ERF3_YEAST
ID ERF3_YEAST Reviewed; 685 AA.
AC P05453; D6VSF4; P05420;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit;
DE AltName: Full=ERF-3;
DE Short=ERF3;
DE AltName: Full=ERF2;
DE AltName: Full=G1 to S phase transition protein 1;
DE AltName: Full=Omnipotent suppressor protein 2;
DE AltName: Full=PSI no more protein 2;
DE AltName: Full=Polypeptide release factor 3;
DE AltName: Full=Translation release factor 3;
GN Name=SUP35; Synonyms=GST1, PNM2, SAL3, SUF12, SUP2;
GN OrderedLocusNames=YDR172W; ORFNames=YD9395.05;
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].
RX PubMed=3047009; DOI=10.1016/0378-1119(88)90223-5;
RA Kushnirov V.V., Ter-Avanesyan M.D., Telckov M.V., Surguchov A.P.,
RA Smirnov V.N., Inge-Vechtomov S.G.;
RT "Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces
RT cerevisiae.";
RL Gene 66:45-54(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3556215; DOI=10.1016/0014-5793(87)80157-6;
RA Kushnirov V.V., Ter-Avanesyan M.D., Surguchov A.P., Smirnov V.N.,
RA Inge-Vechtomov S.G.;
RT "Localization of possible functional domains in sup2 gene product of the
RT yeast Saccharomyces cerevisiae.";
RL FEBS Lett. 215:257-260(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3280807; DOI=10.1016/0022-2836(88)90301-4;
RA Wilson P.G., Culbertson M.R.;
RT "SUF12 suppressor protein of yeast. A fusion protein related to the EF-1
RT family of elongation factors.";
RL J. Mol. Biol. 199:559-573(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841115; DOI=10.1002/j.1460-2075.1988.tb02928.x;
RA Kukuchi Y., Shimatake H., Kikuchi A.;
RT "A yeast gene required for the G1-to-S transition encodes a protein
RT containing an A-kinase target site and GTPase domain.";
RL EMBO J. 7:1175-1182(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=7556078; DOI=10.1002/j.1460-2075.1995.tb00111.x;
RA Stansfield I., Jones K.M., Kushnirov V.V., Dagkesamanskaya A.R.,
RA Poznyakovski A.I., Paushkin S.V., Nierras C.R., Cox B.S.,
RA Ter-Avanesyan M.D., Tuite M.F.;
RT "The products of the SUP45 (eRF1) and SUP35 genes interact to mediate
RT translation termination in Saccharomyces cerevisiae.";
RL EMBO J. 14:4365-4373(1995).
RN [8]
RP PRION FORMATION, AND AGGREGATION.
RX PubMed=8670813; DOI=10.1002/j.1460-2075.1996.tb00675.x;
RA Paushkin S.V., Kushnirov V.V., Smirnov V.N., Ter-Avanesyan M.D.;
RT "Propagation of the yeast prion-like [psi+] determinant is mediated by
RT oligomerization of the SUP35-encoded polypeptide chain release factor.";
RL EMBO J. 15:3127-3134(1996).
RN [9]
RP PRION FORMATION.
RX PubMed=8978027; DOI=10.1093/genetics/144.4.1375;
RA Derkatch I.L., Chernoff Y.O., Kushnirov V.V., Inge-Vechtomov S.G.,
RA Liebman S.W.;
RT "Genesis and variability of [PSI] prion factors in Saccharomyces
RT cerevisiae.";
RL Genetics 144:1375-1386(1996).
RN [10]
RP PRION FORMATION, AND PRION CURING.
RX PubMed=9335589; DOI=10.1093/genetics/147.2.507;
RA Derkatch I.L., Bradley M.E., Zhou P., Chernoff Y.O., Liebman S.W.;
RT "Genetic and environmental factors affecting the de novo appearance of the
RT [PSI+] prion in Saccharomyces cerevisiae.";
RL Genetics 147:507-519(1997).
