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Protein

Deoxyribodipyrimidine photo-lyase

Gene

phrB

Organism
Escherichia coli (strain K12)
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

Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.

Miscellaneous

There are only 10-20 molecules of photolyase per E.coli cell.
Upon absorption of visible light electrons are transferred from Trp-307 through Trp-360 to Trp 383, and from there to FADH, giving rise to the fully reduced catalytic FADH-.

<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

  • Cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA). EC:4.1.99.3

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<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>Absorptioni

Abs(max)=384 nm

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 sitei223FAD1 Publication1
Binding sitei227DNABy similarity1
Binding sitei272FAD1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei307Electron transfer via tryptophanyl radical1
Sitei360Electron transfer via tryptophanyl radical1
Sitei383Electron transfer via tryptophanyl radical1
Binding sitei405DNABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi235 – 239FAD1 Publication5
Nucleotide bindingi275 – 282FAD1 Publication8
Nucleotide bindingi373 – 375FAD1 Publication3

<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

  • deoxyribodipyrimidine photo-lyase activity Source: EcoCyc
  • DNA binding Source: UniProtKB-KW
  • nucleotide binding Source: UniProtKB-KW

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 functionDNA-binding, Lyase
Biological processDNA damage, DNA repair
LigandChromophore, FAD, Flavoprotein, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10736-MONOMER
MetaCyc:EG10736-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.99.3 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00914

<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:
Deoxyribodipyrimidine photo-lyase (EC:4.1.99.3)
Alternative name(s):
DNA photolyase
Photoreactivating enzyme
<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:phrB
Synonyms:phr
Ordered Locus Names:b0708, JW0698
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10736 phrB

<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>Mutagenesisi278W → X: Reduces DNA-binding affinity. 1 Publication1
Mutagenesisi383W → F: Abolishes photolyase activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03147 Flavin adenine dinucleotide

<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_00000851081 – 472Deoxyribodipyrimidine photo-lyaseAdd BLAST472

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00914

PRoteomics IDEntifications database

More...
PRIDEi
P00914

<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

Monomer.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
nfiP687392EBI-555781,EBI-551698

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259920, 166 interactors

Database of interacting proteins

More...
DIPi
DIP-10505N

Protein interaction database and analysis system

More...
IntActi
P00914, 12 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0775

<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

1472
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00914

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

More...
SMRi
P00914

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
P00914

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 134Photolyase/cryptochrome alpha/betaAdd BLAST133

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni109 – 110MTF binding2
Regioni275 – 282Interaction with DNABy similarity8
Regioni342 – 343Interaction with DNABy similarity2

<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 DNA photolyase class-1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CVP Bacteria
COG0415 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000245621

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00914

KEGG Orthology (KO)

More...
KOi
K01669

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00914

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.620, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036134 Crypto/Photolyase_FAD-like_sf
IPR036155 Crypto/Photolyase_N_sf
IPR005101 Cryptochr/Photolyase_FAD-bd
IPR002081 Cryptochrome/DNA_photolyase_1
IPR018394 DNA_photolyase_1_CS_C
IPR006050 DNA_photolyase_N
IPR014729 Rossmann-like_a/b/a_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00875 DNA_photolyase, 1 hit
PF03441 FAD_binding_7, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00147 DNAPHOTLYASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48173 SSF48173, 1 hit
SSF52425 SSF52425, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00394 DNA_PHOTOLYASES_1_1, 1 hit
PS00691 DNA_PHOTOLYASES_1_2, 1 hit
PS51645 PHR_CRY_ALPHA_BETA, 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.

