ID   NEP1_YEAST              Reviewed;         252 AA.
AC   Q06287; D6VYI9; E9P8U2;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase NEP1 {ECO:0000305|PubMed:20972225};
DE            EC=2.1.1.260 {ECO:0000269|PubMed:20972225};
DE   AltName: Full=18S rRNA (pseudouridine(1189)-N1)-methyltransferase {ECO:0000303|PubMed:20972225};
DE            Short=18S rRNA Psi1189 methyltransferase {ECO:0000303|PubMed:20972225};
DE   AltName: Full=Essential for mitotic growth protein 1 {ECO:0000303|PubMed:11694595};
DE   AltName: Full=Nucleolar essential protein 1 {ECO:0000303|PubMed:11935223};
GN   Name=EMG1 {ECO:0000303|PubMed:11694595};
GN   Synonyms=NEP1 {ECO:0000303|PubMed:11935223};
GN   OrderedLocusNames=YLR186W {ECO:0000312|SGD:S000004176};
GN   ORFNames=L9470.5;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   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   FUNCTION, INTERACTION WITH NOP14, AND SUBCELLULAR LOCATION.
RX   PubMed=11694595; DOI=10.1091/mbc.12.11.3644;
RA   Liu P.C., Thiele D.J.;
RT   "Novel stress-responsive genes EMG1 and NOP14 encode conserved, interacting
RT   proteins required for 40S ribosome biogenesis.";
RL   Mol. Biol. Cell 12:3644-3657(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=11935223; DOI=10.1007/s00294-001-0269-4;
RA   Eschrich D., Buchhaupt M., Koetter P., Entian K.-D.;
RT   "Nep1p (Emg1p), a novel protein conserved in eukaryotes and archaea, is
RT   involved in ribosome biogenesis.";
RL   Curr. Genet. 40:326-338(2002).
RN   [6]
RP   FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP   PROCESSOME, AND SUBCELLULAR LOCATION.
RX   PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA   Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA   Baserga S.J.;
RT   "The small-subunit processome is a ribosome assembly intermediate.";
RL   Eukaryot. Cell 3:1619-1626(2004).
RN   [7]
RP   MUTAGENESIS OF ARG-88; ARG-129; ARG-132 AND ARG-136.
RX   PubMed=18208838; DOI=10.1093/nar/gkm1172;
RA   Taylor A.B., Meyer B., Leal B.Z., Kotter P., Schirf V., Demeler B.,
RA   Hart P.J., Entian K.D., Wohnert J.;
RT   "The crystal structure of Nep1 reveals an extended SPOUT-class
RT   methyltransferase fold and a pre-organized SAM-binding site.";
RL   Nucleic Acids Res. 36:1542-1554(2008).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   ASP-90.
RX   PubMed=20972225; DOI=10.1093/nar/gkq931;
RA   Meyer B., Wurm J.P., Kotter P., Leisegang M.S., Schilling V., Buchhaupt M.,
RA   Held M., Bahr U., Karas M., Heckel A., Bohnsack M.T., Wohnert J.,
RA   Entian K.D.;
RT   "The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in
RT   eukaryotic ribosome biogenesis, as an essential assembly factor and in the
RT   methylation of Psi1191 in yeast 18S rRNA.";
RL   Nucleic Acids Res. 39:1526-1537(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH SAM,
RP   RNA-BINDING, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-88;
RP   ASP-214; LEU-232 AND ALA-237.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=18063569; DOI=10.1093/nar/gkm1074;
RA   Leulliot N., Bohnsack M.T., Graille M., Tollervey D., Van Tilbeurgh H.;
RT   "The yeast ribosome synthesis factor Emg1 is a novel member of the
RT   superfamily of alpha/beta knot fold methyltransferases.";
RL   Nucleic Acids Res. 36:629-639(2008).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE AND COGNATE RNA, AND FUNCTION.
RX   PubMed=21087996; DOI=10.1093/nar/gkq1131;
RA   Thomas S.R., Keller C.A., Szyk A., Cannon J.R., Laronde-Leblanc N.A.;
RT   "Structural insight into the functional mechanism of Nep1/Emg1 N1-specific
RT   pseudouridine methyltransferase in ribosome biogenesis.";
RL   Nucleic Acids Res. 39:2445-2457(2011).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)-
CC       methyltransferase that methylates pseudouridine at position 1189
CC       (Psi1189) in 18S rRNA. Involved the biosynthesis of the hypermodified
CC       N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi)
CC       conserved in eukaryotic 18S rRNA. N1-methylation is independent on acp-
CC       modification at the N3-position of U1191. Has also an essential role in
CC       40S ribosomal subunit biogenesis independent on its methyltransferase
CC       activity, facilitating the incorporation of ribosomal protein S19
CC       (RPS19A/RPS19B) during the formation of pre-ribosomes.
