ID A0AA36CNA8_9BILA Unreviewed; 819 AA. AC A0AA36CNA8; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 27-MAR-2024, entry version 2. DE RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606}; GN ORFNames=MSPICULIGERA_LOCUS9879 {ECO:0000313|EMBL:CAJ0571474.1}; OS Mesorhabditis spiculigera. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Mesorhabditinae; OC Mesorhabditis. OX NCBI_TaxID=96644 {ECO:0000313|EMBL:CAJ0571474.1, ECO:0000313|Proteomes:UP001177023}; RN [1] {ECO:0000313|EMBL:CAJ0571474.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AF72 {ECO:0000313|EMBL:CAJ0571474.1}; RA Delattre M.; RL Submitted (JUN-2023) 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=2.7.11.1; CC Evidence={ECO:0000256|PIRNR:PIRNR000606}; 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; Evidence={ECO:0000256|PIRNR:PIRNR000606}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|PIRNR:PIRNR000606}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. S6 kinase subfamily. CC {ECO:0000256|ARBA:ARBA00009804, ECO:0000256|PIRNR:PIRNR000606}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CAJ0571474.1}. 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; CATQJA010002567; CAJ0571474.1; -; Genomic_DNA. DR Proteomes; UP001177023; Unassembled WGS sequence. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR016239; Ribosomal_S6_kinase_II. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24351:SF175; CHROMOSOMAL SERINE_THREONINE-PROTEIN KINASE JIL-1; 1. DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. DR Pfam; PF00069; Pkinase; 2. DR Pfam; PF00433; Pkinase_C; 1. DR PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000606}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000606}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000606}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PIRNR:PIRNR000606}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000606}. FT DOMAIN 71..338 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 339..407 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT DOMAIN 436..699 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 30..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 751..819 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 30..56 FT /note="Polar residues" 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" FT BINDING 465 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CAJ0571474.1" SQ SEQUENCE 819 AA; 92296 MW; FC867D293F3C42C5 CRC64; MTTSVFFNFE QLPQPSYHCW SFGTSSSQYE YPTPPSSNEQ HAEMNSSRPN SNLRKNSMDL PDEEKVDMSS FALLRVLGKG AYGKVYLVRK VGGKDHGTIY AMKVLRKTRV ISKPKTLEHT MAERQVLEKL RGVPFLVNLF YAFQTDTKLH IVMEYVRGGE LFTHLCSRGH FDVPAARVIV AELIVAIDNL HKKNIIYRDL KLENILLDEE GHVKLTDFGL SKLLIPEELM RANSYCGTIE YMSPEVINRP EGGYTDVVDW WSLGVITFEL LTGCSPFTVD GGGNSSKDIA KRILTKKVPF PKNMDNDARS FIGALLDKQL EKRLGFNGVH ELKEHPFLKS IDWDQAERHE LKPAIVPNVV DEMDTTYFAQ EFTNQPPLYS PADAPINSNQ LFRGYSYISP SVMFANNNVI GEELMEEDVQ DLLKNSPFFN KYKLDTTDQG FLGKGSFSVC RRCTRNSDGA VFAVKIISQK FASQAQREAA ILQMVRGHVN IVHMEEMLSD SLHFYIIMEL LAGQELLMRI RRLQQFTECE ASGIMKQLVI AVSFLHSKRI VHRDLKPENI LFESDDPEAK LRLVDFGFAR LLPNSIEQQL KTPCYSLQYA APEVLDIGDS LPEYNEQCDL WSLGVILFTM LSGQVPFRAR SKTESATDIM ERIRAASFSF ESESWKSVSS EAKELITGLL TVDPKKRLTM DKLIRHPWLN ANSINTPLQT PSILPSHADQ SFNEMLQAFL SANRDGFHLL DVAAAPLLKR RLGQKRQSGD GPTAGSAKRQ PIFEPVPEGE ESSSVGRPTT LGLASPDALL AYRDPLPGTL RETRDSNES //