RIO1_CHATD
ID RIO1_CHATD Reviewed; 519 AA.
AC G0S3J5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Serine/threonine-protein kinase RIO1;
DE EC=2.7.11.1;
DE EC=3.6.3.-;
GN ORFNames=CTHT_0021480;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-281
RP AND ASP-298.
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: Involved in the final steps of cytoplasmic maturation of the
CC 40S ribosomal subunit (By similarity). In vitro, has strong ATPase
CC activity and only low protein kinase activity (PubMed:24948609).
CC {ECO:0000250|UniProtKB:Q12196, 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:0000255|PIRNR:PIRNR038147};
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:0000255|PIRNR:PIRNR038147};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:G0S5R3,
CC ECO:0000250|UniProtKB:Q9BRS2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:24948609}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; GL988041; EGS20322.1; -; Genomic_DNA.
DR RefSeq; XP_006692618.1; XM_006692555.1.
DR AlphaFoldDB; G0S3J5; -.
DR SMR; G0S3J5; -.
DR STRING; 759272.G0S3J5; -.
DR EnsemblFungi; EGS20322; EGS20322; CTHT_0021480.
DR GeneID; 18256186; -.
DR KEGG; cthr:CTHT_0021480; -.
DR eggNOG; KOG2270; Eukaryota.
DR HOGENOM; CLU_018693_4_0_1; -.
DR OrthoDB; 1238900at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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 InterPro; IPR017407; Ser/Thr_kinase_Rio1.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 1: Evidence at protein level;
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..519
FT /note="Serine/threonine-protein kinase RIO1"
FT /id="PRO_0000439042"
FT DOMAIN 122..519
FT /note="Protein kinase"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..519
FT /note="Association with (pre-)40S ribosomal particle"
FT /evidence="ECO:0000269|PubMed:24948609"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..519
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT ACT_SITE 298
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305|PubMed:24948609"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT MUTAGEN 281
FT /note="D->A: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:24948609"
FT MUTAGEN 298
FT /note="D->A: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:24948609"
SQ SEQUENCE 519 AA; 59279 MW; D85E503B9FE0AF3F CRC64;
MTPAPEPQDP PTIHEPVATE QTDDISDWDV ESDYEDGYGA PSKSQAQGGA SAADRPKINA
HARIDDQMTD LARHASKIRL DNLTMQQIFR DKDRTDNATS DQVLDNHTRM IILNMLNRNI
ISEIYGTIST GKEANVYNAV AYDNNGERIE RAVKVYKTII LGFKDRERYL AGEQRFKTIV
DKALSAPRKM IKLWAEKEFR NLKRLHTAGI PCPEPIYLKY NVMVMGFLGD HTNGYAFPRL
HDTKITGETL EETEAEWRRL YINLLSMMRR MYQVCGLVHG DLSEYNILYN EGVLYIIDVS
QSVEHDHIEA TNFLRMDIRN VNDFFARRGV DTLSDRTVYH FITDSTGAVD ENGMRKAIDN
LYATRPPLAE SEEARAEQEI DNQVFRNQFI PTTLEEVYNL EVELGKKVDT RLYQHMLADS
KVPESTGGEH KSGEGGESGS EDEEGDEGES GEVESGDEER EEGEGDRFEK KRPRGKKHLD
KAEKHAHKMA VKEAKREKRK EKMPKHVKKK LVAANKKRK
