QIAHPNNPNN
FYFQQQLQQQ QFQQQLQQHQ QHFQQQQQQQ QQQQQQQQQQ QQQQQQQLQQ TGSPIDNRLN
YNFNNSNNSD IQPMQQENNY RMNINDKK
