DCPS_YEAST
ID DCPS_YEAST Reviewed; 350 AA.
AC Q06151; D6VYR7; Q6Q5L1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=m7GpppX diphosphatase;
DE EC=3.6.1.59 {ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:22985415};
DE AltName: Full=DCS-1;
DE AltName: Full=Hint-related 7meGMP-directed hydrolase 1;
DE AltName: Full=Protein Dcs1p;
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS;
GN Name=DCS1 {ECO:0000312|SGD:S000004260}; OrderedLocusNames=YLR270W;
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] {ECO:0000305, ECO:0000312|EMBL:AAN84614.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF HIS-268.
RX PubMed=12198172; DOI=10.1093/emboj/cdf448;
RA Liu H., Rodgers N.D., Jiao X., Kiledjian M.;
RT "The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of
RT pyrophosphatases.";
RL EMBO J. 21:4699-4708(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB67372.1}
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 [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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=14523240; DOI=10.1073/pnas.1635192100;
RA van Dijk E., Le Hir H., Seraphin B.;
RT "DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5'
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12081-12086(2003).
RN [8] {ECO:0000305}
RP FUNCTION, SUBUNIT, PHOSPHORYLATION AT THR-66, SUBCELLULAR LOCATION,
RP INDUCTION, AND MUTAGENESIS OF THR-66.
RX PubMed=15240832; DOI=10.1093/nar/gkh687;
RA Malys N., Carroll K., Miyan J., Tollervey D., McCarthy J.E.G.;
RT "The 'scavenger' m7GpppX pyrophosphatase activity of Dcs1 modulates
RT nutrient-induced responses in yeast.";
RL Nucleic Acids Res. 32:3590-3600(2004).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=15273322; DOI=10.1261/rna.7660804;
RA Liu S.-W., Jiao X., Liu H., Gu M., Lima C.D., Kiledjian M.;
RT "Functional analysis of mRNA scavenger decapping enzymes.";
RL RNA 10:1412-1422(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16207815; DOI=10.1091/mbc.e05-07-0622;
RA Lall S., Piano F., Davis R.E.;
RT "Caenorhabditis elegans decapping proteins: localization and functional
RT analysis of Dcp1, Dcp2, and DcpS during embryogenesis.";
RL Mol. Biol. Cell 16:5880-5890(2005).
RN [11]
RP FUNCTION.
RX PubMed=16260594; DOI=10.1128/mcb.25.22.9764-9772.2005;
RA Liu H., Kiledjian M.;
RT "Scavenger decapping activity facilitates 5' to 3' mRNA decay.";
RL Mol. Cell. Biol. 25:9764-9772(2005).
RN [12]
RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=16963086; DOI=10.1016/j.jmb.2006.08.015;
RA Malys N., McCarthy J.E.;
RT "Dcs2, a novel stress-induced modulator of m7GpppX pyrophosphatase activity
RT that locates to P bodies.";
RL J. Mol. Biol. 363:370-382(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-66; TYR-70 AND
RP THR-120, AND IDENTIFICATION BY 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 [16]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RX PubMed=22985415; DOI=10.1021/bi300781g;
RA Wypijewska A., Bojarska E., Lukaszewicz M., Stepinski J., Jemielity J.,
RA Davis R.E., Darzynkiewicz E.;
RT "7-Methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but strongly
RT bound by decapping scavenger (dcpS) enzymes and potently inhibits their
RT activity.";
RL Biochemistry 51:8003-8013(2012).
RN [17]
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).
CC -!- FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a
CC residual cap structure following the degradation of mRNAs by the 3'->5'
CC exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures
CC like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl
CC guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10
CC nucleotide substrates (small capped oligoribonucleotides) and
CC specifically releases 5'-phosphorylated RNA fragments and 7-
CC methylguanosine monophosphate (m7GMP) or tri-methyl guanosine
CC nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not
CC hydrolyze unmethylated cap analog (GpppG) and shows no decapping
CC activity on intact m7GpppG-capped mRNA molecules longer than 25
CC nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP)
CC and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and
CC m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in
CC the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by
CC the 5'->3' mRNA mediated decapping activity, may be also converted by
CC DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to
CC m7GDP. May also regulate the 5'->3' exoribonucleolytic mRNA decay
CC pathway in a cap-independent manner. Negatively regulates trehalase
CC activity. {ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:14523240,
CC ECO:0000269|PubMed:15240832, ECO:0000269|PubMed:15273322,
CC ECO:0000269|PubMed:16260594, ECO:0000269|PubMed:16963086,
CC ECO:0000269|PubMed:22985415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616;
CC EC=3.6.1.59; Evidence={ECO:0000269|PubMed:15273322,
CC ECO:0000269|PubMed:22985415};
CC -!- ACTIVITY REGULATION: The hydrolytic product 7-methylguanosine
CC diphosphate (m7GDP) efficiently inhibits the decapping scavenger
CC activity and acts as a competitive inhibitor in vitro.
CC {ECO:0000269|PubMed:22985415}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 uM for m7GpppG (homodimer) {ECO:0000269|PubMed:16963086};
CC KM=0.26 uM for m7GDP (homodimer) {ECO:0000269|PubMed:16963086};
CC KM=1.01 uM for m7GpppG (heterodimer) {ECO:0000269|PubMed:16963086};
CC KM=0.76 uM for m7GDP (heterodimer) {ECO:0000269|PubMed:16963086};
CC Note=kcat is 0.012 sec(-1) with m7GpppG as substrate (homodimer).
