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Database: UniProt
Entry: A0A2Y9FNA2_PHYMC
LinkDB: A0A2Y9FNA2_PHYMC
Original site: A0A2Y9FNA2_PHYMC 
ID   A0A2Y9FNA2_PHYMC        Unreviewed;       519 AA.
AC   A0A2Y9FNA2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
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|RefSeq:XP_007127268.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007127268.1};
RN   [1] {ECO:0000313|RefSeq:XP_007127268.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007127268.1};
RG   RefSeq;
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   RefSeq; XP_007127268.1; XM_007127206.4.
DR   AlphaFoldDB; A0A2Y9FNA2; -.
DR   STRING; 9755.ENSPCTP00005031201; -.
DR   Ensembl; ENSPCTT00005034267; ENSPCTP00005031201; ENSPCTG00005022208.
DR   Ensembl; ENSPCTT00005034273; ENSPCTP00005031207; ENSPCTG00005022208.
DR   GeneID; 102980739; -.
DR   KEGG; pcad:102980739; -.
DR   CTD; 8780; -.
DR   InParanoid; A0A2Y9FNA2; -.
DR   OrthoDB; 5481355at2759; -.
DR   Proteomes; UP000248484; Chromosome 19.
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:UP000248484};
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          222..470
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
FT   REGION          121..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  58859 MW;  4BEE70EB186951AA CRC64;
     MDLVGVASPE PGPAAAWGPS KCPWATPQNT ISCSLSDVMS EQLAKELQLE EEAAAFPEVA
     VAEGPFITGE NIDTSSDLML AQMLQMEFDR EYDAQLRREE KKFNGDSKVS ISFENYRKVH
     PYEDSDSSED EVDWQDTRDD PYRPAKPVPT PKKGFIGKGK DITTKHDEVV CGRKNTARME
     NFAPGFQVGD GIGMDLKLSN HVFNALKQHA YSEERRSARL HEKKEHSTAE KAVDPKTRLL
     MYKMVNCGML ETITGCISTG KESVVFHAYG GSMEDEKEDS KVIPTECAIK VFKTTLNEFK
     NRDKYIKDDF RFKDRFSKLN PRKIIRMWAE KEMHNLTRMQ RAGIPCPTVV LLKKHILVMS
     FIGHDQVPAP KLKEVKLSSE EMKEAYYQTL HLMQQLYNEC TLVHADLSEY NMLWHAGKVW
     LIDVSQSVEP THPHGLEFLF RDCRNVSQFF QKGGVKEALS ERELFNAVSG LNISADNEAD
     FLAEIEALEK MNEDHVQKNG RKAASFLKDD GGPPVLYDE
//
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