HMT1_YEAST
ID HMT1_YEAST Reviewed; 348 AA.
AC P38074; D6VQ34;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000303|PubMed:8647869};
DE EC=2.1.1.- {ECO:0000269|PubMed:8647869, ECO:0000269|PubMed:8668183};
DE AltName: Full=Major type I protein arginine N-methyltransferase {ECO:0000305|PubMed:8647869};
DE Short=Type I PRMT {ECO:0000303|PubMed:22997150};
DE AltName: Full=hnRNP arginine N-methyltransferase {ECO:0000303|PubMed:8668183};
GN Name=HMT1 {ECO:0000303|PubMed:8668183};
GN Synonyms=ODP1 {ECO:0000303|PubMed:7896706},
GN RMT1 {ECO:0000303|PubMed:8647869};
GN OrderedLocusNames=YBR034C {ECO:0000312|SGD:S000000238}; ORFNames=YBR0320;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RX PubMed=7896706; DOI=10.1128/jb.177.7.1817-1823.1995;
RA Loubbardi A., Karst F., Guilloton M., Marcireau C.;
RT "Sterol uptake induced by an impairment of pyridoxal phosphate synthesis in
RT Saccharomyces cerevisiae: cloning and sequencing of the PDX3 gene encoding
RT pyridoxine (pyridoxamine) phosphate oxidase.";
RL J. Bacteriol. 177:1817-1823(1995).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8668183; DOI=10.1128/mcb.16.7.3668;
RA Henry M.F., Silver P.A.;
RT "A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding
RT proteins.";
RL Mol. Cell. Biol. 16:3668-3678(1996).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8647869; DOI=10.1074/jbc.271.21.12585;
RA Gary J.D., Lin W.-J., Yang M.C., Herschmann H.R., Clarke S.;
RT "The predominant protein-arginine methyltransferase from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 271:12585-12594(1996).
RN [8]
RP FUNCTION.
RX PubMed=9499403; DOI=10.1101/gad.12.5.679;
RA Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.;
RT "Arginine methylation facilitates the nuclear export of hnRNP proteins.";
RL Genes Dev. 12:679-691(1998).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLU-18 AND GLY-68.
RX PubMed=10652296; DOI=10.1074/jbc.275.5.3128;
RA McBride A.E., Weiss V.H., Kim H.K., Hogle J.M., Silver P.A.;
RT "Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in
RT vivo function. Cofactor binding and substrate interactions.";
RL J. Biol. Chem. 275:3128-3136(2000).
RN [10]
RP FUNCTION.
RX PubMed=11779864; DOI=10.1074/jbc.m110053200;
RA Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H.;
RT "Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and
RT is regulated by arginine methylation via Hmt1p.";
RL J. Biol. Chem. 277:7752-7760(2002).
RN [11]
RP FUNCTION.
RX PubMed=12097318; DOI=10.1074/jbc.c200366200;
RA Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.;
RT "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3
RT methyltransferase.";
RL J. Biol. Chem. 277:30421-30424(2002).
RN [12]
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 [13]
RP FUNCTION.
RX PubMed=12756332; DOI=10.1261/rna.5020803;
RA Xu C., Henry P.A., Setya A., Henry M.F.;
RT "In vivo analysis of nucleolar proteins modified by the yeast arginine
RT methyltransferase Hmt1/Rmt1p.";
RL RNA 9:746-759(2003).
RN [14]
RP FUNCTION.
RX PubMed=15314027; DOI=10.1101/gad.1223204;
RA Yu M.C., Bachand F., McBride A.E., Komili S., Casolari J.M., Silver P.A.;
RT "Arginine methyltransferase affects interactions and recruitment of mRNA
RT processing and export factors.";
RL Genes Dev. 18:2024-2035(2004).
RN [15]
RP FUNCTION.
RX PubMed=17158743; DOI=10.1101/gad.1495206;
RA Yu M.C., Lamming D.W., Eskin J.A., Sinclair D.A., Silver P.A.;
RT "The role of protein arginine methylation in the formation of silent
RT chromatin.";
RL Genes Dev. 20:3249-3254(2006).
RN [16]
RP FUNCTION.
RX PubMed=20035717; DOI=10.1016/j.bbrc.2009.12.112;
RA Lipson R.S., Webb K.J., Clarke S.G.;
RT "Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal
RT protein Rps2 in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 391:1658-1662(2010).
RN [17]
RP FUNCTION.
