Domains within Amycolatopsis mediterranei protein O54666_AMYMD (O54666)
RifA
Alternative representations: 1 /
| Protein length | 4735 aa |
|---|---|
| Source database | UniProt |
| Identifiers | G0FS55_AMYMS, G0FS55, A0A0H3CUX4_AMYMU, A0A0H3CUX4, O54666_AMYMD, O54666 |
Domain architecture analysis
Display all proteins with similar:
| Domain organisation | Proteins having all the domains as the query in the same order. Additional domains are allowed. |
|---|---|
| Domain composition | Proteins with the same domain composition have at least one copy of each of the domains of the query. |
Predicted functional partners
O54666_AMYMD is shown as 
RifA in the network
Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.
The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.
Orthologous groups
Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 713604.RAM_03155 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG3321 | All organisms (root) | fatty acid synthase, animal type [EC:2.3.1.85],chalcone synthase [EC:2.3.1.74],phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292] |
| LCOG0318 | All organisms (root) | long-chain acyl-CoA synthetase [EC:6.2.1.3],fatty-acyl-CoA synthase [EC:6.2.1.-],4-coumarate--CoA ligase [EC:6.2.1.12] |
| LCOG0451 | All organisms (root) | UDP-glucose 4-epimerase [EC:5.1.3.2],UDP-glucuronate decarboxylase [EC:4.1.1.35],GDP-L-fucose synthase [EC:1.1.1.271] |
| LCOG1028 | All organisms (root) | 3-oxoacyl-[acyl-carrier protein] reductase [EC:1.1.1.100],3-hydroxybutyrate dehydrogenase [EC:1.1.1.30],meso-butanediol dehydrogenase / (S,S)-butanediol dehydrogenase / diacetyl reductase [EC:1.1.1.- 1.1.1.76 1.1.1.304] |
| COG0318 | Bacteria (superkingdom) | long-chain acyl-CoA synthetase [EC:6.2.1.3],fatty-acyl-CoA synthase [EC:6.2.1.-],o-succinylbenzoate---CoA ligase [EC:6.2.1.26] |
| COG0451 | Bacteria (superkingdom) | UDP-glucose 4-epimerase [EC:5.1.3.2],UDP-glucuronate 4-epimerase [EC:5.1.3.6],GDP-L-fucose synthase [EC:1.1.1.271] |
| COG3321 | Bacteria (superkingdom) | phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292],polyketide synthase 13,phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase C [EC:2.3.1.292] |
| COG1028 | Bacteria (superkingdom) | 3-oxoacyl-[acyl-carrier protein] reductase [EC:1.1.1.100],3-hydroxybutyrate dehydrogenase [EC:1.1.1.30],meso-butanediol dehydrogenase / (S,S)-butanediol dehydrogenase / diacetyl reductase [EC:1.1.1.- 1.1.1.76 1.1.1.304] |
| 6A302 | Actinobacteria (phylum) | polyketide synthase 13,mycobactin phenyloxazoline synthetase,phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292] |
| FA04H | Actinomycetia (class) | polyketide synthase 13,mycobactin phenyloxazoline synthetase,phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292] |
| DZ5X9 | Pseudonocardiaceae (family) | phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292],polyene macrolide polyketide synthase, A-type KR domains,6-deoxyerythronolide B synthase EryAII [EC:2.3.1.94] |
| GG9VV | Amycolatopsis (genus) | rifamycin polyketide synthase modules 1, 2 and 3 [EC:6.2.1.74] |
The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.