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UniProtKB - P33919 (RADD_ECOLI)

Entry version 147 (23 Feb 2022)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

Putative DNA repair helicase RadD

Gene

radD

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

RadD contains helicase motifs, suggesting it may be a helicase, although that activity has not been observed (Probable). In combination with RadA is important in repair of double-strand DNA breaks (DSB) (PubMed:25425430, PubMed:25484163).

Has DNA-independent ATPase activity that is stimulated by single-stranded DNA-binding protein SSB. ATPase is stimulated by a peptide with the last 10 residues of SSB, but not when the peptide's last Phe residue is missing. Binds ssDNA; binding is slightly better in the presence of nucleotides (PubMed:27519413).

May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds to DNA structures with 3 branches that resemble replication forks (PubMed:31665437).

3 Publications4 Publications

<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

<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

Zn2+Combined sources1 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

ATPase activity in the presence of KCl in the absence of any nucleic acid substrate.1 Publication
  1. KM=0.85 µM for ATP1 Publication
  2. KM=0.63 µM for ATP in the presence of SSB1 Publication
  3. KM=0.40 µM for ATP in the presence of last 10 residues of SSB1 Publication

pH dependencei

Optimum pH is >7.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi384ZincCombined sources1 Publication1
Metal bindingi387ZincCombined sources1 Publication1
Metal bindingi411ZincCombined sources1 Publication1
Metal bindingi425ZincCombined sources1 Publication1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Helicase, Hydrolase
Biological processDNA damage, DNA repair
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG12045-MONOMER

<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:
Putative DNA repair helicase RadD1 Publication (EC:3.6.4.122 Publications)
<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:radD1 Publication
Synonyms:yejH, yejI, yejJ
Ordered Locus Names:b2184, JW2172
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

100- to 10000-fold decrease in survival after IR (PubMed:25049088, PubMed:25425430). Double radA-radD deletions have nearly 106-fold lower survival upon IR, and the double mutant is more severely affected by UV radiation than either of the single mutants alone (up to 100 J/m2). The single mutation is more sensitive to dsDNA breaks induced by CFX, the double radA-radD mutant is inviable upon CFX treatment; the SOS response is slightly induced in the single and more induced in the double mutant. No effect on RecA-mediated conjugational DNA recombination (PubMed:25425430). In another study double radA-radD deletions are sensitive to CFX but not to UV (up to 40 J/m2) or azidothymidine (AZT) (PubMed:25484163). Deletion of radD leads to an increase in DNA crossing over, DNA repeat deletion and DNA repeat expansion; double uup-radD deletion increases the phenotypes. Single radD deletion has no effect on cell growth or filamentation, double uup-radD deletions are filamentous and lack defined nucleoids. Single deletion is more sensitive to CFX (PubMed:31665437).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi37K → R: Partially complements a radD deletion mutant for survival of ionizing radiation (possible loss of ATPase activity), increases sensitivity to UV of a double radA-radD deletion. Has a dominant negative effect on survival of UV in the presence of wild-type enzyme or ciprofloxacin survival. Has no ATPase activity, does not bind ssDNA. 2 Publications1
Mutagenesisi356 – 586Missing : Does not complement sensitivity of a double radA-radD deletion to dsDNA breaks. 1 PublicationAdd BLAST231
Mutagenesisi437C → A: Does not complement sensitivity of a double radA-radD deletion to dsDNA breaks. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001691641 – 586Putative DNA repair helicase RadDAdd BLAST586

Proteomic databases

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

More...PaxDbi		P33919

PRoteomics IDEntifications database

More...PRIDEi		P33919

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:31035307, PubMed:27519413).

Interacts with single-stranded DNA-binding protein SSB (PubMed:27519413).

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4259416, 278 interactors
849903, 1 interactor

Protein interaction database and analysis system

More...IntActi		P33919, 5 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2184

<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

1586
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P33919

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini18 – 171Helicase ATP-binding1 PublicationPROSITE-ProRule annotationAdd BLAST154
Domaini241 – 386Helicase C-terminal1 PublicationPROSITE-ProRule annotationAdd BLAST146

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>Regioni376 – 425Zinc finger domain1 PublicationAdd BLAST50
Regioni429 – 574C-terminal domain1 PublicationAdd BLAST146

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal domain (residues 356-586) is required to alleviate the deleterious effects of UV or ciprofloxacin (CFX) treatment in a double radA-radD mutant; its effect on ionising irradiation (IR) survival in the single radD mutant were not reported (PubMed:25425430). Crystals have 4 domains; helicase ATP-binding (residues 7-185), helicase C-terminal (residues 187-365), a zinc finger domain (residues 376-425) and the C-terminal domain (429-574) (PubMed:31035307).2 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1061, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_014765_1_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P33919

Database for complete collections of gene phylogenies

More...PhylomeDBi		P33919

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006935, Helicase/UvrB_N
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR011332, Ribosomal_zn-bd

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00271, Helicase_C, 1 hit
PF04851, ResIII, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit
SSF57829, SSF57829, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 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.

