Q6FJ70
Gene name |
AKR1 (CAGL0M08712g) |
Protein name |
Palmitoyltransferase AKR1 |
Names |
Ankyrin repeat-containing protein AKR1 |
Species |
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
KEGG Pathway |
cgr:CAGL0M08712g |
EC number |
2.3.1.225: Transferring groups other than amino-acyl groups |
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 Q6FJ70
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6FJ70-F1 | Predicted | AlphaFoldDB |
No variants for Q6FJ70
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6FJ70 | |||||
No associated diseases with Q6FJ70
4 regional properties for Q6FJ70
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Palmitoyltransferase, DHHC domain | 450 - 581 | IPR001594 |
| repeat | Ankyrin repeat | 54 - 124 | IPR002110-1 |
| repeat | Ankyrin repeat | 126 - 158 | IPR002110-2 |
| repeat | Ankyrin repeat | 159 - 262 | IPR002110-3 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.225 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| early endosome membrane | The lipid bilayer surrounding an early endosome. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| G-protein beta/gamma-subunit complex binding | Binding to a complex of G-protein beta/gamma subunits. |
| protein-cysteine S-palmitoyltransferase activity | Catalysis of the transfer of a palmitoyl (systematic name, hexadecanoyl) group to a sulfur atom on the cysteine of a protein molecule, in the reaction hexadecanoyl-CoA + L-cysteinyl- |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion | Any process that decreases the frequency, rate or extent of pheromone-dependent signal transduction during conjugation with cellular fusion, a signal transduction process resulting in the relay, amplification or dampening of a signal generated in response to pheromone exposure in organisms that undergo conjugation with cellular fusion. |
| protein palmitoylation | The covalent attachment of a palmitoyl group to a protein. |
| protein targeting to membrane | The process of directing proteins towards a membrane, usually using signals contained within the protein. |
| regulation of endocytosis | Any process that modulates the frequency, rate or extent of endocytosis. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEDNSEQASV | SSQASMRPLV | SDNGDREAGA | GVEVNIANDN | DTSVGVDGEN | GNEDDDPILS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KYHNACQRGD | LEVVREMIHG | GQVNVSSDAD | REGVTGLHWA | AINNRLNVVD | FLVREGANVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SKAGALEATP | LHWAARYGFV | YVVDYLLQHG | ASATTTDKQG | FNLLHLSVNS | SNIMLVVYVL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FFVVSKGIID | IDYVDPKGRT | ALLWAAYQGD | SLTVAALIKF | NASVKIADEG | GFTPLHWGTV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KGQPHVLKYL | IQDGADFFQK | TNDNKDCFVI | AEEMSNTHSF | QEALRHNNFD | KNGYPINKLV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KRDDHAKIIT | FLIPLLVLGF | AFFGFSHLHI | LFALPVIILL | LLASNKFIKS | FLLPSYETKG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TNSASLLKSP | LIAGILFGSI | FWLAFVWILR | ILPYTFTKRP | LGNLTFCAIL | CFVCYSLFLL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AFSDPGHIGS | ENDHEKIRET | ISNLLKEGKF | DTRSFCLETW | VRKPLRSKYS | YLNDALILRF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DHYCPWIYND | VGLKNHKLFI | FFILALELGI | FSFVKVCLKY | FDELDMDGDC | FILGDDDLCS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GLIGDRFTFL | IMTWACIQAV | WIFSLVIVQL | FQITKGLTNS | ELNALIREGR | RVDIDSQTHN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EFFNTVPEGF | INNKDTEEEA | APPVRNNTNE | RISTTFSGNL | PKPRTCMGMI | CAVTGLHQCV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| AIIKDTFGIA | RHGSSRSTNT | RSLLSSISTD | YGWRRNWCDF | WLLSDTNTPL | WKRIFFSPPS |
| 730 | 740 | 750 | 760 | ||
| TKALLNGKEA | DYATLYEVPN | KNHGSVSQLQ | ELQDPLSEID | DMV |