Q2R0L0
Gene name |
LAC20 (Os11g0641800, LOC_Os11g42220, OsJ_033255) |
Protein name |
Laccase-20 |
Names |
Benzenediol:oxygen oxidoreductase 20, Diphenol oxidase 20, Urishiol oxidase 20 |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
osa:4351006 |
EC number |
1.10.3.2: 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
1 structures for Q2R0L0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2R0L0-F1 | Predicted | AlphaFoldDB |
No variants for Q2R0L0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2R0L0 | |||||
No associated diseases with Q2R0L0
8 regional properties for Q2R0L0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Multicopper oxidase, second cupredoxin domain | 157 - 285 | IPR001117 |
| binding_site | Multicopper oxidase, copper-binding site | 540 - 551 | IPR002355 |
| domain | Multicopper oxidase, C-terminal | 449 - 559 | IPR011706 |
| domain | Multicopper oxidase, N-terminal | 32 - 145 | IPR011707 |
| conserved_site | Multicopper oxidases, conserved site | 535 - 555 | IPR033138 |
| domain | Laccase, second cupredoxin domain | 158 - 307 | IPR034285 |
| domain | Laccase, first cupredoxin domain | 28 - 144 | IPR034288 |
| domain | Laccase, third cupredoxin domain | 415 - 560 | IPR034289 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.10.3.2 | With oxygen as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| apoplast | The cell membranes and intracellular regions in a plant are connected through plasmodesmata, and plants may be described as having two major compartments: the living symplast and the non-living apoplast. The apoplast is external to the plasma membrane and includes cell walls, intercellular spaces and the lumen of dead structures such as xylem vessels. Water and solutes pass freely through it. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| copper ion binding | Binding to a copper (Cu) ion. |
| hydroquinone:oxygen oxidoreductase activity | Catalysis of the reaction: 4 hydroquinone + O2 = 4 benzosemiquinone + 4 H2O. |
| 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 |
|---|---|
| lignin catabolic process | The chemical reactions and pathways resulting in the breakdown of lignins, a class of polymers of phenylpropanoid units. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q2R0L2 | LAC19 | Laccase-19 | Oryza sativa subsp japonica (Rice) | PR |
| Q5N7A3 | LAC6 | Laccase-6 | Oryza sativa subsp japonica (Rice) | PR |
| Q6ID18 | LAC10 | Laccase-10 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q8VZA1 | LAC11 | Laccase-11 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9FY79 | LAC14 | Laccase-14 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LFD1 | LAC9 | Laccase-9 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LFD2 | LAC8 | Laccase-8 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVASLLCTVA | VAVLAVAAVG | GEAGVVEHTF | VVHEMNVTHL | CNTTKIFVVN | GQLPGPTVDV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TEGDTVVIHV | VNKIPHGLTI | HWHGVRQLRS | CWADGAGFIT | ECPIPPGSER | TYRFNVTDQV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GTLWWHAHVT | CLRSTINGAF | IIRPRDGKYP | FPTPVKDVPI | IIGEWWELDL | VELDRRMRDG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NFDDNPLSAT | INGKLGDLSN | CSGIVEESFV | LNVKHGESYL | LRVINTAFFS | EYYFKVAGHT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FTVVGADGNY | LTPFKTDMVT | VAPGEAIDVL | MVADAPPAHY | HMIALANQPP | EPDPQIPKYI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SRGLVRYTGV | DANNNGLPVP | MPIMPNQHNT | MPSYYFHANL | TGLMHPKHRR | VPMHVDERIF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IILGLGTICR | GRNTTCKRQR | SLETIEVATM | NNVSFTHPNT | TALLERYYDG | TPEGVYTEDF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PVRPPRPYNY | TNPALIPPGP | LEEVLEPTFK | ATKLKRFKYN | TSVEIIFQSS | TLLMSDSNPM |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HLHGYDVFLL | AQGLGSFNAK | RDIRKFNYHN | PQLRNTILVP | RGGWAAVRFI | TDNPGMWYLH |
| 550 | 560 | 570 | |||
| CHFEFHIIMG | MATAFIVEDG | PTPETSLPPP | PPEFKRCDAS |