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Protein

Cephalosporin-C deacetylase

Gene

axeA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score:

Annotation score:5 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>

<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

Esterase that removes acetyl groups from a number of O-acetylated small substrates, such as acetylated xylose, short xylo-oligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan, 4-methylumbelliferyl acetate or alpha-naphthyl acetate. Able to catalyze rapid hydrolysis of a range of substrates preferably with acetate groups, independent of the alcohol moiety. Exhibits a narrow selectivity for short chain acyl esters (C2-C3). Displays broad substrate specificity by hydrolyzing acetate at 2, 3, and 4 positions of 4-nitrophenyl-beta-D-xylopyranoside (pNP-Xyl) with similar efficiency. Cannot cleave amide linkages.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity stimulated by up to 40% in the presence of divalent cations such as BaCl2, CaCl2, MgCl2 and MnCl2 at 3 mM concentration, but inhibited by 82-85% in the presence of CdCl2 and ZnCl2 at 3 mM concentration.1 Publication

<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

  1. KM=0.12 mM for p-nitrophenyl-acetate3 Publications
  2. KM=6.05 mM for glucose penta-acetate3 Publications
  3. KM=4.18 mM for cephalosporin-C3 Publications
  4. KM=20.8 mM for 7-aminocephalosporonic acid (7-ACA)3 Publications
  5. KM=760 µM for p-nitrophenyl acetate3 Publications
  6. KM=3.7 µM for fluoroscein di(acetoxymethyl) ether3 Publications
  7. KM=0.97 µM for fluoroscein dipropyloxymethyl ether3 Publications
  8. KM=0.41 µM for fluoroscein dibutyloxymethyl ether3 Publications
  9. KM=1.0 µM for fluoroscein divaleryloxymethyl ether3 Publications
  10. KM=2.6 µM for fluoroscein dicaproyloxymethyl ether3 Publications
  11. KM=0.51 µM for fluoroscein dimethacryloxymethyl ether3 Publications
  12. KM=0.96 µM for fluoroscein dicyclobutylcarboxymethyl ether3 Publications
  13. KM=0.54 µM for fluoroscein dimethylcyclopropanecarboxymethyl ether3 Publications
  14. KM=0.185 mM for p-nitrophenyl-acetate3 Publications
  15. KM=0.137 mM for p-nitrophenyl-propionate3 Publications
  16. KM=3.6 mM for 2-O-acetyl-pNP-Xyl3 Publications
  17. KM=4.2 mM for 3-O-acetyl-pNP-Xyl3 Publications
  18. KM=4.0 mM for 4-O-acetyl-pNP-Xyl3 Publications
  1. Vmax=113.5 µmol/min/mg enzyme with pNP-acetate as substrate3 Publications
  2. Vmax=366.8 µmol/min/mg enzyme with glucose penta-acetate as substrate3 Publications
  3. Vmax=19.2 µmol/min/mg enzyme with cephalosporin-C as substrate3 Publications

pH dependencei

Optimum pH is 6.5. Half-maximal activity between pH 5.0-7.5.3 Publications

Temperature dependencei

Optimum temperature is 90 degrees Celsius. Activity drops sharply above 90 degrees Celsius. Stable up to 100-104 degrees Celsius.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei92Substrate; via amide nitrogenBy similarity1
<p>This subsection of the ‘Function’ 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 sitei188Nucleophile1 Publication1
Binding sitei188Inhibitor1 Publication1
Binding sitei188Inhibitor (covalent)1 Publication1
Active sitei274Charge relay systemBy similarity1
Active sitei303Charge relay systemBy similarity1

<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

GO - Biological processi

<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 functionHydrolase, Serine esterase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation
LigandCalcium, Metal-binding

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
thema-TM0077 Acetyl-esterase_deacetylase

<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_and_taxonomy_section">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:
Cephalosporin-C deacetylaseCurated (EC:3.1.1.412 Publications)
Alternative name(s):
Acetylxylan esterase (EC:3.1.1.721 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:axeA1 Publication
Ordered Locus Names:TM_0077
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri243274 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008183 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi88Q → A: Minimal change in catalytic efficiency toward acetate substrates. 1 Publication1
Mutagenesisi92Y → A: Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication1
Mutagenesisi102W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication1
Mutagenesisi105W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication1
Mutagenesisi124W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication1
Mutagenesisi188S → A: Activity abolished towards fluoroscein diacetoxymethyl ether. 1 Publication1
Mutagenesisi213F → A: Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication1
Mutagenesisi228P → A: Reduces catalytic activity by 33-fold against fluoroscein diacetoxymethyl ether; 8-fold decrease in activity against dimethacryloxymethyl ether; 4-fold increase in catalytic efficiency toward dicyclobutylcarboxymethyl ether. Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-92; A-213 or A-276. 1 Publication1
Mutagenesisi276I → A: Greater than 10-fold reduction in catalytic efficiency toward the acetate substrates. Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication1