RN [11]
RP PRION FORMATION.
RX PubMed=11511345; DOI=10.1016/s0092-8674(01)00427-5;
RA Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.;
RT "Prions affect the appearance of other prions: the story of [PIN(+)].";
RL Cell 106:171-182(2001).
RN [12]
RP INTERACTION WITH PAB1.
RX PubMed=11971964; DOI=10.1128/mcb.22.10.3301-3315.2002;
RA Cosson B., Couturier A., Chabelskaya S., Kiktev D., Inge-Vechtomov S.G.,
RA Philippe M., Zhouravleva G.;
RT "Poly(A)-binding protein acts in translation termination via eukaryotic
RT release factor 3 interaction and does not influence [PSI(+)] propagation.";
RL Mol. Cell. Biol. 22:3301-3315(2002).
RN [13]
RP FUNCTION IN MRNA DECAY, AND INTERACTION WITH PAB1.
RX PubMed=12923185; DOI=10.1074/jbc.c300300200;
RA Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y., Hoshino S.,
RA Katada T.;
RT "Translation termination factor eRF3 mediates mRNA decay through the
RT regulation of deadenylation.";
RL J. Biol. Chem. 278:38287-38291(2003).
RN [14]
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 [15]
RP FUNCTION IN MRNA DECAY, AND INTERACTION WITH PAB1.
RX PubMed=15337765; DOI=10.1074/jbc.m405163200;
RA Kobayashi T., Funakoshi Y., Hoshino S., Katada T.;
RT "The GTP-binding release factor eRF3 as a key mediator coupling translation
RT termination to mRNA decay.";
RL J. Biol. Chem. 279:45693-45700(2004).
RN [16]
RP PRION PROPAGATION, AND AMYLOID STRUCTURE.
RX PubMed=15029195; DOI=10.1038/nature02391;
RA King C.Y., Diaz-Avalos R.;
RT "Protein-only transmission of three yeast prion strains.";
RL Nature 428:319-323(2004).
RN [17]
RP PRION PROPAGATION, AND AMYLOID STRUCTURE.
RX PubMed=15029196; DOI=10.1038/nature02392;
RA Tanaka M., Chien P., Naber N., Cooke R., Weissman J.S.;
RT "Conformational variations in an infectious protein determine prion strain
RT differences.";
RL Nature 428:323-328(2004).
RN [18]
RP INTERACTION WITH PAB1.
RX PubMed=15525991; DOI=10.1038/nature03060;
RA Amrani N., Ganesan R., Kervestin S., Mangus D.A., Ghosh S., Jacobson A.;
RT "A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated
RT mRNA decay.";
RL Nature 432:112-118(2004).
RN [19]
RP INTERACTION WITH TPA1.
RX PubMed=16809762; DOI=10.1128/mcb.02448-05;
RA Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.;
RT "Tpa1p is part of an mRNP complex that influences translation termination,
RT mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 26:5237-5248(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [21]
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 [22]
RP PRION APPEARANCE.
RX PubMed=19917766; DOI=10.1534/genetics.109.110213;
RA Lancaster A.K., Bardill J.P., True H.L., Masel J.;
RT "The spontaneous appearance rate of the yeast prion [PSI+] and its
RT implications for the evolution of the evolvability properties of the [PSI+]
RT system.";
RL Genetics 184:393-400(2010).
RN [23]
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).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 7-13.
RX PubMed=15944695; DOI=10.1038/nature03680;
RA Nelson R., Sawaya M.R., Balbirnie M., Madsen A.O., Riekel C., Grothe R.,
RA Eisenberg D.;
RT "Structure of the cross-beta spine of amyloid-like fibrils.";
RL Nature 435:773-778(2005).
RN [25]
RP STRUCTURE BY NMR OF 1-253.
RX PubMed=17170131; DOI=10.1073/pnas.0609638103;
RA Shewmaker F., Wickner R.B., Tycko R.;
RT "Amyloid of the prion domain of Sup35p has an in-register parallel beta-
RT sheet structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19754-19759(2006).
