Accession | TIGR03913 |
Name | rad_SAM_trio |
Function | Y_X(10)_GDL-associated radical SAM protein |
Trusted Cutoff | 591.75 |
Domain Trusted Cutoff | 591.75 |
Noise Cutoff | 591.45 |
Domain Noise Cutoff | 591.45 |
Isology Type | hypoth_equivalog |
HMM Length | 477 |
Author | Haft DH |
Entry Date | Jan 6 2010 4:57PM |
Last Modified | Jun 9 2011 9:51AM |
Comment | This narrowly distributed protein family contains an N-terminal radical SAM domain. It occurs in Pseudomonas fluorescens Pf0-1, Ralstonia solanacearum, and numerous species and strains of Burkholderia. Members always occur next to a trio of three mutually homologous genes, all of which contain the domain PF08898 as the whole of the protein (about 60 amino acids) or as the C-terminal domain. The function is unknown, but the fact that all phylogenetically correlated proteins are mutually homologous with prominent invariant motifs (an invariant tyrosine and a GDL motif) and as small as 60 amino acids suggests that post-translational modification of PF08898 domain-containing proteins may be its function. This view is supported by closer homology to the PqqE radical SAM protein involved in PQQ biosynthesis from the PqqA precursor peptide than to other characterized radical SAM proteins. |
References | RN [1]
RM PMID:21478363
RT Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational mo
dification.
RA Haft DH, Basu MK
RL J Bacteriol. 2011 Jun;193(11):2745-55. |
Genome Property | GenProp0920: radical SAM Y_X(10)_GDL system (HMM) |