ID A0A2K6G4T3_PROCO Unreviewed; 445 AA.
AC A0A2K6G4T3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-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:ENSPCOP00000021245.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000021245.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000021245.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6G4T3; -.
DR Ensembl; ENSPCOT00000031905.1; ENSPCOP00000021245.1; ENSPCOG00000022631.1.
DR GeneTree; ENSGT00940000157008; -.
DR Proteomes; UP000233160; Unplaced.
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 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:UP000233160};
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 216..444
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 115..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 51211 MW; 7077F1D41398AED1 CRC64;
ESKRRDGESW ESSRDCPWAT PQNTISCSLA DVMSEQLAKE LQLEEEAATF PEVVVTEGPF
ITGENIDTSS DLMLAQMLQM EFDREYDAQL RREEKKFNGD SKVSISFENY RKVHPYEDSD
SSEDEVDWQD TRDDPYRPAK PVPTPKKGFI GKGKDITTKH DEVVCGRKNT ARMENFAPGF
QVGDGIGMDL KLSNHVFNAL KQHAYSEERR SARLHEKKEH STAEKAVDPK TRLLMYKMVN
SGMLETITGC ISTGKESVVF HAYGGSMEDE KEDSKVIPTE CAIKVFKTTL NEFKNRDKYI
KDDFRFKDRF SKLNPRKIIR MWAEKEMHNL TRMQRAGIPC PTVVLLKKHI LVMSFIGHDQ
VPAPKLKEVK LSSEEMKEAY YQTLRLMQQL YNECTLVHAD LSEYNMLWHA GKVWLIDVSQ
SVEPTHPHGL EFLFRDCRNV SQVGM
//
