UniProtKB - Q9LL41 (PCBER_PINTA)
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>sp|Q9LL41|PCBER_PINTA Phenylcoumaran benzylic ether reductase PT1 OS=Pinus taeda OX=3352 GN=PCBER PE=1 SV=1 MGSRSRILLIGATGYIGRHVAKASLDLGHPTFLLVRESTASSNSEKAQLLESFKASGANI VHGSIDDHASLVEAVKNVDVVISTVGSLQIESQVNIIKAIKEVGTVKRFFPSEFGNDVDN VHAVEPAKSVFEVKAKVRRAIEAEGIPYTYVSSNCFAGYFLRSLAQAGLTAPPRDKVVIL GDGNARVVFVKEEDIGTFTIKAVDDPRTLNKTLYLRLPANTLSLNELVALWEKKIDKTLE KAYVPEEEVLKLIADTPFPANISIAISHSIFVKGDQTNFEIGPAGVEASQLYPDVKYTTV DEYLSNFVCommunity curation ()Add a publicationFeedback
Protein
Phenylcoumaran benzylic ether reductase PT1
Gene
PCBER
Organism
Pinus taeda (Loblolly pine)
Status
Reviewed-Annotation score:
Annotation score:4 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Oxidoreductase involved in lignan biosynthesis. Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to tetrahydrodehydrodiconiferyl alcohol (TDDC).2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.2"Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco."
Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.
Plant Mol. Biol. 50:427-440(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- (−)-dehydrodiconiferyl alcohol
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Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.2"Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco."
Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.
Plant Mol. Biol. 50:427-440(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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(−)-dehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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=(S)-isodihydrodehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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- (+)-dehydrodiconiferyl alcohol
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Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.2"Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco."
Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.
Plant Mol. Biol. 50:427-440(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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(+)-dehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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=(R)-isodihydrodehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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- (2R,3S)-dihydrodehydrodiconiferyl alcohol
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Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.2"Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco."
Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.
Plant Mol. Biol. 50:427-440(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
(2R,3S)-dihydrodehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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=(S)-tetrahydrodehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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- (2S,3R)-dihydrodehydrodiconiferyl alcohol
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Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.2"Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco."
Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.
Plant Mol. Biol. 50:427-440(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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(2S,3R)-dihydrodehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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+NADPH- Search proteins in UniProtKB for this molecule.
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=(R)-tetrahydrodehydrodiconiferyl alcohol- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=0.61 mM for dehydrodiconiferyl alcohol1 Publication
Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=1.95 mM for dihydrodehydrodiconiferyl alcohol1 Publication
Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=104.2 nmol/h/mg enzyme toward dehydrodiconiferyl alcohol1 Publication
Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=55.8 nmol/h/mg enzyme toward dihydrodehydrodiconiferyl alcohol1 Publication
Manual assertion based on experiment ini
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 36 | NADPBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| Binding sitei | 46 | NADPBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 134 | Proton acceptorBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Binding sitei | 138 | NADPBy similarity Manual assertion inferred from sequence similarity toi | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 11 – 17 | NADP1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 7 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.2"Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco."
Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.
Plant Mol. Biol. 50:427-440(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
GO - Biological processi
- lignan biosynthetic process Source: UniProtKBInferred from direct assayi
- Ref.1"Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases."
Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G., Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.
J. Biol. Chem. 274:7516-7527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.2"Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco."
Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.
