Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA ligase |
Protein Synonyms/Alias | |
Gene Name | ligA |
Gene Synonyms/Alias | dnaL, lig, lop, pdeC |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 492 | LERMGPKSAQNVVNA | S | HTP | [1] | |
Reference | [1]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium. Soares NC,Spät P,Krug K,Macek B J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [ PMID:23590516] |
Functional Description From UniProt | FUNCTION: 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 |
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| 3D-structure; Completeproteome; Directproteinsequencing; DNAdamage; DNArepair; DNAreplication; Ligase; Magnesium; Metal-binding; NAD; Referenceproteome; Zinc |
Protein Sequence | MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP ELITPDSPTQ 60 RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD RLKNNEKVTW CCELKLDGLA 120 VSILYENGVL VSAATRGDGT TGEDITSNVR TIRAIPLKLH GENIPARLEV RGEVFLPQAG 180 FEKINEDARR TGGKVFANPR NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL 240 GRLLQFKKWG LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL 300 GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG VLVSNATLHN 360 ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR EVVFPTHCPV CGSDVERVEG 420 EAVARCTGGL ICGAQRKESL KHFVSRRAMD VDGMGDKIID QLVEKEYVHT PADLFKLTAG 480 KLTGLERMGP KSAQNVVNAL EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA 540 ASIEELQKVP DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG 600 KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA KAQELGIEVI 660 DEAEMLRLLG S 671 |
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