DRKB_DICDI
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 03-AUG-2022, entry version 104.
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 (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; AAFI02000148; EAL62566.1; -; Genomic_DNA.
DR RefSeq; XP_636073.1; XM_630981.1.
DR AlphaFoldDB; Q54H45; -.
DR SMR; Q54H45; -.
DR STRING; 44689.DDB0229954; -.
DR PaxDb; Q54H45; -.
DR EnsemblProtists; EAL62566; EAL62566; DDB_G0289709.
DR GeneID; 8627283; -.
DR KEGG; ddi:DDB_G0289709; -.
DR dictyBase; DDB_G0289709; drkB.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_399254_0_0_1; -.
DR InParanoid; Q54H45; -.
DR OMA; SPDICIC; -.
DR PRO; PR:Q54H45; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