CC       {ECO:0000269|PubMed:11694595, ECO:0000269|PubMed:11935223,
CC       ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:20972225,
CC       ECO:0000269|PubMed:21087996}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pseudouridine(1191) in yeast 18S rRNA + S-adenosyl-L-
CC         methionine = H(+) + N(1)-methylpseudouridine(1191) in yeast 18S rRNA
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54308, Rhea:RHEA-
CC         COMP:13851, Rhea:RHEA-COMP:13852, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314,
CC         ChEBI:CHEBI:74890; EC=2.1.1.260;
CC         Evidence={ECO:0000269|PubMed:20972225};
CC   -!- SUBUNIT: Homodimer. Interacts with snoRNA U3. Interacts with NOP14 and
CC       MPP10. Component of the ribosomal small subunit (SSU) processome
CC       composed of at least 40 protein subunits and snoRNA U3.
CC       {ECO:0000269|PubMed:11694595, ECO:0000269|PubMed:15590835,
CC       ECO:0000269|PubMed:18063569}.
CC   -!- INTERACTION:
CC       Q06287; Q06287: EMG1; NbExp=3; IntAct=EBI-11979, EBI-11979;
CC       Q06287; Q99207: NOP14; NbExp=7; IntAct=EBI-11979, EBI-35157;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11694595,
CC       ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:20972225}.
CC   -!- DISRUPTION PHENOTYPE: Depletion of EMG1 affects growth and leads to
CC       strong ribosome biogenesis defects, with defects in 20S pre-rRNA and
CC       mature 18S rRNA species. {ECO:0000269|PubMed:18063569}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase NEP1 family. {ECO:0000305}.
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DR   EMBL; U17246; AAB67457.1; -; Genomic_DNA.
DR   EMBL; AY557941; AAS56267.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09505.1; -; Genomic_DNA.
DR   PIR; S51431; S51431.
DR   RefSeq; NP_013287.1; NM_001182073.1.
DR   PDB; 2V3J; X-ray; 2.00 A; A=1-252.
DR   PDB; 2V3K; X-ray; 2.00 A; A=1-252.
DR   PDB; 3OII; X-ray; 1.85 A; A/B=1-252.
DR   PDB; 3OIJ; X-ray; 3.00 A; A/B=1-252.
DR   PDB; 3OIN; X-ray; 1.90 A; A/B=1-252.
DR   PDB; 5JPQ; EM; 7.30 A; e/f=1-252.
DR   PDB; 5TZS; EM; 5.10 A; j/k=1-252.
DR   PDB; 5WLC; EM; 3.80 A; SJ/SK=1-252.
DR   PDB; 5WYJ; EM; 8.70 A; E1/E2=1-252.
DR   PDB; 5WYK; EM; 4.50 A; E1/E2=1-252.
DR   PDB; 6KE6; EM; 3.40 A; RG/RH=1-252.
DR   PDB; 6LQP; EM; 3.20 A; RG/RH=1-252.
DR   PDB; 6LQQ; EM; 4.10 A; RG/RH=1-252.
DR   PDB; 6LQR; EM; 8.60 A; RG/RH=1-252.
DR   PDB; 6LQS; EM; 3.80 A; RG/RH=1-252.
DR   PDB; 6LQT; EM; 4.90 A; RH=1-252.
DR   PDB; 6LQU; EM; 3.70 A; RG/RH=1-252.
DR   PDB; 6LQV; EM; 4.80 A; RG/RH=1-252.
DR   PDB; 6ZQA; EM; 4.40 A; JF/JG=1-252.
DR   PDB; 6ZQB; EM; 3.90 A; JF/JG=1-252.
DR   PDB; 6ZQC; EM; 3.80 A; JF/JG=1-252.
DR   PDB; 6ZQD; EM; 3.80 A; JF/JG=1-252.
DR   PDB; 6ZQE; EM; 7.10 A; JF/JG=1-252.
DR   PDB; 6ZQF; EM; 4.90 A; JF/JG=1-252.
DR   PDB; 6ZQG; EM; 3.50 A; JF/JG=1-252.
DR   PDB; 7AJT; EM; 4.60 A; JF/JG=1-252.
DR   PDB; 7AJU; EM; 3.80 A; JF/JG=1-252.
DR   PDB; 7D4I; EM; 4.00 A; RG/RH=1-252.
