C5E4F2
Gene name |
AIM14 (ZYRO0E05456g) |
Protein name |
Probable metalloreductase AIM14 |
Names |
|
Species |
Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229) (Candida mogii) |
KEGG Pathway |
zro:ZYRO0E05456g |
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 C5E4F2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C5E4F2-F1 | Predicted | AlphaFoldDB |
No variants for C5E4F2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C5E4F2 | |||||
No associated diseases with C5E4F2
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| ion transport | The directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSELVKRHG | HTHYANIPYG | YYVLIVSFFY | LVFLGVLRII | LKPRAAGFNS | SKRSRLAQKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YLVNPVVHLP | ILLVAVLLPF | YRHYSISEHA | TVYIKRLGRL | SYALLPLNLL | LNLRPNWLLR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NNYTYTDLIP | LHKWLSRCII | IIAVVHGILF | LINWALGESG | TLAKKIANPY | NLAGVLLFAP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LISMIFFSIG | PMRRFSYNAF | YVIHNLTGIS | FIFVVAFHAR | PSVTIPYLLI | NIAILLWQGF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AKFYYAKRTD | ILSKNTDYQN | TNLVNVQLPR | MALPDQFEPA | CHIRISPYSR | LHPLYWLYPS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HPFTVASLPS | DTVVDLIISE | SHHPKSFKLE | LGAPYSVINN | FDPAVPRSCL | EQAKRVAIVC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GGSGISFGLP | LYRYFKEIHP | VEYIQFIWLV | KDAYQLKILD | KLDTIGLLDG | SNDCHAFITR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SVDDPNSNQE | TAPDLEFELE | SMTQDVVDEN | GAFVSERDGS | PTSKFKFASI | NLGRRIDWAT |
| 490 | 500 | 510 | 520 | ||
| DLSQFVEPAL | VDNTWLLTCG | PSDLIESGRQ | YAADNSINFA | SEIYAL |