ID Q9GSP5_DROME Unreviewed; 764 AA. AC Q9GSP5; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 02-SEP-2026, entry version 139. DE RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; GN Name=SRPK {ECO:0000313|FlyBase:FBgn0286813}; GN ORFNames=CG8174 {ECO:0000313|FlyBase:FBgn0286813}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAG15387.1}; RN [1] {ECO:0000313|EMBL:AAG15387.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11158320; DOI=10.1128/MCB.21.4.1345-1359.2001; RA Allemand E., Gattoni R., Bourbon H.M., Stevenin J., Caceres J.F., Soret J., RA Tazi J.; RT "Distinctive features of Drosophila alternative splicing factor RS domain: RT implication for specific phosphorylation, shuttling, and splicing RT activation."; RL Mol. Cell. Biol. 21:1345-1359(2001). 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 Evidence={ECO:0000256|ARBA:ARBA00048679, ECO:0000256|PROSITE- CC ProRule:PRU10027}; 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 Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. 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; AF301149; AAG15387.1; -; mRNA. DR AlphaFoldDB; Q9GSP5; -. DR UCSC; CG8174-RB; d. melanogaster. DR AGR; FB:FBgn0286813; -. DR FlyBase; FBgn0286813; SRPK. DR VEuPathDB; VectorBase:FBgn0286813; -. DR OrthoDB; 2649at2759; -. DR ExpressionAtlas; Q9GSP5; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR FunFam; 1.10.510.10:FF:001652; SR protein kinase, isoform D; 1. DR FunFam; 3.30.200.20:FF:000163; SRSF protein kinase 2 isoform X1; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR47634:SF9; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF00069; Pkinase; 2. 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PROSITE-ProRule:PRU00159}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}. FT DOMAIN 170..763 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 346..370 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 386..405 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 421..594 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..27 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..47 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 56..76 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..95 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 105..117 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 124..134 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..370 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 457..467 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 468..516 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 537..560 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 561..577 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 303 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" FT BINDING 199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 764 AA; 85090 MW; DCD502545D1C6A8F CRC64; MNKADVNRRV LAIQAKKKRH KSRKRGKQNG TNPQEQSNSS QNQNPKPSSN PIPEPNRSSE NLQAPDNANN SHLNAPSSAA FSKATATATA STSSGGSAGT PDQYQPPKKT QAKAKPNTQK EHQQQPPRSS SNESYESETF SDNEDQELME DYCKGGYHPV NIGDLFHDRY HVIRKLGWGH FSTVWLCWDL QAMGYVAIKI VKSAPHFAET ARDEIKILKT VRETDPSNPR RHKTVQMLDD FKITGVNGTH ICMVFEVLGD NLLKLIRKSN YRGIPLANVK TITRQVLEGL DYLHTCCKII HTDIKPENVL LCVDEPHVRS LATEATQLYC MNSKMYPSLV SRAPKEYREP PITGKMSKNR KKKLKKKAKK RMELFKQQRD YLEQADGQGA INPNEVQNGD AGISDADEYF DANSVEDNVH VAAGQPSRKQ RDERKAPPEQ SEEAQEQDPL TEGTDKAKKK KKKKNKNKSN QSKGQQPPQL ENSTSSAESS SALKSQQANG SNSTTNNKSN TNSSGTLKGQ SNGKKMPLRP KQEKQGSNHQ LNNNNSKPNS NSDSKISSGS VENTSSATNG PHSNSTLPTP PPPPQAKHKA KKDPALDECN VHVKIADLGN ACWVDRHFTE DIQTRQYRSL EVIIGAGYNT SADIWSTACM VFELATGDYL FEPHSGESYT RDEDHLAHII ELLGPIPREI LLNGTYAAKS FTRSCELRNI SGLKPWGLMD VLLEKYEWSQ KDAASFASFL TPMLEFDPNK RATAAECLQH PWLR //