Domains within Aquifex aeolicus VF5 protein O66728_AQUAE (O66728)
Poly A polymerase
Alternative representations: 1 /
| Protein length | 824 aa |
|---|---|
| Source database | UniProt |
| Identifiers | O66728_AQUAE, O66728 |
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. |
This domain architecture was probably invented with the emergence of cellular organisms
Predicted functional partners
O66728_AQUAE is shown as 
pcnB1 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 O66728_AQUAE is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
KEGG pathways
| Pathway | Description | |
|---|---|---|
| map03018 | RNA degradation |
KEGG orthologous groups
| KO | Name | Description | |
|---|---|---|---|
| K00974 | cca | tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-] | |
| K06881 | nrnA | bifunctional oligoribonuclease and PAP phosphatase NrnA [EC:3.1.3.7 3.1.13.3] | iPath3 |
| K00970 | pcnB | poly(A) polymerase [EC:2.7.7.19] | |
| K06041 | kdsD, kpsF | arabinose-5-phosphate isomerase [EC:5.3.1.13] | iPath3 |
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 224324.aq_411 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG2905 | All organisms (root) | arabinose-5-phosphate isomerase [EC:5.3.1.13],CBS domain-containing protein,IMP dehydrogenase [EC:1.1.1.205] |
| 770IH | All organisms (root) | tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-] |
| LCOG0618 | All organisms (root) | bifunctional oligoribonuclease and PAP phosphatase NrnA [EC:3.1.3.7 3.1.13.3],tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-],single-stranded-DNA-specific exonuclease [EC:3.1.-.-] |
| LCOG0617 | All organisms (root) | tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-],poly(A) polymerase [EC:2.7.7.19],lincosamide nucleotidyltransferase A/C/D/E |
| COG0617 | Bacteria (superkingdom) | poly(A) polymerase [EC:2.7.7.19],tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-],protein archease |
| D93J0 | Bacteria (superkingdom) | tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-] |
| COG0618 | Bacteria (superkingdom) | bifunctional oligoribonuclease and PAP phosphatase NrnA [EC:3.1.3.7 3.1.13.3],tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-],arylsulfatase A [EC:3.1.6.8] |
| COG2905 | Bacteria (superkingdom) | arabinose-5-phosphate isomerase [EC:5.3.1.13],CBS domain-containing protein,IMP dehydrogenase [EC:1.1.1.205] |
| AFSIR | Aquificae (class) | tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-] |
| FM402 | Aquificales (order) | tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-] |
| 8I2FH | Aquificaceae (family) | tRNA nucleotidyltransferase (CCA-adding enzyme) [EC:2.7.7.72 3.1.3.- 3.1.4.-] |
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.