Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 93 (26 Feb 2020)
Sequence version 2 (19 Mar 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Multifunctional non-homologous end joining protein LigD

Gene

ligD

Organism
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
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

With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs blunt-end and 5'-overhang DNA double strand breaks (DSB) with about 50% fidelity, and DSB with non-complementary 3' ends. Plays a partial role in NHEJ during 3'-overhang repair. NHEJ repairs DSB with blunt ends and 5' overhangs with a high level of nucleotide insertion/deletion, without a need for microhomology. Acts as a DNA ligase on singly nicked dsDNA, as a DNA-directed DNA polymerase on 5' overhangs, and adds non-templated nucleotides to 3' overhangs (terminal transferase). Fills in gaps in dsDNA, prefers a 5'-phosphate in the gap. Site-directed mutations leading to ligase loss alter the bias from insertion to deletion mutations, and indicate another ligase (LigC1 and/or LigC2) can compensate.
The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in dormant cells, where the dNTP pool may be limiting.By similarity7 Publications
The ligase activity is required for replication of viruses with short cos ends (4 bases) such as Mycobacterium phage Omega and Corndog, but not D29 which has a 9 base cos end. Stimulates dsDNA end joining by LigD; when expressed with endogenous or Mycobacterium phage Omega Ku, can reconstitute NHEJ in S.cerevisiae.

Miscellaneous

LigD has variable architecture; domain order can be permutated, domains can be independently encoded, while some bacteria lack the 3'-phosphoesterase domain entirely.

<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

  • ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate. EC:6.5.1.1

<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

Mn2+By similarityNote: Binds 4 Mn2+; 2 Mn2+ for polymerase/primase activity, 1 each for 3-phosphoesterase and ligase.By similarity

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 sitei57Substrate; for polymerase activityBy similarity1
Binding sitei116Substrate; for polymerase activityBy similarity1
<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 bindingi136Manganese 1By similarity1
Metal bindingi136Manganese 2By similarity1
Metal bindingi138Manganese 1By similarity1
Metal bindingi138Manganese 2By similarity1
Metal bindingi226Manganese 2By similarity1
Binding sitei229Substrate; for polymerase activityBy similarity1
Binding sitei235Substrate; for polymerase activityBy similarity1
Binding sitei243Substrate; for polymerase activityBy similarity1
Metal bindingi330Manganese 3; via pros nitrogen; catalytic; for 3'-phosphoesterase activityBy similarity1
Metal bindingi336Manganese 3; via tele nitrogen; catalytic; for 3'-phosphoesterase activityBy similarity1
Metal bindingi338Manganese 3; catalytic; for 3'-phosphoesterase activityBy similarity1
<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>Sitei372Transition state stabilizer; for 3'-phosphoesterase activityBy similarity1
<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 sitei484N6-AMP-lysine intermediateCurated1
Metal bindingi486Manganese 4By similarity1
Metal bindingi616Manganese 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi18 – 21By similarity4
DNA bindingi31By similarity1
DNA bindingi58 – 60By similarity3
DNA bindingi68 – 72By similarity5
DNA bindingi76By similarity1
DNA bindingi88 – 93By similarity6
DNA bindingi109By similarity1
<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 bindingi136 – 138Substrate; for polymerase activityBy similarity3
Nucleotide bindingi171 – 177Substrate; for polymerase activityBy similarity7
DNA bindingi233 – 234By similarity2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Ligase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA recombination, DNA repair, Host-virus interaction
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

<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:
Multifunctional non-homologous end joining protein LigD
Alternative name(s):
NHEJ DNA polymerase
Including the following 3 domains:
DNA repair polymerase
Short name:
Pol
Alternative name(s):
Polymerase/primase
3'-phosphoesterase
Short name:
3'-ribonuclease/3'-phosphatase
Short name:
PE
DNA ligase (EC:6.5.1.1)
Short name:
Lig
Alternative name(s):
Polydeoxyribonucleotide synthase [ATP]
<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:ligD
Ordered Locus Names:MSMEG_5570, MSMEI_5419
<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>OrganismiMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
<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 identifieri246196 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
<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
  • UP000006158 <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
  • UP000000757 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

