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Q9I1X7

- LIGD_PSEAE

UniProt

Q9I1X7 - LIGD_PSEAE

Protein

Multifunctional non-homologous end joining protein LigD

Gene

ligD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    With Ku probably forms a non-homologous end joining (NHEJ) repair enzyme, which repairs dsDNA breaks (DSB) with reduced fidelity. Acts as a DNA ligase on singly nicked dsDNA, fills dsDNA gaps (3- or 4- nucleotide gaps, prefers a 5'-phosphate at the gap distal end, prefers dNTPs over rNTPs) (PubMed:20018881), has DNA-directed DNA polymerase activity (templated primer extension) and DNA-directed RNA polymerase activity (PubMed:15897197), adds 1 or 2 non-templated rNTP (or less well dNTP) to ssDNA or blunt-end dsDNA (primer extension). Has 3' resection activity, removing 3'-rNMPs from DNA using its 3'-ribonuclease and 3'-phosphatase activities sequentially. Resection requires a 2'-OH in the penultimate nucleoside position (i.e. a ribo- not deoxyribonucleoside) (PubMed:15897197), although the 3'-phosphatase activity does not, and its specific activity is 16-fold higher on a DNA substrate (PubMed:16046407). On appropriate substrates will extend a DNA primer to the end of the template strand and then incorporate a non-templated nucleotide.3 Publications
    The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in quiescent cells where the dNTP pool may be limiting.

    Catalytic activityi

    ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).

    Cofactori

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

    Enzyme regulationi

    rNTP addition and end joining activities are stimulated by Ku homodimer.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi42 – 421Manganese 1; catalytic; via pros nitrogen; for 3'-phosphoesterase activity2 Publications
    Metal bindingi48 – 481Manganese 1; catalytic; via tele nitrogen; for 3'-phosphoesterase activity2 Publications
    Metal bindingi50 – 501Manganese 1; catalytic; for 3'-phosphoesterase activity2 Publications
    Sitei84 – 841Transition state stabilizer; for 3'-phosphoesterase activityCurated
    Active sitei238 – 2381N6-AMP-lysine intermediateCurated
    Metal bindingi240 – 2401Manganese 2By similarity
    Metal bindingi376 – 3761Manganese 2By similarity
    Binding sitei604 – 6041ATP1 Publication
    Binding sitei651 – 6511ATP1 Publication
    Metal bindingi669 – 6691Manganese 32 Publications
    Metal bindingi669 – 6691Manganese 42 Publications
    Metal bindingi671 – 6711Manganese 32 Publications
    Binding sitei671 – 6711ATP1 Publication
    Metal bindingi759 – 7591Manganese 42 Publications
    Binding sitei768 – 7681ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi704 – 7107ATP1 Publication
    Nucleotide bindingi776 – 7783ATP1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA-directed DNA polymerase activity Source: UniProtKB
    4. DNA ligase (ATP) activity Source: UniProtKB
    5. DNA primase activity Source: InterPro
    6. exoribonuclease activity Source: UniProtKB
    7. metal ion binding Source: UniProtKB-KW
    8. nucleotidyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. DNA ligation Source: GOC
    2. DNA recombination Source: UniProtKB-KW
    3. DNA repair Source: UniProtKB-KW
    4. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Exonuclease, Hydrolase, Ligase, Nuclease, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Manganese, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multifunctional non-homologous end joining protein LigD
    Alternative name(s):
    NHEJ DNA polymerase
    Including the following 3 domains:
    3'-phosphoesterase
    Short name:
    3'-ribonuclease/3'-phosphatase
    DNA ligase D (EC:6.5.1.1)
    Short name:
    LigD
    Alternative name(s):
    Polydeoxyribonucleotide synthase [ATP]
    DNA repair polymerase
    Short name:
    Pol
    Alternative name(s):
    Polymerase/primase
    Gene namesi
    Name:ligD
    Ordered Locus Names:PA2138
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA2138.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141R → A: 77% ribonuclease activity, loss of 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi15 – 151D → A: 3% 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi21 – 211E → A: Loss of 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi40 – 401Q → A: 41% ribonuclease activity, 7% 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi42 – 421H → A: Loss of ribonuclease and 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi46 – 461R → A: 16% ribonuclease activity, 20% 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi48 – 481H → A: Loss of ribonuclease and 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi50 – 501D → A: Loss of nuclease and 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi52 – 521R → A: Loss of nuclease and 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi54 – 541E → A: Nearly wild-type nuclease and 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi66 – 661K → A: 3% ribonuclease activity, 28% 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi76 – 761R → A: 1% ribonuclease activity, 16% 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi82 – 821E → A: Selective loss of 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi83 – 831D → A: 57% ribonuclease activity, 50% 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi84 – 841H → A: Loss of nuclease and 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi88 – 881Y → A: 7% ribonuclease activity, loss of 3'-phosphatase activity (in PE domain). 2 Publications
    Mutagenesisi553 – 56614HPQRL…IQASK → APQALIDPSIQASA: 5'-phosphate at distal end of gap no longer advantageous for rNTP or dNTP addition (in Pol domain). 2 PublicationsAdd
    BLAST
    Mutagenesisi553 – 56614HPQRL…IQASK → APQRLIDPSIQASA: Addition of rNTP to gapped molecule decreases to 1 or 2 nucleotides, dNTP addition decreased, 5'-phosphate at distal end of gap no longer advantageous (in Pol domain). 2 PublicationsAdd
    BLAST
    Mutagenesisi553 – 5531H → A: Wild-type gap closing by rNTP or dNTP addition (in Pol domain). 2 Publications
    Mutagenesisi556 – 5561R → A: Decreases gap closing efficiency by rNTP, wild-type by dNTP (in Pol domain). 2 Publications
    Mutagenesisi566 – 5661K → A: No change in dNTP addition to gapped molecule, 5'-phosphate at distal of the gap no longer advantageous for rNTP addition (in Pol domain). 2 Publications
    Mutagenesisi603 – 6031F → A: Last nucleotide rarely added during gap closing for dNTP or rNTP addition, (in Pol domain). Stacks a DNA template base. 2 Publications
    Mutagenesisi604 – 6041F → A: Nearly complete loss of templated dNTP or rNTP addition (in Pol domain). 2 Publications
    Mutagenesisi669 – 6713DLD → ALA: Loss of templated and non-templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi669 – 6691D → A or N: Loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi669 – 6691D → E: Partial loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi671 – 6711D → A, E or N: Loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi710 – 7101H → A: Loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi710 – 7101H → N: Partial loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi710 – 7101H → Q: Nearly wild-type templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi752 – 7521R → A or Q: Loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi752 – 7521R → K: Partial loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi759 – 7591D → A or N: Loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi759 – 7591D → E: Partial loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi776 – 7761R → A: Loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi776 – 7761R → K: Nearly wild-type templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi776 – 7761R → Q: Partial loss of templated DNA synthesis (in Pol domain). 2 Publications
    Mutagenesisi778 – 7781R → A: Nearly wild-type templated dNTP or rNTP addition (in Pol domain). 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 840840Multifunctional non-homologous end joining protein LigDPRO_0000425950Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer. Interacts with Ku By similarity.By similarity

