Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15042

- DNLJ_ECOLI

UniProt

P15042 - DNLJ_ECOLI

Protein

DNA ligase

Gene

ligA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Catalytic activityi

    NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)(n+m).1 Publication

    Cofactori

    Magnesium.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei113 – 1131NAD
    Active sitei115 – 1151N6-AMP-lysine intermediate1 Publication
    Binding sitei136 – 1361NAD
    Binding sitei173 – 1731NADBy similarity
    Binding sitei290 – 2901NAD
    Binding sitei314 – 3141NADCurated
    Metal bindingi408 – 4081Zinc
    Metal bindingi411 – 4111Zinc
    Metal bindingi426 – 4261Zinc
    Metal bindingi432 – 4321Zinc
    Sitei487 – 4871Interaction with target DNA
    Sitei492 – 4921Interaction with target DNA

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 365NADCurated
    Nucleotide bindingi81 – 822NAD

    GO - Molecular functioni

    1. DNA binding Source: EcoCyc
    2. DNA ligase (NAD+) activity Source: EcoCyc
    3. metal ion binding Source: UniProtKB-KW
    4. NAD+ binding Source: EcoCyc

    GO - Biological processi

    1. base-excision repair, DNA ligation Source: EcoCyc
    2. DNA ligation Source: EcoCyc
    3. DNA replication Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    Magnesium, Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10534-MONOMER.
    ECOL316407:JW2403-MONOMER.
    MetaCyc:EG10534-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA ligase (EC:6.5.1.2)
    Alternative name(s):
    Polydeoxyribonucleotide synthase [NAD(+)]
    Gene namesi
    Name:ligA
    Synonyms:dnaL, lig, lop, pdeC
    Ordered Locus Names:b2411, JW2403
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10534. ligA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101E → A: No effect. 1 Publication
    Mutagenesisi22 – 221Y → A or S: Reduces nick joining activity by 99.9%. 1 Publication
    Mutagenesisi22 – 221Y → F: Reduces nick joining activity by 91%. 1 Publication
    Mutagenesisi23 – 231H → A or Y: Reduces nick joining activity by 90%. 1 Publication
    Mutagenesisi32 – 321D → A or E: Reduces nick joining activity by 99%. 1 Publication
    Mutagenesisi32 – 321D → N: Reduces nick joining activity by 91%. 1 Publication
    Mutagenesisi35 – 351Y → A: Reduces nick joining activity by 98%. 1 Publication
    Mutagenesisi35 – 351Y → F: Reduces nick joining activity by 77%. 1 Publication
    Mutagenesisi35 – 351Y → S: Reduces nick joining activity by 99.9%. 1 Publication
    Mutagenesisi36 – 361D → A: Reduces nick joining activity by 99.8%. 1 Publication
    Mutagenesisi36 – 361D → E: Reduces nick joining activity by 96%. 1 Publication
    Mutagenesisi36 – 361D → N: Reduces nick joining activity by 88%. 1 Publication
    Mutagenesisi115 – 1151K → Q or R: Reduces nick joining activity by 99.9%. 1 Publication
    Mutagenesisi117 – 1171D → E: Reduces nick joining activity by 97%. 1 Publication
    Mutagenesisi117 – 1171D → N: Reduces nick joining activity by 99.9%. 1 Publication
    Mutagenesisi118 – 1181G → A: Reduces nick joining activity by 99.9%. 1 Publication
    Mutagenesisi138 – 1381D → A: Reduces nick joining activity by 63%. 1 Publication
    Mutagenesisi143 – 1431E → A: Reduces nick joining activity by 48%. 1 Publication
    Mutagenesisi172 – 1721G → A: Reduces nick joining activity by 64%. 1 Publication
    Mutagenesisi173 – 1731E → A, D or Q: Reduces nick joining activity by 99.9%. 1 Publication
    Mutagenesisi198 – 1981N → A: Reduces nick joining activity by 74%. 1 Publication
    Mutagenesisi200 – 2001R → A, K or Q: Reduces nick joining activity by 99.9%. 1 Publication
    Mutagenesisi208 – 2081R → A, K or Q: Reduces nick joining activity by 99%. 1 Publication
    Mutagenesisi277 – 2771R → A: Reduces nick joining activity by 99%. 1 Publication
    Mutagenesisi285 – 2851D → E: Reduces nick joining activity by 96%. 1 Publication
    Mutagenesisi285 – 2851D → N: Reduces nick joining activity by 99%. 1 Publication
    Mutagenesisi286 – 2861G → A: Reduces nick joining activity by 86%. 1 Publication
    Mutagenesisi288 – 2881V → A: Reduces nick joining activity by 25%. 1 Publication
    Mutagenesisi290 – 2901K → A: Reduces nick joining activity by 87%. 1 Publication
    Mutagenesisi314 – 3141K → Q: Reduces nick joining activity by 99%. 1 Publication
    Mutagenesisi314 – 3141K → R: Reduces nick joining activity by 95%. 1 Publication
    Mutagenesisi333 – 3331R → A or Q: Reduces nick joining activity by over 95%. Abolishes nick joining activity; when associated with A-334. 1 Publication
    Mutagenesisi334 – 3341T → A: Abolishes nick joining activity; when associated with A-333. 1 Publication
    Mutagenesisi342 – 3421R → A: Reduces nick joining activity by 80%. 1 Publication
    Mutagenesisi379 – 3791R → A or Q: Reduces nick joining activity by over 95%. 1 Publication
    Mutagenesisi383 – 3842VI → AA: Reduces nick joining activity by 95%.
    Mutagenesisi446 – 4472RR → AA: Reduces nick joining activity by 95%.
    Mutagenesisi455 – 4551G → A: Reduces nick joining activity by 50%. 1 Publication
    Mutagenesisi455 – 4551G → D or V: Reduces nick joining activity by 95%. 1 Publication
    Mutagenesisi487 – 4871R → A: Reduces nick joining activity by over 90%. 1 Publication
    Mutagenesisi489 – 4891G → D or V: Reduces nick joining activity by 95%. 1 Publication
    Mutagenesisi521 – 5211G → A: Reduces nick joining activity by 95%. 1 Publication
    Mutagenesisi521 – 5211G → D or V: Loss of nick joining activity. 1 Publication
    Mutagenesisi553 – 5531G → D or V: Reduces nick joining activity by 95%. 1 Publication
    Mutagenesisi614 – 6141R → A: Reduces nick joining activity by 85%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 671671DNA ligasePRO_0000161745Add
    BLAST

