DRKC_DICDI
ID DRKC_DICDI Reviewed; 749 AA.
AC Q54TA1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable serine/threonine-protein kinase drkC;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like kinase 3;
DE AltName: Full=Receptor-like kinase C;
DE AltName: Full=Vesicle-associated receptor tyrosine kinase-like protein 3;
DE Flags: Precursor;
GN Name=drkC; Synonyms=rk3; ORFNames=DDB_G0281899;
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).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000043; EAL66509.1; -; Genomic_DNA.
DR RefSeq; XP_640488.1; XM_635396.1.
DR AlphaFoldDB; Q54TA1; -.
DR SMR; Q54TA1; -.
DR STRING; 44689.DDB0229964; -.
DR PaxDb; Q54TA1; -.
DR PRIDE; Q54TA1; -.
DR EnsemblProtists; EAL66509; EAL66509; DDB_G0281899.
DR GeneID; 8623302; -.
DR KEGG; ddi:DDB_G0281899; -.
DR dictyBase; DDB_G0281899; drkC.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_371524_0_0_1; -.
DR InParanoid; Q54TA1; -.
DR OMA; WKINTER; -.
DR PRO; PR:Q54TA1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0032010; C:phagolysosome; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0001845; P:phagolysosome assembly; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01833; TIG; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..749
FT /note="Probable serine/threonine-protein kinase drkC"
FT /id="PRO_0000358883"
FT TOPO_DOM 32..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..749
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 491..749
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 124..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 615
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 497..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 749 AA; 83465 MW; 7872FEE45D33BAB6 CRC64;
MIIINKYIRM NKIAILFSFF ILICCTGYSI SYKINGINEN KVLSLSSSPS PSSSSSSSQI
LEKGKEEIKK IKKTNKNKLL YNVAIVDLEP KLEIEQELLT RNNKKKMEMK EEMDIAMMMM
KAADRTDQVS TSSSSSSFSE ENKKSSSDDS APAIQSNLTF SGYMTGGEQV CDPKSCNSPS
VFTQNYLCNT SSAWANGYVF HDPVPPTGLF VVHKIVVTFT GMFNVIPPTS MVFSLVNGEE
NAGIFFISKS SPSQCPNCQI SFSPRTLPDV DPNGLASYRY GSNNSIIFNL FETDVACIGK
VTANIFYGPV AFKVNSVVPN TAPSTGGETV YFIGEQFYQS SQIQCKFGTV ISTGTYINST
CASCVVPPML QSNSTTPSDY NVTIQLSEDG GSSFCLNTTF FIYTAASIPF VKPTSPNYQK
IIYIVVGVGI AVLLIIAVGI YFIIRLRIKN KRLNGSKHAL PIGINDDERS PLLKTDYKTL
FEIKPIDISE IVVQNRIGRG SCAEVFTGTW RGIIVAIKKA KLLNEDDEDF LNELAQEATI
MSQLRHPNIC QFLGTCNNPP EILIVMEYMP LGSLYRILHD PSISLDWPRM KSMALDIAKG
MNYLHCCDPI VIHRDLKSHN LLVDEHYRVK ISDFGLSTRF KKHLDKKTAM TPVGTPCWTA
PEVLRNDPYT EKADVFSFAI VLWEIVTRED PYQGMPTFQI VISVGQHKLR PIVPPQVSAP
FTRLITECWS EDPQQRPSFQ EIVKRLEAM
