ID RIOK2_CAEEL Reviewed; 529 AA. AC Q95Q34; DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 2. DT 12-OCT-2022, entry version 144. DE RecName: Full=Serine/threonine-protein kinase RIO2 {ECO:0000250|UniProtKB:Q9BVS4}; DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P40160}; GN Name=riok-2 {ECO:0000312|WormBase:Y105E8B.3}; GN ORFNames=Y105E8B.3 {ECO:0000312|WormBase:Y105E8B.3}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940}; RN [1] {ECO:0000312|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] {ECO:0000305} RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=25688864; DOI=10.1371/journal.pone.0117444; RA Mendes T.K., Novakovic S., Raymant G., Bertram S.E., Esmaillie R., RA Nadarajan S., Breugelmans B., Hofmann A., Gasser R.B., Colaiacovo M.P., RA Boag P.R.; RT "Investigating the role of RIO protein kinases in Caenorhabditis elegans."; RL PLoS ONE 10:E0117444-E0117444(2015). CC -!- FUNCTION: Required for larval development. CC {ECO:0000269|PubMed:25688864}. 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:0000250|UniProtKB:P40160}; 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:0000250|UniProtKB:P40160}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; CC -!- TISSUE SPECIFICITY: Expressed in pharynx (metacorpus and posterior CC bulbus). Expression is restricted to adult stage. CC {ECO:0000269|PubMed:25688864}. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes early larval CC arrest. In adults, results in no obvious phenotype. CC {ECO:0000269|PubMed:25688864}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr CC kinase family. {ECO:0000305}. 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; BX284601; CAC70109.2; -; Genomic_DNA. DR RefSeq; NP_493544.2; NM_061143.5. DR AlphaFoldDB; Q95Q34; -. DR SMR; Q95Q34; -. DR STRING; 6239.Y105E8B.3.2; -. DR EPD; Q95Q34; -. DR PaxDb; Q95Q34; -. DR PeptideAtlas; Q95Q34; -. DR EnsemblMetazoa; Y105E8B.3.1; Y105E8B.3.1; WBGene00013688. DR GeneID; 173322; -. DR KEGG; cel:CELE_Y105E8B.3; -. DR UCSC; Y105E8B.3; c. elegans. DR CTD; 173322; -. DR WormBase; Y105E8B.3; CE33542; WBGene00013688; riok-2. DR eggNOG; KOG2268; Eukaryota. DR GeneTree; ENSGT00390000003255; -. DR HOGENOM; CLU_018693_0_3_1; -. DR InParanoid; Q95Q34; -. DR OMA; MIHHENT; -. DR OrthoDB; 1010730at2759; -. DR PhylomeDB; Q95Q34; -. DR Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR PRO; PR:Q95Q34; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00013688; Expressed in adult organism and 4 other tissues. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion 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:0030490; P:maturation of SSU-rRNA; IBA:GO_Central. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR CDD; cd05144; RIO2_C; 1. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR030484; Rio2. DR InterPro; IPR015285; RIO2_wHTH_N. DR InterPro; IPR000687; RIO_kinase. DR InterPro; IPR018935; RIO_kinase_CS. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR Pfam; PF09202; Rio2_N; 1. DR SMART; SM00090; RIO; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS01245; RIO1; 1. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..529 FT /note="Serine/threonine-protein kinase RIO2" FT /evidence="ECO:0000305" FT /id="PRO_0000434606" FT DOMAIN 97..273 FT /note="Protein kinase" FT /evidence="ECO:0000305" FT REGION 331..366 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 411..452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 336..363 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 411..430 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..450 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 228 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:O30245" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O30245" SQ SEQUENCE 529 AA; 60485 MW; 0671C8143EFB8D21 CRC64; MGRMNVSMMR YLEGDHFRVL IAVEMGMKNH EVVPLALVSA IAGIHRGGVA RTLNDLCKHS LVAFERSKKF DGYRLTIRGY DYLALRALCS REVVGSVGNQ IGIGKESDVY VGGDPELNDL CLKFHRLGRT SFRKIKEKRD YHKKRKSASW LYLSRLAAAK EFAFLKALQE RGFPVPKAVD VCRHLVVMQL VVGQTLCNVT HVEDAGALYD RLMALIVKMA RHGVIHGDFN EFNLIMLEDE RIVMIDFPQM VSIDHPNAEY YFDRDVTCVR TFFKRKFDYE SEDWPKFDEV ERKGNMDVLL EASGFTKKMA LDLNKAYDEG DFLAHCEQEL RNRQEEDLGE DEDDSDDSKS MEDIQEEPED LEKDHEELQA QENTVKQQKI VLSQTTRFTD WLSDATNQLE AVDLDALKSE EGYKDIELPP EDFKRPADSE NDDENDEDEE EGEEEDADGH VAVEEQVAKV VKKKRVPSGA RSVASSAATF TAEDVKRRLA LDRKRNKEKI RLKVKGKQSA VGRNRKDNKD VIAEYAGWI //