ID A0A1S3FMF3_DIPOR Unreviewed; 545 AA.
AC A0A1S3FMF3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|RefSeq:XP_012877530.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012877530.1};
RN [1] {ECO:0000313|RefSeq:XP_012877530.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012877530.1};
RG RefSeq;
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}.
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DR RefSeq; XP_012877530.1; XM_013022076.1.
DR AlphaFoldDB; A0A1S3FMF3; -.
DR STRING; 10020.ENSDORP00000015381; -.
DR GeneID; 105989832; -.
DR KEGG; dord:105989832; -.
DR CTD; 55781; -.
DR InParanoid; A0A1S3FMF3; -.
DR OrthoDB; 21899at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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, ECO:0000313|RefSeq:XP_012877530.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
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..292
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 309..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 62228 MW; 22FE6C2C10F3809A CRC64;
MGKVNVAKLR YLSRDDFRVL TAVEMGMKNH EIVPCSLIAS IASLKHGGCN KVLRELVKHK
LIAWERTKTV QGYRLTNAGY DYLALKTLSS RQIVESVGNQ MGVGKESDIY IVANEEGQQF
ALKLHRLGRT SFRNLKNKRD YHKHRHSVSW LYLSRLSAMK EFAYMKALHD RKFPVPKPVD
YNRHAVVMEL INGYPLCQIH HVEDPASVYD EAMELIVKLA NHGLIHGDFN EFNLILDKDD
HITMIDFPQM VSTSHPNAEW YFDRDVKCIR DFFIKRFSYE SELYPTFNDI RREDSLDVEV
SASGYTKEMQ ADDELLHPVG PDEKNTETEE GSEFSLSDEE GLEKATVCRL EIESEQNSVD
EIGSSSGILE QIKEDVSEET ANAQNFEMTK FIEAIEEIKG QSVENNSLSQ CFEKNRAEND
SVQNGHTGQG CPAGFEEYED ECPRLIALSS LNKEFRPFRD EESVTSIKQY RTRTLSVTSA
GSAVSCSTIP PELVKLKVKR HLTKQQKSAA RRRLQKGEAN VFTKQRRENM QNIKSSLEAA
SFWGE
//