ID A0A9N9S298_9DIPT Unreviewed; 952 AA. AC A0A9N9S298; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 29-MAY-2024, entry version 5. DE RecName: Full=dual-specificity kinase {ECO:0000256|ARBA:ARBA00013203}; DE EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203}; GN ORFNames=CHIRRI_LOCUS10898 {ECO:0000313|EMBL:CAG9808052.1}; OS Chironomus riparius. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae; OC Chironominae; Chironomus. OX NCBI_TaxID=315576 {ECO:0000313|EMBL:CAG9808052.1, ECO:0000313|Proteomes:UP001153620}; RN [1] {ECO:0000313|EMBL:CAG9808052.1} RP NUCLEOTIDE SEQUENCE. RA King R.; RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAG9808052.1} RP NUCLEOTIDE SEQUENCE. RG ENA_rothamsted_submissions; RG culmorum; RA King R.; RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases. 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=2.7.12.1; CC Evidence={ECO:0000256|ARBA:ARBA00000972}; 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=2.7.12.1; Evidence={ECO:0000256|ARBA:ARBA00001076}; 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=2.7.12.1; CC Evidence={ECO:0000256|ARBA:ARBA00001687}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. {ECO:0000256|ARBA:ARBA00005843}. 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; OU895879; CAG9808052.1; -; Genomic_DNA. DR Proteomes; UP001153620; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:TreeGrafter. DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:TreeGrafter. 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 PANTHER; PTHR46485:SF5; CENTER DIVIDER, ISOFORM A; 1. DR PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Reference proteome {ECO:0000313|Proteomes:UP001153620}. FT DOMAIN 74..330 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 341..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 103 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 952 AA; 107403 MW; A191FB2A2B9B3915 CRC64; MIMNLTQNNY CGQGPGPPII NKTKNAVNNS STKSNEIISA HKEKILEQCS DRLVTGPSCR ALKTAVSALF SVDDFHREKI GSGFFSEVFK VTHRTTGEVM VLKMNQLRSN RPNMLREVQL LNKLSHPNIL KFMGVCVQEG QLHALTEFIP DGSLEQLIQN KAEYVSPTSK IQLALGIAKG MKYVHSINVF HRDLTSKNVL VRRFSNGELD AVVGDFGLAA KIPKKCGKFR LDTVGSPYWM SPECLNGKFY DQSSDVFSYG IILCELIARI DADPDILPRT DAFGLDYIAF VDLCPSDTLP AFLRIAFYCC NYDPKNRYTF NDVAKKLTLL LDDRNNDLIE DKTNSISPSN NSLNDISMSP SKEDIQNSKY NKRNSIDSTL NNNDNSCKES TNNKSYKHSI SESPPKQRNE SKVLPYTSLT YRRSYSSENI MLHTVPADKA RCHPLLNRTN NTSQQTINET DSNMTLRKIA ETMLLKDPKY KPRPKENSKL NPFTNLAQLR GVKKIIGANA NQLTPGTNDL FSSCFEMSSP FLKSLKELNY TKKKKKNQIP NEPKSLPSSP LIKRKDFNVD SLLPNYENVS SLMRSDSSAK CCKKYFDKLQ NHPLYKNGKQ EETDLCGSNS CKLRIIGLSA NPSNIKFTNT NCYESNCLME PISMAGKSLY ETPRLLTRRG STESGFFSCL NEDFCDKTRD YDQGACSYFC TCCLMSSTPS TSNEKKDDTS NVSTSISLRS LDDLDLTDTK LSQKLQHCIH HRIDVNTKSI DMGLINRLTL DSEINSIIQK HQLSNQLFYC KNRTSSIYSD SSDSLAGSDS LLWDDRSYSI PNTRSAQIAK IVEYFERKGS NFSASNFSVS GLKSNFSSST TSASNYLPSS NYHHHHKQLT DYFVDLRRDF HDIGSNNDSS NPNLTFKRDY ETFCFDFTEK KPSQNFHKIC EGSVRSKLPL FDKSKQGNQS EK //