DTD_ECOLI
ID DTD_ECOLI Reviewed; 145 AA.
AC P0A6M4; P32147; Q2M8I4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518, ECO:0000303|PubMed:10918062};
DE Short=DTD {ECO:0000255|HAMAP-Rule:MF_00518};
DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518, ECO:0000269|PubMed:10383414, ECO:0000269|PubMed:10918062, ECO:0000269|PubMed:4292198};
DE AltName: Full=D-tyrosyl RNA deacylase {ECO:0000303|PubMed:4292198};
DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase {ECO:0000303|PubMed:10383414};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518, ECO:0000303|PubMed:28362257};
DE AltName: Full=Gly-tRNA(Gly) deacylase {ECO:0000303|PubMed:27224426};
GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518, ECO:0000303|PubMed:10918062};
GN Synonyms=yihZ; OrderedLocusNames=b3887, JW3858;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / EC989, and K12 / K37;
RX PubMed=10383414; DOI=10.1074/jbc.274.27.19109;
RA Soutourina J., Plateau P., Delort F., Peirotes A., Blanquet S.;
RT "Functional characterization of the D-Tyr-tRNATyr deacylase from
RT Escherichia coli.";
RL J. Biol. Chem. 274:19109-19114(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=B;
RX PubMed=4292198; DOI=10.1016/0022-2836(67)90259-8;
RA Calendar R., Berg P.;
RT "D-tyrosyl RNA: formation, hydrolysis and utilization for protein
RT synthesis.";
RL J. Mol. Biol. 26:39-54(1967).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / K37;
RX PubMed=10918062; DOI=10.1074/jbc.m005166200;
RA Soutourina J., Plateau P., Blanquet S.;
RT "Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces
RT cerevisiae cells.";
RL J. Biol. Chem. 275:32535-32542(2000).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / K37;
RX PubMed=15292242; DOI=10.1074/jbc.m402931200;
RA Soutourina O., Soutourina J., Blanquet S., Plateau P.;
RT "Formation of D-tyrosyl-tRNATyr accounts for the toxicity of D-tyrosine
RT toward Escherichia coli.";
RL J. Biol. Chem. 279:42560-42565(2004).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF MET-129.
RX PubMed=16902403; DOI=10.1038/sj.emboj.7601278;
RA Hussain T., Kruparani S.P., Pal B., Dock-Bregeon A.C., Dwivedi S.,
RA Shekar M.R., Sureshbabu K., Sankaranarayanan R.;
RT "Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like
RT domain in threonyl-tRNA synthetase from archaea.";
RL EMBO J. 25:4152-4162(2006).
RN [9]
RP FUNCTION, REACTION MECHANISM, DOMAIN, AND MUTAGENESIS OF SER-77; GLN-78;
RP THR-80; ALA-102; PHE-125; GLY-137 AND PRO-138.
RX PubMed=24302572; DOI=10.7554/elife.01519;
RA Ahmad S., Routh S.B., Kamarthapu V., Chalissery J., Muthukumar S.,
RA Hussain T., Kruparani S.P., Deshmukh M.V., Sankaranarayanan R.;
RT "Mechanism of chiral proofreading during translation of the genetic code.";
RL Elife 2:E01519-E01519(2013).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25441601; DOI=10.1016/j.micres.2014.11.001;
RA Geraskina N.V., Butov I.A., Yomantas Y.A., Stoynova N.V.;
RT "The dtd gene from Bacillus amyloliquefaciens encodes a putative D-tyrosyl-
RT tRNATyr deacylase and is a selectable marker for Bacillus subtilis.";
RL Microbiol. Res. 171:90-96(2015).
RN [11]
RP FUNCTION, SUBSTRATE SPECIFICITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ALA-102 AND PHE-125.
RC STRAIN=K12;
RX PubMed=27224426; DOI=10.1371/journal.pbio.1002465;
RA Routh S.B., Pawar K.I., Ahmad S., Singh S., Suma K., Kumar M., Kuncha S.K.,
RA Yadav K., Kruparani S.P., Sankaranarayanan R.;
RT "Elongation factor Tu prevents misediting of Gly-tRNA(Gly) caused by the
RT design behind the chiral proofreading site of D-aminoacyl-tRNA deacylase.";
RL PLoS Biol. 14:E1002465-E1002465(2016).
