ID   RIO1_ENCCU              Reviewed;         387 AA.
AC   Q8SVI7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Probable serine/threonine-protein kinase RIO1 homolog;
DE            EC=2.7.11.1;
DE            EC=3.6.3.-;
GN   Name=RIO1; OrderedLocusNames=ECU05_1070;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
RP   PREDICTION OF FUNCTION.
RX   PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA   Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA   Barton G.J.;
RT   "The complement of protein kinases of the microsporidium Encephalitozoon
RT   cuniculi in relation to those of Saccharomyces cerevisiae and
RT   Schizosaccharomyces pombe.";
RL   BMC Genomics 8:309-309(2007).
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.
CC       Despite the protein kinase domain is proposed to act predominantly as
CC       an ATPase. Has a role in the cell cycle where it is required for
CC       entrance into S-phase and in the control of the onset of anaphase.
CC       Appears to also be involved in the maintenance of chromosome stability
CC       and correct mitotic segregation (By similarity).
CC       {ECO:0000250|UniProtKB:G0S3J5, ECO:0000250|UniProtKB:Q12196}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O42650,
CC       ECO:0000250|UniProtKB:Q12196}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AL590445; CAD26627.2; -; Genomic_DNA.
DR   RefSeq; NP_597450.1; NM_001041316.1.
DR   AlphaFoldDB; Q8SVI7; -.
DR   SMR; Q8SVI7; -.
DR   STRING; 284813.Q8SVI7; -.
DR   GeneID; 859116; -.
DR   KEGG; ecu:ECU05_1070; -.
DR   VEuPathDB; MicrosporidiaDB:ECU05_1070; -.
DR   HOGENOM; CLU_018693_3_1_1; -.
DR   InParanoid; Q8SVI7; -.
DR   OrthoDB; 1238900at2759; -.
DR   Proteomes; UP000000819; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000687; RIO_kinase.
DR   InterPro; IPR018935; RIO_kinase_CS.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01245; RIO1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Ribosome biogenesis;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..387
FT                   /note="Probable serine/threonine-protein kinase RIO1
FT                   homolog"
FT                   /id="PRO_0000384426"
FT   DOMAIN          41..387
FT                   /note="Protein kinase"
FT   REGION          309..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..372
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   ACT_SITE        221
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
SQ   SEQUENCE   387 AA;  44100 MW;  F88A9A9DB02669A4 CRC64;
     MKETRAEKRK KDKSDRATVD KVLDKRTLKV LERLQARGKL VNLQGSLCTG KESNVYLGEA
     STSLCSKFIK NRYSVTEEPG REGQIVPVVV KIFKTSIMSF RDRERYIRSE KRFQRFCTSN
     SRKLIKVWAE KEVRNLKRLN NAGIPSPEPI YLKNNILVMT QIGRCSEVAP RLRDASIKDL
     EGCYQQCVKI IRDMYKKAGL VHADLSEFNL LYFEGVVYVI DVGQSVEIDH DNAQRFLIMD
     INNINSFFSR KGVSVAKGND LFEEISGNVI PLYLKDIDIG RDAFIPSRVS EVGNEEDLLA
     FAADSRSREF GSTTDSDLSS TGEASVEDSD ASLGATESRG GGNIREEKKR KKKTVKELNR
     IRRASRISKK EKKRIFKRYI GMKKRKN