ID DRKA_DICDI Reviewed; 642 AA.
AC Q54H46;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE RecName: Full=Probable serine/threonine-protein kinase drkA;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like kinase 1;
DE AltName: Full=Receptor-like kinase A;
DE AltName: Full=Vesicle-associated receptor tyrosine kinase-like protein 1;
DE Flags: Precursor;
GN Name=drkA; Synonyms=rk1, vsk1; ORFNames=DDB_G0289791;
OS Dictyostelium discoideum (Social amoeba).
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; AAFI02000148; EAL62607.1; -; Genomic_DNA.
DR RefSeq; XP_636072.1; XM_630980.1.
DR AlphaFoldDB; Q54H46; -.
DR SMR; Q54H46; -.
DR STRING; 44689.Q54H46; -.
DR GlyCosmos; Q54H46; 5 sites, No reported glycans.
DR PaxDb; 44689-DDB0230060; -.
DR ABCD; Q54H46; 4 sequenced antibodies.
DR EnsemblProtists; EAL62607; EAL62607; DDB_G0289791.
DR GeneID; 8627282; -.
DR KEGG; ddi:DDB_G0289791; -.
DR dictyBase; DDB_G0289791; drkA.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_399254_0_0_1; -.
DR InParanoid; Q54H46; -.
DR OMA; FENTIPV; -.
DR PRO; PR:Q54H46; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0097677; F:STAT family protein binding; IPI:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0097696; P:receptor signaling pathway via STAT; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_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 PANTHER; PTHR44329:SF146; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..642
FT /note="Probable serine/threonine-protein kinase drkA"
FT /id="PRO_0000358881"
FT TOPO_DOM 24..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 374..627
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 106..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 380..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 642 AA; 72324 MW; 951910C4C96E86A5 CRC64;
MKKLPFLIII IYIFLILISI SSSIDYNYNN DIDNNNNNII NRNKNKNKNN LYNNKVIIKN
DDNDDEINNK FKIRLDDNED QDIYNEYHFL SKVHNRLAFN IFGSSSENSG SGSNSNSNSK
NTDSSTGPTP SPISINGTLN STATVYWSGG KSSCKSVNCT EEGFSTGDSY ACSYEITPTY
QRGQWEKGVK YFKDPLPKSI LTSQVVGVSF VINGVVGCTP LKQELTTIEF LIQDVQVGQT
ISTNRSDDCS CGICYKDYEI LPQSYDLLGY NKSGLNKVQL LLLDNSICAT SLDIIFYYHP
STIPPTPTPT PSKPTISLLK KYLIIGFSIV GGLLIIGGCF LLIRNRYRSS GYYKPDKNDY
TQIKDGKDID IHQIKIGVRI GKGNYGEVYL GTWRGSQVAV KKLPAHNINE NILKEFHREI
NLMKNLRHPN VIQFLGSCLI PPDICICTEY MPRGSLYSIL HDQALQLQWS LLIKMMIDAA
KGVIYLHNST PVILHRDLKS HNLLVDENWK VKVADFGLST IEQQGATMTA CGTPCWTSPE
VLRSQRYTEK ADVYSFGIIL WECATRQDPY FGIPPFQVIF AVGREGMRPP VPQNGPPKYI
QLLIDCLNEN PSHRPTMEQC LERLESIDSS GYSDLQYVRQ QL
//