A5DN78
Gene name |
TUF1 (PGUG_04729) |
Protein name |
Elongation factor Tu, mitochondrial |
Names |
tufM |
Species |
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) |
KEGG Pathway |
pgu:PGUG_04729 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A5DN78
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5DN78-F1 | Predicted | AlphaFoldDB |
No variants for A5DN78
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5DN78 | |||||
No associated diseases with A5DN78
7 regional properties for A5DN78
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Translational (tr)-type GTP-binding domain | 34 - 230 | IPR000795 |
| domain | Translation elongation factor EFTu/EF1A, C-terminal | 326 - 424 | IPR004160 |
| domain | Translation elongation factor EFTu-like, domain 2 | 251 - 320 | IPR004161 |
| domain | Small GTP-binding protein domain | 37 - 174 | IPR005225 |
| conserved_site | Tr-type G domain, conserved site | 75 - 90 | IPR031157 |
| domain | Elongation factor Tu, domain 2 | 237 - 323 | IPR033720 |
| domain | Elongation factor Tu (EF-Tu), GTP-binding domain | 35 - 229 | IPR041709 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| translation elongation factor activity | Functions in chain elongation during polypeptide synthesis at the ribosome. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFKNLAGSFR | AVSRVAFKTR | PSLVRSYAAF | DRSKPHVNIG | TIGHVDHGKT | TLTAAITKVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SEKGGANFLD | YGSIDRAPEE | RARGITISTA | HVEYQTDKRH | YAHVDCPGHA | DYIKNMITGA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AQMDGAIIVV | AATDGQMPQT | REHLLLARQV | GVQHLVVFVN | KVDTIDDPEM | LELVEMEMRE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LLSQYGFDGD | NTPVIMGSAL | CALESKQPEI | GVQAIEKLLD | AVDEHIPTPT | RDLEQPFLLP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VEDVFSISGR | GTVVTGRVER | GSLKKGEEIE | IVGDFDKPFK | TTVTGIEMFK | KELDAAMAGD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NAGILLRGVK | RDDVKRGMVL | AKPSTVTSHK | KVLASLYILS | KEEGGRHSPF | GENYKPQLFI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RTTDVTGTLR | FPAGEGVDHS | QMVMPGDNVE | MEIELVRKTP | LEVNQRFNIR | EGGKTVGTGL |
| VTRIIE |