P00914-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTHLVWFRQ DLRLHDNLAL AAACRNSSAR VLALYIATPR QWATHNMSPR
60 70 80 90 100
QAELINAQLN GLQIALAEKG IPLLFREVDD FVASVEIVKQ VCAENSVTHL
110 120 130 140 150
FYNYQYEVNE RARDVEVERA LRNVVCEGFD DSVILPPGAV MTGNHEMYKV
160 170 180 190 200
FTPFKNAWLK RLREGMPECV AAPKVRSSGS IEPSPSITLN YPRQSFDTAH
210 220 230 240 250
FPVEEKAAIA QLRQFCQNGA GEYEQQRDFP AVEGTSRLSA SLATGGLSPR
260 270 280 290 300
QCLHRLLAEQ PQALDGGAGS VWLNELIWRE FYRHLITYHP SLCKHRPFIA
310 320 330 340 350
WTDRVQWQSN PAHLQAWQEG KTGYPIVDAA MRQLNSTGWM HNRLRMITAS
360 370 380 390 400
FLVKDLLIDW REGERYFMSQ LIDGDLAANN GGWQWAASTG TDAAPYFRIF
410 420 430 440 450
NPTTQGEKFD HEGEFIRQWL PELRDVPGKV VHEPWKWAQK AGVTLDYPQP
460 470
IVEHKEARVQ TLAAYEAARK GK
Length:472
Mass (Da):53,667
Last modified:July 21, 1986 - 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:iB06048703F18F7AE
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
K01299 Genomic DNA Translation: AAA24388.1
X57399 Genomic DNA Translation: CAB56782.1
U00096 Genomic DNA Translation: AAC73802.1
AP009048 Genomic DNA Translation: BAA35367.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A01137 WZECD

NCBI Reference Sequences

More...
RefSeqi
NP_415236.1, NC_000913.3
WP_000207142.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73802; AAC73802; b0708
BAA35367; BAA35367; BAA35367

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947005

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0698
eco:b0708

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1565

<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
K01299 Genomic DNA Translation: AAA24388.1
X57399 Genomic DNA Translation: CAB56782.1
U00096 Genomic DNA Translation: AAC73802.1
AP009048 Genomic DNA Translation: BAA35367.1
PIRiA01137 WZECD
RefSeqiNP_415236.1, NC_000913.3
WP_000207142.1, NZ_LN832404.1

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
1DNPX-ray2.30A/B2-472[»]
ProteinModelPortaliP00914
SMRiP00914
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259920, 166 interactors
DIPiDIP-10505N
IntActiP00914, 12 interactors
STRINGi316385.ECDH10B_0775

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide

Proteomic databases

PaxDbiP00914
PRIDEiP00914

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73802; AAC73802; b0708
BAA35367; BAA35367; BAA35367
GeneIDi947005
KEGGiecj:JW0698
eco:b0708
PATRICifig|1411691.4.peg.1565

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0729
EcoGeneiEG10736 phrB

Phylogenomic databases

eggNOGiENOG4105CVP Bacteria
COG0415 LUCA
HOGENOMiHOG000245621
InParanoidiP00914
KOiK01669
PhylomeDBiP00914

Enzyme and pathway databases

BioCyciEcoCyc:EG10736-MONOMER
MetaCyc:EG10736-MONOMER
BRENDAi4.1.99.3 2026
SABIO-RKiP00914

Miscellaneous databases

EvolutionaryTraceiP00914

Protein Ontology

More...
PROi
PR:P00914

Family and domain databases

Gene3Di3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR036134 Crypto/Photolyase_FAD-like_sf
IPR036155 Crypto/Photolyase_N_sf
IPR005101 Cryptochr/Photolyase_FAD-bd
IPR002081 Cryptochrome/DNA_photolyase_1
IPR018394 DNA_photolyase_1_CS_C
IPR006050 DNA_photolyase_N
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF00875 DNA_photolyase, 1 hit
PF03441 FAD_binding_7, 1 hit
PRINTSiPR00147 DNAPHOTLYASE
SUPFAMiSSF48173 SSF48173, 1 hit
SSF52425 SSF52425, 1 hit
PROSITEiView protein in PROSITE
PS00394 DNA_PHOTOLYASES_1_1, 1 hit
PS00691 DNA_PHOTOLYASES_1_2, 1 hit
PS51645 PHR_CRY_ALPHA_BETA, 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 nameiPHR_ECOLI
<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: P00914
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 5, 2018
This is version 162 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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