NUDC_ECOLI
ID NUDC_ECOLI Reviewed; 257 AA.
AC P32664; Q2M8T3; Q6BEX6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=NAD-capped RNA hydrolase NudC {ECO:0000305};
DE Short=DeNADding enzyme NudC {ECO:0000305};
DE EC=3.6.1.- {ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816};
DE AltName: Full=NADH pyrophosphatase {ECO:0000303|PubMed:7829480};
DE EC=3.6.1.22 {ECO:0000269|PubMed:7829480};
GN Name=nudC; Synonyms=yjaD; OrderedLocusNames=b3996, JW5548;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nishimura K., Inokuchi H.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 33.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7829480; DOI=10.1074/jbc.270.4.1529;
RA Frick D.N., Bessman M.J.;
RT "Cloning, purification, and properties of a novel NADH pyrophosphatase.
RT Evidence for a nucleotide pyrophosphatase catalytic domain in MutT-like
RT enzymes.";
RL J. Biol. Chem. 270:1529-1534(1995).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-178.
RX PubMed=25533955; DOI=10.1038/nature14020;
RA Cahova H., Winz M.L., Hoefer K., Nuebel G., Jaeschke A.;
RT "NAD captureSeq indicates NAD as a bacterial cap for a subset of regulatory
RT RNAs.";
RL Nature 519:374-377(2015).
RN [8] {ECO:0007744|PDB:1VK6, ECO:0007744|PDB:2GB5}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
RP COFACTOR.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli
RT K12 at 2.20 A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [9] {ECO:0007744|PDB:5ISY}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND MUTAGENESIS OF
RP GLU-178.
RX PubMed=27561816; DOI=10.1038/cr.2016.98;
RA Zhang D., Liu Y., Wang Q., Guan Z., Wang J., Liu J., Zou T., Yin P.;
RT "Structural basis of prokaryotic NAD-RNA decapping by NudC.";
RL Cell Res. 26:1062-1066(2016).
RN [10] {ECO:0007744|PDB:5IW4, ECO:0007744|PDB:5IW5}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH NAD; NMN AND ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND MUTAGENESIS OF ARG-69;
RP PHE-160; GLU-174; GLU-178; TYR-188; TRP-194; VAL-214; GLU-219 AND PRO-236.
RX PubMed=27428510; DOI=10.1038/nchembio.2132;
RA Hofer K., Li S., Abele F., Frindert J., Schlotthauer J., Grawenhoff J.,
RA Du J., Patel D.J., Jaschke A.;
RT "Structure and function of the bacterial decapping enzyme NudC.";
RL Nat. Chem. Biol. 12:730-734(2016).
CC -!- FUNCTION: mRNA decapping enzyme that specifically removes the
CC nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by
CC hydrolyzing the diphosphate linkage to produce nicotinamide
CC mononucleotide (NMN) and 5' monophosphate mRNA (PubMed:25533955,
CC PubMed:27561816, PubMed:27428510). The NAD-cap is present at the 5'-end
CC of some mRNAs and stabilizes RNA against 5'-processing
CC (PubMed:25533955). Has preference for mRNAs with a 5'-end purine
CC (PubMed:27428510). Catalyzes the hydrolysis of a broad range of
CC dinucleotide pyrophosphates, but uniquely prefers the reduced form of
CC NADH (PubMed:7829480, PubMed:25533955). {ECO:0000269|PubMed:25533955,
CC ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816,
CC ECO:0000269|PubMed:7829480}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC ChEBI:CHEBI:144051; Evidence={ECO:0000269|PubMed:25533955,
CC ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC Evidence={ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:27428510,
CC ECO:0000269|PubMed:27561816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2
CC H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC EC=3.6.1.22; Evidence={ECO:0000269|PubMed:25533955,
CC ECO:0000269|PubMed:7829480};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-
CC ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832,
CC ChEBI:CHEBI:456215; EC=3.6.1.22;
CC Evidence={ECO:0000269|PubMed:25533955, ECO:0000269|PubMed:7829480};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:27561816, ECO:0000269|PubMed:7829480};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7829480};
CC Note=Divalent metal cations. Mg(2+) or Mn(2+).