RN [12]
RP FUNCTION, REACTION MECHANISM, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28362257; DOI=10.7554/elife.24001;
RA Pawar K.I., Suma K., Seenivasan A., Kuncha S.K., Routh S.B.,
RA Kruparani S.P., Sankaranarayanan R.;
RT "Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a
RT cellular defense against glycine mischarging by AlaRS.";
RL Elife 6:0-0(2017).
RN [13] {ECO:0007744|PDB:1JKE}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), AND SUBUNIT.
RC STRAIN=K12 / K37;
RX PubMed=11568181; DOI=10.1074/jbc.m106550200;
RA Ferri-Fioni M.-L., Schmitt E., Soutourina J., Plateau P., Mechulam Y.,
RA Blanquet S.;
RT "Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a
RT new class of tRNA-dependent hydrolases.";
RL J. Biol. Chem. 276:47285-47290(2001).
CC -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged
CC with cognate L-amino acid (PubMed:10383414, PubMed:4292198,
CC PubMed:10918062, PubMed:24302572, PubMed:27224426). Edits mischarged
CC glycyl-tRNA(Ala) more efficiently than AlaRS (PubMed:28362257). Acts
CC via tRNA-based rather than protein-based catalysis (PubMed:24302572,
CC PubMed:27224426, PubMed:28362257). Rejects correctly charged L-amino
CC acid-tRNAs from its binding site rather than specifically recognizing
CC incorrectly charged D-amino acid-tRNAs (PubMed:27224426). Hydrolyzes
CC correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested
CC with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-tRNA(Gly)
CC from hydrolysis, while increasing Dtd levels or inactivating EF-Tu
CC decreases protection (PubMed:27224426). Hydrolyzes mischarged glycyl-
CC tRNA(Ala) (but not seryl-tRNA(Ala)) even in the presence of EF-Tu,
CC edits about 4-fold better than the editing domain of AlaRS
CC (PubMed:28362257). Has greater activity on glycyl-tRNA(Ala) than
CC glycyl-tRNA(Gly) due in part to its recognition of the conserved
CC tRNA(Ala) G3.U70 wobble base pair (PubMed:28362257). Binds D-amino
CC acids but not L-amino acids (PubMed:16902403). Overexpression of E.coli
CC or P.falciparum Dtd is toxic in E.coli, toxicity can be rescued by
CC supplementation with Gly (PubMed:27224426). By recycling D-aminoacyl-
CC tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts
CC the toxicity associated with the formation of D-aminoacyl-tRNA entities
CC in vivo and helps enforce protein L-homochirality (PubMed:15292242).
CC Hydrolyzes D-tyrosyl-tRNA(Tyr) (PubMed:4292198, PubMed:10383414,
CC PubMed:24302572, PubMed:27224426). Hydrolyzes D-phenylalanyl-tRNA(Phe)
CC (PubMed:4292198, PubMed:24302572). Hydrolyzes D-aspartyl-tRNA(Asp)
CC (PubMed:10918062). Hydrolyzes D-tryptophanyl-tRNA(Trp)
CC (PubMed:10918062). Hydrolyzes glycyl-tRNA(Gly) (PubMed:27224426).
CC Hydrolyzes glycyl-tRNA(Ala) (PubMed:28362257).
