| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT3G24230.1 |
| Family | PL1 |
| Protein Properties | Length: 453 Molecular Weight: 49985.4 Isoelectric Point: 8.4361 |
| Chromosome | Chromosome/Scaffold: 3 Start: 8774616 End: 8777407 |
| Description | pectate lyase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL1 | 165 | 371 | 0 |
| VIQVEPLWIIFKRDMVIKLKQELIMNSFKTIDARGANVHIANGACITIQNITNVIVHGLHIHDCKRTGNVTVRSSPSQAGFRGTADGDAINIFGSSHIWI DHNSLSNCTDGLVDVVNGSTAITISNNHFTHHDEVMLLGHNDSYTRDKMMQVTVAYNHFGEGLIQRMPRCRHGYFHVVNNDYTHWKMYAIGGSANPTINS QGNRFAA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 453 Download |
| MATSSLKLTS ACFVLLFIFV GCVLTATNLR NNEISRSRKL KTEDSKSFNS SPMTTRLDGV 60 VELNEHAVTD PDKVAHEVSN LIHMSEQNIT ARRKLGFFSC GNGNLIDDCW RCDRNWNKNR 120 KHLADCGMGF GSKAFGGRNG SYYVVTDHSD DDVVNPKPGT LRHAVIQVEP LWIIFKRDMV 180 IKLKQELIMN SFKTIDARGA NVHIANGACI TIQNITNVIV HGLHIHDCKR TGNVTVRSSP 240 SQAGFRGTAD GDAINIFGSS HIWIDHNSLS NCTDGLVDVV NGSTAITISN NHFTHHDEVM 300 LLGHNDSYTR DKMMQVTVAY NHFGEGLIQR MPRCRHGYFH VVNNDYTHWK MYAIGGSANP 360 TINSQGNRFA APKNHSAKEV TKRLDTKGNE WMEWNWRSEK DLLVNGAFFT PSGEGASGDS 420 QTLSLPAKPA SMVDAITASA GALSCRRGKP CY* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG3866 | PelB | 2.0e-27 | 191 | 369 | 191 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
| pfam00544 | Pec_lyase_C | 5.0e-72 | 184 | 369 | 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 | 2.0e-79 | 178 | 373 | 207 | + 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 | 33 | 451 | 29 | 445 | pectase lyase [Prunus persica] |
| DDBJ | BAF43573.1 | 0 | 33 | 451 | 9 | 425 | pectate lyase [Prunus persica] |
| EMBL | CAB36835.1 | 0 | 82 | 451 | 4 | 374 | putative pectate lyase A11 (fragment) [Arabidopsis thaliana] |
| RefSeq | NP_189065.2 | 0 | 1 | 452 | 1 | 452 | pectate lyase family protein [Arabidopsis thaliana] |
| RefSeq | NP_567409.1 | 0 | 1 | 451 | 1 | 470 | pectate lyase family protein [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1pxz_B | 0 | 104 | 414 | 2 | 314 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1pxz_A | 0 | 104 | 414 | 2 | 314 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 3zsc_A | 8e-20 | 173 | 369 | 50 | 246 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1vbl_A | 2e-16 | 207 | 370 | 147 | 331 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 1pcl_A | 0.0000000000001 | 182 | 410 | 71 | 315 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