    Proteomic databases

    PaxDbiP15042.
    PRIDEiP15042.

    Expressioni

    Gene expression databases

    GenevestigatoriP15042.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-10098N.
    IntActiP15042. 20 interactions.
    MINTiMINT-204717.
    STRINGi511145.b2411.

    Structurei

    Secondary structure

    1
    671
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2421
    Beta strandi28 – 303
    Helixi34 – 4815
    Helixi50 – 523
    Helixi58 – 603
    Beta strandi72 – 743
    Beta strandi83 – 853
    Helixi88 – 10013
    Beta strandi102 – 1043
    Beta strandi110 – 12617
    Beta strandi129 – 1357
    Beta strandi139 – 1446
    Helixi146 – 1494
    Beta strandi161 – 1633
    Beta strandi166 – 17510
    Helixi178 – 19013
    Helixi199 – 2079
    Helixi212 – 2165
    Beta strandi221 – 23313
    Helixi239 – 24810
    Beta strandi258 – 2625
    Helixi263 – 27614
    Helixi277 – 2793
    Beta strandi280 – 2823
    Beta strandi284 – 29310
    Helixi294 – 3007
    Beta strandi304 – 31310
    Beta strandi319 – 33113
    Beta strandi335 – 34814
    Beta strandi351 – 3577
    Helixi361 – 3677
    Beta strandi374 – 3807
    Turni381 – 3833
    Beta strandi384 – 3907
    Helixi392 – 3943
    Turni409 – 4113
    Beta strandi414 – 4163
    Beta strandi425 – 4273
    Helixi429 – 4313
    Helixi433 – 44412
    Turni446 – 4494
    Helixi456 – 4649
    Helixi471 – 4755
    Helixi479 – 4835
    Helixi490 – 50314
    Helixi508 – 5147
    Helixi522 – 53211
    Helixi535 – 5406
    Helixi543 – 5464
    Helixi554 – 56512
    Helixi567 – 57812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OWOX-ray2.30A1-671[»]
    4GLXX-ray1.90A1-586[»]
    ProteinModelPortaliP15042.
    SMRiP15042. Positions 1-586, 600-669.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15042.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini593 – 67179BRCTAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni330 – 3345Interaction with target DNA
    Regioni453 – 4586Interaction with target DNA
    Regioni519 – 5246Interaction with target DNA
    Regioni551 – 5566Interaction with target DNA