    Protein-protein interaction databases

    STRINGi208964.PA2138.

    Structurei

    Secondary structure

    1
    840
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 5521
    Beta strandi58 – 647
    Beta strandi72 – 743
    Beta strandi76 – 849
    Helixi86 – 905
    Beta strandi91 – 955
    Turni97 – 1004
    Beta strandi104 – 11714
    Helixi119 – 1257
    Beta strandi127 – 13610
    Beta strandi138 – 1458
    Beta strandi148 – 1536
    Beta strandi154 – 1596
    Turni168 – 1703
    Helixi173 – 1764
    Turni181 – 1833
    Turni544 – 5485
    Beta strandi556 – 5594
    Helixi560 – 5623
    Helixi566 – 57510
    Helixi577 – 5848
    Beta strandi587 – 5937
    Beta strandi603 – 6053
    Helixi621 – 6233
    Beta strandi630 – 6323
    Helixi636 – 6449
    Beta strandi647 – 6526
    Beta strandi664 – 6729
    Helixi678 – 69518
    Beta strandi700 – 7034
    Beta strandi705 – 71410
    Helixi721 – 73818
    Turni740 – 7423
    Helixi749 – 7513
    Beta strandi755 – 7595
    Helixi761 – 7633
    Helixi789 – 7946
    Turni803 – 8053
    Helixi806 – 8138
    Turni818 – 8247
    Helixi831 – 8366

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FAOX-ray1.50A/B533-840[»]
    2FAQX-ray1.90A/B533-840[»]
    2FARX-ray1.90A/B533-840[»]
    2LJ6NMR-A1-177[»]
    3N9BX-ray1.92A/B17-187[»]
    3N9DX-ray2.30A17-187[»]
    ProteinModelPortaliQ9I1X7.
    SMRiQ9I1X7. Positions 33-163, 172-523, 543-837.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9I1X7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 1621563'-phosphoesterase domain (PE)Add
    BLAST
    Regioni219 – 521303Ligase domain (Lig)Add
    BLAST
    Regioni549 – 793245DNA repair polymerase domain (Pol)Add
    BLAST