CC {ECO:0000269|PubMed:10383414, ECO:0000269|PubMed:10918062,
CC ECO:0000269|PubMed:15292242, ECO:0000269|PubMed:16902403,
CC ECO:0000269|PubMed:24302572, ECO:0000269|PubMed:25441601,
CC ECO:0000269|PubMed:27224426, ECO:0000269|PubMed:28362257,
CC ECO:0000269|PubMed:4292198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00518,
CC ECO:0000269|PubMed:28362257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00518,
CC ECO:0000269|PubMed:10383414, ECO:0000269|PubMed:10918062,
CC ECO:0000269|PubMed:4292198};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr);
CC Xref=Rhea:RHEA:25347, Rhea:RHEA-COMP:9707, Rhea:RHEA-COMP:9872,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78723; Evidence={ECO:0000269|PubMed:10383414,
CC ECO:0000269|PubMed:24302572, ECO:0000269|PubMed:27224426,
CC ECO:0000269|PubMed:4292198};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for D-tyrosyl-tRNA(Tyr) {ECO:0000269|PubMed:10383414};
CC KM=1.0 uM for glycyl-tRNA(Gly) {ECO:0000269|PubMed:27224426};
CC Note=kcat/KM is 6 uM(-1)sec(-1) for D-tyrosyl-tRNA(Tyr)
CC (PubMed:10383414). kcat/KM is 2.8 uM(-1)sec(-1) for D-tryptophanyl-
CC tRNA(Trp) (PubMed:10918062). kcat/KM is 12 uM(-1)sec(-1) for D-
CC aspartyl-tRNA(Asp) (PubMed:10918062). kcat/KM is 10 uM (-1)sec(-1)
CC for glycyl-tRNA(Gly) (PubMed:27224426). {ECO:0000269|PubMed:10383414,
CC ECO:0000269|PubMed:10918062, ECO:0000269|PubMed:27224426};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00518,
CC ECO:0000269|PubMed:10383414, ECO:0000269|PubMed:11568181}.
CC -!- INTERACTION:
CC P0A6M4; P06961: cca; NbExp=2; IntAct=EBI-562575, EBI-545256;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518,
CC ECO:0000305|PubMed:4292198}.
CC -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC of the other monomer to allow specific chiral rejection of L-amino
CC acids (PubMed:24302572, PubMed:27224426). {ECO:0000255|HAMAP-
CC Rule:MF_00518, ECO:0000269|PubMed:24302572,
CC ECO:0000269|PubMed:27224426}.
CC -!- DISRUPTION PHENOTYPE: No phenotype in rich or minimal medium, decreased
CC growth rate in the presence of excess D-tyrosine (PubMed:10383414). A
CC double dtd-dadA deletion mutant has a more pronounced growth defect in
CC the presence of D-Tyr (in strain K12 / EC989) (PubMed:10383414). In a
CC dtd deletion mutant about 40% of tRNA(Tyr) is D-tyrosyl-tRNA(Tyr);
CC overexpressing the gene for tRNA(Tyr) suppresses the toxicity of D-Tyr
CC by increasing the levels of L-tyrosyl-tRNA(Tyr) available for
CC translation (PubMed:15292242). Decreased growth in the presence of D-
CC Asp, D-Ser, D-Gln and D-Trp (PubMed:10918062). Poor growth on 20 mg/ml
CC D-Tyr, no growth on 500 mg/ml D-Tyr or 20 mg/ml D-Trp
CC (PubMed:25441601). Overexpression of genes for tRNA(Asp) or tRNA(Trp)
CC suppresses the toxicity of their respective D-amino acids
CC (PubMed:15292242). No effect seen when grown in 3 or 10 mM Gly; in a
CC mutant that no longer edits mischarged glycyl-tRNA(Ala) or seryl-
CC tRNA(Ala) (triple mutation in alaS) Gly becomes toxic, but excess Ala
CC restores growth (PubMed:28362257). {ECO:0000269|PubMed:10383414,
CC ECO:0000269|PubMed:10918062, ECO:0000269|PubMed:15292242,
CC ECO:0000269|PubMed:25441601, ECO:0000269|PubMed:28362257}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP-
CC Rule:MF_00518}.
CC -!- CAUTION: Initially the conserved reside Thr-80 was thought to be a
CC nucleophile; mutagenesis in this organism and P.falciparum indicates it
CC is not. {ECO:0000269|PubMed:24302572}.
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DR EMBL; L19201; AAB03020.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13449.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77422.1; -; Genomic_DNA.
DR PIR; S40831; S40831.
DR RefSeq; NP_418323.1; NC_000913.3.
DR RefSeq; WP_000560983.1; NZ_STEB01000017.1.
DR PDB; 1JKE; X-ray; 1.55 A; A/B/C/D=1-145.
DR PDBsum; 1JKE; -.
DR AlphaFoldDB; P0A6M4; -.
DR SMR; P0A6M4; -.
DR BioGRID; 4262640; 2.
DR DIP; DIP-47962N; -.
DR IntAct; P0A6M4; 9.
DR STRING; 511145.b3887; -.
DR jPOST; P0A6M4; -.
DR PaxDb; P0A6M4; -.
DR PRIDE; P0A6M4; -.
DR EnsemblBacteria; AAD13449; AAD13449; b3887.
