RIOK2_CAEEL
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 03-AUG-2022, entry version 143.
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}.
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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 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
