| Accession | TIGR03793 |
| Name | TOMM_pelo |
| Function | NHLP leader peptide domain |
| Trusted Cutoff | 50.90 |
| Domain Trusted Cutoff | 50.90 |
| Noise Cutoff | 43.40 |
| Domain Noise Cutoff | 43.40 |
| Isology Type | domain |
| HMM Length | 77 |
| Author | Haft DH |
| Entry Date | Jul 16 2009 2:57PM |
| Last Modified | Mar 10 2014 5:46PM |
| Comment | This HMM represents a domain that is conserved among a large number of putative ribosomal natural products (RNP) precursor, including the thiazole/oxazole-modified microcins (TOMMs). As a leader peptide domain, likely to be removed from the mature product, this domain is unusual in several ways. First, it is longer than most previously described RNP leader peptides. Second, most of the domain is homologous to nitrile hydratase alpha subunits. Finally, it appears that this domain correlates with a specific family of cleavage/export proteins while members undergo modifications by different classes of peptide maturase, including cyclodehydratases, lantibiotic synthases, radical SAM peptide maturases. This family is expanded especially in Pelotomaculum thermopropionicum SI. |
| References | RN [1]
RM PMID:20500830
RT Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family.
RA Haft DH, Basu MK, Mitchell DA
RL BMC Biol. 2010 May 25;8:70.
RN [2]
RM PMID:22983711
RT Metagenome mining reveals polytheonamides as posttranslationally modified ribosomal peptides.
RA Freeman MF, Gurgui C, Helf MJ, Morinaka BI, Uria AR, Oldham NJ, Sahl HG, Matsunaga S, Piel J
RL Science. 2012 Oct 19;338(6105):387-90. doi: 10.1126/science.1226121. |
| Genome Property | GenProp0807: bacteriocin system, heterocycle biosynthesis group (HMM) |
| | GenProp0861: bacteriocin system, NHLP (nif11/nitrile hydratase leader peptide) transport group (HMM) |