P33919-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIFTLRPYQQ EAVDATLNHF RRHKTPAVIV LPTGAGKSLV IAELARLARG 
        60         70         80         90        100
RVLVLAHVKE LVAQNHAKYQ ALGLEADIFA AGLKRKESHG KVVFGSVQSV 
       110        120        130        140        150
ARNLDAFQGE FSLLIVDECH RIGDDEESQY QQILTHLTKV NPHLRLLGLT 
       160        170        180        190        200
ATPFRLGKGW IYQFHYHGMV RGDEKALFRD CIYELPLRYM IKHGYLTPPE 
       210        220        230        240        250
RLDMPVVQYD FSRLQAQSNG LFSEADLNRE LKKQQRITPH IISQIMEFAA 
       260        270        280        290        300
TRKGVMIFAA TVEHAKEIVG LLPAEDAALI TGDTPGAERD VLIENFKAQR 
       310        320        330        340        350
FRYLVNVAVL TTGFDAPHVD LIAILRPTES VSLYQQIVGR GLRLAPGKTD 
       360        370        380        390        400
CLILDYAGNP HDLYAPEVGT PKGKSDNVPV QVFCPACGFA NTFWGKTTAD 
       410        420        430        440        450
GTLIEHFGRR CQGWFEDDDG HREQCDFRFR FKNCPQCNAE NDIAARRCRE 
       460        470        480        490        500
CDTVLVDPDD MLKAALRLKD ALVLRCSGMS LQHGHDEKGE WLKITYYDED 
       510        520        530        540        550
GADVSERFRL QTPAQRTAFE QLFIRPHTRT PGIPLRWITA ADILAQQALL 
       560        570        580 
RHPDFVVARM KGQYWQVREK VFDYEGRFRL AHELRG
Length:586
Mass (Da):66,413
Last modified:November 1, 1997 - v2
<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:i2D173250F83333DF
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA16381 differs from that shown. Reason: Frameshift.Curated

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
U00096 Genomic DNA Translation: AAC75245.1
AP009048 Genomic DNA Translation: BAE76649.1
U00008 Genomic DNA Translation: AAA16381.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...PIRi		G64987

NCBI Reference Sequences

More...RefSeqi		NP_416689.1, NC_000913.3
WP_000578061.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75245; AAC75245; b2184
BAE76649; BAE76649; BAE76649

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945529

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2172
eco:b2184

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.52

<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
U00096 Genomic DNA Translation: AAC75245.1
AP009048 Genomic DNA Translation: BAE76649.1
U00008 Genomic DNA Translation: AAA16381.1 Frameshift.
PIRiG64987
RefSeqiNP_416689.1, NC_000913.3
WP_000578061.1, 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
6JDEX-ray2.80A/B1-586[»]
SMRiP33919
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259416, 278 interactors
849903, 1 interactor
IntActiP33919, 5 interactors
STRINGi511145.b2184

Proteomic databases

PaxDbiP33919
PRIDEiP33919

Genome annotation databases

EnsemblBacteriaiAAC75245; AAC75245; b2184
BAE76649; BAE76649; BAE76649
GeneIDi945529
KEGGiecj:JW2172
eco:b2184
PATRICifig|1411691.4.peg.52

Organism-specific databases

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

More...EchoBASEi		EB1979

Phylogenomic databases

eggNOGiCOG1061, Bacteria
HOGENOMiCLU_014765_1_0_6
InParanoidiP33919
PhylomeDBiP33919

Enzyme and pathway databases

BioCyciEcoCyc:EG12045-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P33919

Family and domain databases

Gene3Di3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR006935, Helicase/UvrB_N
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR011332, Ribosomal_zn-bd
PfamiView protein in Pfam
PF00271, Helicase_C, 1 hit
PF04851, ResIII, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF57829, SSF57829, 1 hit
PROSITEiView protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit

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 nameiRADD_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: P33919
Secondary accession number(s): P36926
, P36927, P76449, Q2MAQ7
<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 historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: February 23, 2022
This is version 147 of the entry and version 2 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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