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UniProtKB - P15042 (DNLJ_ECOLI)

Entry version 190 (07 Apr 2021)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

DNA ligase

Gene

ligA

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

DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.

<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

  • NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta-nicotinamide D-nucleotide.1 Publication EC:6.5.1.2

<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

Mg2+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 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 sitei113NADUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei115N6-AMP-lysine intermediateUniRule annotation1 Publication1
Binding sitei136NADUniRule annotation1 Publication1
Binding sitei173NADUniRule annotation1
Binding sitei290NADUniRule annotation1 Publication1
Binding sitei314NADUniRule annotation1
<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 bindingi408ZincUniRule annotation1 Publication1
Metal bindingi411ZincUniRule annotation1 Publication1
Metal bindingi426ZincUniRule annotation1 Publication1
Metal bindingi432ZincUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi32 – 36NADUniRule annotation5
Nucleotide bindingi81 – 82NADUniRule annotation1 Publication2

<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 functionLigase
Biological processDNA damage, DNA repair, DNA replication
LigandMagnesium, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10534-MONOMER
MetaCyc:EG10534-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.5.1.2, 2026

<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:
DNA ligase (EC:6.5.1.2)
Alternative name(s):
Polydeoxyribonucleotide synthase [NAD(+)]
<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:ligA
Synonyms:dnaL, lig, lop, pdeC
Ordered Locus Names:b2411, JW2403
<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>Mutagenesisi10E → A: No effect. 1 Publication1
Mutagenesisi22Y → A or S: Reduces nick joining activity by 99.9%. 1 Publication1
Mutagenesisi22Y → F: Reduces nick joining activity by 91%. 1 Publication1
Mutagenesisi23H → A or Y: Reduces nick joining activity by 90%. 1 Publication1
Mutagenesisi32D → A or E: Reduces nick joining activity by 99%. 1 Publication1
Mutagenesisi32D → N: Reduces nick joining activity by 91%. 1 Publication1
Mutagenesisi35Y → A: Reduces nick joining activity by 98%. 1 Publication1
Mutagenesisi35Y → F: Reduces nick joining activity by 77%. 1 Publication1
Mutagenesisi35Y → S: Reduces nick joining activity by 99.9%. 1 Publication1
Mutagenesisi36D → A: Reduces nick joining activity by 99.8%. 1 Publication1
Mutagenesisi36D → E: Reduces nick joining activity by 96%. 1 Publication1
Mutagenesisi36D → N: Reduces nick joining activity by 88%. 1 Publication1
Mutagenesisi115K → Q or R: Reduces nick joining activity by 99.9%. 1 Publication1
Mutagenesisi117D → E: Reduces nick joining activity by 97%. 1 Publication1
Mutagenesisi117D → N: Reduces nick joining activity by 99.9%. 1 Publication1
Mutagenesisi118G → A: Reduces nick joining activity by 99.9%. 1 Publication1
Mutagenesisi138D → A: Reduces nick joining activity by 63%. 1 Publication1
Mutagenesisi143E → A: Reduces nick joining activity by 48%. 1 Publication1
Mutagenesisi172G → A: Reduces nick joining activity by 64%. 1 Publication1
Mutagenesisi173E → A, D or Q: Reduces nick joining activity by 99.9%. 1 Publication1
Mutagenesisi198N → A: Reduces nick joining activity by 74%. 1 Publication1
Mutagenesisi200R → A, K or Q: Reduces nick joining activity by 99.9%. 1 Publication1
Mutagenesisi208R → A, K or Q: Reduces nick joining activity by 99%. 1 Publication1
Mutagenesisi277R → A: Reduces nick joining activity by 99%. 1 Publication1
Mutagenesisi285D → E: Reduces nick joining activity by 96%. 1 Publication1
Mutagenesisi285D → N: Reduces nick joining activity by 99%. 1 Publication1
Mutagenesisi286G → A: Reduces nick joining activity by 86%. 1 Publication1
Mutagenesisi288V → A: Reduces nick joining activity by 25%. 1 Publication1
Mutagenesisi290K → A: Reduces nick joining activity by 87%. 1 Publication1
Mutagenesisi314K → Q: Reduces nick joining activity by 99%. 1 Publication1
Mutagenesisi314K → R: Reduces nick joining activity by 95%. 1 Publication1
Mutagenesisi333R → A or Q: Reduces nick joining activity by over 95%. Abolishes nick joining activity; when associated with A-334. 1 Publication1
Mutagenesisi334T → A: Abolishes nick joining activity; when associated with A-333. 1 Publication1
Mutagenesisi342R → A: Reduces nick joining activity by 80%. 1 Publication1
Mutagenesisi379R → A or Q: Reduces nick joining activity by over 95%. 1 Publication1
Mutagenesisi383 – 384VI → AA: Reduces nick joining activity by 95%. 1 Publication2
Mutagenesisi446 – 447RR → AA: Reduces nick joining activity by 95%. 1 Publication2
Mutagenesisi455G → A: Reduces nick joining activity by 50%. 1 Publication1
Mutagenesisi455G → D or V: Reduces nick joining activity by 95%. 1 Publication1
Mutagenesisi487R → A: Reduces nick joining activity by over 90%. 1 Publication1
Mutagenesisi489G → D or V: Reduces nick joining activity by 95%. 1 Publication1
Mutagenesisi521G → A: Reduces nick joining activity by 95%. 1 Publication1
Mutagenesisi521G → D or V: Loss of nick joining activity. 1 Publication1
Mutagenesisi553G → D or V: Reduces nick joining activity by 95%. 1 Publication1
Mutagenesisi614R → A: Reduces nick joining activity by 85%. 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_00001617451 – 671DNA ligaseAdd BLAST671

