ID F1MBN7_BOVIN Unreviewed; 551 AA.
AC F1MBN7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=RIOK2 {ECO:0000313|Ensembl:ENSBTAP00000015624.3,
GN ECO:0000313|VGNC:VGNC:50056};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000015624.3, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000015624.3, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000015624.3,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000015624.3}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000015624.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; NP_001178220.1; NM_001191291.1.
DR AlphaFoldDB; F1MBN7; -.
DR SMR; F1MBN7; -.
DR STRING; 9913.ENSBTAP00000015624; -.
DR PaxDb; 9913-ENSBTAP00000015624; -.
DR Ensembl; ENSBTAT00000015624.4; ENSBTAP00000015624.3; ENSBTAG00000011763.4.
DR GeneID; 540772; -.
DR KEGG; bta:540772; -.
DR CTD; 55781; -.
DR VEuPathDB; HostDB:ENSBTAG00000011763; -.
DR VGNC; VGNC:50056; RIOK2.
DR eggNOG; KOG2268; Eukaryota.
DR GeneTree; ENSGT00390000003255; -.
DR HOGENOM; CLU_018693_0_3_1; -.
DR InParanoid; F1MBN7; -.
DR OMA; TSHHNAE; -.
DR OrthoDB; 21899at2759; -.
DR TreeFam; TF321400; -.
DR Reactome; R-BTA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000011763; Expressed in spermatid and 106 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000208; P:positive regulation of ribosomal small subunit export from nucleus; IEA:Ensembl.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IEA:Ensembl.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
DR CDD; cd05144; RIO2_C; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR Pfam; PF01163; RIO1; 1.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 66..289
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 316..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 63397 MW; DC4102544A649B6D CRC64;
MGKVNVAKLR YMSRDDFRVL TAVEMGMKNH EIVPCSLVAS IASLKHGGCN KVLRELVKHK
LIAWERTKTV QGYRLTNAGY DYLALKTLSS RQVVESVGNQ MGVGKESDIY IVANEEGQQF
ALKLHRLGRT SFRNLKNKRD YHKHRHNMSW LYLSRLSAMK EFAYMKALYE RKFPVPKPID
YNRHAVVMEL ISGYPLCQIH HVEDPASVYD EAMELIVKLA NHGLIHGDFN EFNLILDEDD
HITMIDFPQM VSTSHPNAEW YFDRDVKCIR DFFMKRFNYE SELFPTFSDI RREDSLDVEV
SASGYTKEMQ ADDELLHPAG PEDKNTETEE RSDFPFSDEE MSERARDCRS ENEGGWNCAA
ESVDCCCRSF ENLEQIKEES LSEDSADAHR FEMTEFSQAL EEIEGQVVEN SSVSEFSGEN
RRERDARQDG ETGQGGILVG PEEDEDECPH LIALSSLSKE FRPFRDEENM EDTNRHRTRT
LSVTSVGSVL SCSTIPPELV KQKVKRQLTK QQKSAVRRRL QKGEANTFTK QRRENMQNIK
SSLEAASFWG E
//