    Domaini

    The N-terminal 3'-phosphoesterase domain (PE) has 3'-ribonuclease and 3'-phosphatase activities.1 Publication
    The central ATP-dependent ligase domain (Lig) functions as an independent domain.1 Publication
    The C-terminal polymerase/primase domain (Pol) (PubMed:15520014) adds up to 4 rNTPs in a DNA template-directed fashion (PubMed:15897197).2 Publications

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000222509.
    KOiK01971.
    OMAiNGLPDFQ.
    OrthoDBiEOG661H49.
    PhylomeDBiQ9I1X7.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR012309. DNA_ligase_ATP-dep_C.
    IPR012310. DNA_ligase_ATP-dep_cent.
    IPR014146. DNA_pol_LigD_ligase_dom.
    IPR002755. DNA_primase_S.
    IPR014144. LigD_PE_domain.
    IPR014145. LigD_pol.
    IPR012340. NA-bd_OB-fold.
    IPR014143. NHEJ_ligase_prk.
    [Graphical view]
    PfamiPF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF01896. DNA_primase_S. 1 hit.
    PF13298. LigD_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR02777. LigD_PE_dom. 1 hit.
    TIGR02778. ligD_pol. 1 hit.
    TIGR02779. NHEJ_ligase_lig. 1 hit.
    TIGR02776. NHEJ_ligase_prk. 1 hit.
    PROSITEiPS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9I1X7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSSKPLAEY ARKRDFRQTP EPSGRKPRKD STGLLRYCVQ KHDASRLHYD    50
    FRLELDGTLK SWAVPKGPCL DPAVKRLAVQ VEDHPLDYAD FEGSIPQGHY 100
    GAGDVIVWDR GAWTPLDDPR EGLEKGHLSF ALDGEKLSGR WHLIRTNLRG 150
    KQSQWFLVKA KDGEARSLDR FDVLKERPDS VLSERTLLPR HGEAATPAAR 200
    PARRGKSGGK TPMPEWIAPE LASLVEQPPR GEWAYELKLD GYRLMSRIED 250
    GHVRLLTRNG HDWTERLPHL EKALAGLGLQ RSWLDGELVV LDEEGRPDFQ 300
    ALQNAFEEGR GENILYVLFD LPYHEGEDLR DVALEERRAR LEALLEGRDE 350
    DPLRFSATLA EDPRDLLASA CKLGLEGVIG KRLGSAYRSR RSNDWIKLKC 400
    QLRQEFVIVG YTEPKGSRRH IGALLLGLYS PDEERRLRYA GKVGSGFTAA 450
    SLKKVRERLE PLAVRSSPLA KVPPARETGS VQWVRPQQLC EVSYAQMTRG 500
    GIIRQAVFHG LREDKPAREV TGERPAGPPP LRGARKASAG ASRAATAGVR 550
    ISHPQRLIDP SIQASKLELA EFHARYADLL LRDLRERPVS LVRGPDGIGG 600
    ELFFQKHAAR LKIPGIVQLD PALDPGHPPL LQIRSAEALV GAVQMGSIEF 650
    HTWNASLANL ERPDRFVLDL DPDPALPWKR MLEATQLSLT LLDELGLRAF 700
    LKTSGGKGMH LLVPLERRHG WDEVKDFAQA ISQHLARLMP ERFSAVSGPR 750
    NRVGKIFVDY LRNSRGASTV AAYSVRAREG LPVSVPVFRE ELDSLQGANQ 800
    WNLRSLPQRL DELAGDDPWA DYAGTRQRIS AAMRRQLGRG 840
    Length:840
    Mass (Da):94,030
    Last modified:March 1, 2001 - v1
    Checksum:i5CAE7929CC5F29C7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG05526.1.
    PIRiC83378.
    RefSeqiNP_250828.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG05526; AAG05526; PA2138.
    GeneIDi880451.
    KEGGipae:PA2138.
    PATRICi19838710. VBIPseAer58763_2235.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG05526.1 .
    PIRi C83378.
    RefSeqi NP_250828.1. NC_002516.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FAO X-ray 1.50 A/B 533-840 [» ]
    2FAQ X-ray 1.90 A/B 533-840 [» ]
    2FAR X-ray 1.90 A/B 533-840 [» ]
    2LJ6 NMR - A 1-177 [» ]
    3N9B X-ray 1.92 A/B 17-187 [» ]
    3N9D X-ray 2.30 A 17-187 [» ]
    ProteinModelPortali Q9I1X7.
    SMRi Q9I1X7. Positions 33-163, 172-523, 543-837.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA2138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG05526 ; AAG05526 ; PA2138 .
    GeneIDi 880451.
    KEGGi pae:PA2138.
    PATRICi 19838710. VBIPseAer58763_2235.