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P15042

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

More...PaxDbi		P15042

PRoteomics IDEntifications database

More...PRIDEi		P15042

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei487Interaction with target DNA1 Publication1
Sitei492Interaction with target DNA1 Publication1

<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		4259672, 152 interactors
851225, 9 interactors

Database of interacting proteins

More...DIPi		DIP-10098N

Protein interaction database and analysis system

More...IntActi		P15042, 20 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2411

<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

1671
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		P15042

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P15042

<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>Domaini593 – 671BRCTAdd BLAST79

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>Regioni330 – 334Interaction with target DNA1 Publication5
Regioni453 – 458Interaction with target DNA1 Publication6
Regioni519 – 524Interaction with target DNA1 Publication6
Regioni551 – 556Interaction with target DNA1 Publication6

<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 NAD-dependent DNA ligase family. LigA subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0272, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_007764_2_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P15042

Database for complete collections of gene phylogenies

More...PhylomeDBi		P15042

Family and domain databases

Conserved Domains Database

More...CDDi		cd00114, LIGANc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.10190, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01588, DNA_ligase_A, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001357, BRCT_dom
IPR036420, BRCT_dom_sf
IPR041663, DisA/LigA_HHH
IPR018239, DNA_ligase_AS
IPR033136, DNA_ligase_CS
IPR001679, DNAligase
IPR013839, DNAligase_adenylation
IPR013840, DNAligase_N
IPR003583, Hlx-hairpin-Hlx_DNA-bd_motif
IPR012340, NA-bd_OB-fold
IPR004150, NAD_DNA_ligase_OB
IPR010994, RuvA_2-like
IPR004149, Znf_DNAligase_C4

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00533, BRCT, 1 hit
PF01653, DNA_ligase_aden, 1 hit
PF03120, DNA_ligase_OB, 1 hit
PF03119, DNA_ligase_ZBD, 1 hit
PF12826, HHH_2, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001604, LigA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00292, BRCT, 1 hit
SM00278, HhH1, 4 hits
SM00532, LIGANc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47781, SSF47781, 1 hit
SSF50249, SSF50249, 1 hit
SSF52113, SSF52113, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00575, dnlj, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50172, BRCT, 1 hit
PS01055, DNA_LIGASE_N1, 1 hit
PS01056, DNA_LIGASE_N2, 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.

P15042-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP 
        60         70         80         90        100
ELITPDSPTQ RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD 
       110        120        130        140        150
RLKNNEKVTW CCELKLDGLA VSILYENGVL VSAATRGDGT TGEDITSNVR 
       160        170        180        190        200
TIRAIPLKLH GENIPARLEV RGEVFLPQAG FEKINEDARR TGGKVFANPR 
       210        220        230        240        250
NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL GRLLQFKKWG 
       260        270        280        290        300
LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL 
       310        320        330        340        350
GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG 
       360        370        380        390        400
VLVSNATLHN ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR 
       410        420        430        440        450
EVVFPTHCPV CGSDVERVEG EAVARCTGGL ICGAQRKESL KHFVSRRAMD 
       460        470        480        490        500
VDGMGDKIID QLVEKEYVHT PADLFKLTAG KLTGLERMGP KSAQNVVNAL 
       510        520        530        540        550
EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA ASIEELQKVP 
       560        570        580        590        600
DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG 
       610        620        630        640        650
KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA 
       660        670 
KAQELGIEVI DEAEMLRLLG S
Length:671
Mass (Da):73,606
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:iDD2BDC64D8E65256
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 conflicti69A → R in AAA24071 (PubMed:3018436).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
M30255 Genomic DNA Translation: AAA24071.1
M24278 Genomic DNA Translation: AAA24070.1
U00096 Genomic DNA Translation: AAC75464.1
AP009048 Genomic DNA Translation: BAA16282.2
U74650 Genomic DNA Translation: AAB42062.1

