ID Q4R6R5_MACFA Unreviewed; 614 AA.
AC Q4R6R5;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Serine/threonine-protein kinase RIO3 {ECO:0000256|PIRNR:PIRNR038146};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038146};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|EMBL:BAE01209.1};
RN [1] {ECO:0000313|EMBL:BAE01209.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15944441; DOI=10.1093/molbev/msi187;
RA Osada N., Hirata M., Tanuma R., Kusuda J., Hida M., Suzuki Y., Sugano S.,
RA Gojobori T., Shen C.K., Wu C.I., Hashimoto K.;
RT "Substitution rate and structural divergence of 5'UTR evolution:
RT comparative analysis between human and cynomolgus monkey cDNAs.";
RL Mol. Biol. Evol. 22:1976-1982(2005).
RN [2] {ECO:0000313|EMBL:BAE01209.1}
RP NUCLEOTIDE SEQUENCE.
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB169115; BAE01209.1; -; mRNA.
DR RefSeq; NP_001271012.1; NM_001284083.1.
DR AlphaFoldDB; Q4R6R5; -.
DR OrthoDB; 5481355at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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 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 317..565
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 69551 MW; 62CB244DEBD236B6 CRC64;
MAVRGQGRAW AKGSHTQFLP CPARHRQRDT KRLSRRRGRK RRDPVPDAAA AVAAICHLQL
RHQQPVVPAP PVSSAEPASH LATSLLCSCL CLHPRMDLVG VASPEPGPAA AWGPSKCPWA
IPQNTISCSL ADVMSEQLAK ELQLEEEAAV FPEVAVAEGP FITGENIDTS SDLMLAQMLQ
MEYDREYDAQ LRREEKKFNG DSKVSISFEN YRKVHPYEDS DSSEDEVDWQ DTRDDPYRPA
KPVPTPKKGF IGKGKDITTK HDEVVCGRKN TARMENFAPE FQVGDGIGMD LKLSNHVFNA
LKQRAYSEER RSARLHEKKE HSTAEKAVDP KTRLLMYKMV NSGMLETITG CISTGKESVV
FHAYGGSMED EKEDSKVIPT ECAIKVFKTT LNEFKNRDKY IKDDFRFKDR FSKLNPRKII
RMWAEKEMHN LARMQTAGIP CPTVVLLKKH ILVMSFIGHD QVPAPKLKEV KLNSEEMKEA
YYQTLHLMRQ LYHECRLVHA DLSEYNMLWH AGKVWLIDVS QSVEPTHPHG LEFLFRDCRN
ASQFFQKGGV KEALSERELF NAVSGLNISA DNEADFLAEI EALEKMNEDH VQKNGRKAAS
FLKDDGDPPV LYYE
//