CC -!- FUNCTION: Involved in translation termination. Stimulates the activity
CC of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding
CC protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also
CC required for regulation of normal mRNA decay through translation
CC termination-coupled poly(A) shortening. {ECO:0000269|PubMed:12923185,
CC ECO:0000269|PubMed:15337765, ECO:0000269|PubMed:7556078}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP. Interacts
CC with polyadenylate-binding protein PAB1, and TPA1.
CC {ECO:0000269|PubMed:11971964, ECO:0000269|PubMed:12923185,
CC ECO:0000269|PubMed:15337765, ECO:0000269|PubMed:15525991,
CC ECO:0000269|PubMed:16809762}.
CC -!- INTERACTION:
CC P05453; P32644: ECM32; NbExp=3; IntAct=EBI-6540, EBI-22223;
CC P05453; Q12315: GLE1; NbExp=2; IntAct=EBI-6540, EBI-7635;
CC P05453; Q04638: ITT1; NbExp=3; IntAct=EBI-6540, EBI-27858;
CC P05453; P05453: SUP35; NbExp=10; IntAct=EBI-6540, EBI-6540;
CC P05453; P12385: SUP45; NbExp=4; IntAct=EBI-6540, EBI-6533;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is
CC unstructured in its native, soluble form, and which forms a parallel
CC in-register beta-sheet in its amyloid form.
CC -!- MISCELLANEOUS: [PSI+] is the prion form of SUP35 (PubMed:8978027).
CC [PSI+] is the result of a conformational change of the cellular SUP35
CC protein that becomes self-propagating and infectious. This
CC conformational change generates a form of SUP35 that assembles into
CC amyloid fibrils. [PSI+]-aggregates sequester soluble SUP35, resulting
CC in defects in faithful translation termination by read-through of
CC translation termination codons (PubMed:8670813). [PSI+] can be cured by
CC GdnHCl and by deletion of the molecular chaperone HSP104, which is
CC required for [PSI+] propagation (PubMed:9335589). It is speculated that
CC the prion form would be at least mildly deleterious in most
CC environments, but it might sometimes increase evolvability in certain
CC harsh environments (PubMed:19917766). {ECO:0000305|PubMed:19917766,
CC ECO:0000305|PubMed:8670813, ECO:0000305|PubMed:8978027,
CC ECO:0000305|PubMed:9335589}.
CC -!- MISCELLANEOUS: Present with 78900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. ERF3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; M21129; AAA35133.1; -; Genomic_DNA.
DR EMBL; X07163; CAA30155.1; -; Genomic_DNA.
DR EMBL; Y00829; CAA68760.1; -; Genomic_DNA.
DR EMBL; Z46727; CAA86677.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12014.1; -; Genomic_DNA.
DR PIR; S00733; EFBYS2.
DR RefSeq; NP_010457.3; NM_001180479.3.
DR PDB; 1YJO; X-ray; 1.30 A; A=8-13.
DR PDB; 1YJP; X-ray; 1.80 A; A=7-13.
DR PDB; 2OMM; X-ray; 2.00 A; A=7-13.
DR PDB; 4CRN; EM; 9.10 A; P=256-685.
DR PDB; 5K2E; EM; 1.00 A; A=8-13.
DR PDB; 5K2F; EM; 1.00 A; A=8-13.
DR PDB; 5K2G; EM; 1.10 A; A=7-13.
DR PDB; 5K2H; EM; 1.05 A; A=7-13.
DR PDBsum; 1YJO; -.
DR PDBsum; 1YJP; -.
DR PDBsum; 2OMM; -.
DR PDBsum; 4CRN; -.
DR PDBsum; 5K2E; -.
DR PDBsum; 5K2F; -.
DR PDBsum; 5K2G; -.
DR PDBsum; 5K2H; -.
