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| PROSITE documentation PDOC00809 |
NAD-dependent DNA ligase signatures
Description:
DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA
fragments by catalyzing the formation of an internucleotide ester bond between
phosphate and deoxyribose. It is active during DNA replication, DNA repair and
DNA recombination. There are two forms of DNA ligase: one requires ATP
(EC 6.5.1.1), the other NAD (EC 6.5.1.2).
Bacterial DNA ligases are NAD-dependent. They are proteins of about 75 to 85
Kd whose sequence is well conserved [1]. They also show similarity to yicF, an
Escherichia coli hypothetical protein of 63 Kd. We developed two signature
patterns for this family of proteins; these signatures are based on conserved
regions in the N-terminal half.
Last update:
December 2004 / Patterns and text revised.
Technical section:
PROSITE methods (with tools and information) covered by this documentation:
| DNA_LIGASE_N1, PS01055; NAD-dependent DNA ligase signature 1 (PATTERN) |
| Consensus pattern: |
K-[LIVMF]-D-G-[LIVMAS]-[SAG]-x(4)-Y-x(2)-[GRD]-x-[LF]-x(4)-[ST]-R-G-[DN]-G-x(2)-G-[DE]-[DENL]
K is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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| Matching PDB structures:
1TA8 1TAE 1V9P 1ZAU ... [ALL] |
| DNA_LIGASE_N2, PS01056; NAD-dependent DNA ligase signature 2 (PATTERN) |
| Consensus pattern: |
[IV]-G-[KR]-[ST]-G-x-[LIVM]-[STNK]-x-[VTLYF]-x(2)-[LVMF]-x-[PS]-[IV]
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| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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| Matching PDB structures:
1DGS 1V9P 2OWO [ALL] |
References:
| 1 |
Authors | Shark K.B., Conway T. |
| Title | Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis. |
| Source | FEMS Microbiol. Lett. 75:19-26(1992). |
| PubMed ID | 1526462 |
| 2 |
Authors | Gentry D., Bengra C., Ikehara K., Cashel M. |
| Title | Guanylate kinase of Escherichia coli K-12. |
| Source | J. Biol. Chem. 268:14316-14321(1993). |
| PubMed ID | 8390989 |
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