Protein sequence database of the Protein Information Resource

More...PIRi		B65015, LQECC6

NCBI Reference Sequences

More...RefSeqi		NP_416906.1, NC_000913.3
WP_000443661.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75464; AAC75464; b2411
BAA16282; BAA16282; BAA16282

Database of genes from NCBI RefSeq genomes

More...GeneIDi		57729416
946885

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2403
eco:b2411

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4320

<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
M30255 Genomic DNA Translation: AAA24071.1
M24278 Genomic DNA Translation: AAA24070.1
U00096 Genomic DNA Translation: AAC75464.1
AP009048 Genomic DNA Translation: BAA16282.2
U74650 Genomic DNA Translation: AAB42062.1
PIRiB65015, LQECC6
RefSeqiNP_416906.1, NC_000913.3
WP_000443661.1, 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
2OWOX-ray2.30A1-671[»]
4GLXX-ray1.90A1-586[»]
5TT5X-ray1.55A1-671[»]
SMRiP15042
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259672, 152 interactors
851225, 9 interactors
DIPiDIP-10098N
IntActiP15042, 20 interactors
STRINGi511145.b2411

Proteomic databases

jPOSTiP15042
PaxDbiP15042
PRIDEiP15042

Genome annotation databases

EnsemblBacteriaiAAC75464; AAC75464; b2411
BAA16282; BAA16282; BAA16282
GeneIDi57729416
946885
KEGGiecj:JW2403
eco:b2411
PATRICifig|1411691.4.peg.4320

Organism-specific databases

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

More...EchoBASEi		EB0529

Phylogenomic databases

eggNOGiCOG0272, Bacteria
HOGENOMiCLU_007764_2_1_6
InParanoidiP15042
PhylomeDBiP15042

Enzyme and pathway databases

BioCyciEcoCyc:EG10534-MONOMER
MetaCyc:EG10534-MONOMER
BRENDAi6.5.1.2, 2026

Miscellaneous databases

EvolutionaryTraceiP15042

Protein Ontology

More...PROi		PR:P15042

Family and domain databases

CDDicd00114, LIGANc, 1 hit
Gene3Di3.40.50.10190, 1 hit
HAMAPiMF_01588, DNA_ligase_A, 1 hit
InterProiView protein in InterPro
IPR001357, BRCT_dom
IPR036420, BRCT_dom_sf
IPR041663, DisA/LigA_HHH
IPR018239, DNA_ligase_AS
IPR033136, DNA_ligase_CS
IPR001679, DNAligase
IPR013839, DNAligase_adenylation
IPR013840, DNAligase_N
IPR003583, Hlx-hairpin-Hlx_DNA-bd_motif
IPR012340, NA-bd_OB-fold
IPR004150, NAD_DNA_ligase_OB
IPR010994, RuvA_2-like
IPR004149, Znf_DNAligase_C4
PfamiView protein in Pfam
PF00533, BRCT, 1 hit
PF01653, DNA_ligase_aden, 1 hit
PF03120, DNA_ligase_OB, 1 hit
PF03119, DNA_ligase_ZBD, 1 hit
PF12826, HHH_2, 1 hit
PIRSFiPIRSF001604, LigA, 1 hit
SMARTiView protein in SMART
SM00292, BRCT, 1 hit
SM00278, HhH1, 4 hits
SM00532, LIGANc, 1 hit
SUPFAMiSSF47781, SSF47781, 1 hit
SSF50249, SSF50249, 1 hit
SSF52113, SSF52113, 1 hit
TIGRFAMsiTIGR00575, dnlj, 1 hit
PROSITEiView protein in PROSITE
PS50172, BRCT, 1 hit
PS01055, DNA_LIGASE_N1, 1 hit
PS01056, DNA_LIGASE_N2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDNLJ_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: P15042
Secondary accession number(s): P78197, P78198
<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: April 1, 1990
Last sequence update: November 1, 1997
Last modified: April 7, 2021
This is version 190 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, Direct protein sequencing, Reference proteome

Documents

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