ID   RBG2_YEAST              Reviewed;         368 AA.
AC   P53295; D6VUV7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Ribosome-interacting GTPase 2;
DE   AltName: Full=GTP-binding protein RBG2;
GN   Name=RBG2; Synonyms=GIR1; OrderedLocusNames=YGR173W;
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=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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   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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP   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   [6]
RP   FUNCTION.
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, 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).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   -!- INTERACTION:
CC       P53295; Q03768: GIR2; NbExp=5; IntAct=EBI-23421, EBI-7618;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 6200 molecules/cell in log phase SD medium.
CC       {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; Z72958; CAA97199.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08268.1; -; Genomic_DNA.
DR   PIR; S64487; S64487.
DR   RefSeq; NP_011689.1; NM_001181302.1.
DR   PDB; 7NRC; EM; 3.90 A; So=2-367.
DR   PDBsum; 7NRC; -.
DR   AlphaFoldDB; P53295; -.
DR   EMDB; EMD-12534; -.
DR   SMR; P53295; -.
DR   BioGRID; 33425; 106.
DR   DIP; DIP-2827N; -.
DR   IntAct; P53295; 25.
DR   MINT; P53295; -.
DR   STRING; 4932.YGR173W; -.
DR   iPTMnet; P53295; -.
DR   MaxQB; P53295; -.
DR   PaxDb; 4932-YGR173W; -.
DR   PeptideAtlas; P53295; -.
DR   EnsemblFungi; YGR173W_mRNA; YGR173W; YGR173W.
DR   GeneID; 853083; -.
DR   KEGG; sce:YGR173W; -.
DR   AGR; SGD:S000003405; -.
DR   SGD; S000003405; RBG2.
DR   VEuPathDB; FungiDB:YGR173W; -.
DR   eggNOG; KOG1486; Eukaryota.
DR   GeneTree; ENSGT00940000153340; -.
DR   HOGENOM; CLU_044997_0_0_1; -.
DR   InParanoid; P53295; -.
DR   OMA; VCDQVHR; -.
DR   OrthoDB; 146471at2759; -.
DR   BioCyc; YEAST:G3O-30869-MONOMER; -.
DR   BioGRID-ORCS; 853083; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P53295; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53295; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005525; F:GTP binding; ISS: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   CDD; cd17231; TGS_DRG2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 6.10.140.1070; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43127; DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR43127:SF2; DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 2; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF81271; TGS-like; 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; Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..368
FT                   /note="Ribosome-interacting GTPase 2"
FT                   /id="PRO_0000205450"
FT   DOMAIN          64..292
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   DOMAIN          292..367
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   BINDING         70..77
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         116..120
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         364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   368 AA;  41006 MW;  D144569C9C5D777C CRC64;
     MGIIDKIKAI EEEMARTQKN KATEHHLGLL KGKLARYRQQ LLADEAGSGG GGGSGFEVAK
     SGDARVVLIG YPSVGKSSLL GKITTTKSEI AHYAFTTLTS VPGVLKYQGA EIQIVDLPGI
     IYGASQGKGR GRQVVATART ADLVLMVLDA TKSEHQRASL EKELENVGIR LNKEKPNIYY
     KKKETGGVKV TFTSPPKTNL TEQAIKMILR DYRIHNAEVL VRDDQCTIDD FIDVINEQHR
     NYVKCLYVYN KIDAVSLEEV DKLAREPNTV VMSCEMDLGL QDVVEEIWYQ LNLSRVYTKK
     RGVRPVFDDP LVVRNNSTIG DLCHGIHRDF KDKFKYALVW GSSAKHSPQK CGLNHRIDDE
     DVVSLFAK
//