| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT4G13710.1 |
| Family | PL1 |
| Protein Properties | Length: 471 Molecular Weight: 51935.9 Isoelectric Point: 8.2354 |
| Chromosome | Chromosome/Scaffold: 4 Start: 7962432 End: 7966461 |
| Description | pectate lyase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL1 | 184 | 389 | 0 |
| IQEEPLWIVFKRDMVIELKQELIMNSFKTIDARGSNVHIANGACITIQFITNVIIHGLHIHDCKPTGNAMVRSSPSHFGWRTMADGDAVSIFGSSHIWID HNSLSHCADGLVDAVMGSTAITVSNNHFTHHNEVMLLGHSDSYTKDKLMQVTIAYNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAEPTINSQ GNRYAA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 471 Download |
| MASSSQKLIS VCVAVLVVLA LTAMIFRNSE ISLSRKLKTE VIQSSNSSTM AAIRKLKTEE 60 FQSLNSSTMA ATRLDGEPQQ QQHAVADDPD MVADEVAKLV QMSEQNRTAR RKLGFFSCGT 120 GNPIDDCWRC DRNWHKNRKR LADCGIGFGR NAIGGRDGRF YIVTDPTDED VVNPKPGTLR 180 HAVIQEEPLW IVFKRDMVIE LKQELIMNSF KTIDARGSNV HIANGACITI QFITNVIIHG 240 LHIHDCKPTG NAMVRSSPSH FGWRTMADGD AVSIFGSSHI WIDHNSLSHC ADGLVDAVMG 300 STAITVSNNH FTHHNEVMLL GHSDSYTKDK LMQVTIAYNH FGEGLVQRMP RCRHGYFHVV 360 NNDYTHWEMY AIGGSAEPTI NSQGNRYAAP MDRFAKEVTK RVETDASEWK KWNWRSEGDL 420 LLNGAFFRPS GAGASASYGR ASSLAAKPSS MVDTITSTAG ALGCRKGRPC * 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG3866 | PelB | 1.0e-27 | 209 | 385 | 191 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
| pfam00544 | Pec_lyase_C | 1.0e-71 | 202 | 387 | 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-81 | 196 | 390 | 206 | + Amb_all domain. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008150 | biological_process |
| GO:0012505 | endomembrane system |
| GO:0016829 | lyase activity |
| GO:0030570 | pectate lyase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ADD62392.1 | 0 | 54 | 470 | 34 | 445 | pectase lyase [Prunus persica] |
| DDBJ | BAF43573.1 | 0 | 54 | 470 | 14 | 425 | pectate lyase [Prunus persica] |
| EMBL | CAB36835.1 | 0 | 103 | 470 | 7 | 374 | putative pectate lyase A11 (fragment) [Arabidopsis thaliana] |
| RefSeq | NP_567409.1 | 0 | 1 | 470 | 1 | 470 | pectate lyase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002297822.1 | 0 | 45 | 470 | 29 | 450 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1pxz_B | 0 | 122 | 462 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1pxz_A | 0 | 122 | 462 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 3zsc_A | 2e-16 | 191 | 378 | 50 | 227 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1vbl_A | 0.00000000000007 | 270 | 392 | 190 | 335 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 1pcl_A | 0.000000000004 | 202 | 387 | 73 | 276 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