CC kcat is 0.0015 sec(-1) with m7GpppG as substrate (heterodimer). kcat
CC is 0.0017 sec(-1) with m7GDP as substrate (homodimer). kcat is 0.0005
CC sec(-1) with m7GDP as substrate (heterodimer). The homodimer
CC catalytic efficiency with m7GpppG is at least 8-fold higher than with
CC the heterodimer. The homodimer catalytic efficiency with m7GDP is at
CC least 3.4-fold higher than with the heterodimer.;
CC -!- SUBUNIT: Homodimer. Forms heterodimer with DCS2; the interaction
CC inhibits the DCS1 scavenger decapping activity during post-diauxic
CC growth. {ECO:0000269|PubMed:15240832, ECO:0000269|PubMed:16963086}.
CC -!- INTERACTION:
CC Q06151; Q06151: DCS1; NbExp=4; IntAct=EBI-38973, EBI-38973;
CC Q06151; Q12123: DCS2; NbExp=8; IntAct=EBI-38973, EBI-38701;
CC Q06151; P32356: NTH1; NbExp=3; IntAct=EBI-38973, EBI-19509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Cytoplasm, P-body. Note=Predominantly cytoplasmic.
CC -!- INDUCTION: By nutrient, osmotic, oxidative and heat stress. Up-
CC regulated during the diauxic shift. {ECO:0000269|PubMed:15240832}.
CC -!- DOMAIN: The C-terminal histidine triad (HIT) motif and the N-terminal
CC domain are required for the decapping activity.
CC {ECO:0000269|PubMed:15273322}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs upon glucose deprivation.
CC {ECO:0000269|PubMed:15240832}.
CC -!- MISCELLANEOUS: Present with 9920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000255}.
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DR EMBL; AY165035; AAN84614.1; -; mRNA.
DR EMBL; U17244; AAB67372.1; -; Genomic_DNA.
DR EMBL; AY557955; AAS56281.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09583.1; -; Genomic_DNA.
DR PIR; S51406; S51406.
DR RefSeq; NP_013372.1; NM_001182157.1.
DR PDB; 5BV3; X-ray; 2.25 A; A/B/C/D=8-350.
DR PDB; 6TRQ; X-ray; 2.94 A; A/B/C/D=8-350.
DR PDBsum; 5BV3; -.
DR PDBsum; 6TRQ; -.
DR AlphaFoldDB; Q06151; -.
DR SMR; Q06151; -.
DR BioGRID; 31537; 83.
DR ComplexPortal; CPX-1179; DCS1 decapping scavenger complex.
DR ComplexPortal; CPX-1185; DCS1-DCS2 regulator of decapping scavenger complex.
DR DIP; DIP-1480N; -.
DR IntAct; Q06151; 4.
DR MINT; Q06151; -.
DR STRING; 4932.YLR270W; -.
DR iPTMnet; Q06151; -.
DR MaxQB; Q06151; -.
DR PaxDb; Q06151; -.
DR PRIDE; Q06151; -.
DR EnsemblFungi; YLR270W_mRNA; YLR270W; YLR270W.
DR GeneID; 850974; -.
DR KEGG; sce:YLR270W; -.
DR SGD; S000004260; DCS1.
DR VEuPathDB; FungiDB:YLR270W; -.
DR eggNOG; KOG3969; Eukaryota.
DR GeneTree; ENSGT00390000003924; -.
DR HOGENOM; CLU_041045_0_1_1; -.
DR InParanoid; Q06151; -.
DR OMA; WVYNCLE; -.
DR BioCyc; YEAST:G3O-32369-MON; -.
DR BRENDA; 3.6.1.59; 984.
DR Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:Q06151; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06151; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0106095; C:m7G(5')pppN diphosphatase complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0044692; F:exoribonuclease activator activity; IDA:SGD.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:SGD.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:SGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
DR GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; IMP:SGD.
DR GO; GO:1901919; P:positive regulation of exoribonuclease activity; IDA:SGD.
DR GO; GO:1903398; P:regulation of m7G(5')pppN diphosphatase activity; IDA:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0007584; P:response to nutrient; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR Gene3D; 3.30.200.40; -; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; PTHR12978; 1.
DR Pfam; PF05652; DcpS; 1.
DR PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR SUPFAM; SSF102860; SSF102860; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..350
FT /note="m7GpppX diphosphatase"
FT /id="PRO_0000109798"
FT MOTIF 266..270
FT /note="Histidine triad motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96C86"
FT BINDING 259..270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15240832,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 66
FT /note="Phosphothreonine; by YAK1"
FT /evidence="ECO:0000305|PubMed:15240832,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 70
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 66
FT /note="T->A: Strongly reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:15240832"
FT MUTAGEN 268
FT /note="H->N: Loss of function."
FT /evidence="ECO:0000269|PubMed:12198172"
FT CONFLICT 66
FT /note="T -> I (in Ref. 4; AAS56281)"
FT /evidence="ECO:0000305"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:6TRQ"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:5BV3"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:5BV3"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:5BV3"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:5BV3"
SQ SEQUENCE 350 AA; 40770 MW; 06A57C2344A3580A CRC64;
MSQLPTDFAS LIKRFQFVSV LDSNPQTKVM SLLGTIDNKD AIITAEKTHF LFDETVRRPS
QDGRSTPVLY NCENEYSCIN GIQELKEITS NDIYYWGLSV IKQDMESNPT AKLNLIWPAT
PIHIKKYEQQ NFHLVRETPE MYKRIVQPYI EEMCNNGRLK WVNNILYEGA ESERVVYKDF
SEENKDDGFL ILPDMKWDGM NLDSLYLVAI VYRTDIKTIR DLRYSDRQWL INLNNKIRSI
VPGCYNYAVH PDELRILVHY QPSYYHFHIH IVNIKHPGLG NSIAAGKAIL LEDIIEMLNY
LGPEGYMNKT ITYAIGENHD LWKRGLEEEL TKQLERDGIP KIPKIVNGFK
