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DRKA_DICDI
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   03-AUG-2022, entry version 108.
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 (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; EAL62607.1; -; Genomic_DNA.
DR   RefSeq; XP_636072.1; XM_630980.1.
DR   AlphaFoldDB; Q54H46; -.
DR   SMR; Q54H46; -.
DR   STRING; 44689.DDB0230060; -.
DR   PaxDb; Q54H46; -.
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: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:0004713; F:protein tyrosine kinase activity; IDA:dictyBase.
DR   GO; GO:0097677; F:STAT family protein binding; IPI:dictyBase.
DR   GO; GO:0097696; P:receptor signaling pathway via STAT; IMP:dictyBase.
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..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
 
 
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