ID   IF2P_YEAST              Reviewed;        1002 AA.
AC   P39730; D6VPI2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000305|PubMed:12507428};
DE            Short=eIF-5B {ECO:0000303|PubMed:12507428};
DE            EC=3.6.5.3 {ECO:0000269|PubMed:12507428, ECO:0000269|PubMed:18976658};
DE   AltName: Full=Translation initiation factor IF-2 {ECO:0000303|PubMed:9624054};
GN   Name=FUN12 {ECO:0000303|PubMed:8076820};
GN   OrderedLocusNames=YAL035W {ECO:0000312|SGD:S000000033};
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   SEQUENCE REVISION.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RA   Vo D.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-1002.
RX   PubMed=8076820; DOI=10.1016/0378-1119(94)90294-1;
RA   Sutrave P., Shafer B.K., Strathern J.N., Hughes S.H.;
RT   "Isolation, identification and characterization of the FUN12 gene of
RT   Saccharomyces cerevisiae.";
RL   Gene 146:209-213(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=9624054; DOI=10.1126/science.280.5370.1757;
RA   Choi S.K., Lee J.H., Zoll W.L., Merrick W.C., Dever T.E.;
RT   "Promotion of met-tRNAiMet binding to ribosomes by yIF2, a bacterial IF2
RT   homolog in yeast.";
RL   Science 280:1757-1760(1998).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-439 AND HIS-480.
RX   PubMed=12507428; DOI=10.1016/s0092-8674(02)01171-6;
RA   Shin B.S., Maag D., Roll-Mecak A., Arefin M.S., Burley S.K., Lorsch J.R.,
RA   Dever T.E.;
RT   "Uncoupling of initiation factor eIF5B/IF2 GTPase and translational
RT   activities by mutations that lower ribosome affinity.";
RL   Cell 111:1015-1025(2002).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF HIS-480.
RX   PubMed=12471154; DOI=10.1073/pnas.262569399;
RA   Lee J.H., Pestova T.V., Shin B.S., Cao C., Choi S.K., Dever T.E.;
RT   "Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic
RT   translation initiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16689-16694(2002).
RN   [8]
RP   FUNCTION.
RX   PubMed=12008673; DOI=10.1017/s1355838202029527;
RA   Algire M.A., Maag D., Savio P., Acker M.G., Tarun S.Z. Jr., Sachs A.B.,
RA   Asano K., Nielsen K.H., Olsen D.S., Phan L., Hinnebusch A.G., Lorsch J.R.;
RT   "Development and characterization of a reconstituted yeast translation
RT   initiation system.";
RL   RNA 8:382-397(2002).
RN   [9]
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   [10]
RP   IDENTIFICATION BY 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   [11]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18976658; DOI=10.1016/j.jmb.2008.10.029;
RA   Acker M.G., Shin B.S., Nanda J.S., Saini A.K., Dever T.E., Lorsch J.R.;
RT   "Kinetic analysis of late steps of eukaryotic translation initiation.";
RL   J. Mol. Biol. 385:491-506(2009).
RN   [12]
RP   MUTAGENESIS OF GLY-479.
RX   PubMed=17913624; DOI=10.1016/s0076-6879(07)29009-3;
RA   Shin B.S., Dever T.E.;
RT   "Molecular genetic structure-function analysis of translation initiation
RT   factor eIF5B.";
RL   Methods Enzymol. 429:185-201(2007).
RN   [13]
RP   FUNCTION.
RX   PubMed=19029250; DOI=10.1128/mcb.00896-08;
RA   Shin B.S., Kim J.R., Acker M.G., Maher K.N., Lorsch J.R., Dever T.E.;
RT   "rRNA suppressor of a eukaryotic translation initiation factor
RT   5B/initiation factor 2 mutant reveals a binding site for translational
RT   GTPases on the small ribosomal subunit.";
RL   Mol. Cell. Biol. 29:808-821(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, 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   [15]
RP   FUNCTION.