DR AlphaFoldDB; P05453; -.
DR BMRB; P05453; -.
DR SMR; P05453; -.
DR BioGRID; 32225; 902.
DR ComplexPortal; CPX-435; Translation release factor ERF1-ERF3 complex.
DR DIP; DIP-376N; -.
DR IntAct; P05453; 40.
DR MINT; P05453; -.
DR STRING; 4932.YDR172W; -.
DR BindingDB; P05453; -.
DR ChEMBL; CHEMBL3308902; -.
DR iPTMnet; P05453; -.
DR MaxQB; P05453; -.
DR PaxDb; P05453; -.
DR PRIDE; P05453; -.
DR EnsemblFungi; YDR172W_mRNA; YDR172W; YDR172W.
DR GeneID; 851752; -.
DR KEGG; sce:YDR172W; -.
DR SGD; S000002579; SUP35.
DR VEuPathDB; FungiDB:YDR172W; -.
DR eggNOG; KOG0459; Eukaryota.
DR GeneTree; ENSGT00940000169696; -.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; P05453; -.
DR OMA; PGHVEYT; -.
DR BioCyc; YEAST:G3O-29761-MON; -.
DR Reactome; R-SCE-72764; Eukaryotic Translation Termination.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P05453; -.
DR PRO; PR:P05453; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P05453; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0018444; C:translation release factor complex; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003747; F:translation release factor activity; IDA:SGD.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006415; P:translational termination; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003285; Sup35.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01343; YEASTERF.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amyloid; Cytoplasm; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Prion; Protein biosynthesis;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..685
FT /note="Eukaryotic peptide chain release factor GTP-binding
FT subunit"
FT /id="PRO_0000091482"
FT DOMAIN 258..484
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..239
FT /note="Interaction with PAB1"
FT REGION 5..135
FT /note="Prion domain (PrD)"
FT REGION 63..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..249
FT /note="Charged"
FT REGION 267..274
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 323..327
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 344..347
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 406..409
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 448..450
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 112..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..274
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 344..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 406..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 273
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
FT SITE 407
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 53
FT /note="S -> C (in Ref. 4; CAA68760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 685 AA; 76551 MW; 43912A6D77DFA153 CRC64;
MSDSNQGNNQ QNYQQYSQNG NQQQGNNRYQ GYQAYNAQAQ PAGGYYQNYQ GYSGYQQGGY
QQYNPDAGYQ QQYNPQGGYQ QYNPQGGYQQ QFNPQGGRGN YKNFNYNNNL QGYQAGFQPQ
SQGMSLNDFQ KQQKQAAPKP KKTLKLVSSS GIKLANATKK VGTKPAESDK KEEEKSAETK
EPTKEPTKVE EPVKKEEKPV QTEEKTEEKS ELPKVEDLKI SESTHNTNNA NVTSADALIK
EQEEEVDDEV VNDMFGGKDH VSLIFMGHVD AGKSTMGGNL LYLTGSVDKR TIEKYEREAK
DAGRQGWYLS WVMDTNKEER NDGKTIEVGK AYFETEKRRY TILDAPGHKM YVSEMIGGAS
QADVGVLVIS ARKGEYETGF ERGGQTREHA LLAKTQGVNK MVVVVNKMDD PTVNWSKERY
DQCVSNVSNF LRAIGYNIKT DVVFMPVSGY SGANLKDHVD PKECPWYTGP TLLEYLDTMN
HVDRHINAPF MLPIAAKMKD LGTIVEGKIE SGHIKKGQST LLMPNKTAVE IQNIYNETEN
EVDMAMCGEQ VKLRIKGVEE EDISPGFVLT SPKNPIKSVT KFVAQIAIVE LKSIIAAGFS
CVMHVHTAIE EVHIVKLLHK LEKGTNRKSK KPPAFAKKGM KVIAVLETEA PVCVETYQDY
PQLGRFTLRD QGTTIAIGKI VKIAE
