Q69Q02
Gene name |
DPE2 (Os07g0662900, LOC_Os07g46790, P0453E03.120) |
Protein name |
4-alpha-glucanotransferase DPE2 |
Names |
Amylomaltase, Disproportionating enzyme, D-enzyme, Protein DISPROPORTIONATING ENZYME 2 |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
osa:4344192 |
EC number |
2.4.1.25: Hexosyltransferases |
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 Q69Q02
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q69Q02-F1 | Predicted | AlphaFoldDB |
No variants for Q69Q02
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q69Q02 | |||||
No associated diseases with Q69Q02
8 regional properties for Q69Q02
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | SH3 domain | 8 - 69 | IPR001452 |
| domain | Dedicator of cytokinesis protein 2, DHR2 domain | 1200 - 1620 | IPR026799 |
| domain | C2 DOCK-type domain | 419 - 615 | IPR027007 |
| domain | DOCKER domain | 1211 - 1622 | IPR027357 |
| domain | Dedicator of cytokinesis, N-terminal domain | 72 - 414 | IPR032376 |
| domain | DOCKER, Lobe A | 1205 - 1334 | IPR046769 |
| domain | DOCKER, Lobe B | 1395 - 1474 | IPR046770 |
| domain | DOCKER, Lobe C | 1516 - 1615 | IPR046773 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.25 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4-alpha-glucanotransferase activity | Catalysis of the transfer of a segment of a (1->4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1->4)-alpha-D-glucan. |
| beta-maltose 4-alpha-glucanotransferase activity | Catalysis of the reaction: beta-D-glucose + a plant soluble heteroglycan = a plant soluble heteroglycan + maltose. |
| heteropolysaccharide binding | Binding to a heteropolysaccharide, a glycan composed of more than one type of monosaccharide residue. |
| starch binding | Binding to starch. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| maltose catabolic process | The chemical reactions and pathways resulting in the breakdown of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTNLSGKKSL | NTVTLVFKLP | YYTQWGQSLL | IAGSEPALGS | WNVKQGLSLS | PVHQGNELIW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SGRVSVATGF | TCQYNYYVVD | DNKNVLRSES | GEKRKLVLPE | GVQDGDVVEI | RDWWQDASEA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LFLRSAFKNV | IFNGSENAKR | ELKTTSLNKS | LEPEDIVVQF | IVSCPRLGAG | STVVVTGSNP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QLGRWQTQDG | LKLNYVGDSI | WKANCLLRKS | EFPIKYKYCK | ISEAGVSSLE | FGPNREADVD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSSPKPSRYV | LLSDGALRES | PWRGAGVAVP | IFSIRSNEDL | GVGEFLDLKL | LVDWAVNSGF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HLVQLLPIND | TSVHGMWWDS | YPYSSLSVFA | LHPLYLRVQA | LSDAIPGDIK | DEISQAKKQL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DKKDVDYEAS | LASKLSIARK | IFKLEKDKVL | NSSSFKQFLS | ENEEWLKPYA | AFCFLRDFFE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TSDHSQWGRF | SQFSKEKLDK | LVSEGTLHHD | VICFHYYIQY | HLYMQLSEAA | AYARKKKVIL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KGDLPIGVDR | NSVDTWVYPT | LFRMNTATGA | PPDYFDKNGQ | NWGFPTYNWE | EMSKDNYGWW |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RARLTQMAKY | FTAYRIDHIL | GFFRIWELPD | HAATGLVGKF | RPSIALSQEE | LLSEGLWDFD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RMSRPYILQE | TLEEKFGSFW | TVIAANFLNE | YKKQHYEFKE | DCNTEKKIIA | KLKNSSEKSL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| WLEKEDSIRR | GLFDLLQNIV | LIRDPEDSTK | FYPRFNQEDT | SSFNDLDEHS | KNILRRLYYD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| YYFARQENLW | RQNALKTLPV | LLNSSDMLAC | GEDLGLIPAC | VHPVMQELGL | IGLRIQRMPS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EPNLEFGIPS | QYSYMTVCAP | SCHDCSTLRA | WWEEDGGRRS | RFYQTVIGSD | DEPPSRCTPE |
| 850 | 860 | 870 | 880 | 890 | 900 |
| VANFIVKQHF | DAPSMWAIFP | LQDLLALKDK | YTTRPAKEET | INDPTNPKHY | WRFRLHVTLD |
| 910 | 920 | 930 | 940 | ||
| SLLDDKDIQA | TIKELVTSSG | RSFPGKVDGA | EESGEKLAKV | QLNGKP |