RIOK3_CAEEL
ID RIOK3_CAEEL Reviewed; 510 AA.
AC P34649;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine/threonine-protein kinase RIO3 {ECO:0000250|UniProtKB:O14730};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=riok-3; ORFNames=ZK632.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP 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 -!- 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:0000305};
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:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- TISSUE SPECIFICITY: Expressed in tail neurons (PVQ and PHAL/PQR).
CC {ECO:0000269|PubMed:25688864}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no obvious
CC phenotype. {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; Z22181; CAA80180.1; -; Genomic_DNA.
DR PIR; S40935; S40935.
DR RefSeq; NP_499173.1; NM_066772.7.
DR AlphaFoldDB; P34649; -.
DR SMR; P34649; -.
DR STRING; 6239.ZK632.3.1; -.
DR EPD; P34649; -.
DR PaxDb; P34649; -.
DR PeptideAtlas; P34649; -.
DR PRIDE; P34649; -.
DR EnsemblMetazoa; ZK632.3.1; ZK632.3.1; WBGene00014012.
DR GeneID; 176387; -.
DR KEGG; cel:CELE_ZK632.3; -.
DR UCSC; ZK632.3.1; c. elegans.
DR CTD; 176387; -.
DR WormBase; ZK632.3; CE00420; WBGene00014012; riok-3.
DR eggNOG; KOG2269; Eukaryota.
DR GeneTree; ENSGT00940000157008; -.
DR HOGENOM; CLU_018693_5_0_1; -.
DR InParanoid; P34649; -.
DR OMA; IMCRMYK; -.
DR OrthoDB; 1238900at2759; -.
DR PhylomeDB; P34649; -.
DR PRO; PR:P34649; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00014012; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017406; Ser/Thr_kinase_Rio3.
DR PIRSF; PIRSF038146; Ser/Thr_PK_RIO3; 1.
DR SMART; SM00090; RIO; 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..510
FT /note="Serine/threonine-protein kinase RIO3"
FT /id="PRO_0000213533"
FT DOMAIN 235..510
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 100..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 241..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 510 AA; 58566 MW; 3A3F689A8EE62CA6 CRC64;
MANCENNPWK KNAWGKNEET AEEPIVSFAD VLSEEFIEDL SVQEKLEEER YMKQLDQMFG
DTSVSDDQLP INTEGMTDEE VALALQRHFD READVARAVG SSSSVHFTPD RYHPKTMQET
DSENEDDDAL RQAATDMLYA KLDEENATNS RLRPEGPSTS RTKHDTGVSG RRNADKTFND
RNTLPTGDMV GDKLNNKVFN KLMAFGKSES KRQMRNKDKE EKATMDTSVD SDTRLLLLKW
INQGVFDSVD GIIATGKESA VLHAAQDSAT SYAIKVYKTT LSEFKNRSEY VKDDFRFKNP
RGVLKIWAER EFMNLSRMAK HGLPCPQPVK VRRNVLVMSF LGDQGLAAPR LKNVEWEFFT
DDERRNVYDQ VQSIMCRMYK ECLLVHADLS EFNLLLTPDN KVHVIDVSQA MDLSHPRSLQ
FLTRDIQNII TFFTRIGTPN LPTYVQLFNL ITDLDMVEDH DLLVQVEQFS EENRSVDLRH
DKSRPADMEL KKYNEEKKAN RGISPAREYN
