ID DRKB_DICDI Reviewed; 690 AA. AC Q54H45; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 27-NOV-2024, entry version 114. DE RecName: Full=Probable serine/threonine-protein kinase drkB; DE EC=2.7.11.1; DE AltName: Full=Receptor-like kinase 2; DE AltName: Full=Receptor-like kinase B; DE AltName: Full=Vesicle-associated receptor tyrosine kinase-like protein 2; DE Flags: Precursor; GN Name=drkB; Synonyms=rk2; ORFNames=DDB_G0289709; 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000148; EAL62566.1; -; Genomic_DNA. DR RefSeq; XP_636073.1; XM_630981.1. DR AlphaFoldDB; Q54H45; -. DR SMR; Q54H45; -. DR STRING; 44689.Q54H45; -. DR GlyCosmos; Q54H45; 4 sites, No reported glycans. DR GlyGen; Q54H45; 4 sites. DR PaxDb; 44689-DDB0229954; -. DR EnsemblProtists; EAL62566; EAL62566; DDB_G0289709. DR GeneID; 8627283; -. DR KEGG; ddi:DDB_G0289709; -. DR dictyBase; DDB_G0289709; drkB. DR VEuPathDB; AmoebaDB:DDB_G0289709; -. DR eggNOG; KOG0192; Eukaryota. DR HOGENOM; CLU_399254_0_0_1; -. DR InParanoid; Q54H45; -. DR OMA; SPDICIC; -. DR Reactome; R-DDI-5675482; Regulation of necroptotic cell death. DR PRO; PR:Q54H45; -. 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:0044024; F:histone H2AS1 kinase activity; IEA:UniProtKB-EC. 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:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd13999; STKc_MAP3K-like; 1. DR FunFam; 1.10.510.10:FF:000476; PAS domain-containing protein tyrosine kinase family protein; 1. DR FunFam; 3.30.200.20:FF:000060; Serine/threonine-protein kinase isoform 1; 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 InterPro; IPR050167; Ser_Thr_protein_kinase. DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1. DR PANTHER; PTHR23257:SF921; SERINE_THREONINE-PROTEIN KINASE DRKA-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..24 FT /evidence="ECO:0000255" FT CHAIN 25..690 FT /note="Probable serine/threonine-protein kinase drkB" FT /id="PRO_0000358882" FT TRANSMEM 346..366 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 391..644 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 51..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 287..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 649..690 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..319 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 650..690 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 514 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 397..405 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 418 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 250 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 690 AA; 76041 MW; 5A0A8373D8D4DFE5 CRC64; MKVQIVFFSI TVFIFVLFLL SVESNTKIKI VPSFLENSNE IEDLYINLDS DSKSSEHTTS SSSSSNSKNK GDSSSSSSNS GSSSNSIISG DSNSKDAPTT SSDSLSPATP IPTDGLLSAS TYVTFTGGKV LCENITFCPN GYMYSSDYAC NYDIVQNDPA THRGDWNDGI KMFEDPLPKN TTIDQVEGIS FTISGAVGCQ VTSSATTLEF YIQDLLVLTN TTSRYDICTC GSCYVTFGTE VYKYNMLGYN ITGENKFQIQ VSVNSMCATT IGITLYYKPP TITPTPTITP TPTITPTPTI TPTVTPTATP STTPSTTPTT TPSTPTPTPT KSPYSGALSP QVKKYIIIAS SITGGLLISI FSFVFIRKRL NSKRSGYTQI KDGKDIDTQQ IKIGVRIGKG NFGEVYLGTW RGSQVAVKKL PAHNINENIL KEFHREINLM KNLRHPNVIQ FLGSCLISPD ICICTEYMPR GSLYSILHNE KIKISWSLVK RMMIDAAKGI IYLHGSTPVI LHRDLKSHNL LVDENWKVKV ADFGLSTIEQ QGATMTACGT PCWTSPEVLR SQRYTEKADV YSFGIILWEC ATRQDPYFGI PPFQVIFAVG REGMRPPTPK YGPPKYIQLL KDCLNENPSQ RPTMEQCLEI LESIETKGFD DIPVNNNNNN NSNNNENNNE NNNNSDNNNN DINYSNRVIN //