Literature summary extracted from

Kito, H.; Fujikawa, T.; Moriwaki, A.; Tomono, A.; Izawa, M.; Kamakura, T.; Ohashi, M.; Sato, H.; Abe, K.; Nishimura, M.
MgLig4, a homolog of Neurospora crassa Mus-53 (DNA ligase IV), is involved in, but not essential for, non-homologous end-joining events in Magnaporthe grisea (2008), Fungal Genet. Biol., 45, 1543-1551.

Protein Variants

EC Number	Protein Variants	Comment	Organism
6.5.1.1	additional information	mutants (mglig4) show no defects in asexual or sexual growth, and are fully pathogenic, compared to the wild type enzyme, mglig4 exhibits weak sensitivity to a DNA-damaging agent camptothecin, non-homologous integration of DNA is frequently observed in mglig4 transformants	Pyricularia grisea

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
6.5.1.1	camptothecin	-	Pyricularia grisea

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.5.1.1	Pyricularia grisea	B6ZH51	strains Guy11 and P2	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6.5.1.1	ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m	-	Pyricularia grisea	AMP + diphosphate + (deoxyribonucleotide)m+n	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
6.5.1.1	DNA ligase	-	Pyricularia grisea
6.5.1.1	Lig4	Lig4 is involved in, but not essential for, the non-homologous end-joining system in Magnaporthe grisea	Pyricularia grisea

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
6.5.1.1	ATP	-	Pyricularia grisea

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Release 2023.1 (January 2023)