Q12284
Gene name |
ERV2 (YPR037C, YP3085.03C) |
Protein name |
FAD-linked sulfhydryl oxidase ERV2 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YPR037C |
EC number |
1.8.3.2: With oxygen as acceptor |
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
3 structures for Q12284
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1JR8 | X-ray | 150 A | A/B | 71-187 | PDB |
| 1JRA | X-ray | 200 A | A/B/C/D | 71-187 | PDB |
| AF-Q12284-F1 | Predicted | AlphaFoldDB |
1 variants for Q12284
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s16-646987 | 17 | L>I | No | SGRP |
No associated diseases with Q12284
6 regional properties for Q12284
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site | 229 - 238 | IPR002464 |
| domain | Helicase-like, DEXD box c2 type | 8 - 280 | IPR006554 |
| domain | ATP-dependent helicase, C-terminal | 524 - 699 | IPR006555 |
| domain | RAD3-like helicase, DEAD | 72 - 256 | IPR010614 |
| domain | Helical and beta-bridge domain | 272 - 413 | IPR010643 |
| domain | Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type | 7 - 283 | IPR014013 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.8.3.2 | With oxygen as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| fungal-type vacuole | A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure. |
| fungal-type vacuole membrane | The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae. |
| integral component of endoplasmic reticulum membrane | The component of the endoplasmic reticulum 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. |
| 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 |
|---|---|
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| flavin-linked sulfhydryl oxidase activity | Catalysis of the formation of disulfide bridges in proteins using FAD as the electron acceptor. |
| thiol oxidase activity | Catalysis of the reaction: 4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O2. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKQIVKRSHA | IRIVAALGII | GLWMFFSSNE | LSIATPGLIK | AKSGIDEVQG | AAAEKNDARL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KEIEKQTIMP | LMGDDKVKKE | VGRASWKYFH | TLLARFPDEP | TPEEREKLHT | FIGLYAELYP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CGECSYHFVK | LIEKYPVQTS | SRTAAAMWGC | HIHNKVNEYL | KKDIYDCATI | LEDYDCGCSD |
| 190 | |||||
| SDGKRVSLEK | EAKQHG |