ID E9HHQ5_DAPPU Unreviewed; 419 AA. AC E9HHQ5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 24-JAN-2024, entry version 63. DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011}; GN ORFNames=DAPPUDRAFT_114299 {ECO:0000313|EMBL:EFX68746.1}; OS Daphnia pulex (Water flea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda; OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX68746.1, ECO:0000313|Proteomes:UP000000305}; RN [1] {ECO:0000313|EMBL:EFX68746.1, ECO:0000313|Proteomes:UP000000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21292972; DOI=10.1126/science.1197761; RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A., RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J., RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q., RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D., RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D., RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J., RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M., RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y., RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H., RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R., RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P., RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.; RT "The ecoresponsive genome of Daphnia pulex."; RL Science 331:555-561(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000256|ARBA:ARBA00001171}; 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; GL732649; EFX68746.1; -; Genomic_DNA. DR AlphaFoldDB; E9HHQ5; -. DR STRING; 6669.E9HHQ5; -. DR EnsemblMetazoa; EFX68746; EFX68746; DAPPUDRAFT_114299. DR KEGG; dpx:DAPPUDRAFT_114299; -. DR eggNOG; KOG0200; Eukaryota. DR HOGENOM; CLU_000288_7_40_1; -. DR InParanoid; E9HHQ5; -. DR PhylomeDB; E9HHQ5; -. DR Proteomes; UP000000305; Unassembled WGS sequence. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR CDD; cd00192; PTKc; 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; IPR008266; Tyr_kinase_AS. DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS. DR PANTHER; PTHR24416:SF600; PDGF-AND VEGF-RECEPTOR RELATED, ISOFORM J; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 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; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Reference proteome {ECO:0000313|Proteomes:UP000000305}. FT DOMAIN 14..365 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 393..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..411 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 198 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1" FT BINDING 49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 203 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" SQ SEQUENCE 419 AA; 47477 MW; D4C5488D1A1B6772 CRC64; MGESGSYACQ WKVSFPGIQL GTGCFGRVVK AEAVGLKDSE EAVKTIAVKM VRSQANIEAM EALISELKIL VYLGSHLNVV NLLGACTKQI HKGELFVIVE YCRFGNLQTF LINHRNSFVN LVDEFGNLKT QHEIESNNFT RKPTYGINPS IFLADFNLEE ELDGNLDRSI STTNLISWSF QMARGMDYLV SKKVLHGDLA ARNILLADDG VAKVADFGMA KKMYYEDCYE KRGQGLLPVN WMAIESLTDR IFSSQSDVWS YGIVLWELFS LGRVPYPGWT FPSIIKMNCR GYEYVSVNLG MDVGHILMKE ILNGYRMDKP ELAPKFFGEM MADCWKSDPK ERPTFSQMEK VICGHMESSV SSDYLNMNAI YVKLNEDKEN ASPKEHFGLA KLLREKSETQ SKRDATRHSS FPIRFSKKR //