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:0005575 | cellular_component | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005634 | nucleus | CC |
| GO:0005886 | plasma membrane | CC |
| GO:0005911 | cell-cell junction | CC |
| GO:0009506 | plasmodesma | CC |
| GO:0016020 | membrane | CC |
| GO:0030054 | cell junction | CC |
| GO:0043226 | organelle | CC |
| GO:0043227 | membrane-bounded organelle | CC |
| GO:0043229 | intracellular organelle | CC |
| GO:0043231 | intracellular membrane-bounded organelle | CC |
| GO:0044424 | obsolete intracellular part | CC |
| GO:0044464 | obsolete cell part | CC |
| GO:0055044 | symplast | CC |
| GO:0071944 | cell periphery | CC |
| KEGG Term | Name | Description |
|---|---|---|
| map02010 | ABC transporters | The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD). |