RIA1_YEAST
ID RIA1_YEAST Reviewed; 1110 AA.
AC P53893; D6W119;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Ribosome assembly protein 1;
DE EC=3.6.5.- {ECO:0000269|PubMed:11779510};
DE AltName: Full=EF-2-like GTPase;
DE AltName: Full=Elongation factor-like 1;
GN Name=RIA1; Synonyms=EFL1; OrderedLocusNames=YNL163C; ORFNames=N1718;
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=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=11779510; DOI=10.1016/s1097-2765(01)00403-8;
RA Senger B., Lafontaine D.L.J., Graindorge J.-S., Gadal O., Camasses A.,
RA Sanni A., Garnier J.-M., Breitenbach M., Hurt E., Fasiolo F.;
RT "The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step
RT of ribosome synthesis.";
RL Mol. Cell 8:1363-1373(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11713675; DOI=10.1007/s004380100548;
RA Becam A.-M., Nasr F., Racki W.J., Zagulski M., Herbert C.J.;
RT "Ria1p (Ynl163c), a protein similar to elongation factors 2, is involved in
RT the biogenesis of the 60S subunit of the ribosome in Saccharomyces
RT cerevisiae.";
RL Mol. Genet. Genomics 266:454-462(2001).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=16095611; DOI=10.1016/j.jmb.2005.07.037;
RA Graindorge J.-S., Rousselle J.-C., Senger B., Lenormand P., Namane A.,
RA Lacroute F., Fasiolo F.;
RT "Deletion of EFL1 results in heterogeneity of the 60 S GTPase-associated
RT rRNA conformation.";
RL J. Mol. Biol. 352:355-369(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: GTPase involved in the biogenesis of the 60S ribosomal
CC subunit and translational activation of ribosomes. Together with SDO1,
CC may trigger the GTP-dependent release of TIF6 from 60S pre-ribosomes in
CC the cytoplasm, thereby activating ribosomes for translation competence
CC by allowing 80S ribosome assembly and facilitating TIF6 recycling to
CC the nucleus, where it is required for 60S rRNA processing and nuclear
CC export. Inhibits GTPase activity of ribosome-bound EF-2.
CC {ECO:0000269|PubMed:11713675, ECO:0000269|PubMed:11779510,
CC ECO:0000269|PubMed:16095611}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:11779510};
CC -!- ACTIVITY REGULATION: GTPase activity is stimulated in the presence of
CC 60S subunits. {ECO:0000269|PubMed:11779510}.
CC -!- INTERACTION:
CC P53893; Q07953: SDO1; NbExp=2; IntAct=EBI-28980, EBI-27124;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11713675,
CC ECO:0000269|PubMed:11779510, ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; X92517; CAA63276.1; -; Genomic_DNA.
DR EMBL; Z71439; CAA96050.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10385.1; -; Genomic_DNA.
DR PIR; S60964; S60964.
DR RefSeq; NP_014236.1; NM_001183001.1.
DR AlphaFoldDB; P53893; -.
DR SASBDB; P53893; -.
DR SMR; P53893; -.
DR BioGRID; 35665; 369.
DR DIP; DIP-2553N; -.
DR IntAct; P53893; 5.
DR MINT; P53893; -.
DR STRING; 4932.YNL163C; -.
DR iPTMnet; P53893; -.
DR MaxQB; P53893; -.
DR PaxDb; P53893; -.
DR PRIDE; P53893; -.
DR EnsemblFungi; YNL163C_mRNA; YNL163C; YNL163C.
DR GeneID; 855558; -.
DR KEGG; sce:YNL163C; -.
DR SGD; S000005107; RIA1.
DR VEuPathDB; FungiDB:YNL163C; -.
DR eggNOG; KOG0467; Eukaryota.
DR GeneTree; ENSGT00550000074806; -.
DR HOGENOM; CLU_002794_3_1_1; -.
DR InParanoid; P53893; -.
DR OMA; ERFARCE; -.
DR BioCyc; YEAST:G3O-33179-MON; -.
DR BRENDA; 3.6.5.3; 984.
DR PRO; PR:P53893; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53893; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:SGD.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis.
FT CHAIN 1..1110
FT /note="Ribosome assembly protein 1"
FT /id="PRO_0000091559"
FT DOMAIN 17..262
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 102..106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 156..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1110 AA; 124464 MW; 6FFD6ACD53F4510C CRC64;
MPRVESETYK RLQNDPSCIR NICIVAHVDH GKTSLSDSLL ASNGIISQRL AGKIRFLDAR
PDEQLRGITM ESSAISLYFR VLRKQEGSDE PLVSEHLVNL IDSPGHIDFS SEVSAASRLC
DGAVVLVDVV EGVCSQTVTV LRQCWTEKLK PILVLNKIDR LITELQLTPQ EAYIHLSKVI
EQVNSVIGSF FANERQLDDL FWREQLEKNE NAEYIEKDDS GIYFNPTDNN VIFASAIDGW
GFNIGQLAKF YEQKLGAKRE NLQKVLWGDF YMDPKTKKII NNKGLKGRSL KPLFTSLILE
NIWKIYQNII TSRDSEMVEK IAKTLNIKLL ARDLRSKDDK QLLRTIMGQW LPVSTAVLLT
VIEKLPSPLE SQTDRLNTIL VSESDTAAMD PRLLKAMKTC DKEGPVSAYV SKMLSIPREE
LPVESKRIAS SDELMERSRK AREEALNAAK HAGMVENMAM MDLNDNSKNT SDLYKRAKDT
VMTPEVGEQT KPKPSRNNDV FCVVSEPSSA LDLEFEYEGE DDSDSQDNFG LDFVPTDIDP
NDPLSSMFEY EEEDPLLESI KQISEDVNDE VDDIFDEKEE CLVAFARIYS GTLRVGQEIS
VLGPKYDPKC PEEHIETAII THLYLFMGKE LVPLDVCPSG NIVGIRGLAG KVLKSGTLIE
KGVQGVNLAG VNFHFTPIVR VAVEPANPVE MSKLVRGLKL LDQADPCVHT YVENTGEHIL
CTAGELHLER CLKDLTERFA GIEITHSEPA IPYRETFLSA SDMNPPQNSQ LGRGVHELLL
SQYKITFRTF PLSGKVTDFL SQHQNSIKNI LKTSTSSMDP VIESTGSSFL DKKSLLVAFE
EVINQEEKSR ELLSGFKVKL AGFGPSRVGC NILLSQDNLL GSLFEGTPAA FEYSDSIKNG
FQLAVSEGPL ANEPVQGMCV LVESVHKMSQ DEIESIEDPR YQQHIVDLSG RLITSTRDAI
HEAFLDWSPR IMWAIYSCDI QTSVDVLGKV YAVILQRHGK IISEEMKEGT PFFQIEAHVP
VVEAFGLSED IRKRTSGAAQ PQLVFSGFEC IDLDPFWVPT TEEELEELGD TADRENIARK
HMNAIRRRKG LFIEEKVVEN AEKQRTLKKN
