| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_017_00127.1 |
| Family | GH28 |
| Protein Properties | Length: 464 Molecular Weight: 48678 Isoelectric Point: 5.4091 |
| Chromosome | Chromosome/Scaffold: 17 Start: 826441 End: 828191 |
| Description | Pectin lyase-like superfamily protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH28 | 76 | 408 | 0 |
| ACSYAAGQSTFLVPKGDFLVGPVTFKGPCQKTPKVEIKGTLKAPTDLKAFNDLPTWLEFKDLSDLNITGCGTGVIDGQGESSYTHTGCQNSGGKCKNFPI NLRLTKVECGSVSELTLLNSKGFHMNLCFSNNINIHDMTITAPGNSPNTDGIHLSDSAHIDITSSKIAVGDDCISIGQGSSDIFVEKIHCGPGHGISIGS LGKYPNERDVQGVHVKNCTIEGTDNGVRVKTWPGSPPSKAFNFTFEDIIVNNVKNPIIIDQEYCPGHKCGSKGPSQVKISDIVFKKIRGTGSTNSPVKLV CSSAGCQNVVLNDINIKHVSDSPISSTCTNVKG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 464 Download |
| MALSQSYVLI CLTGSLIFLW SFPSLDATRI PVSAHAPAPS QSPGVSCGVF DVTKYGAVSD 60 GKTESCKAFE AAWADACSYA AGQSTFLVPK GDFLVGPVTF KGPCQKTPKV EIKGTLKAPT 120 DLKAFNDLPT WLEFKDLSDL NITGCGTGVI DGQGESSYTH TGCQNSGGKC KNFPINLRLT 180 KVECGSVSEL TLLNSKGFHM NLCFSNNINI HDMTITAPGN SPNTDGIHLS DSAHIDITSS 240 KIAVGDDCIS IGQGSSDIFV EKIHCGPGHG ISIGSLGKYP NERDVQGVHV KNCTIEGTDN 300 GVRVKTWPGS PPSKAFNFTF EDIIVNNVKN PIIIDQEYCP GHKCGSKGPS QVKISDIVFK 360 KIRGTGSTNS PVKLVCSSAG CQNVVLNDIN IKHVSDSPIS STCTNVKGLN VIAMLSPKPC 420 SSAEATAPAG PVSEEAPVSE EAPVSEEAPV SEEAPESEDP PIV* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| PLN02793 | PLN02793 | 4.0e-71 | 8 | 426 | 423 | + Probable polygalacturonase |
| PLN02155 | PLN02155 | 2.0e-71 | 49 | 420 | 375 | + polygalacturonase |
| PLN02218 | PLN02218 | 2.0e-73 | 52 | 405 | 356 | + polygalacturonase ADPG |
| pfam00295 | Glyco_hydro_28 | 4.0e-85 | 84 | 407 | 328 | + Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism. |
| PLN02188 | PLN02188 | 3.0e-114 | 32 | 420 | 392 | + polygalacturonase/glycoside hydrolase family protein |
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004650 | polygalacturonase activity |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN69218.1 | 0 | 33 | 399 | 474 | 841 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN69218.1 | 0 | 49 | 407 | 55 | 414 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI22963.1 | 0 | 33 | 399 | 16 | 383 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270999.1 | 0 | 33 | 399 | 55 | 422 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002282573.1 | 0 | 49 | 421 | 27 | 395 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bhe_A | 2e-17 | 93 | 407 | 52 | 360 | A Chain A, Polygalacturonase From Erwinia Carotovora Ssp. Carotovora |
| PDB | 2iq7_G | 3e-17 | 138 | 406 | 68 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 2iq7_F | 3e-17 | 138 | 406 | 68 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 2iq7_E | 3e-17 | 138 | 406 | 68 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 2iq7_D | 3e-17 | 138 | 406 | 68 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