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004197661 – 325Cephalosporin-C deacetylaseAdd BLAST325

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer, formed by a trimer of dimers. Also exists as a homodimer.2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
243274.TM0077

<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

1325
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VLQX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L1-325[»]
3M81X-ray2.50A/B/C/D/E/F1-325[»]
3M82X-ray2.40A/B/C/D/E/F1-325[»]
3M83X-ray2.12A/B/C/D/E/F1-325[»]
5FDFX-ray1.76A/B/C/D/E/F1-325[»]
5GMAX-ray2.10A/B/C/D/E/F1-325[»]
5HFNX-ray2.75A/B/C/D/E/F1-325[»]
5JIBX-ray1.86A/B/C/D/E/F1-325[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9WXT2

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9WXT2

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9WXT2

<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

Belongs to the carbohydrate esterase 7 family.Sequence analysis

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105I82 Bacteria
COG3458 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9WXT2

KEGG Orthology (KO)

More...
KOi
K01060

Identification of Orthologs from Complete Genome Data

More...
OMAi
YDVVNFA

Database of Orthologous Groups

More...
OrthoDBi
721431at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058 AB_hydrolase
IPR008391 AXE1_dom
IPR039069 CE7

The PANTHER Classification System

More...
PANTHERi
PTHR40111 PTHR40111, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05448 AXE1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53474 SSF53474, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q9WXT2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAFFDLPLEE LKKYRPERYE EKDFDEFWEE TLAESEKFPL DPVFERMESH
60 70 80 90 100
LKTVEAYDVT FSGYRGQRIK GWLLVPKLEE EKLPCVVQYI GYNGGRGFPH
110 120 130 140 150
DWLFWPSMGY ICFVMDTRGQ GSGWLKGDTP DYPEGPVDPQ YPGFMTRGIL
160 170 180 190 200
DPRTYYYRRV FTDAVRAVEA AASFPQVDQE RIVIAGGSQG GGIALAVSAL
210 220 230 240 250
SKKAKALLCD VPFLCHFRRA VQLVDTHPYA EITNFLKTHR DKEEIVFRTL
260 270 280 290 300
SYFDGVNFAA RAKIPALFSV GLMDNICPPS TVFAAYNYYA GPKEIRIYPY
310 320
NNHEGGGSFQ AVEQVKFLKK LFEKG
Length:325
Mass (Da):37,156
Last modified:November 1, 1999 - 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:iAF2879D86680A3C4
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AE000512 Genomic DNA Translation: AAD35171.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E72421

NCBI Reference Sequences

More...
RefSeqi
NP_227893.1, NC_000853.1
WP_004082599.1, NZ_CP011107.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAD35171; AAD35171; TM_0077

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
896903

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
tma:TM0077

<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

<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
AE000512 Genomic DNA Translation: AAD35171.1
PIRiE72421
RefSeqiNP_227893.1, NC_000853.1
WP_004082599.1, NZ_CP011107.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VLQX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L1-325[»]
3M81X-ray2.50A/B/C/D/E/F1-325[»]
3M82X-ray2.40A/B/C/D/E/F1-325[»]
3M83X-ray2.12A/B/C/D/E/F1-325[»]
5FDFX-ray1.76A/B/C/D/E/F1-325[»]
5GMAX-ray2.10A/B/C/D/E/F1-325[»]
5HFNX-ray2.75A/B/C/D/E/F1-325[»]
5JIBX-ray1.86A/B/C/D/E/F1-325[»]
ProteinModelPortaliQ9WXT2
SMRiQ9WXT2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0077

Protein family/group databases

ESTHERithema-TM0077 Acetyl-esterase_deacetylase

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35171; AAD35171; TM_0077
GeneIDi896903
KEGGitma:TM0077

Phylogenomic databases

eggNOGiENOG4105I82 Bacteria
COG3458 LUCA
InParanoidiQ9WXT2
KOiK01060
OMAiYDVVNFA
OrthoDBi721431at2

Miscellaneous databases

EvolutionaryTraceiQ9WXT2

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR008391 AXE1_dom
IPR039069 CE7
PANTHERiPTHR40111 PTHR40111, 1 hit
PfamiView protein in Pfam
PF05448 AXE1, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCAH_THEMA
<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>AccessioniPrimary (citable) accession number: Q9WXT2
Secondary accession number(s): G4FGZ2
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: November 1, 1999
Last modified: January 16, 2019
This is version 108 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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