DR EnsemblBacteria; BAE77422; BAE77422; BAE77422.
DR GeneID; 67417241; -.
DR GeneID; 948378; -.
DR KEGG; ecj:JW3858; -.
DR KEGG; eco:b3887; -.
DR PATRIC; fig|1411691.4.peg.2824; -.
DR EchoBASE; EB1798; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_0_6; -.
DR InParanoid; P0A6M4; -.
DR OMA; GVFQAHM; -.
DR PhylomeDB; P0A6M4; -.
DR BioCyc; EcoCyc:EG11852-MON; -.
DR BioCyc; MetaCyc:EG11852-MON; -.
DR BRENDA; 3.1.1.96; 2026.
DR EvolutionaryTrace; P0A6M4; -.
DR PRO; PR:P0A6M4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:EcoCyc.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IDA:EcoCyc.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IDA:EcoCyc.
DR GO; GO:0106026; F:Gly-tRNA(Ala) hydrolase activity; IDA:EcoCyc.
DR GO; GO:0043908; F:Ser(Gly)-tRNA(Ala) hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0006399; P:tRNA metabolic process; IMP:EcoCyc.
DR CDD; cd00563; Dtyr_deacylase; 1.
DR Gene3D; 3.50.80.10; -; 1.
DR HAMAP; MF_00518; Deacylase_Dtd; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
DR TIGRFAMs; TIGR00256; TIGR00256; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..145
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000164537"
FT MOTIF 137..138
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00518,
FT ECO:0000269|PubMed:24302572"
FT MUTAGEN 77
FT /note="S->A,P: Wild-type deacylation of D-tyrosyl-
FT tRNA(Tyr)."
FT /evidence="ECO:0000269|PubMed:24302572"
FT MUTAGEN 78
FT /note="Q->A: Wild-type deacylation of D-tyrosyl-tRNA(Tyr)."
FT /evidence="ECO:0000269|PubMed:24302572"
FT MUTAGEN 80
FT /note="T->A: Wild-type deacylation of D-tyrosyl-tRNA(Tyr)."
FT /evidence="ECO:0000269|PubMed:24302572"
FT MUTAGEN 102
FT /note="A->F: Loss of deacylation of D-tyrosyl-tRNA(Tyr),
FT loss of deacylation of glycyl-tRNA(Gly), not toxic upon
FT overexpression."
FT /evidence="ECO:0000269|PubMed:24302572,
FT ECO:0000269|PubMed:27224426"
FT MUTAGEN 125
FT /note="F->A: Loss of deacylation of D-tyrosyl-tRNA(Tyr),
FT loss of deacylation of glycyl-tRNA(Gly)."
FT /evidence="ECO:0000269|PubMed:24302572,
FT ECO:0000269|PubMed:27224426"
FT MUTAGEN 129
FT /note="M->K: Alters stereospecificity, confers binding of
FT L-amino acids while slightly decreasing binding of D-amino
FT acids."
FT /evidence="ECO:0000269|PubMed:16902403"
FT MUTAGEN 137
FT /note="G->A: Loss of deacylation of D-tyrosyl-tRNA(Tyr)."
FT /evidence="ECO:0000269|PubMed:24302572"
FT MUTAGEN 138
FT /note="P->A: Loss of deacylation of D-tyrosyl-tRNA(Tyr)."
FT /evidence="ECO:0000269|PubMed:24302572"
FT STRAND 2..15
FT /evidence="ECO:0007829|PDB:1JKE"
FT STRAND 18..32
FT /evidence="ECO:0007829|PDB:1JKE"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1JKE"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1JKE"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:1JKE"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1JKE"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1JKE"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1JKE"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1JKE"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:1JKE"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1JKE"
FT STRAND 129..144
FT /evidence="ECO:0007829|PDB:1JKE"
SQ SEQUENCE 145 AA; 15950 MW; 5CF0C0DB0819EC9B CRC64;
MIALIQRVTR ASVTVEGEVT GEIGAGLLVL LGVEKDDDEQ KANRLCERVL GYRIFSDAEG
KMNLNVQQAG GSVLVVSQFT LAADTERGMR PSFSKGASPD RAEALYDYFV ERCRQQEMNT
QTGRFAADMQ VSLVNDGPVT FWLQV
