ID   RIO2_DICDI              Reviewed;         522 AA.
AC   Q54T05;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Serine/threonine-protein kinase rio2;
DE            EC=2.7.11.1;
GN   Name=rio2; ORFNames=DDB_G0282099;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Required for the final endonucleolytic cleavage of 20S pre-
CC       rRNA at site D in the cytoplasm, converting it into the mature 18S
CC       rRNA. Involved in normal export of the pre-40S particles from the
CC       nucleus to the cytoplasm (By similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Component of a late pre-40S ribosomal particle. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000045; EAL66375.1; -; Genomic_DNA.
DR   RefSeq; XP_640350.1; XM_635258.1.
DR   AlphaFoldDB; Q54T05; -.
DR   SMR; Q54T05; -.
DR   STRING; 44689.DDB0216429; -.
DR   PaxDb; Q54T05; -.
DR   EnsemblProtists; EAL66375; EAL66375; DDB_G0282099.
DR   GeneID; 8623405; -.
DR   KEGG; ddi:DDB_G0282099; -.
DR   dictyBase; DDB_G0282099; rio2.
DR   eggNOG; KOG2268; Eukaryota.
DR   HOGENOM; CLU_018693_0_3_1; -.
DR   InParanoid; Q54T05; -.
DR   OMA; MIHHENT; -.
DR   PhylomeDB; Q54T05; -.
DR   Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q54T05; -.
DR   Proteomes; UP000002195; Chromosome 3.
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; ISS:dictyBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:0006468; P:protein phosphorylation; ISS:dictyBase.
DR   CDD; cd05144; RIO2_C; 1.
DR   Gene3D; 1.10.10.10; -; 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   Pfam; PF09202; Rio2_N; 1.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01245; RIO1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..522
FT                   /note="Serine/threonine-protein kinase rio2"
FT                   /id="PRO_0000373994"
FT   DOMAIN          93..248
FT                   /note="Protein kinase"
FT   REGION          313..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..357
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..411
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        226
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   522 AA;  61089 MW;  2B0EEBB155E43118 CRC64;
     MKLDPKALRY LSKDDFRTLV AVEMGMKNHE LVPVSLICTI ANLKYGGTKK SIQTLHKFKL
     LFHDGRNYDG YKLTYLGYDF LALKTLVSRG VCSYVGNQIG VGKESDIYIV ANDDNQEMVL
     KLHRLGRVSF KTIKNNRDYL KHRKSASWLY LSRLAALKEF AYMKALYENG FPVPTPIDYN
     RHCIVMSRAR GYPLTQIVQL RHPSKVYSDL MNLIVKLASY GLIHGDFNEF NILINDEEEI
     TLIDFPQMVS TSHLNAEMYF DRDVTCIRVF FEKRFNFIGE RWPKFKDCQN IHSLDVEISA
     SGFTRDMEKE FQDLSKQQDD DEINNNDSDE NDEDDDEDDD DDDENNDDDE NNDNNIENEN
     EENIKKSSKV NKKEVGKEIK KEEEENNNSE EEDEEEEEEE DSDSEESVED NTPVIEEFKG
     LSLNKNRDFK FSNLKDEDQN APIVLRKEFI ENLDENQPTE PKKEKVELTE EEKQRRKEEK
     RQKMITDKVK RQLGKTMREK VSVRNNVKSR TKKEVQAHIS SY