ID A0A2I3H8B1_NOMLE Unreviewed; 598 AA.
AC A0A2I3H8B1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Serine/threonine-protein kinase RIO3 {ECO:0000256|PIRNR:PIRNR038146};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038146};
GN Name=RIOK3 {ECO:0000313|Ensembl:ENSNLEP00000039707.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000039707.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000039707.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000039707.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in regulation of type I interferon (IFN)-dependent
CC immune response which plays a critical role in the innate immune
CC response against DNA and RNA viruses. {ECO:0000256|PIRNR:PIRNR038146}.
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:PIRNR038146};
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:PIRNR038146};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR038146};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196,
CC ECO:0000256|PIRNR:PIRNR038146}.
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DR EMBL; ADFV01007141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01007142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3H8B1; -.
DR STRING; 61853.ENSNLEP00000039707; -.
DR Ensembl; ENSNLET00000048035.1; ENSNLEP00000039707.1; ENSNLEG00000006758.3.
DR GeneTree; ENSGT00940000157008; -.
DR InParanoid; A0A2I3H8B1; -.
DR OMA; HDPQLCA; -.
DR Proteomes; UP000001073; Chromosome 4.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0089720; F:caspase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1990786; P:cellular response to dsDNA; IEA:Ensembl.
DR GO; GO:0071359; P:cellular response to dsRNA; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR CDD; cd05146; RIO3_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; IPR017406; Ser/Thr_kinase_Rio3.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF1; SERINE_THREONINE-PROTEIN KINASE RIO3; 1.
DR Pfam; PF01163; RIO1; 1.
DR PIRSF; PIRSF038146; Ser/Thr_PK_RIO3; 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};
KW Immunity {ECO:0000256|PIRNR:PIRNR038146};
KW Innate immunity {ECO:0000256|PIRNR:PIRNR038146};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038146};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR038146};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR038146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038146};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038146};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038146}.
FT DOMAIN 301..549
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 200..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 67393 MW; 84671649D898287E CRC64;
MAVRGQGRAW AKGSHTQFLP CPGRAANCKR LGRKRRDPVP DAAAAVAQPV ALAPPVSSAE
PASRPATSLL CSCFCLHPRM DLVGVASPEP GPAAAWGPSK CPWAIPQNTI SCSLADVMSE
QLAKELQLEE EAAVFPEVAV AEGPFITGEN IDTSSDLMLA QMLQMEYDRE YDAQLRREEK
KFNGDSKVSI SFENYRKVHP YEDSDSSEDE VDWQDTRDDP YRPAKPVPTP KKGFIGKGKD
ITTKHDEVVC GRKNTARMEN FAPEFQVGDG IGMDLKLSNH VFNALKQHAY SEERRSARLH
EKKEHSTAEK AVDPKTRLLM YKMVNSGMLE TITGCISTGK ESVVFHAYGG SMEDEKEDSK
VIPTECAIKV FKTTLNEFKN RDKYIKDDFR FKDRFSKLNP RKIIRMWAEK EMHNLTRMQR
AGIPCPTVVL LKKHILVMSF IGHDQVPALK LKEVKLNSEE MKEAYYQTLH LMRQLYHECT
LVHADLSEYN MLWHAGKVWL IDVSQSVEPT HPHGLEFLFR DCRNVSQFFQ KGGVKEALSE
RELFNAVSGL NISADNEADF LAEIEALEKM NEDHVQKNGR KAASFLKDDG DPPLLYDE
//