RX   PubMed=22751017; DOI=10.1038/nsmb.2308;
RA   Lebaron S., Schneider C., van Nues R.W., Swiatkowska A., Walsh D.,
RA   Boettcher B., Granneman S., Watkins N.J., Tollervey D.;
RT   "Proofreading of pre-40S ribosome maturation by a translation initiation
RT   factor and 60S subunits.";
RL   Nat. Struct. Mol. Biol. 19:744-753(2012).
RN   [16]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 401-739.
RX   PubMed=24200810; DOI=10.1126/science.1240585;
RA   Fernandez I.S., Bai X.C., Hussain T., Kelley A.C., Lorsch J.R.,
RA   Ramakrishnan V., Scheres S.H.;
RT   "Molecular architecture of a eukaryotic translational initiation complex.";
RL   Science 342:1240585-1240585(2013).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 401-1002.
RX   PubMed=25478828; DOI=10.1107/s1399004714021476;
RA   Zheng A., Yu J., Yamamoto R., Ose T., Tanaka I., Yao M.;
RT   "X-ray structures of eIF5B and the eIF5B-eIF1A complex: the conformational
RT   flexibility of eIF5B is restricted on the ribosome by interaction with
RT   eIF1A.";
RL   Acta Crystallogr. D 70:3090-3098(2014).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 399-852 IN COMPLEX WITH GTP, AND
RP   FUNCTION.
RX   PubMed=24686316; DOI=10.1002/embj.201387344;
RA   Kuhle B., Ficner R.;
RT   "eIF5B employs a novel domain release mechanism to catalyze ribosomal
RT   subunit joining.";
RL   EMBO J. 33:1177-1191(2014).
CC   -!- FUNCTION: Plays a role in translation initiation (PubMed:9624054).
CC       Translational GTPase that catalyzes the joining of the 40S and 60S
CC       subunits to form the 80S initiation complex with the initiator
CC       methionine-tRNA in the P-site base paired to the start codon
CC       (PubMed:12507428, PubMed:12471154, PubMed:12008673). GTP binding and
CC       hydrolysis induces conformational changes in the enzyme that renders it
CC       active for productive interactions with the ribosome (PubMed:25478828).
CC       The release of the enzyme after formation of the initiation complex is
CC       a prerequisite to form elongation-competent ribosomes (PubMed:12507428,
CC       PubMed:18976658, PubMed:19029250). Stimulates 20S pre-rRNA cleavage to
CC       mature 18S rRNA by PIN-domain endonuclease NOB1 (PubMed:22751017).
CC       {ECO:0000269|PubMed:12008673, ECO:0000269|PubMed:12471154,
CC       ECO:0000269|PubMed:12507428, ECO:0000269|PubMed:18976658,
CC       ECO:0000269|PubMed:19029250, ECO:0000269|PubMed:22751017,
CC       ECO:0000269|PubMed:25478828, ECO:0000269|PubMed:9624054}.
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; EC=3.6.5.3;
CC         Evidence={ECO:0000269|PubMed:12507428, ECO:0000269|PubMed:18976658};
CC   -!- COFACTOR:
CC       Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC       Note=Binds 1 monovalent cation per monomer in the active site, which
CC       can be sodium or potassium. This structural cofactor stabilizes the
CC       GTP-bound 'on' state, and may also act as a transition state stabilizer
CC       of the hydrolysis reaction. {ECO:0000250|UniProtKB:G0S8G9};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9624054}.
CC   -!- MISCELLANEOUS: Present with 13400 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. IF-2 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57228.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U12980; AAC04996.1; -; Genomic_DNA.
DR   EMBL; L29389; AAA57228.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006935; DAA06952.1; -; Genomic_DNA.
DR   PIR; S70292; S70292.
DR   RefSeq; NP_009365.1; NM_001178180.1.
DR   PDB; 3WBI; X-ray; 2.35 A; A=401-1002.
DR   PDB; 3WBJ; X-ray; 2.50 A; A=401-855.
DR   PDB; 3WBK; X-ray; 3.30 A; A/B=401-1002.
DR   PDB; 4N3S; X-ray; 1.83 A; A/B=399-852.
DR   PDB; 4NCF; X-ray; 3.02 A; A/B=399-852.