Not essential for growth in the absence of DNA damage. 320-fold reduction in NHEJ on blunt-ended DSB, with a loss of nucleotide insertions. 100-fold less efficient repair of 5'-overhang DSBs with little nucleotide insertion. Upon deletion, the fidelity of DNA repair depends on the form of the DSB; for blunt-ends fidelity is very low, for 5'-overhangs remains 50% faithful, for 3'-overhangs repair is fully faithful. NHEJ on blunt-ended plasmid is 24-fold further decreased in a triple ligC1-ligC2-ligD deletion. In quadruple ligB-ligC1-ligC2-ligD deletions NHEJ on blunt and 5'-overhangs is 0.22 and 0.12% of wild-type respectively; only 4-fold decrease in 3'-overhang NHEJ. 100-fold decrease in viability when exposed to ionizing radiation in late and stationary phase; 1000-fold decrease in a double ligD-ku deletion. Decreased resistance to desiccation-induced DSBs. Mycobacterium phage Omega and Corndog are unable to infect a deletion strain. Loss of NHEJ on incompatible 3'-chromosomal overhangs, partial reduction in single-strand annealing DSB repair.6 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>Mutagenesisi136 – 138DLD → ALA in vivo 30% reduction in NHEJ on blunt-end DSB, fidelity doubles, loss of non-templated nucleotide insertion during NHEJ. No effect on efficiency of DSB on 5'- or 3'-overhangs, increased fidelity on 5'-overhangs. No effect on viral infection. 3 Publications3
Mutagenesisi136D → A: Loss of templated and non-templated DNA synthesis, but not ligase activity. 1 Publication1
Mutagenesisi138D → A: Loss of templated and non-templated DNA synthesis, but not ligase activity. 1 Publication1
Mutagenesisi310E → A: No effect on efficiency or fidelity on NHEJ of blunt, 5'-overhangs or 3'-overhangs. 1 Publication1
Mutagenesisi336H → A: No effect on efficiency or fidelity on NHEJ of blunt, 5'-overhangs or 3'-overhangs. 1 Publication1
Mutagenesisi484K → A: 2.7 and 3.7-fold decrease in efficiency of NHEJ on blunt and 5'-overhangs respectively. Considerably decreases NHEJ fidelity on both DSBs. No viral infection. 3 Publications1
Mutagenesisi533E → A: 3-fold and 9-fold decrease in efficiency of NHEJ on blunt and 5'-overhangs respectively, with very decreased fidelity on both DSBs. No viral infection. 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_00004259491 – 762Multifunctional non-homologous end joining protein LigDAdd BLAST762

<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

Interacts with Sir2 and probably also with Ku; may form a trimeric complex during NHEJ.

Interacts with Mycobacterium phage Omega and Corndog Ku homologs (AC Q853W0, AC Q856K7).

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
246196.MSMEI_5419

<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

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

More...
SMRi
A0R3R7

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

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>Regioni14 – 260DNA repair polymerase domain (Pol)Add BLAST247
Regioni296 – 4533'-phosphoesterase domain (PE)Add BLAST158
Regioni463 – 760Ligase domain (Lig)Add BLAST298

<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 N-terminal divalent cation-dependent polymerase/primase domain (Pol) functions as an independent domain (PubMed:17174332). Deletion of the Pol domain (residues 1-288) yields a protein severely impaired in NHEJ on blunt or 5'-overhangs (PubMed:18281464).2 Publications
The central 3'-phosphoesterase domain (PE) (PubMed:17174332). Mutations in the PE domain argue against this domain being involved in residue deletion during NHEJ (PubMed:18281464).2 Publications
The C-terminal ATP-dependent ligase domain (Lig) functions as an independent domain (PubMed:17174332). Loss of the Lig domain (residues 449 to 762) forces NHEJ to rely on another ligase, which decreases fidelity for blunt and 5'-overhang DSB (PubMed:18281464).2 Publications

<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

In the N-terminal section; belongs to the LigD polymerase family.Curated
In the central section; belongs to the LigD 3'-phosphoesterase family.Curated
In the C-terminal section; belongs to the ATP-dependent DNA ligase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DQE Bacteria
COG1793 LUCA
COG3285 LUCA

KEGG Orthology (KO)

More...
KOi
K10747

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04863 MtLigD_Pol_like, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012309 DNA_ligase_ATP-dep_C
IPR012310 DNA_ligase_ATP-dep_cent
IPR014146 LigD_ligase_dom
IPR014144 LigD_PE_domain
IPR014145 LigD_pol_dom
IPR033649 MtLigD_Pol-like
IPR012340 NA-bd_OB-fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04679 DNA_ligase_A_C, 1 hit
PF01068 DNA_ligase_A_M, 1 hit
PF13298 LigD_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50249 SSF50249, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02777 LigD_PE_dom, 1 hit
TIGR02778 ligD_pol, 1 hit
TIGR02779 NHEJ_ligase_lig, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50160 DNA_LIGASE_A3, 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.

