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UniProtKB - P28903 (NRDD_ECOLI)

Entry version 166 (25 May 2022)
Sequence version 2 (29 Aug 2003)
Previous versions | rss
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Protein

Anaerobic ribonucleoside-triphosphate reductase

Gene

nrdD

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

Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.

5 Publications

Miscellaneous

The glycyl radical is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl radical bridge between methionine and cysteine residues. Oxidation of formate by the thiosulfuranyl radical results in the release of CO2 and regeneration of the thiyl radical.1 Publication

Caution

Was originally thought to contain an iron sulfur cluster (PubMed:8381402). It was shown later that only NrdG contains an iron sulfur center (PubMed:8621608).1 Publication1 Publication

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Activated under anaerobic conditions by NrdG, a tightly associated activase (PubMed:1460049, PubMed:7852304, PubMed:9305874). Activation involves the formation of a glycyl radical at Gly-681 (PubMed:7852304, PubMed:8636106, PubMed:9305874). Exposure of the activated reductase to oxygen leads to C-terminal truncation and inactivation of the protein, by cleavage at the N-terminal side of Gly-681 (PubMed:8421692, PubMed:7826394). The presence of zinc protects the protein from proteolysis and prevents the formation of disulfide bridges within it (PubMed:19381696).7 Publications

<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=0.35 mM for CTP1 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 bindingi644Zinc2 Publications1
Metal bindingi647Zinc2 Publications1
Metal bindingi662Zinc2 Publications1
Metal bindingi665Zinc2 Publications1

<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 functionOxidoreductase
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.98.6, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P28903

<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:
Anaerobic ribonucleoside-triphosphate reductaseCurated (EC:1.1.98.65 Publications)
Alternative name(s):
Class III ribonucleoside-triphosphate reductaseCurated
<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:nrdD1 Publication
Ordered Locus Names:b4238, JW4197
<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 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

<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%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>Mutagenesisi644C → A: Loss of activity. 1 Publication1
Mutagenesisi647C → A: Almost loss of activity. 1 Publication1
Mutagenesisi662C → A: Loss of activity. 1 Publication1
Mutagenesisi665C → A: Loss of activity. 1 Publication1
Mutagenesisi680C → S: Still retains some radical and some enzyme activity. 1 Publication1
Mutagenesisi681G → A: Lacks both radical and enzyme activity. 1 Publication1
Mutagenesisi682Y → F: Still retains some radical and some enzyme activity. 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_00001666831 – 712Anaerobic ribonucleoside-triphosphate reductaseAdd BLAST712

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei681Glycine radicalPROSITE-ProRule annotation2 Publications1

Keywords - PTMi

Organic radical

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P28903

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

More...PaxDbi		P28903

PRoteomics IDEntifications database

More...PRIDEi		P28903

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced 2-fold by hydroxyurea.1 Publication

<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

Homodimer (PubMed:1460049, PubMed:8621608).

Forms a tetramer composed of two NrdD and two NrdG subunits (PubMed:8621608, PubMed:9305874).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4259318, 27 interactors
853044, 4 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3821, nrdDG class III anaerobic ribonucleotide reductase activation complex
CPX-3822, nrdD class III anaerobic ribonucleotide reductase complex

Database of interacting proteins

More...DIPi		DIP-10358N

Protein interaction database and analysis system

More...IntActi		P28903, 9 interactors

STRING: functional protein association networks

More...STRINGi		511145.b4238

<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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P28903

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

More...SMRi		P28903

Database of comparative protein structure models

More...ModBasei		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>Domaini3 – 92ATP-conePROSITE-ProRule annotationAdd BLAST90
Domaini583 – 708Glycine radicalPROSITE-ProRule annotationAdd BLAST126

<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 anaerobic ribonucleoside-triphosphate reductase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1328, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002707_2_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P28903

Identification of Orthologs from Complete Genome Data

More...OMAi		YSYDRVP

Database for complete collections of gene phylogenies

More...PhylomeDBi		P28903

Family and domain databases

Conserved Domains Database

More...CDDi		cd01675, RNR_III, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005144, ATP-cone_dom
IPR019777, Form_AcTrfase_GR_CS
IPR001150, Gly_radical
IPR012833, NrdD

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03477, ATP-cone, 1 hit
PF13597, NRDD, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02487, NrdD, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51161, ATP_CONE, 1 hit
PS00850, GLY_RADICAL_1, 1 hit
PS51149, GLY_RADICAL_2, 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.

