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Q9I1X7

- LIGD_PSEAE

UniProt

Q9I1X7 - LIGD_PSEAE

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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

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
Complete GO annotation...

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

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.
InParanoidiQ9I1X7.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSSKPLAEY ARKRDFRQTP EPSGRKPRKD STGLLRYCVQ KHDASRLHYD
60 70 80 90 100
FRLELDGTLK SWAVPKGPCL DPAVKRLAVQ VEDHPLDYAD FEGSIPQGHY
110 120 130 140 150
GAGDVIVWDR GAWTPLDDPR EGLEKGHLSF ALDGEKLSGR WHLIRTNLRG
160 170 180 190 200
KQSQWFLVKA KDGEARSLDR FDVLKERPDS VLSERTLLPR HGEAATPAAR
210 220 230 240 250
PARRGKSGGK TPMPEWIAPE LASLVEQPPR GEWAYELKLD GYRLMSRIED
260 270 280 290 300
GHVRLLTRNG HDWTERLPHL EKALAGLGLQ RSWLDGELVV LDEEGRPDFQ
310 320 330 340 350
ALQNAFEEGR GENILYVLFD LPYHEGEDLR DVALEERRAR LEALLEGRDE
360 370 380 390 400
DPLRFSATLA EDPRDLLASA CKLGLEGVIG KRLGSAYRSR RSNDWIKLKC
410 420 430 440 450
QLRQEFVIVG YTEPKGSRRH IGALLLGLYS PDEERRLRYA GKVGSGFTAA
460 470 480 490 500
SLKKVRERLE PLAVRSSPLA KVPPARETGS VQWVRPQQLC EVSYAQMTRG
510 520 530 540 550
GIIRQAVFHG LREDKPAREV TGERPAGPPP LRGARKASAG ASRAATAGVR
560 570 580 590 600
ISHPQRLIDP SIQASKLELA EFHARYADLL LRDLRERPVS LVRGPDGIGG
610 620 630 640 650
ELFFQKHAAR LKIPGIVQLD PALDPGHPPL LQIRSAEALV GAVQMGSIEF
660 670 680 690 700
HTWNASLANL ERPDRFVLDL DPDPALPWKR MLEATQLSLT LLDELGLRAF
710 720 730 740 750
LKTSGGKGMH LLVPLERRHG WDEVKDFAQA ISQHLARLMP ERFSAVSGPR
760 770 780 790 800
NRVGKIFVDY LRNSRGASTV AAYSVRAREG LPVSVPVFRE ELDSLQGANQ
810 820 830 840
WNLRSLPQRL DELAGDDPWA DYAGTRQRIS AAMRRQLGRG
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.
InParanoidi Q9I1X7.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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