C5M5S1
Gene name |
AIM14 (CTRG_01201) |
Protein name |
Probable metalloreductase AIM14 |
Names |
|
Species |
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast) |
KEGG Pathway |
ctp:CTRG_01201 |
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 C5M5S1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C5M5S1-F1 | Predicted | AlphaFoldDB |
No variants for C5M5S1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C5M5S1 | |||||
No associated diseases with C5M5S1
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 |
| MNTISPVVIE | PRHGGEHHSV | NVKYGIIIFA | ISVIHILFFL | LVKFIEINRW | KSNGRFNKSL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WKLNNTPTWM | LITLWILIIF | FIGGANITEF | SEEYITIAKR | YGRIAYCLLP | LNIYLILRPT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NCVYLKPGYY | LENLSLHKWL | SRLISICTLI | HAIGYFYKWN | KEGKILIKSF | RFLNFLGIVV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FVMFAVLIIV | SIRILRRKYY | SLFYIIHNIT | AWSMVVLIIF | HARPGVTIFG | IICLILMCYQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LLYLRFYKSY | PVNNLKIVDI | PMSTLQIIKI | PKPSNFPTWL | PGSHVRLNYT | TSNIKSWINS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SHPFTIANIP | EDGVNYLSLV | IKKPGNFIID | QYLTYLLTGP | YISIDYPFYN | SANLINIICG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GSGISFGLPI | LNHYKSLNSN | IPIKLIWCVR | NRNDCFIMNQ | LDMTNVEVFI | TSAGDSSSDE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QSPSSSSYQP | VPLFVVDDEQ | DESHAKVEQT | QGEEEVDGLL | NQDENGIPLQ | SMKKESFPKK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EEGEDEEKSS | KDVFKYGRPK | FDEVFAIDDP | TLNPNYNDSW | VIACGPDQLI | EDAKYWSQEK |
| 550 | |||||
| GYRFFSEKYE | M |