RBG1_YEAST
ID RBG1_YEAST Reviewed; 369 AA.
AC P39729; D6VPI1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ribosome-interacting GTPase 1;
DE AltName: Full=GTP-binding protein RBG1;
DE AltName: Full=Genetically interacts with ribosomal genes protein 1;
GN Name=RBG1; Synonyms=FUN11; OrderedLocusNames=YAL036C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RIBOSOMES AND
RP TMA46.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [7]
RP FUNCTION, ASSOCIATION WITH POLYRIBOSOMES, AND INTERACTION WITH GIR2; TMA46;
RP YAP1 AND YGR250C.
RX PubMed=19448108; DOI=10.1128/ec.00356-08;
RA Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R.;
RT "Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2
RT interact on polyribosomes with Gcn1.";
RL Eukaryot. Cell 8:1061-1071(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in ribosomal function.
CC {ECO:0000269|PubMed:19448108}.
CC -!- SUBUNIT: Associates with translating polyribosomes. Interacts with
CC GIR2, TMA46, YAP1 and YGR250C. {ECO:0000269|PubMed:16702403,
CC ECO:0000269|PubMed:19448108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
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DR EMBL; U12980; AAC04995.1; -; Genomic_DNA.
DR EMBL; AY693042; AAT93061.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06951.1; -; Genomic_DNA.
DR PIR; S51983; S51983.
DR RefSeq; NP_009364.1; NM_001178181.1.
DR PDB; 4A9A; X-ray; 2.67 A; A/B=1-369.
DR PDBsum; 4A9A; -.
DR AlphaFoldDB; P39729; -.
DR SMR; P39729; -.
DR BioGRID; 31729; 132.
DR DIP; DIP-1750N; -.
DR IntAct; P39729; 26.
DR MINT; P39729; -.
DR STRING; 4932.YAL036C; -.
DR iPTMnet; P39729; -.
DR MaxQB; P39729; -.
DR PaxDb; P39729; -.
DR PRIDE; P39729; -.
DR EnsemblFungi; YAL036C_mRNA; YAL036C; YAL036C.
DR GeneID; 851195; -.
DR KEGG; sce:YAL036C; -.
DR SGD; S000000034; RBG1.
DR VEuPathDB; FungiDB:YAL036C; -.
DR eggNOG; KOG1487; Eukaryota.
DR GeneTree; ENSGT00940000153340; -.
DR HOGENOM; CLU_044997_0_0_1; -.
DR InParanoid; P39729; -.
DR OMA; SAKHPGQ; -.
DR BioCyc; YEAST:G3O-28846-MON; -.
DR PRO; PR:P39729; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39729; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0002181; P:cytoplasmic translation; IGI:SGD.
DR GO; GO:1903833; P:positive regulation of cellular response to amino acid starvation; IGI:SGD.
DR CDD; cd01896; DRG; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR045001; DRG.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR031662; GTP-binding_2.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR PANTHER; PTHR43127; PTHR43127; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF16897; MMR_HSR1_Xtn; 1.
DR Pfam; PF02824; TGS; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..369
FT /note="Ribosome-interacting GTPase 1"
FT /id="PRO_0000205449"
FT DOMAIN 66..292
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 292..368
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 72..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 118..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 250..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:4A9A"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4A9A"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:4A9A"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4A9A"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4A9A"
SQ SEQUENCE 369 AA; 40701 MW; D25C6C732B462A6B CRC64;
MSTTVEKIKA IEDEMARTQK NKATSFHLGQ LKAKLAKLRR ELLTSASSGS GGGAGIGFDV
ARTGVASVGF VGFPSVGKST LLSKLTGTES EAAEYEFTTL VTVPGVIRYK GAKIQMLDLP
GIIDGAKDGR GRGKQVIAVA RTCNLLFIIL DVNKPLHHKQ IIEKELEGVG IRLNKTPPDI
LIKKKEKGGI SITNTVPLTH LGNDEIRAVM SEYRINSAEI AFRCDATVDD LIDVLEASSR
RYMPAIYVLN KIDSLSIEEL ELLYRIPNAV PISSGQDWNL DELLQVMWDR LNLVRIYTKP
KGQIPDFTDP VVLRSDRCSV KDFCNQIHKS LVDDFRNALV YGSSVKHQPQ YVGLSHILED
EDVVTILKK