A0R3R7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARHPWGMER YERVRLTNPD KVLYPATGTT KAEVFDYYLS IAQVMVPHIA
60 70 80 90 100
GRPVTRKRWP NGVAEEAFFE KQLASSAPSW LERGSITHKS GTTTYPIINT
110 120 130 140 150
REGLAWVAQQ ASLEVHVPQW RFEDGDQGPA TRIVFDLDPG EGVTMTQLCE
160 170 180 190 200
IAHEVRALMT DLDLETYPLT SGSKGLHLYV PLAEPISSRG ASVLARRVAQ
210 220 230 240 250
QLEQAMPKLV TATMTKSLRA GKVFLDWSQN NAAKTTIAPY SLRGRDHPTV
260 270 280 290 300
AAPRTWDEIA DPELRHLRFD EVLDRLDEYG DLLAPLDADA PIADKLTTYR
310 320 330 340 350
SMRDASKTPE PVPKEIPKTG NNDKFVIQEH HARRLHYDLR LERDGVLVSF
360 370 380 390 400
AVPKNLPETT AENRLAVHTE DHPIEYLAFH GSIPKGEYGA GDMVIWDSGS
410 420 430 440 450
YETEKFRVPE ELDNPDDSHG EIIVTLHGEK VDGRYALIQT KGKNWLAHRM
460 470 480 490 500
KDQKNARPED FAPMLATEGS VAKYKAKQWA FEGKWDGYRV IIDADHGQLQ
510 520 530 540 550
IRSRTGREVT GEYPQFKALA ADLAEHHVVL DGEAVALDES GVPSFGQMQN
560 570 580 590 600
RARSTRVEFW AFDILWLDGR SLLRAKYSDR RKILEALADG GGLIVPDQLP
610 620 630 640 650
GDGPEAMEHV RKKRFEGVVA KKWDSTYQPG RRSSSWIKDK IWNTQEVVIG
660 670 680 690 700
GWRQGEGGRS SGIGALVLGI PGPEGLQFVG RVGTGFTEKE LSKLKDMLKP
710 720 730 740 750
LHTDESPFNA PLPKVDARGV TFVRPELVGE VRYSERTSDG RLRQPSWRGL
760
RPDKTPDEVV WE
Length:762
Mass (Da):85,516
Last modified:March 19, 2014 - 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:iED1853A73A3E552E
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 ABK75957 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.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
CP000480 Genomic DNA Translation: ABK75957.1 Different initiation.
CP001663 Genomic DNA Translation: AFP41860.1

NCBI Reference Sequences

More...
RefSeqi
YP_889805.1, NC_008596.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABK75957; ABK75957; MSMEG_5570
AFP41860; AFP41860; MSMEI_5419

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4535131

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
msg:MSMEI_5419
msm:MSMEG_5570

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|246196.19.peg.5431

<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
CP000480 Genomic DNA Translation: ABK75957.1 Different initiation.
CP001663 Genomic DNA Translation: AFP41860.1
RefSeqiYP_889805.1, NC_008596.1

3D structure databases

SMRiA0R3R7
ModBaseiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEI_5419

Genome annotation databases

EnsemblBacteriaiABK75957; ABK75957; MSMEG_5570
AFP41860; AFP41860; MSMEI_5419
GeneIDi4535131
KEGGimsg:MSMEI_5419
msm:MSMEG_5570
PATRICifig|246196.19.peg.5431

Phylogenomic databases

eggNOGiENOG4105DQE Bacteria
COG1793 LUCA
COG3285 LUCA
KOiK10747

Family and domain databases

CDDicd04863 MtLigD_Pol_like, 1 hit
InterProiView protein in InterPro
IPR012309 DNA_ligase_ATP-dep_C
IPR012310 DNA_ligase_ATP-dep_cent
IPR014146 LigD_ligase_dom
IPR014144 LigD_PE_domain
IPR014145 LigD_pol_dom
IPR033649 MtLigD_Pol-like
IPR012340 NA-bd_OB-fold
PfamiView protein in Pfam
PF04679 DNA_ligase_A_C, 1 hit
PF01068 DNA_ligase_A_M, 1 hit
PF13298 LigD_N, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
TIGRFAMsiTIGR02777 LigD_PE_dom, 1 hit
TIGR02778 ligD_pol, 1 hit
TIGR02779 NHEJ_ligase_lig, 1 hit
PROSITEiView protein in PROSITE
PS50160 DNA_LIGASE_A3, 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 nameiLIGD_MYCS2
<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: A0R3R7
Secondary accession number(s): I7FKR9
<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: March 19, 2014
Last sequence update: March 19, 2014
Last modified: February 26, 2020
This is version 93 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

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again