DR   PDB; 7D5S; EM; 4.60 A; RG/RH=1-252.
DR   PDB; 7D63; EM; 12.30 A; RG/RH=1-252.
DR   PDB; 7SUK; EM; 3.99 A; SJ/SK=16-251.
DR   PDBsum; 2V3J; -.
DR   PDBsum; 2V3K; -.
DR   PDBsum; 3OII; -.
DR   PDBsum; 3OIJ; -.
DR   PDBsum; 3OIN; -.
DR   PDBsum; 5JPQ; -.
DR   PDBsum; 5TZS; -.
DR   PDBsum; 5WLC; -.
DR   PDBsum; 5WYJ; -.
DR   PDBsum; 5WYK; -.
DR   PDBsum; 6KE6; -.
DR   PDBsum; 6LQP; -.
DR   PDBsum; 6LQQ; -.
DR   PDBsum; 6LQR; -.
DR   PDBsum; 6LQS; -.
DR   PDBsum; 6LQT; -.
DR   PDBsum; 6LQU; -.
DR   PDBsum; 6LQV; -.
DR   PDBsum; 6ZQA; -.
DR   PDBsum; 6ZQB; -.
DR   PDBsum; 6ZQC; -.
DR   PDBsum; 6ZQD; -.
DR   PDBsum; 6ZQE; -.
DR   PDBsum; 6ZQF; -.
DR   PDBsum; 6ZQG; -.
DR   PDBsum; 7AJT; -.
DR   PDBsum; 7AJU; -.
DR   PDBsum; 7D4I; -.
DR   PDBsum; 7D5S; -.
DR   PDBsum; 7D63; -.
DR   PDBsum; 7SUK; -.
DR   AlphaFoldDB; Q06287; -.
DR   EMDB; EMD-0949; -.
DR   EMDB; EMD-0950; -.
DR   EMDB; EMD-0951; -.
DR   EMDB; EMD-0952; -.
DR   EMDB; EMD-0953; -.
DR   EMDB; EMD-0954; -.
DR   EMDB; EMD-0955; -.
DR   EMDB; EMD-11357; -.
DR   EMDB; EMD-11358; -.
DR   EMDB; EMD-11359; -.
DR   EMDB; EMD-11360; -.
DR   EMDB; EMD-11361; -.
DR   EMDB; EMD-11362; -.
DR   EMDB; EMD-11363; -.
DR   EMDB; EMD-11807; -.
DR   EMDB; EMD-11808; -.
DR   EMDB; EMD-25441; -.
DR   EMDB; EMD-30574; -.
DR   EMDB; EMD-30584; -.
DR   EMDB; EMD-30588; -.
DR   EMDB; EMD-6695; -.
DR   EMDB; EMD-6696; -.
DR   EMDB; EMD-8473; -.
DR   EMDB; EMD-9964; -.
DR   SMR; Q06287; -.
DR   BioGRID; 31456; 500.
DR   ComplexPortal; CPX-1604; Small ribosomal subunit processome.
DR   DIP; DIP-6504N; -.
DR   IntAct; Q06287; 29.
DR   STRING; 4932.YLR186W; -.
DR   iPTMnet; Q06287; -.
DR   MaxQB; Q06287; -.
DR   PaxDb; 4932-YLR186W; -.
DR   PeptideAtlas; Q06287; -.
DR   TopDownProteomics; Q06287; -.
DR   EnsemblFungi; YLR186W_mRNA; YLR186W; YLR186W.
DR   GeneID; 850883; -.
DR   KEGG; sce:YLR186W; -.
DR   AGR; SGD:S000004176; -.
DR   SGD; S000004176; EMG1.
DR   VEuPathDB; FungiDB:YLR186W; -.
DR   eggNOG; KOG3073; Eukaryota.
DR   GeneTree; ENSGT00390000000305; -.
DR   HOGENOM; CLU_055846_1_1_1; -.
DR   InParanoid; Q06287; -.
DR   OMA; VHNTFEL; -.
DR   OrthoDB; 275493at2759; -.
DR   BioCyc; MetaCyc:G3O-32309-MONOMER; -.
DR   BioCyc; YEAST:G3O-32309-MONOMER; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 850883; 6 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q06287; -.
DR   PRO; PR:Q06287; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06287; Protein.
DR   GO; GO:0030686; C:90S preribosome; IDA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005880; C:nuclear microtubule; IDA:SGD.
DR   GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; IMP:SGD.
DR   GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR   GO; GO:0070475; P:rRNA base methylation; IMP:SGD.
