ID E3MYE2_CAERE Unreviewed; 510 AA.
AC E3MYE2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Serine/threonine-protein kinase RIO1 {ECO:0000256|ARBA:ARBA00016038, ECO:0000256|PIRNR:PIRNR038147};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038147};
GN Name=Cre-riok-1 {ECO:0000313|EMBL:EFP12083.1};
GN ORFNames=CRE_30047 {ECO:0000313|EMBL:EFP12083.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR038147};
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|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR038147};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR038147-3};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196,
CC ECO:0000256|PIRNR:PIRNR038147}.
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DR EMBL; DS268496; EFP12083.1; -; Genomic_DNA.
DR RefSeq; XP_003098834.1; XM_003098786.1.
DR AlphaFoldDB; E3MYE2; -.
DR STRING; 31234.E3MYE2; -.
DR EnsemblMetazoa; CRE30047.1; CRE30047.1; WBGene00057111.
DR GeneID; 9816428; -.
DR KEGG; crq:GCK72_000898; -.
DR CTD; 9816428; -.
DR eggNOG; KOG2270; Eukaryota.
DR HOGENOM; CLU_018693_4_3_1; -.
DR InParanoid; E3MYE2; -.
DR OMA; THAIGPN; -.
DR OrthoDB; 5481355at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0036093; P:germ cell proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0008406; P:gonad development; IEA:EnsemblMetazoa.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:EnsemblMetazoa.
DR GO; GO:0002119; P:nematode larval development; IEA:EnsemblMetazoa.
DR GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:EnsemblMetazoa.
DR GO; GO:0040026; P:positive regulation of vulval development; IEA:EnsemblMetazoa.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd05147; RIO1_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017407; Ser/Thr_kinase_Rio1.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR Pfam; PF01163; RIO1; 1.
DR PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038147};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038147};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038147};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038147};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038147}.
FT DOMAIN 118..353
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 426..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT ACT_SITE 307
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
SQ SEQUENCE 510 AA; 59104 MW; 27314DC90730CFFA CRC64;
MDRIEQLNLN IQNILDDVDI DPAETESSSE DEEEVVIEDK KIAEKIPEVS EEPEYSESDY
EDDNDIVDFA EATGDFTKKL NAARTHAIGP NAARNRLTVD VERHADTNED RKRKRVKDRA
DRATVEQVLD PRTRLVLFRL LQRGTLLNID GCISTGKEAN VYHATGTEND LAVKIYKTSI
LTFKDRERYV TGEFRYRHGY CKSNPRKMVA VWAEKEMRNL ARMHEVGLPV PKPHMLKGHV
LVMDFLGKDG WPAPLLKNAN LSTEDAEPMY VGLIRDMRRL YRECKLVHAD LSEFNMLVHD
GKLWIIDVSQ SVEQDHPHAL EFLRMDCNNV NKFFRELGVK VLSVRRLFEV IVDPLMNSKE
METIIEEERV LVNSEDDTLF MNAFIPHKLE HVLHFERDGK LAKDGIEANN PFQNIVSKID
LKGNGFGEEG SCSDDDDGEN EKKSRKKRAE PTEEEIEEKE RKIAMHTRNR DETAEERKLR
KAAVKEEKRD QRKEKTPKHV KKRAHRQHMK
//
