RIO1_YEAST
ID RIO1_YEAST Reviewed; 484 AA.
AC Q12196; D6W2H8; Q00602;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Serine/threonine-protein kinase RIO1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:12135737};
DE EC=3.6.3.-;
DE AltName: Full=Ribosomal RNA-processing protein 10;
GN Name=RIO1; Synonyms=RRP10; OrderedLocusNames=YOR119C;
GN ORFNames=O3266, YOR3266C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-354.
RC STRAIN=ATCC 25657 / D273-10B;
RA Angermayr M.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11483523; DOI=10.1093/emboj/20.15.4204;
RA Vanrobays E., Gleizes P.-E., Bousquet-Antonelli C., Noaillac-Depeyre J.,
RA Caizergues-Ferrer M., Gelugne J.-P.;
RT "Processing of 20S pre-rRNA to 18S ribosomal RNA in yeast requires Rrp10p,
RT an essential non-ribosomal cytoplasmic protein.";
RL EMBO J. 20:4204-4213(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND MUTAGENESIS OF LYS-125 AND ASP-244.
RX PubMed=12135737; DOI=10.1016/s0014-5793(02)02993-9;
RA Angermayr M., Bandlow W.;
RT "RIO1, an extraordinary novel protein kinase.";
RL FEBS Lett. 524:31-36(2002).
RN [8]
RP FUNCTION.
RX PubMed=11972772; DOI=10.1046/j.1365-2958.2002.02881.x;
RA Angermayr M., Roidl A., Bandlow W.;
RT "Yeast Rio1p is the founding member of a novel subfamily of protein serine
RT kinases involved in the control of cell cycle progression.";
RL Mol. Microbiol. 44:309-324(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12612080; DOI=10.1128/mcb.23.6.2083-2095.2003;
RA Vanrobays E., Gelugne J.-P., Gleizes P.-E., Caizergues-Ferrer M.;
RT "Late cytoplasmic maturation of the small ribosomal subunit requires RIO
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:2083-2095(2003).
RN [10]
RP INTERACTION WITH CKA2, AND PHOSPHORYLATION AT SER-402; SER-403; SER-409;
RP SER-416; SER-417 AND SER-419.
RX PubMed=17725716; DOI=10.1111/j.1742-4658.2007.05993.x;
RA Angermayr M., Hochleitner E., Lottspeich F., Bandlow W.;
RT "Protein kinase CK2 activates the atypical Rio1p kinase and promotes its
RT cell-cycle phase-dependent degradation in yeast.";
RL FEBS J. 274:4654-4667(2007).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ASP-244 AND ASP-261.
RX PubMed=24948609; DOI=10.1093/nar/gku542;
RA Ferreira-Cerca S., Kiburu I., Thomson E., LaRonde N., Hurt E.;
RT "Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-
RT 40S biogenesis factors in 80S-like ribosomes.";
RL Nucleic Acids Res. 42:8635-8647(2014).
CC -!- FUNCTION: Required for the final endonucleolytic cleavage at site D
CC converting 20S pre-rRNA into the mature 18S rRNA. Required for the
CC final steps of cytoplasmic maturation of the 40S ribosomal subunit. The
CC association with the very late 40S subunit intermediate seems to follow
CC RIO2 association with precursors of the 40S subunit and may involve a
CC translation-like checkpoint point cycle preceeding the binding to the
CC 60S ribosomal subunit. Despite the protein kinase domain is proposed to
CC act predominantly as an ATPase. The catalytic activity regulates its
CC dynamic association with the 40S subunit. Has a role in the cell cycle
CC where it is required for entrance into S-phase and in the control of
CC the onset of anaphase. Appears to also be involved in the maintenance
CC of chromosome stability and correct mitotic segregation.
CC {ECO:0000250|UniProtKB:G0S3J5, ECO:0000269|PubMed:11483523,
CC ECO:0000269|PubMed:11972772, ECO:0000269|PubMed:12135737,
CC ECO:0000269|PubMed:24948609}.
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:0000269|PubMed:12135737};
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:0000269|PubMed:12135737};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12135737};
CC Note=Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity
CC with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
CC {ECO:0000305};
CC -!- SUBUNIT: Interacts with CKA2. {ECO:0000269|PubMed:17725716}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11483523,
CC ECO:0000269|PubMed:12135737, ECO:0000269|PubMed:12612080}.
CC -!- PTM: Autophosphorylated. Phosphorylated by casein kinase II (CK2).
CC Phosphorylation by CK2 stimulates RIO1 kinase activity and targets it
CC for degradation at the G1/S transition of the cell cycle.