DR   PDB; 4V8Y; EM; 4.30 A; CP=401-739.
DR   PDB; 4V8Z; EM; 6.60 A; CV=401-739.
DR   PDB; 6WOO; EM; 2.90 A; 1=401-1000.
DR   PDBsum; 3WBI; -.
DR   PDBsum; 3WBJ; -.
DR   PDBsum; 3WBK; -.
DR   PDBsum; 4N3S; -.
DR   PDBsum; 4NCF; -.
DR   PDBsum; 4V8Y; -.
DR   PDBsum; 4V8Z; -.
DR   PDBsum; 6WOO; -.
DR   AlphaFoldDB; P39730; -.
DR   EMDB; EMD-21859; -.
DR   SMR; P39730; -.
DR   BioGRID; 31730; 222.
DR   DIP; DIP-3790N; -.
DR   IntAct; P39730; 58.
DR   MINT; P39730; -.
DR   STRING; 4932.YAL035W; -.
DR   CarbonylDB; P39730; -.
DR   iPTMnet; P39730; -.
DR   MaxQB; P39730; -.
DR   PaxDb; 4932-YAL035W; -.
DR   PeptideAtlas; P39730; -.
DR   EnsemblFungi; YAL035W_mRNA; YAL035W; YAL035W.
DR   GeneID; 851196; -.
DR   KEGG; sce:YAL035W; -.
DR   AGR; SGD:S000000033; -.
DR   SGD; S000000033; FUN12.
DR   VEuPathDB; FungiDB:YAL035W; -.
DR   eggNOG; KOG1144; Eukaryota.
DR   GeneTree; ENSGT00940000163243; -.
DR   HOGENOM; CLU_002656_1_0_1; -.
DR   InParanoid; P39730; -.
DR   OMA; EFAVMLC; -.
DR   OrthoDB; 169393at2759; -.
DR   BioCyc; YEAST:G3O-28845-MONOMER; -.
DR   Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   BioGRID-ORCS; 851196; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P39730; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P39730; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IDA:SGD.
DR   GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:SGD.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR   GO; GO:0042256; P:cytosolic ribosome assembly; IMP:SGD.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IDA:SGD.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0006446; P:regulation of translational initiation; IMP:SGD.
DR   GO; GO:0042255; P:ribosome assembly; IMP:SGD.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   CDD; cd03703; aeIF5B_II; 1.
DR   CDD; cd16266; IF2_aeIF5B_IV; 1.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   InterPro; IPR029459; EFTU-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; GTP-binding; Hydrolase; Initiation factor;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Protein biosynthesis; Reference proteome; Sodium.
FT   CHAIN           1..1002
FT                   /note="Eukaryotic translation initiation factor 5B"
FT                   /id="PRO_0000137296"
FT   DOMAIN          403..621
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          1..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..419
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          437..441
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          476..479
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          530..533
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          598..600
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   COMPBIAS        25..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..340
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..371
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         415..420
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:24686316"
FT   BINDING         415
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         415
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         419
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         431
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         437..439
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         437
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         437
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         439
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT   BINDING         530..533
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:24686316"
FT   BINDING         599..600
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|PubMed:24686316"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         439
FT                   /note="T->A: Impairs the GTPase activity, but not the
FT                   ribosome joining function."
FT                   /evidence="ECO:0000269|PubMed:12507428"
FT   MUTAGEN         479
FT                   /note="G->A: Reduces GTP binding and impairs subunit
FT                   joining and ribosome-dependent GTP hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:17913624"
FT   MUTAGEN         480
FT                   /note="H->E: Impairs the GTPase activity, but not the
FT                   ribosome joining function."
