AT3G27710.1
Arabidopsis thaliana [ath]
RING/U-box superfamily protein
No PTMs currently found
Link out to other resources with this protein ID : TAIR | PeptideAtlas | ARAPORT | PhosPhAt
PTMs
There are no stored PTMs for this protein
Sequence
Length: 537
MDDDYMMLDDDYGEEEDENYSEDDNYSEAEVDLQPVTSTKSTSQVIKKESLVAAQKEILVRVMELLSVKENQARTLLIYYQWNVEKLFSVFADQGKDRMFSCAGLTVFVPSLVTSKKTMKCDVCMEDDLPSNVMTRMECGHRFCNDCWIGHFTVKINEGESKRILCMAHECKAICDEDVVRKLVSPELADRYDRFLIESYVEDNNMVKWCPSKPHCGSAIRKIEDGHDVVEVGCSCGLQFCFSCLSESHSPCSCLMWKLWKKKCEDESETVNWITVNTKLCPKCSKPIQKRDGCNLMTCKCGQHFCWLCGQATGRDHTYTSIAGHSCGRYKDEKVRQLERAQRDLDRYTHYHYRYKAHIDSLKLEDKLRKSILEKAVSNSETKDQKVFKEYSWVTDAVNRLFISRRILSQSYPFAFYMFGEELFKDEMSEKEREIKKNLFEDQQQQLEGNVEKLSKILEEPFDEYDHEKVVEMMRHLTNLTAVVDNLCKEMYECIENELLGPIQFGNHNIAPYRSKGIEQATEFCAESSDCGSSGSS
Domains & Sites
Clear highlighted range| Show | IPR ID | Description | From | To |
|---|---|---|---|---|
| IPR001841 | Zinc finger, RING-type | 121 | 170 | |
| IPR002867 | IBR domain | 190 | 254 | |
| 262 | 327 |
| Show | Type | Description | Position |
|---|---|---|---|
| Active Site | ECO:0000255|PROSITE-ProRule:PRU01221 | 294 | |
| Binding Site | Zn(2+) | 121 | |
| Binding Site | Zn(2+) | 124 | |
| Binding Site | Zn(2+) | 139 | |
| Binding Site | Zn(2+) | 141 | |
| Binding Site | Zn(2+) | 144 | |
| Binding Site | Zn(2+) | 147 | |
| Binding Site | Zn(2+) | 166 | |
| Binding Site | Zn(2+) | 171 | |
| Binding Site | Zn(2+) | 210 | |
| Binding Site | Zn(2+) | 216 | |
| Binding Site | Zn(2+) | 234 | |
| Binding Site | Zn(2+) | 236 | |
| Binding Site | Zn(2+) | 241 | |
| Binding Site | Zn(2+) | 244 | |
| Binding Site | Zn(2+) | 249 | |
| Binding Site | Zn(2+) | 254 | |
| Binding Site | Zn(2+) | 281 | |
| Binding Site | Zn(2+) | 284 | |
| Binding Site | Zn(2+) | 299 | |
| Binding Site | Zn(2+) | 301 | |
| Binding Site | Zn(2+) | 306 | |
| Binding Site | Zn(2+) | 309 | |
| Binding Site | Zn(2+) | 317 | |
| Binding Site | Zn(2+) | 327 |
| Type | Comment |
|---|---|
| Domain | Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. {ECO:0000250|UniProtKB:Q9Y4X5}. |