CC {ECO:0000269|PubMed:12135737, ECO:0000269|PubMed:17725716}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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 EMBL; X90518; CAA62127.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64039.1; -; Genomic_DNA.
DR EMBL; Z75027; CAA99317.1; -; Genomic_DNA.
DR EMBL; X96739; CAA65511.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10894.1; -; Genomic_DNA.
DR PIR; S61006; S61006.
DR RefSeq; NP_014762.3; NM_001183538.3.
DR AlphaFoldDB; Q12196; -.
DR SMR; Q12196; -.
DR BioGRID; 34515; 264.
DR DIP; DIP-4146N; -.
DR IntAct; Q12196; 65.
DR MINT; Q12196; -.
DR STRING; 4932.YOR119C; -.
DR iPTMnet; Q12196; -.
DR MaxQB; Q12196; -.
DR PaxDb; Q12196; -.
DR PRIDE; Q12196; -.
DR EnsemblFungi; YOR119C_mRNA; YOR119C; YOR119C.
DR GeneID; 854286; -.
DR KEGG; sce:YOR119C; -.
DR SGD; S000005645; RIO1.
DR VEuPathDB; FungiDB:YOR119C; -.
DR eggNOG; KOG2270; Eukaryota.
DR GeneTree; ENSGT00940000157075; -.
DR HOGENOM; CLU_018693_4_1_1; -.
DR InParanoid; Q12196; -.
DR OMA; QEINGCI; -.
DR BioCyc; YEAST:G3O-33648-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q12196; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12196; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030874; C:nucleolar chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:SGD.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007096; P:regulation of exit from mitosis; IDA:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017407; Ser/Thr_kinase_Rio1.
DR PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Hydrolase; Kinase;
KW Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..484
FT /note="Serine/threonine-protein kinase RIO1"
FT /id="PRO_0000213531"
FT DOMAIN 76..402
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 398..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..484
FT /note="Interaction with CKA2"
FT /evidence="ECO:0000269|PubMed:17725716"
FT REGION 440..484
FT /note="Association with (pre-)40S ribosomal subunit"
FT /evidence="ECO:0000269|PubMed:24948609"
FT COMPBIAS 405..431
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..484
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Proton acceptor"
FT ACT_SITE 261
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT MOD_RES 402
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17725716"
FT MOD_RES 403
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17725716"
FT MOD_RES 409
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17725716"
FT MOD_RES 416
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17725716"
FT MOD_RES 417
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17725716"
FT MOD_RES 419
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17725716"
FT MUTAGEN 125
FT /note="K->R: No activity."
FT /evidence="ECO:0000269|PubMed:12135737"
FT MUTAGEN 244
FT /note="D->A: Inhibits cell growth; enhances association
FT with pre-40S ribosomal subunits; inhibits 20S pre-rRNA to
FT mature 18S rRNA processing; translation initiation-like
FT defect."
FT /evidence="ECO:0000269|PubMed:24948609"
FT MUTAGEN 244
FT /note="D->E,N: No activity."
FT /evidence="ECO:0000269|PubMed:12135737"
FT MUTAGEN 261
FT /note="D->A: Inhibits cell growth."
FT /evidence="ECO:0000269|PubMed:24948609"
FT CONFLICT 203
FT /note="G -> A (in Ref. 5; CAA65511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 56122 MW; 7051A55BFD37D0C0 CRC64;
MSLEDKFDSL SVSQGASDHI NNQLLEKYSH KIKTDELSFS RAKTSKDKAN RATVENVLDP
RTMRFLKSMV TRGVIADLNG CLSTGKEANV YHAFAGTGKA PVIDEETGQY EVLETDGSRA
EYAIKIYKTS ILVFKDRERY VDGEFRFRNS RSQHNPRKMI KIWAEKEFRN LKRIYQSGVI
PAPKPIEVKN NVLVMEFLSR GNGFASPKLK DYPYKNRDEI FHYYHTMVAY MRLLYQVCRL
VHADLSEYNT IVHDDKLYMI DVSQSVEPEH PMSLDFLRMD IKNVNLYFEK MGISIFPERV
IFQFVISETL EKFKGDYNNI SALVAYIASN LPIKSTEQDE AEDEIFRSLH LVRSLGGLEE
RDFDRYTDGK FDLLKSLIAH DNERNFAASE QFEFDNADHE CSSGTEEFSD DEEDGSSGSE
EDDEEEGEYY DDDEPKVLKG KKHEDKDLKK LRKQEAKDAK REKRKTKVKK HIKKKLVKKT
KSKK