FT                   /evidence="ECO:0000269|PubMed:12471154,
FT                   ECO:0000269|PubMed:12507428"
FT   CONFLICT        266
FT                   /note="L -> V (in Ref. 4; AAA57228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="A -> S (in Ref. 4; AAA57228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="A -> D (in Ref. 4; AAA57228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="G -> R (in Ref. 4; AAA57228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        641
FT                   /note="E -> Q (in Ref. 4; AAA57228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        722
FT                   /note="L -> H (in Ref. 4; AAA57228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        970
FT                   /note="R -> T (in Ref. 4; AAA57228)"
FT                   /evidence="ECO:0000305"
FT   STRAND          407..411
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           414..416
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   HELIX           421..425
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          428..430
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          439..441
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          442..448
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           449..456
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           457..461
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          469..475
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          478..480
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           481..483
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           487..489
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           490..493
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          495..502
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   TURN            503..505
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           509..521
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          525..530
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           532..534
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           546..551
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           555..573
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   TURN            574..576
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          578..581
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           582..584
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   TURN            588..590
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          591..596
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   TURN            599..601
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           605..619
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   TURN            621..624
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          631..640
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   TURN            641..643
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          644..657
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          661..666
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          669..681
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           685..688
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          692..709
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          720..723
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          726..728
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           730..746
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          750..752
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          755..761
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           762..774
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          779..781
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          784..787
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           789..796
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           798..801
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           803..805
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          807..812
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           817..826
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          829..835
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   HELIX           836..851
FT                   /evidence="ECO:0007829|PDB:4N3S"
FT   STRAND          866..879
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          881..892
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          896..903
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   TURN            904..907
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          908..922
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          925..931
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          939..944
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   TURN            954..956
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   STRAND          963..965
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   HELIX           969..974
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   HELIX           978..981
FT                   /evidence="ECO:0007829|PDB:3WBI"
FT   HELIX           986..999
FT                   /evidence="ECO:0007829|PDB:3WBI"
SQ   SEQUENCE   1002 AA;  112268 MW;  1A496195DAE1C283 CRC64;
     MAKKSKKNQQ NYWDEEFEED AAQNEEISAT PTPNPESSAG ADDTSREASA SAEGAEAIEG
     DFMSTLKQSK KKQEKKVIEE KKDGKPILKS KKEKEKEKKE KEKQKKKEQA ARKKAQQQAQ
     KEKNKELNKQ NVEKAAAEKA AAEKSQKSKG ESDKPSASAK KPAKKVPAGL AALRRQLELK
     KQLEEQEKLE REEEERLEKE EEERLANEEK MKEEAKAAKK EKEKAKREKR KAEGKLLTRK
     QKEEKKLLER RRAALLSSGN VKVAGLAKKD GEENKPKKVV YSKKKKRTTQ ENASEAIKSD
     SKKDSEVVPD DELKESEDVL IDDWENLALG DDDEEGTNEE TQESTASHEN EDQNQGEEEE
     EGEEEEEEEE ERAHVHEVAK STPAATPAAT PTPSSASPNK KDLRSPICCI LGHVDTGKTK
     LLDKIRQTNV QGGEAGGITQ QIGATYFPID AIKAKTKVMA EYEKQTFDVP GLLVIDTPGH
     ESFSNLRSRG SSLCNIAILV IDIMHGLEQQ TIESIKLLRD RKAPFVVALN KIDRLYDWKA
     IPNNSFRDSF AKQSRAVQEE FQSRYSKIQL ELAEQGLNSE LYFQNKNMSK YVSIVPTSAV
     TGEGVPDLLW LLLELTQKRM SKQLMYLSHV EATILEVKVV EGFGTTIDVI LSNGYLREGD
     RIVLCGMNGP IVTNIRALLT PQPLRELRLK SEYVHHKEVK AALGVKIAAN DLEKAVSGSR
     LLVVGPEDDE DELMDDVMDD LTGLLDSVDT TGKGVVVQAS TLGSLEALLD FLKDMKIPVM
     SIGLGPVYKR DVMKASTMLE KAPEYAVMLC FDVKVDKEAE QYAEQEGIKI FNADVIYHLF
     DSFTAYQEKL LEERRKDFLD YAIFPCVLQT LQIINKRGPM IIGVDVLEGT LRVGTPICAV
     KTDPTTKERQ TLILGKVISL EINHQPVQEV KKGQTAAGVA VRLEDPSGQQ PIWGRHVDEN
     DTLYSLVSRR SIDTLKDKAF RDQVARSDWL LLKKLKVVFG IE
//