Alternative representations: 1 /
| Protein length | 944 aa |
|---|---|
| Source database | UniProt |
| Identifiers | C7RM82_ACCPU, C7RM82 |
| 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. |
This domain architecture was probably invented with the emergence of cellular organisms
C7RM82_ACCPU is shown as
ACV37160.1 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.
Protein C7RM82_ACCPU is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
| Pathway | Description | |
|---|---|---|
| map01053 | Biosynthesis of siderophore group nonribosomal peptides | iPath3 |
| map00071 | Fatty acid degradation | iPath3 |
| map00564 | Glycerophospholipid metabolism | iPath3 |
| KO | Name | Description | |
|---|---|---|---|
| K00655 | plsC | 1-acyl-sn-glycerol-3-phosphate acyltransferase [EC:2.3.1.51] | iPath3 |
| K08227 | lplT | MFS transporter, LPLT family, lysophospholipid transporter | |
| K01897 | ACSL, fadD | long-chain-fatty-acid---CoA ligase [EC:6.2.1.3] | iPath3 |
| K02078 | acpP, acpM | acyl carrier protein | |
| K12444 | ppsE | phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292] |
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 522306.CAP2UW1_3910 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG0236 | All organisms (root) | acyl carrier protein,NADH dehydrogenase (ubiquinone) 1 alpha/beta subcomplex 1, acyl-carrier protein,D-alanine--poly(phosphoribitol) ligase subunit 2 [EC:6.1.1.13] |
| 7E1AI | Betaproteobacteria incertae sedis (no rank) | PP-binding,AMP-binding,Acyltransferase |
| 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] |
| LCOG0204 | All organisms (root) | 1-acyl-sn-glycerol-3-phosphate acyltransferase [EC:2.3.1.51],lysophosphatidylcholine acyltransferase / lyso-PAF acetyltransferase [EC:2.3.1.23 2.3.1.67],lysophosphatidate acyltransferase [EC:2.3.1.51] |
| COG0236 | Bacteria (superkingdom) | acyl carrier protein,D-alanine--poly(phosphoribitol) ligase subunit 2 [EC:6.1.1.13],polyketide synthase 13 |
| 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] |
| COG0204 | Bacteria (superkingdom) | 1-acyl-sn-glycerol-3-phosphate acyltransferase [EC:2.3.1.51],lyso-ornithine lipid O-acyltransferase [EC:2.3.1.270],acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20] |
| 633R2 | Proteobacteria (phylum) | MFS transporter, LPLT family, lysophospholipid transporter,acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 6.2.1.20],L-serine---[L-seryl-carrier protein] ligase [EC:6.3.2.14 6.2.1.72] |
| 8VCRG | Betaproteobacteria (class) | phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase E [EC:2.3.1.292],phthiocerol/phenolphthiocerol synthesis type-I polyketide synthase C [EC:2.3.1.292],L-serine---[L-seryl-carrier protein] ligase [EC:6.3.2.14 6.2.1.72] |
| CAPTX | Candidatus Accumulibacter (genus) | PP-binding,AMP-binding,Acyltransferase |
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.