| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT3G54920.1 |
| Family | PL1 |
| Protein Properties | Length: 502 Molecular Weight: 53929 Isoelectric Point: 6.4481 |
| Chromosome | Chromosome/Scaffold: 3 Start: 20345082 End: 20348582 |
| Description | pectate lyase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL1 | 148 | 339 | 0 |
| WIVFSSNMLIRLKQELIINSYKTLDGRGSAVHITGNGCLTLQYVQHIIIHNLHIYDCKPSAGFEKRGRSDGDGISIFGSQKIWVDHCSMSHCTDGLIDAV MGSTAITISNNYFTHHDEVMLLGHDDNYAPDTGMQVTIAFNHFGQGLVQRMPRCRRGYIHVVNNDFTEWKMYAIGGSGNPTINSQGNRYSAP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 502 Download |
| MLLQNFSNTI FLLCLFFTLL SATKPLNLTL PHQHPSPDSV ALHVIRSVNE SLARRQLSSP 60 SSSSSSSSSS SSSSCRTGNP IDDCWRCSDA DWSTNRQRLA DCSIGFGHGT LGGKNGKIYV 120 VTDSSDNNPT NPTPGTLRYG VIQEEPLWIV FSSNMLIRLK QELIINSYKT LDGRGSAVHI 180 TGNGCLTLQY VQHIIIHNLH IYDCKPSAGF EKRGRSDGDG ISIFGSQKIW VDHCSMSHCT 240 DGLIDAVMGS TAITISNNYF THHDEVMLLG HDDNYAPDTG MQVTIAFNHF GQGLVQRMPR 300 CRRGYIHVVN NDFTEWKMYA IGGSGNPTIN SQGNRYSAPS DPSAKEVTKR VDSKDDGEWS 360 NWNWRTEGDL MENGAFFVAS GEGMSSMYSK ASSVDPKAAS LVDQLTRNAG VFGGPRDDQG 420 QSGNSYSPYG GDGGGGGSSG GSSGGGMDVM GGTTRGSSSS SGDDSNVFQM IFGSDAPSRP 480 RLTLLFSLLM ISVLSLSTLL L* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG3866 | PelB | 4.0e-26 | 109 | 334 | 238 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
| pfam00544 | Pec_lyase_C | 3.0e-64 | 160 | 336 | 201 | + 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-78 | 154 | 340 | 198 | + Amb_all domain. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0009814 | defense response, incompatible interaction |
| GO:0016829 | lyase activity |
| GO:0030570 | pectate lyase activity |
| GO:0031225 | anchored to membrane |
| GO:0042547 | cell wall modification involved in multidimensional cell growth |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAQ87025.1 | 0 | 1 | 501 | 1 | 499 | pectate lyase-like protein [Brassica napus] |
| EMBL | CAB41092.1 | 0 | 1 | 499 | 1 | 497 | pectate lyase-like protein [Arabidopsis thaliana] |
| RefSeq | NP_191052.2 | 0 | 1 | 491 | 1 | 491 | PMR6 (powdery mildew resistant 6); lyase/ pectate lyase [Arabidopsis thaliana] |
| RefSeq | XP_002268818.1 | 0 | 20 | 474 | 20 | 457 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316399.1 | 0 | 10 | 416 | 8 | 415 | 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 | 79 | 411 | 2 | 344 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1pxz_A | 0 | 79 | 411 | 2 | 344 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 3zsc_A | 6e-20 | 99 | 336 | 2 | 246 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1vbl_A | 0.00000000000002 | 163 | 313 | 128 | 301 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 3krg_A | 0.00000000000004 | 154 | 348 | 116 | 337 | A Chain A, Structural Insights Into Substrate Specificity And The Anti Beta-Elimination Mechanism Of Pectate Lyase |
