| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma19g07490.1 |
| Family | PL1 |
| Protein Properties | Length: 405 Molecular Weight: 44632.1 Isoelectric Point: 7.2478 |
| Chromosome | Chromosome/Scaffold: 19 Start: 8859652 End: 8863031 |
| Description | Pectin lyase-like superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL1 | 125 | 323 | 0 |
| IIFKRDMVITLKEELLVNSFKTIDGRGASVHIANGGCITIHYVSNIIIHGIHIHDCKPTGNTNIRDSPHHSGFWTQSDGDGVSIFNSKHIWVDHCSLSNC RDGLIDAIHGSTAITISNNYMTHHDKVMLLGHSDSYTQDKDMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRFLA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 405 Download |
| MAPLSCIIVL FALSLLTPCF VSSSAVRDPE LVVQEVQRSI NASRRNLGYL SCGTGNPIDD 60 CWRCESNWEN NRQRLADCAI GFGKDAIGGK NGRIYVVTDS GDDDAVNPRP GTLRYAAIQD 120 EPLWIIFKRD MVITLKEELL VNSFKTIDGR GASVHIANGG CITIHYVSNI IIHGIHIHDC 180 KPTGNTNIRD SPHHSGFWTQ SDGDGVSIFN SKHIWVDHCS LSNCRDGLID AIHGSTAITI 240 SNNYMTHHDK VMLLGHSDSY TQDKDMQVTI AFNHFGEGLV QRMPRCRHGY FHVVNNDYTH 300 WEMYAIGGSA NPTINSQGNR FLAPNIRFSK EVTKHEDAPQ SEWMGWNWRS EGDMFLNGAY 360 FRQSGAGASS SYARASSLSA RPSSLVGSMT TTAGALTCRK GNRC* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG3866 | PelB | 2.0e-29 | 81 | 321 | 260 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
| pfam00544 | Pec_lyase_C | 4.0e-77 | 136 | 321 | 208 | + Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. | ||
| smart00656 | Amb_all | 1.0e-82 | 130 | 325 | 207 | + Amb_all domain. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAF63756.1 | 0 | 22 | 404 | 16 | 398 | AF243475_1 pectate lyase [Vitis vinifera] |
| EMBL | CBI14899.1 | 0 | 18 | 404 | 17 | 403 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002275781.1 | 0 | 18 | 404 | 72 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002300069.1 | 0 | 7 | 404 | 6 | 403 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526952.1 | 0 | 7 | 404 | 7 | 396 | Pectate lyase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1pxz_B | 0 | 56 | 397 | 2 | 346 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1pxz_A | 0 | 56 | 397 | 2 | 346 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 3zsc_A | 5e-20 | 125 | 323 | 50 | 248 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1pe9_B | 9e-17 | 136 | 395 | 80 | 358 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1pe9_A | 9e-17 | 136 | 395 | 80 | 358 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
