Q6BW21
Gene name |
DEHA2B14960g |
Protein name |
Leucine aminopeptidase 2 |
Names |
Epoxide hydrolase, Leukotriene A-4 hydrolase homolog, LTA-4 hydrolase |
Species |
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) |
KEGG Pathway |
dha:DEHA2B14960g |
EC number |
3.3.2.10: Ether hydrolases |
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 Q6BW21
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6BW21-F1 | Predicted | AlphaFoldDB |
No variants for Q6BW21
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6BW21 | |||||
No associated diseases with Q6BW21
3 regional properties for Q6BW21
Functions
| Description | ||
|---|---|---|
| EC Number | 3.3.2.10 | Ether hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. |
| epoxide hydrolase activity | Catalysis of the reaction: an epoxide + H2O = a glycol. |
| metallopeptidase activity | Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| peptide catabolic process | The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTLEYINKKR | PSVSPELDPC | SNSNYKDFQV | SNTELDISVS | FDKKIVSGQV | TYKLTAKTPN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TTSIVLDTSY | LKIIKIRING | LPSDNYELVK | RKEPFGSPLK | ISLPTTINKE | FELNIEFSTT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DKCTALQFIE | KEATDGQTAP | YLFSQCQAIH | ARSLFPCFDT | PGIKSPYNMK | VKSPYACLMS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GRPKETNEEG | VYCFHQPIPI | PSYLVALASG | DLASAPIGPR | STVYSERVGL | SDCQWEFEKD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MENFIQVAEG | LIFKYEWLKF | DALILPSSFP | YGGMENPNIT | FATPTLISKD | RSQVKVMAHE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LAHSWSGNLV | TNCSWEHFWL | NEGWTVYLER | RIIGGIAAAE | AKSLGEKEAA | QYGEKRRHFS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AIVGWNSLVD | SVKTLDPKYT | SLVWNLKEGS | DPDDAFSRIP | YEKGFNFLFY | IEQQVGGIKE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FDPFIPYYFK | KFRYESLDTY | QFIDVLYEFF | EPRGKAAKLD | AIDWKGWIFG | EGLPPNIPQF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DPSLADECYR | LVDKWVDFAK | SNSTDISGFN | ESRDIGNFEP | DQHKLFLESL | TEKFGAYSVS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EQIIRKLPSI | YPFYAASTNG | EIKSSWNELL | IRFGNYNTTD | QIVQDFAMWL | GTVGRMKFVR |
| 610 | 620 | 630 | 640 | ||
| PGYKLLQAYV | SKEFAISTFT | KFESSYHPIC | KTMVKKDLSL | I |