Basic Information
Gene Structure
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Domain
| Database | EntryID | E-Value | Start | end | InterPro ID | Description |
|---|
Regulation&Interaction
Annotation
Orthologous Group
| Orthologous ID | Species Number | All hits in PereRegDB | Hits of this species | Orthologous Detail |
|---|
Expression Profile
| DataSet | Number of Samples expressed(TPM>1) | Mean | Min | Max | Standard deviation(SD) | Coeffcient variation(CV) |
|---|
Pathway
| GO Term | Description | GO Category |
|---|---|---|
| GO:0000166 | nucleotide binding | MF |
| GO:0003674 | molecular_function | MF |
| GO:0003824 | catalytic activity | MF |
| GO:0005215 | transporter activity | MF |
| GO:0005488 | binding | MF |
| GO:0005524 | ATP binding | MF |
| GO:0006810 | transport | BP |
| GO:0008104 | protein localization | BP |
| GO:0008144 | obsolete drug binding | MF |
| GO:0008150 | biological_process | BP |
| GO:0008320 | protein transmembrane transporter activity | MF |
| GO:0008565 | obsolete protein transporter activity | MF |
| GO:0015031 | protein transport | BP |
| GO:0015399 | primary active transmembrane transporter activity | MF |
| GO:0015405 | ATPase-coupled transmembrane transporter activity | MF |
| GO:0015440 | ABC-type peptide transporter activity | MF |
| GO:0015450 | protein-transporting ATPase activity | MF |
| GO:0015462 | ABC-type protein transporter activity | MF |
| GO:0015833 | peptide transport | BP |
| GO:0016462 | pyrophosphatase activity | MF |
| GO:0016787 | hydrolase activity | MF |
| GO:0016817 | hydrolase activity, acting on acid anhydrides | MF |
| GO:0016818 | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides | MF |
| GO:0016887 | ATP hydrolysis activity | MF |
| GO:0017076 | purine nucleotide binding | MF |
| GO:0017111 | ribonucleoside triphosphate phosphatase activity | MF |
| GO:0022804 | active transmembrane transporter activity | MF |
| GO:0022857 | transmembrane transporter activity | MF |
| GO:0022884 | macromolecule transmembrane transporter activity | MF |
| GO:0030554 | adenyl nucleotide binding | MF |
| GO:0032553 | ribonucleotide binding | MF |
| GO:0032555 | purine ribonucleotide binding | MF |
| GO:0032559 | adenyl ribonucleotide binding | MF |
| GO:0033036 | macromolecule localization | BP |
| GO:0033220 | obsolete ATPase-coupled amide-transporter activity | MF |
| GO:0035639 | purine ribonucleoside triphosphate binding | MF |
| GO:0036094 | small molecule binding | MF |
| GO:0042623 | ATP hydrolysis activity | MF |
| GO:0042626 | ATPase-coupled transmembrane transporter activity | MF |
| GO:0042886 | amide transport | BP |
| GO:0042887 | amide transmembrane transporter activity | MF |
| GO:0043167 | ion binding | MF |
| GO:0043168 | anion binding | MF |
| GO:0043492 | ATPase-coupled transmembrane transporter activity | MF |
| GO:0045184 | establishment of protein localization | BP |
| GO:0051179 | localization | BP |
| GO:0051234 | establishment of localization | BP |
| GO:0055085 | transmembrane transport | BP |
| GO:0071702 | organic substance transport | BP |
| GO:0071705 | nitrogen compound transport | BP |
| GO:0071806 | protein transmembrane transport | BP |
| GO:0097159 | organic cyclic compound binding | MF |
| GO:0097367 | carbohydrate derivative binding | MF |
| GO:1901265 | nucleoside phosphate binding | MF |
| GO:1901363 | heterocyclic compound binding | MF |
| GO:1904680 | peptide transmembrane transporter activity | MF |
| KEGG Term | Name | Description |
|---|---|---|
| map03060 | Protein export | The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role. |

