RIO1_DICDI
ID RIO1_DICDI Reviewed; 574 AA.
AC Q54VD8;
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 rio1;
DE EC=2.7.11.1;
DE EC=3.6.3.-;
GN Name=rio1; ORFNames=DDB_G0280431;
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 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 (By similarity). {ECO:0000250|UniProtKB:Q12196,
CC ECO:0000250|UniProtKB:Q9BRS2}.
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; AAFI02000036; EAL67194.1; -; Genomic_DNA.
DR RefSeq; XP_641171.1; XM_636079.1.
DR AlphaFoldDB; Q54VD8; -.
DR SMR; Q54VD8; -.
DR STRING; 44689.DDB0216428; -.
DR PaxDb; Q54VD8; -.
DR EnsemblProtists; EAL67194; EAL67194; DDB_G0280431.
DR GeneID; 8622551; -.
DR KEGG; ddi:DDB_G0280431; -.
DR dictyBase; DDB_G0280431; rio1.
DR eggNOG; KOG2270; Eukaryota.
DR HOGENOM; CLU_018693_4_3_1; -.
DR InParanoid; Q54VD8; -.
DR OMA; QEINGCI; -.
DR PhylomeDB; Q54VD8; -.
DR Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q54VD8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005829; C:cytosol; 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: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; ISS:dictyBase.
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:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
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 PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
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..574
FT /note="Serine/threonine-protein kinase rio1"
FT /id="PRO_0000373993"
FT DOMAIN 171..462
FT /note="Protein kinase"
FT REGION 474..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..574
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT ACT_SITE 344
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
SQ SEQUENCE 574 AA; 67270 MW; DFD717D491C59F71 CRC64;
MEDSFKNLTI ENKEQQTVTT TTTTTTTTTK KIQTLEVPLR RNGDLIEFSD SDEEYYYDDD
YEEIEYDSDL SDEENEDRIL GIRSSIPLNK TLQPKAQALE QKYQNKINVN SIANSISSKR
VIDDDSHRAL PNSVQNSIKE IKKKDDKQGV RIVDKEDRAT TEQVLDPRTR LMLFKMINKG
AFSEINGCIS TGKEANVYHA FTPNEEERAV KVYKTSILVF KDRDRYVTGE FRFRRGYSKH
NPRKMVKVWA EKEFRNLTRL KNAGIPCPTP LILRNHILVM TFIGKDGYAA PRLKDATVSQ
EKFGVIYLDC IKMMRTLFHK CRLVHADLSE YNMLYYKNQL YIIDVSQSVE HDHPHSLDFL
RMDCSNVTDF FRKKEVNTMF IQELFEFITD LTITEDNIDQ YLEKMLEKIQ SRGETTDEQK
IQEEVFRNAY IPRTLDQIID LDRDMEKIER GEGRDIFYQN LTGLSKDLQN IKSKNDLIND
SNENKDSDDS SSDSSEDSDD DSDSDQLNED DEKIRKLVVI DPITKMEIRL EDMPKKDRKK
FVKEMNKERR KTKIPKHIKK LTKKRKAEKF GKKK
