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}; 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
//