P28903-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPHVMKRDG CKVPFKSERI KEAILRAAKA AEVDDADYCA TVAAVVSEQM 
        60         70         80         90        100
QGRNQVDINE IQTAVENQLM SGPYKQLARA YIEYRHDRDI EREKRGRLNQ 
       110        120        130        140        150
EIRGLVEQTN ASLLNENANK DSKVIPTQRD LLAGIVAKHY ARQHLLPRDV 
       160        170        180        190        200
VQAHERGDIH YHDLDYSPFF PMFNCMLIDL KGMLTQGFKM GNAEIEPPKS 
       210        220        230        240        250
ISTATAVTAQ IIAQVASHIY GGTTINRIDE VLAPFVTASY NKHRKTAEEW 
       260        270        280        290        300
NIPDAEGYAN SRTIKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTS 
       310        320        330        340        350
WESRLIQESI LRNRIAGLGK NRKTAVFPKL VFAIRDGLNH KKGDPNYDIK 
       360        370        380        390        400
QLALECASKR MYPDILNYDQ VVKVTGSFKT PMGCRSFLGV WENENGEQIH 
       410        420        430        440        450
DGRNNLGVIS LNLPRIALEA KGDEATFWKL LDERLVLARK ALMTRIARLE 
       460        470        480        490        500
GVKARVAPIL YMEGACGVRL NADDDVSEIF KNGRASISLG YIGIHETINA 
       510        520        530        540        550
LFGGEHVYDN EQLRAKGIAI VERLRQAVDQ WKEETGYGFS LYSTPSENLC 
       560        570        580        590        600
DRFCRLDTAE FGVVPGVTDK GYYTNSFHLD VEKKVNPYDK IDFEAPYPPL 
       610        620        630        640        650
ANGGFICYGE YPNIQHNLKA LEDVWDYSYQ HVPYYGTNTP IDECYECGFT 
       660        670        680        690        700
GEFECTSKGF TCPKCGNHDA SRVSVTRRVC GYLGSPDARP FNAGKQEEVK 
       710 
RRVKHLGNGQ IG
Length:712
Mass (Da):80,023
Last modified:August 29, 2003 - 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:i943589D653EB0C38
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti257G → R in AAA24226 (PubMed:8421692).Curated1
Sequence conflicti420A → P in AAA24226 (PubMed:8421692).Curated1

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
L06097 Genomic DNA Translation: AAA24226.1
U14003 Genomic DNA Translation: AAA97135.1
U00096 Genomic DNA Translation: AAC77195.1
AP009048 Genomic DNA Translation: BAE78237.1
U06195 Genomic DNA Translation: AAC43383.1
Z46865 Genomic DNA Translation: CAA86938.1

Protein sequence database of the Protein Information Resource

More...PIRi		A47331

NCBI Reference Sequences

More...RefSeqi		NP_418659.1, NC_000913.3
WP_000187778.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC77195; AAC77195; b4238
BAE78237; BAE78237; BAE78237

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66671845
948755

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW4197
eco:b4238

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2464

<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
L06097 Genomic DNA Translation: AAA24226.1
U14003 Genomic DNA Translation: AAA97135.1
U00096 Genomic DNA Translation: AAC77195.1
AP009048 Genomic DNA Translation: BAE78237.1
U06195 Genomic DNA Translation: AAC43383.1
Z46865 Genomic DNA Translation: CAA86938.1
PIRiA47331
RefSeqiNP_418659.1, NC_000913.3
WP_000187778.1, NZ_LN832404.1

3D structure databases

AlphaFoldDBiP28903
SMRiP28903
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4259318, 27 interactors
853044, 4 interactors
ComplexPortaliCPX-3821, nrdDG class III anaerobic ribonucleotide reductase activation complex
CPX-3822, nrdD class III anaerobic ribonucleotide reductase complex
DIPiDIP-10358N
IntActiP28903, 9 interactors
STRINGi511145.b4238

Proteomic databases

jPOSTiP28903
PaxDbiP28903
PRIDEiP28903

Genome annotation databases

EnsemblBacteriaiAAC77195; AAC77195; b4238
BAE78237; BAE78237; BAE78237
GeneIDi66671845
948755
KEGGiecj:JW4197
eco:b4238
PATRICifig|1411691.4.peg.2464

Organism-specific databases

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

More...EchoBASEi		EB1388

Phylogenomic databases

eggNOGiCOG1328, Bacteria
HOGENOMiCLU_002707_2_0_6
InParanoidiP28903
OMAiYSYDRVP
PhylomeDBiP28903

Enzyme and pathway databases

BioCyciEcoCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MONOMER
BRENDAi1.1.98.6, 2026
SABIO-RKiP28903

Miscellaneous databases

Protein Ontology

More...PROi		PR:P28903

Family and domain databases

CDDicd01675, RNR_III, 1 hit
InterProiView protein in InterPro
IPR005144, ATP-cone_dom
IPR019777, Form_AcTrfase_GR_CS
IPR001150, Gly_radical
IPR012833, NrdD
PfamiView protein in Pfam
PF03477, ATP-cone, 1 hit
PF13597, NRDD, 1 hit
TIGRFAMsiTIGR02487, NrdD, 1 hit
PROSITEiView protein in PROSITE
PS51161, ATP_CONE, 1 hit
PS00850, GLY_RADICAL_1, 1 hit
PS51149, GLY_RADICAL_2, 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 nameiNRDD_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: P28903
Secondary accession number(s): Q2M669
<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: December 1, 1992
Last sequence update: August 29, 2003
Last modified: May 25, 2022
This is version 166 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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