DR   GO; GO:0031167; P:rRNA methylation; TAS:Reactome.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   CDD; cd18088; Nep1-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR12636; NEP1/MRA1; 1.
DR   PANTHER; PTHR12636:SF5; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE NEP1; 1.
DR   Pfam; PF03587; EMG1; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; Nucleus; Reference proteome;
KW   Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW   rRNA-binding; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..252
FT                   /note="Ribosomal RNA small subunit methyltransferase NEP1"
FT                   /id="PRO_0000158612"
FT   BINDING         180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:18063569,
FT                   ECO:0000269|PubMed:21087996"
FT   BINDING         207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:18063569,
FT                   ECO:0000269|PubMed:21087996"
FT   BINDING         212..214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:18063569,
FT                   ECO:0000269|PubMed:21087996"
FT   BINDING         227..232
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:18063569,
FT                   ECO:0000269|PubMed:21087996"
FT   SITE            88
FT                   /note="Interaction with substrate rRNA"
FT                   /evidence="ECO:0000269|PubMed:21087996"
FT   SITE            90
FT                   /note="Stabilizes Arg-88"
FT                   /evidence="ECO:0000303|PubMed:21087996"
FT   SITE            129
FT                   /note="Interaction with substrate rRNA"
FT                   /evidence="ECO:0000269|PubMed:21087996"
FT   SITE            132
FT                   /note="Interaction with substrate rRNA"
FT                   /evidence="ECO:0000269|PubMed:21087996"
FT   SITE            136
FT                   /note="Interaction with substrate rRNA"
FT                   /evidence="ECO:0000269|PubMed:21087996"
FT   MUTAGEN         88
FT                   /note="R->A: Loss of substrate rRNA binding."
FT                   /evidence="ECO:0000269|PubMed:18208838"
FT   MUTAGEN         88
FT                   /note="R->D: Loss of substrate rRNA binding. No effect on
FT                   growth."
FT                   /evidence="ECO:0000269|PubMed:18063569"
FT   MUTAGEN         90
FT                   /note="D->G: Loses its exclusive nucleolar localization and
FT                   mislocalizes to the cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:20972225"
FT   MUTAGEN         129
FT                   /note="R->A: Loss of substrate rRNA binding."
FT                   /evidence="ECO:0000269|PubMed:18208838"
FT   MUTAGEN         132
FT                   /note="R->A: Loss of substrate rRNA binding."
FT                   /evidence="ECO:0000269|PubMed:18208838"
FT   MUTAGEN         136
FT                   /note="R->A: Loss of substrate rRNA binding."
FT                   /evidence="ECO:0000269|PubMed:18208838"
FT   MUTAGEN         214
FT                   /note="D->R: Almost complete loss of SAM binding. No effect
FT                   on growth and ribosome biogenesis."
FT                   /evidence="ECO:0000269|PubMed:18063569"
FT   MUTAGEN         232
FT                   /note="L->S: Almost complete loss of SAM binding. No effect
FT                   on growth and ribosome biogenesis."
FT                   /evidence="ECO:0000269|PubMed:18063569"
FT   MUTAGEN         237
FT                   /note="A->D: Almost complete loss of SAM binding. No effect
FT                   on growth and ribosome biogenesis."
FT                   /evidence="ECO:0000269|PubMed:18063569"
FT   CONFLICT        114
FT                   /note="I -> T (in Ref. 3; AAS56267)"
FT                   /evidence="ECO:0000305"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:2V3J"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:3OIN"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:3OIN"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           74..79
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           89..100
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          110..116
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           134..147
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          155..163
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          173..180
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           189..194
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          201..207
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   TURN            216..220
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   STRAND          222..227
FT                   /evidence="ECO:0007829|PDB:3OII"
FT   HELIX           234..248
FT                   /evidence="ECO:0007829|PDB:3OII"
SQ   SEQUENCE   252 AA;  27895 MW;  4A8FCDA812051AD1 CRC64;
     MVEDSRVRDA LKGGDQKALP ASLVPQAPPV LTSKDKITKR MIVVLAMASL ETHKISSNGP
     GGDKYVLLNC DDHQGLLKKM GRDISEARPD ITHQCLLTLL DSPINKAGKL QVYIQTSRGI
     LIEVNPTVRI PRTFKRFSGL MVQLLHKLSI RSVNSEEKLL KVIKNPITDH LPTKCRKVTL
     SFDAPVIRVQ DYIEKLDDDE SICVFVGAMA RGKDNFADEY VDEKVGLSNY PLSASVACSK
     FCHGAEDAWN IL
//