RX PubMed=20823272; DOI=10.1128/mcb.00359-10;
RA Chen Y.C., Milliman E.J., Goulet I., Cote J., Jackson C.A.,
RA Vollbracht J.A., Yu M.C.;
RT "Protein arginine methylation facilitates cotranscriptional recruitment of
RT pre-mRNA splicing factors.";
RL Mol. Cell. Biol. 30:5245-5256(2010).
RN [18]
RP FUNCTION.
RX PubMed=20053728; DOI=10.1093/nar/gkp1133;
RA Wong C.M., Tang H.M., Kong K.Y., Wong G.W., Qiu H., Jin D.Y.,
RA Hinnebusch A.G.;
RT "Yeast arginine methyltransferase Hmt1p regulates transcription elongation
RT and termination by methylating Npl3p.";
RL Nucleic Acids Res. 38:2217-2228(2010).
RN [19]
RP FUNCTION, AND INTERACTION WITH BRE5; MTR4; SNF2; SUM1 AND SSD1.
RX PubMed=22997150; DOI=10.1002/pmic.201200132;
RA Jackson C.A., Yadav N., Min S., Li J., Milliman E.J., Qu J., Chen Y.C.,
RA Yu M.C.;
RT "Proteomic analysis of interactors for yeast protein arginine
RT methyltransferase Hmt1 reveals novel substrate and insights into additional
RT biological roles.";
RL Proteomics 12:3304-3314(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-348, FUNCTION, INTERACTION WITH
RP NPL3, AND SUBUNIT.
RX PubMed=11101900; DOI=10.1038/82028;
RA Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A.,
RA Hogle J.M.;
RT "The structure and oligomerization of the yeast arginine methyltransferase,
RT Hmt1.";
RL Nat. Struct. Biol. 7:1165-1171(2000).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC methyltransferase that catalyzes both the mono- and asymmetric (type I)
CC dimethylation of the guanidino nitrogens of arginine residues in a
CC variety of RNA-binding proteins such as heterogeneous nuclear
CC ribonucleoproteins (hnRNPs) and small nuclear ribonucleoproteins
CC (snRNPs) (PubMed:8668183, PubMed:8647869). Methylates NAB2, NPL3, HRP1
CC and YRA1, shuttling hnRNPs involved in mRNA processing and export,
CC facilitating their export out of the nucleus (PubMed:8668183,
CC PubMed:9499403, PubMed:10652296, PubMed:11779864, PubMed:15314027).
CC Methylation of NPL3 weakens its interaction with THO2, a component of
CC the TREX (transcription/export) complex important for transcriptional
CC elongation and recruitment of mRNA export factors (PubMed:15314027,
CC PubMed:20053728). Methylates the hnRNP HRB1, but does not influence its
CC subcellular location (PubMed:9499403). Methylates the nucleolar
CC proteins GAR1, NOP1 and NSR1 (PubMed:12756332). Methylates the snRNP
CC SNP1 and modulates the cotranscriptional recruitment of splicing
CC factors (PubMed:20823272). Dimethylates free histone H4 (HHF1/HHF2) at
CC 'Arg-4' (H4R3me2a) and plays a role in preservation and establishment
CC of silent chromatin domains (PubMed:12097318, PubMed:17158743).
CC Mono- and dimethylates ribosomal protein S2 (RPS2) at 'Arg-11'
CC (PubMed:20035717). Methylates the catalytic subunit of the SWI/SNF
CC chromatin-remodeling complex SNF2 (PubMed:22997150).
CC {ECO:0000269|PubMed:10652296, ECO:0000269|PubMed:11101900,
CC ECO:0000269|PubMed:11779864, ECO:0000269|PubMed:12097318,
CC ECO:0000269|PubMed:12756332, ECO:0000269|PubMed:15314027,
CC ECO:0000269|PubMed:17158743, ECO:0000269|PubMed:20035717,
CC ECO:0000269|PubMed:20053728, ECO:0000269|PubMed:20823272,
CC ECO:0000269|PubMed:22997150, ECO:0000269|PubMed:8647869,
CC ECO:0000269|PubMed:8668183, ECO:0000269|PubMed:9499403}.
CC -!- SUBUNIT: Homodimer. The dimers can then associate to form a ring-shaped
CC homohexamer. Interacts with NPL3, BRE5, MTR4, SNF2, SUM1, AND SSD1.
CC {ECO:0000269|PubMed:11101900, ECO:0000269|PubMed:22997150}.