CC {ECO:0000269|PubMed:7829480};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816,
CC ECO:0000269|Ref.8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:27428510,
CC ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for NADH {ECO:0000269|PubMed:7829480};
CC KM=5.1 mM for NAD(+) {ECO:0000269|PubMed:7829480};
CC KM=0.29 mM for deamino-NADH {ECO:0000269|PubMed:7829480};
CC KM=2.6 mM for deamino-NAD(+) {ECO:0000269|PubMed:7829480};
CC KM=0.67 mM for AppA {ECO:0000269|PubMed:7829480};
CC KM=1.8 mM for ADP-ribose {ECO:0000269|PubMed:7829480};
CC Vmax=7.6 umol/min/mg enzyme with NADH as substrate
CC {ECO:0000269|PubMed:7829480};
CC Vmax=2.9 umol/min/mg enzyme with NAD(+) as substrate
CC {ECO:0000269|PubMed:7829480};
CC Vmax=8.9 umol/min/mg enzyme with deamino-NADH as substrate
CC {ECO:0000269|PubMed:7829480};
CC Vmax=3.2 umol/min/mg enzyme with deamino-NAD(+) as substrate
CC {ECO:0000269|PubMed:7829480};
CC Vmax=4.7 umol/min/mg enzyme with AppA as substrate
CC {ECO:0000269|PubMed:7829480};
CC Vmax=4.8 umol/min/mg enzyme with ADP-ribose as substrate
CC {ECO:0000269|PubMed:7829480};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:7829480};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27428510,
CC ECO:0000269|PubMed:27561816, ECO:0000305|PubMed:7829480,
CC ECO:0000305|Ref.8}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=D12624; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D12624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00006; AAC43094.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48238.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77323.1; -; Genomic_DNA.
DR PIR; G65206; G65206.
DR RefSeq; WP_000373940.1; NZ_STEB01000045.1.
DR RefSeq; YP_026280.1; NC_000913.3.
DR PDB; 1VK6; X-ray; 2.20 A; A=1-257.
DR PDB; 2GB5; X-ray; 2.30 A; A/B=1-257.
DR PDB; 5ISY; X-ray; 2.35 A; A/C=1-257.
DR PDB; 5IW4; X-ray; 2.60 A; A/B=1-257.
DR PDB; 5IW5; X-ray; 2.70 A; A/B=1-257.
DR PDBsum; 1VK6; -.
DR PDBsum; 2GB5; -.
DR PDBsum; 5ISY; -.
DR PDBsum; 5IW4; -.
DR PDBsum; 5IW5; -.
DR AlphaFoldDB; P32664; -.
DR SMR; P32664; -.
DR BioGRID; 4263215; 137.
DR IntAct; P32664; 1.
DR STRING; 511145.b3996; -.
DR jPOST; P32664; -.
DR PaxDb; P32664; -.
DR PRIDE; P32664; -.
DR EnsemblBacteria; AAT48238; AAT48238; b3996.
DR EnsemblBacteria; BAE77323; BAE77323; BAE77323.
DR GeneID; 66672092; -.
DR GeneID; 948498; -.
DR KEGG; ecj:JW5548; -.
DR KEGG; eco:b3996; -.
DR PATRIC; fig|1411691.4.peg.2715; -.
DR EchoBASE; EB1653; -.
DR eggNOG; COG2816; Bacteria.
DR HOGENOM; CLU_037162_0_1_6; -.
DR InParanoid; P32664; -.
DR OMA; TWAREHR; -.
DR PhylomeDB; P32664; -.
DR BioCyc; EcoCyc:EG11702-MON; -.
DR BioCyc; MetaCyc:EG11702-MON; -.
DR EvolutionaryTrace; P32664; -.
DR PRO; PR:P32664; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IDA:UniProtKB.
DR GO; GO:0110153; F:RNA NAD-cap (NMN-forming) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:EcoCyc.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0019677; P:NAD catabolic process; IBA:GO_Central.
DR GO; GO:0110155; P:NAD-cap decapping; IDA:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006742; P:NADP catabolic process; IBA:GO_Central.
DR GO; GO:0034661; P:ncRNA catabolic process; IDA:EcoCyc.
DR HAMAP; MF_00297; Nudix_NudC; 1.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR022925; RNA_Hydrolase_NudC.
DR InterPro; IPR015376; Znr_NADH_PPase.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09297; zf-NADH-PPase; 1.
DR SUPFAM; SSF55811; SSF55811; 2.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Manganese; Metal-binding; NAD;
KW Reference proteome; Zinc.