    Sequence similaritiesi

    Contains 1 BRCT domain.Curated

    Phylogenomic databases

    eggNOGiCOG0272.
    HOGENOMiHOG000218459.
    KOiK01972.
    OMAiFPAQEQL.
    OrthoDBiEOG6TTVM9.
    PhylomeDBiP15042.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    3.40.50.10190. 1 hit.
    HAMAPiMF_01588. DNA_ligase_A.
    InterProiIPR001357. BRCT_dom.
    IPR018239. DNA_ligase_AS.
    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.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    PF01653. DNA_ligase_aden. 1 hit.
    PF03120. DNA_ligase_OB. 1 hit.
    PF03119. DNA_ligase_ZBD. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001604. LigA. 1 hit.
    SMARTiSM00292. BRCT. 1 hit.
    SM00278. HhH1. 4 hits.
    SM00532. LIGANc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47781. SSF47781. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF52113. SSF52113. 1 hit.
    TIGRFAMsiTIGR00575. dnlj. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS01055. DNA_LIGASE_N1. 1 hit.
    PS01056. DNA_LIGASE_N2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P15042-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP    50
    ELITPDSPTQ RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD 100
    RLKNNEKVTW CCELKLDGLA VSILYENGVL VSAATRGDGT TGEDITSNVR 150
    TIRAIPLKLH GENIPARLEV RGEVFLPQAG FEKINEDARR TGGKVFANPR 200
    NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL GRLLQFKKWG 250
    LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL 300
    GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG 350
    VLVSNATLHN ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR 400
    EVVFPTHCPV CGSDVERVEG EAVARCTGGL ICGAQRKESL KHFVSRRAMD 450
    VDGMGDKIID QLVEKEYVHT PADLFKLTAG KLTGLERMGP KSAQNVVNAL 500
    EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA ASIEELQKVP 550
    DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG 600
    KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA 650
    KAQELGIEVI DEAEMLRLLG S 671
    Length:671
    Mass (Da):73,606
    Last modified:November 1, 1997 - v2
    Checksum:iDD2BDC64D8E65256
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691A → R in AAA24071. (PubMed:3018436)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490647.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75464; AAC75464; b2411.
    BAA16282; BAA16282; BAA16282.
    GeneIDi12930678.
    946885.
    KEGGiecj:Y75_p2372.
    eco:b2411.
    PATRICi32120205. VBIEscCol129921_2505.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi B65015. LQECC6.
    RefSeqi NP_416906.1. NC_000913.3.
    YP_490647.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OWO X-ray 2.30 A 1-671 [» ]
    4GLX X-ray 1.90 A 1-586 [» ]
    ProteinModelPortali P15042.
    SMRi P15042. Positions 1-586, 600-669.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10098N.
    IntActi P15042. 20 interactions.
    MINTi MINT-204717.
    STRINGi 511145.b2411.

    Proteomic databases

    PaxDbi P15042.
    PRIDEi P15042.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75464 ; AAC75464 ; b2411 .
    BAA16282 ; BAA16282 ; BAA16282 .
    GeneIDi 12930678.
    946885.
    KEGGi ecj:Y75_p2372.
    eco:b2411.
    PATRICi 32120205. VBIEscCol129921_2505.

    Organism-specific databases

    EchoBASEi EB0529.
    EcoGenei EG10534. ligA.

    Phylogenomic databases

    eggNOGi COG0272.
    HOGENOMi HOG000218459.
    KOi K01972.
    OMAi FPAQEQL.
    OrthoDBi EOG6TTVM9.
    PhylomeDBi P15042.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10534-MONOMER.
    ECOL316407:JW2403-MONOMER.
    MetaCyc:EG10534-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P15042.
    PROi P15042.

    Gene expression databases

    Genevestigatori P15042.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    3.40.50.10190. 1 hit.
    HAMAPi MF_01588. DNA_ligase_A.
    InterProi IPR001357. BRCT_dom.
    IPR018239. DNA_ligase_AS.
    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.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    PF01653. DNA_ligase_aden. 1 hit.
    PF03120. DNA_ligase_OB. 1 hit.
    PF03119. DNA_ligase_ZBD. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001604. LigA. 1 hit.
    SMARTi SM00292. BRCT. 1 hit.
    SM00278. HhH1. 4 hits.
    SM00532. LIGANc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47781. SSF47781. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF52113. SSF52113. 1 hit.
    TIGRFAMsi TIGR00575. dnlj. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS01055. DNA_LIGASE_N1. 1 hit.
    PS01056. DNA_LIGASE_N2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli."
      Ishino Y., Shinagawa H., Makino K., Tsunasawa S., Sakiyama F., Nakata A.
      Mol. Gen. Genet. 204:1-7(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13 AND 666-671.
      Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
    2. O'Connor M.J., Ally A., Ally D., Zhang X., Robichaud M., Backman K.
      Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli."
      Hale C.A., de Boer P.A.J.
      Cell 88:175-185(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
      Strain: PB103.
    7. "Conserved residues in domain Ia are required for the reaction of Escherichia coli DNA ligase with NAD+."
      Sriskanda V., Shuman S.
      J. Biol. Chem. 277:9695-9700(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF GLU-10; TYR-22; HIS-23; ASP-32; TYR-35 AND ASP-36, ACTIVE SITE.
    8. "Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA)."
      Zhu H., Shuman S.
      J. Biol. Chem. 280:12137-12144(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-115; ASP-117; GLY-118; ASP-138; GLU-143; GLY-172; GLU-173; ASN-198; ARG-200; ARG-208; ARG-277; ASP-285; GLY-286; VAL-288; LYS-290 AND LYS-314.
    9. "Structure-guided mutational analysis of the OB, HhH, and BRCT domains of Escherichia coli DNA ligase."
      Wang L.K., Nair P.A., Shuman S.
      J. Biol. Chem. 283:23343-23352(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-333; THR-334; ARG-342; ARG-379; 383-VAL-ILE-384; 446-ARG-ARG-447; GLY-455; ARG-487; GLY-489; GLY-521; GLY-553 AND ARG-614.
    10. "Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate."
      Nandakumar J., Nair P.A., Shuman S.
      Mol. Cell 26:257-271(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS; AMP AND DNA.

    Entry informationi

    Entry nameiDNLJ_ECOLI
    AccessioniPrimary (citable) accession number: P15042
    Secondary accession number(s): P78197, P78198
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3