Plant Mol. Biol. 50:427-440(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Oxidoreductase |
| Ligand | NADP |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Phenylcoumaran benzylic ether reductase PT11 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: PCBER-Pt11 Publication Manual assertion based on opinion ini
Alternative name(s): PtPCBER1 Publication Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:PCBERCurated |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Pinus taeda (Loblolly pine) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 3352 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Acrogymnospermae › Pinopsida › Pinidae › Pinales › Pinaceae › Pinus › Pinus subgen. Pinus |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000442613 | 1 – 308 | Phenylcoumaran benzylic ether reductase PT1Add BLAST | 308 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 7 – 11 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 17 – 26 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 31 – 34 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 40 – 43 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 44 – 54 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Turni | 55 – 57 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 59 – 61 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 68 – 76 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 79 – 83 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 87 – 89 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 91 – 93 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 94 – 103 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 107 – 110 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 127 – 144 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| Beta strandi | 148 – 152 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 157 – 160 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 161 – 165 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 174 – 180 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 186 – 190 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 192 – 200 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 206 – 208 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 211 – 214 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 218 – 220 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 221 – 223 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 224 – 234 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 240 – 244 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 246 – 254 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 260 – 271 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Turni | 275 – 277 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 285 – 287 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 288 – 291 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 300 – 305 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9LL41 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9LL41 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR036291, NAD(P)-bd_dom_sf IPR008030, NmrA-like |
Pfam protein domain database More...Pfami | View protein in Pfam PF05368, NmrA, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735, SSF51735, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
Q9LL41-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MGSRSRILLI GATGYIGRHV AKASLDLGHP TFLLVRESTA SSNSEKAQLL
60 70 80 90 100
ESFKASGANI VHGSIDDHAS LVEAVKNVDV VISTVGSLQI ESQVNIIKAI
110 120 130 140 150
KEVGTVKRFF PSEFGNDVDN VHAVEPAKSV FEVKAKVRRA IEAEGIPYTY
160 170 180 190 200
VSSNCFAGYF LRSLAQAGLT APPRDKVVIL GDGNARVVFV KEEDIGTFTI
210 220 230 240 250
KAVDDPRTLN KTLYLRLPAN TLSLNELVAL WEKKIDKTLE KAYVPEEEVL
260 270 280 290 300
KLIADTPFPA NISIAISHSI FVKGDQTNFE IGPAGVEASQ LYPDVKYTTV
DEYLSNFV
Length:308
Mass (Da):33,524
Last modified:October 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iE93FA4456C7854BF
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 103 | V → I in AAC32591 (PubMed:10066819).Curated | 1 | |
| Sequence conflicti | 129 | S → N in AAC32591 (PubMed:10066819).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF081678 mRNA Translation: AAC32591.1 AF242490 mRNA Translation: AAF64173.2 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q9LL41 | NmrA domain-containing protein | 308 | UniRef90_Q9LL41 | |||
| NmrA domain-containing protein | 308 | |||||
| NmrA domain-containing protein | 308 | |||||
| NmrA domain-containing protein | 308 | |||||
| Isoflavone reductase-like protein (Fragment) | 61 | |||||
| +1 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q9LL41 | Eugenol synthase 2 | 309 | UniRef50_B2WSN0 | |||
| Phenylcoumaran benzylic ether reductase POP1 | 306 | |||||
| Phenylcoumaran benzylic ether reductase IRL1 | 306 | |||||
| Isoflavone reductase-like protein | 308 | |||||
| Phenylcoumaran benzylic ether reductase TP7 | 308 | |||||
| +410 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF081678 mRNA Translation: AAC32591.1 AF242490 mRNA Translation: AAF64173.2 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1QYC | X-ray | 2.20 | A/B | 1-308 | [»] | |
| SMRi | Q9LL41 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | Q9LL41 |
Family and domain databases
| InterProi | View protein in InterPro IPR036291, NAD(P)-bd_dom_sf IPR008030, NmrA-like |
| Pfami | View protein in Pfam PF05368, NmrA, 1 hit |
| SUPFAMi | SSF51735, SSF51735, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PCBER_PINTA | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9LL41Primary (citable) accession number: Q9LL41 Secondary accession number(s): O81651 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2017 |
| Last sequence update: | October 1, 2000 | |
| Last modified: | August 12, 2020 | |
| This is version 65 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Plant Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