FT CHAIN 1..257
FT /note="NAD-capped RNA hydrolase NudC"
FT /id="PRO_0000056963"
FT DOMAIN 125..248
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 159..180
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0007744|PDB:5IW4"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0007744|PDB:5IW5"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1VK6, ECO:0007744|PDB:2GB5,
FT ECO:0007744|PDB:5ISY, ECO:0007744|PDB:5IW4,
FT ECO:0007744|PDB:5IW5"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1VK6, ECO:0007744|PDB:2GB5,
FT ECO:0007744|PDB:5ISY, ECO:0007744|PDB:5IW4,
FT ECO:0007744|PDB:5IW5"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27561816,
FT ECO:0007744|PDB:5ISY"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1VK6, ECO:0007744|PDB:2GB5,
FT ECO:0007744|PDB:5ISY, ECO:0007744|PDB:5IW4,
FT ECO:0007744|PDB:5IW5"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1VK6, ECO:0007744|PDB:2GB5,
FT ECO:0007744|PDB:5ISY, ECO:0007744|PDB:5IW4,
FT ECO:0007744|PDB:5IW5"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0000269|PubMed:27561816, ECO:0007744|PDB:5ISY,
FT ECO:0007744|PDB:5IW4"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 178
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 178
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 192..199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0000269|PubMed:27561816, ECO:0007744|PDB:5ISY,
FT ECO:0007744|PDB:5IW4"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27428510,
FT ECO:0000269|PubMed:27561816, ECO:0007744|PDB:5ISY,
FT ECO:0007744|PDB:5IW4"
FT MUTAGEN 69
FT /note="R->A: Does not affect deNADding activity."
FT /evidence="ECO:0000269|PubMed:27428510"
FT MUTAGEN 160
FT /note="F->A: Abolished deNADding activity."
FT /evidence="ECO:0000269|PubMed:27428510"
FT MUTAGEN 174
FT /note="E->Q: Abolished deNADding activity."
FT /evidence="ECO:0000269|PubMed:27428510"
FT MUTAGEN 178
FT /note="E->Q: Abolished deNADding activity."
FT /evidence="ECO:0000269|PubMed:25533955,
FT ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816"
FT MUTAGEN 188
FT /note="Y->A,Q: Abolished deNADding activity without
FT disrupting homodimerization."
FT /evidence="ECO:0000269|PubMed:27428510"
FT MUTAGEN 194
FT /note="W->A: Abolished deNADding activity."
FT /evidence="ECO:0000269|PubMed:27428510"
FT MUTAGEN 214
FT /note="V->A: Abolished deNADding activity."
FT /evidence="ECO:0000269|PubMed:27428510"
FT MUTAGEN 219
FT /note="E->Q: Abolished deNADding activity."
FT /evidence="ECO:0000269|PubMed:27428510"
FT MUTAGEN 236
FT /note="P->A: Strongly reduced but not abolished deNADding
FT activity."
FT /evidence="ECO:0000269|PubMed:27428510"
FT CONFLICT 33
FT /note="A -> R (in Ref. 2; AAC43094)"
FT /evidence="ECO:0000305"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:5IW4"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1VK6"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1VK6"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 42..58
FT /evidence="ECO:0007829|PDB:1VK6"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1VK6"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:1VK6"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1VK6"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1VK6"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 182..194
FT /evidence="ECO:0007829|PDB:1VK6"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:1VK6"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1VK6"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:1VK6"
FT HELIX 240..254
FT /evidence="ECO:0007829|PDB:1VK6"
SQ SEQUENCE 257 AA; 29689 MW; 368FAE0480AF4CB3 CRC64;
MDRIIEKLDH GWWVVSHEQK LWLPKGELPY GEAANFDLVG QRALQIGEWQ GEPVWLVQQQ
RRHDMGSVRQ VIDLDVGLFQ LAGRGVQLAE FYRSHKYCGY CGHEMYPSKT EWAMLCSHCR
ERYYPQIAPC IIVAIRRDDS ILLAQHTRHR NGVHTVLAGF VEVGETLEQA VAREVMEESG
IKVKNLRYVT SQPWPFPQSL MTAFMAEYDS GDIVIDPKEL LEANWYRYDD LPLLPPPGTV
ARRLIEDTVA MCRAEYE