CC -!- INTERACTION:
CC P38074; P53741: BRE5; NbExp=2; IntAct=EBI-8394, EBI-28528;
CC P38074; P22204: DBF2; NbExp=4; IntAct=EBI-8394, EBI-5569;
CC P38074; P38074: HMT1; NbExp=3; IntAct=EBI-8394, EBI-8394;
CC P38074; P47047: MTR4; NbExp=2; IntAct=EBI-8394, EBI-11592;
CC P38074; P32505: NAB2; NbExp=2; IntAct=EBI-8394, EBI-11770;
CC P38074; Q01560: NPL3; NbExp=9; IntAct=EBI-8394, EBI-12114;
CC P38074; P23595: PPH22; NbExp=3; IntAct=EBI-8394, EBI-12752;
CC P38074; P22082: SNF2; NbExp=3; IntAct=EBI-8394, EBI-17526;
CC P38074; P24276: SSD1; NbExp=2; IntAct=EBI-8394, EBI-18153;
CC P38074; P46676: SUM1; NbExp=2; IntAct=EBI-8394, EBI-18547;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8668183}.
CC -!- MISCELLANEOUS: Present with 37600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; X76078; CAA53689.1; -; Genomic_DNA.
DR EMBL; Z35903; CAA84976.1; -; Genomic_DNA.
DR EMBL; X76992; CAA54296.1; -; Genomic_DNA.
DR EMBL; AY557869; AAS56195.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07154.1; -; Genomic_DNA.
DR PIR; S45890; S45890.
DR RefSeq; NP_009590.1; NM_001178382.1.
DR PDB; 1G6Q; X-ray; 2.90 A; 1/2/3/4/5/6=21-348.
DR PDBsum; 1G6Q; -.
DR AlphaFoldDB; P38074; -.
DR SMR; P38074; -.
DR BioGRID; 32735; 445.
DR DIP; DIP-2608N; -.
DR IntAct; P38074; 264.
DR MINT; P38074; -.
DR STRING; 4932.YBR034C; -.
DR iPTMnet; P38074; -.
DR MaxQB; P38074; -.
DR PaxDb; P38074; -.
DR PRIDE; P38074; -.
DR EnsemblFungi; YBR034C_mRNA; YBR034C; YBR034C.
DR GeneID; 852322; -.
DR KEGG; sce:YBR034C; -.
DR SGD; S000000238; HMT1.
DR VEuPathDB; FungiDB:YBR034C; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000175369; -.
DR HOGENOM; CLU_017375_1_1_1; -.
DR InParanoid; P38074; -.
DR OMA; RNDFVHA; -.
DR BioCyc; YEAST:G3O-29011-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; P38074; -.
DR PRO; PR:P38074; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38074; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:SGD.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:SGD.
DR GO; GO:0046656; P:folic acid biosynthetic process; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0060567; P:negative regulation of DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..348
FT /note="Protein arginine N-methyltransferase 1"
FT /id="PRO_0000212341"
FT DOMAIN 20..322
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 132
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT ACT_SITE 141
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT MUTAGEN 18
FT /note="E->V: Cold-sensitive; reduces catalytic activity
FT more than 20-fold at 14 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:10652296"
FT MUTAGEN 68
FT /note="G->A: Reduces catalytic activity between 5- to 25-
FT fold."
FT /evidence="ECO:0000269|PubMed:10652296"
FT MUTAGEN 68
FT /note="G->R: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:10652296"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 40..57
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:1G6Q"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1G6Q"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:1G6Q"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 286..296
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 302..312
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 315..328
FT /evidence="ECO:0007829|PDB:1G6Q"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:1G6Q"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:1G6Q"
SQ SEQUENCE 348 AA; 39786 MW; 383AF61033FB4AC2 CRC64;
MSKTAVKDSA TEKTKLSESE QHYFNSYDHY GIHEEMLQDT VRTLSYRNAI IQNKDLFKDK
IVLDVGCGTG ILSMFAAKHG AKHVIGVDMS SIIEMAKELV ELNGFSDKIT LLRGKLEDVH
LPFPKVDIII SEWMGYFLLY ESMMDTVLYA RDHYLVEGGL IFPDKCSIHL AGLEDSQYKD
EKLNYWQDVY GFDYSPFVPL VLHEPIVDTV ERNNVNTTSD KLIEFDLNTV KISDLAFKSN
FKLTAKRQDM INGIVTWFDI VFPAPKGKRP VEFSTGPHAP YTHWKQTIFY FPDDLDAETG
DTIEGELVCS PNEKNNRDLN IKISYKFESN GIDGNSRSRK NEGSYLMH
