| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
9.B.308.1.1 | The P5 protein of 39 aas and 1 N-terminal TMS. It may be capable of forming an oligomeric channel in plant cell membranes, causing ER stress and inducing cell death (Qiao et al. 2018). | Viruses |
Orthornavirae, Kitrinoviricota | P5 of Lettuce infectious yellows virus |
|
9.B.308.2.1 | P6 protein of 51 aas and 1 N-terminal TMS. | Viruses |
Orthornavirae, Kitrinoviricota | P6 of the Citrus tristeza virus |
|
9.B.308.3.1 | P6 protein of 56 aas and 1 N-terminal TMS. | Viruses |
Orthornavirae, Kitrinoviricota | P6 protein of the fig mild mottle-associated virus |
|
9.B.308.3.2 | ER movement protein p6 (6 kDa protein) (or ORF2) of 54 aas and 1 N-terminal TMS. Cell-to-cell movement of beet yellows closterovirus requires four structural proteins and the 6-kDa protein (p6). Either virus infection or p6 overexpression results in association of p6 with the rough endoplasmic reticulum. The p6 protein has a hydrophilic, C-terminal domain that is localized on the cytoplasmic face of the ER. In the infected cells, p6 forms a disulfide bridge via a cysteine residue located near the protein's N terminus. Mutagenic analyses indicated that each of the p6 domains, as well as protein dimerization, is essential for p6 function in virus movement (Peremyslov et al. 2004). | Viruses |
Orthornavirae, Kitrinoviricota | P6 of beet yellows virus |
|
9.B.308.4.1 | The P4 protein of 37 aas and 1 N-terminal TMS. | Viruses |
Orthornavirae, Kitrinoviricota | P4 protein of Cordyline virus 1 |
|
9.B.308.4.2 | 4.2 kDa transmembrane protein of 35 aas and 1 N-terminal TMS. | Viruses |
Orthornavirae, Kitrinoviricota | Protein of Cordyline virus 2 |
|
9.B.308.5.1 | P5 protein of 44 aas and 1 N-terminal TMS. | Viruses |
Orthornavirae, Kitrinoviricota | P5 protein of the Blackberry vein banding-associated viru |
|
9.B.308.6.1 | Three comoponent (triple gene block, TGB) TGBp1, 2 and 3, of 463 and 0 - 2 TMSs; 119 aas with 2 TMSs, N- and C-terminal, and 190 aas with 2 TMSs, N- and C-terminal, respectively, of potato mop-top virus (PMTV) (Cowan et al. 2002; Zamyatnin et al. 2004). This 3-component complex participates in the transport of viral RNA to the plasmodemata (Haupt et al. 2005). TGBp3 most probably contains signals of plasmodesmata targeting and is therefore involved in the targeting of TGBp2 and viral RNAs-TGBp1 (RNP complex), to plasmodesmata (Tilsner et al. 2010). TGBp2 can gate plasmodesmata and increase their size exclusion limit. TGBp2 and TGBp3 are necessary for the intracellular delivery of TGBp1-containing vRNPs to plasmodesmata (Shemyakina et al. 2011). Microtubule association is required for plasmodesmal targeting of TGBp1 (Shemyakina et al. 2011).
| Viruses |
Orthornavirae, Kitrinoviricota | PGBp1, PGBp2 and PGBp3 of Potato mop-top virus (isolate Potato/Sweden/Sw) (PMTV) |