    Organism-specific databases

    PseudoCAPi PA2138.

    Phylogenomic databases

    HOGENOMi HOG000222509.
    KOi K01971.
    OMAi NGLPDFQ.
    OrthoDBi EOG661H49.
    PhylomeDBi Q9I1X7.

    Miscellaneous databases

    EvolutionaryTracei Q9I1X7.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR012309. DNA_ligase_ATP-dep_C.
    IPR012310. DNA_ligase_ATP-dep_cent.
    IPR014146. DNA_pol_LigD_ligase_dom.
    IPR002755. DNA_primase_S.
    IPR014144. LigD_PE_domain.
    IPR014145. LigD_pol.
    IPR012340. NA-bd_OB-fold.
    IPR014143. NHEJ_ligase_prk.
    [Graphical view ]
    Pfami PF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF01896. DNA_primase_S. 1 hit.
    PF13298. LigD_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR02777. LigD_PE_dom. 1 hit.
    TIGR02778. ligD_pol. 1 hit.
    TIGR02779. NHEJ_ligase_lig. 1 hit.
    TIGR02776. NHEJ_ligase_prk. 1 hit.
    PROSITEi PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    2. "A primer-dependent polymerase function of pseudomonas aeruginosa ATP-dependent DNA ligase (LigD)."
      Zhu H., Shuman S.
      J. Biol. Chem. 280:418-427(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A LIGASE, FUNCTION AS A DNA POLYMERASE, COFACTOR, SUBUNIT, DOMAIN, MUTAGENESIS OF 669-ASP--ASP-671.
    3. "Novel 3'-ribonuclease and 3'-phosphatase activities of the bacterial non-homologous end-joining protein, DNA ligase D."
      Zhu H., Shuman S.
      J. Biol. Chem. 280:25973-25981(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RESECTION, COFACTOR, DOMAIN, MUTAGENESIS OF ASP-50; ARG-52; GLU-54; GLU-82 AND HIS-84.
    4. "Essential constituents of the 3'-phosphoesterase domain of bacterial DNA ligase D, a nonhomologous end-joining enzyme."
      Zhu H., Wang L.K., Shuman S.
      J. Biol. Chem. 280:33707-33715(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, DOMAIN, MUTAGENESIS OF ARG-14; ASP-15; GLU-21; GLN-40; HIS-42; ARG-46; HIS-48; LYS-66; ARG-76; ASP-83 AND TYR-88.
    5. "Gap filling activities of Pseudomonas DNA ligase D (LigD) polymerase and functional interactions of LigD with the DNA end-binding Ku protein."
      Zhu H., Shuman S.
      J. Biol. Chem. 285:4815-4825(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GAP-FILLING, ENZYME REGULATION, MUTAGENESIS OF HIS-553; 553-HIS--LYS-566; ARG-556; LYS-566 AND PHE-603.
    6. "Atomic structure and nonhomologous end-joining function of the polymerase component of bacterial DNA ligase D."
      Zhu H., Nandakumar J., Aniukwu J., Wang L.K., Glickman M.S., Lima C.D., Shuman S.
      Proc. Natl. Acad. Sci. U.S.A. 103:1711-1716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 533-840 OF APOENZYME AND IN COMPLEX WITH ATP AND MANGANESE, COFACTOR, ATP-BINDING, MUTAGENESIS OF PHE-604; ASP-669; ASP-671; HIS-710; ARG-752; ASP-759; ARG-776 AND ARG-778.
    7. "Structure of bacterial LigD 3'-phosphoesterase unveils a DNA repair superfamily."
      Nair P.A., Smith P., Shuman S.
      Proc. Natl. Acad. Sci. U.S.A. 107:12822-12827(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 17-187 IN COMPLEX WITH MANGANESE, FUNCTION, REACTION MECHANISM.
    8. "Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D."
      Natarajan A., Dutta K., Temel D.B., Nair P.A., Shuman S., Ghose R.
      Nucleic Acids Res. 40:2076-2088(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-177, DNA-BINDING.

    Entry informationi

    Entry nameiLIGD_PSEAE
    AccessioniPrimary (citable) accession number: Q9I1X7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 19, 2014
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3