| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT1G04680.1 |
| Family | PL1 |
| Protein Properties | Length: 432 Molecular Weight: 47770.8 Isoelectric Point: 7.9652 |
| Chromosome | Chromosome/Scaffold: 1 Start: 1303529 End: 1307884 |
| Description | pectate lyase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL1 | 143 | 348 | 0 |
| IQDRPLWIVFKRDMVIQLKQELIVNSFKTIDGRGANVHIANGGCITIQFVTNVIVHGLHIHDCKPTGNAMVRSSETHFGWRTMADGDAISIFGSSHVWID HNSLSHCADGLVDAVMGSTAITISNNHLTHHNEVMLLGHSDSYMRDKAMQVTIAYNHFGVGLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQ GNRYAA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 432 Download |
| MAVLPTWLLA MMCLLFFVGA MENTTHDNIS SLPRSDETEW NQHAVTNPDE VADEVLALTE 60 MSVRNHTERR KLGYFTCGTG NPIDDCWRCD PNWHKNRKRL ADCGIGFGRN AIGGRDGRFY 120 VVTDPRDDNP VNPRPGTLRH AVIQDRPLWI VFKRDMVIQL KQELIVNSFK TIDGRGANVH 180 IANGGCITIQ FVTNVIVHGL HIHDCKPTGN AMVRSSETHF GWRTMADGDA ISIFGSSHVW 240 IDHNSLSHCA DGLVDAVMGS TAITISNNHL THHNEVMLLG HSDSYMRDKA MQVTIAYNHF 300 GVGLIQRMPR CRHGYFHVVN NDYTHWEMYA IGGSANPTIN SQGNRYAAPK NPFAKEVTKR 360 VDTPASHWKG WNWRSEGDLL QNGAYFTSSG AAASGSYARA SSLSAKSSSL VGHITSDAGA 420 LPCRRGRQCS S* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG3866 | PelB | 5.0e-27 | 161 | 344 | 196 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
| pfam00544 | Pec_lyase_C | 1.0e-70 | 161 | 346 | 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-80 | 155 | 350 | 207 | + Amb_all domain. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008150 | biological_process |
| GO:0016020 | membrane |
| 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 | AAK66161.1 | 0 | 62 | 429 | 1 | 368 | pectate lyase [Fragaria x ananassa] |
| DDBJ | BAF43573.1 | 0 | 21 | 429 | 21 | 425 | pectate lyase [Prunus persica] |
| RefSeq | NP_563715.1 | 0 | 22 | 431 | 22 | 431 | pectate lyase family protein [Arabidopsis thaliana] |
| RefSeq | NP_567409.1 | 0 | 37 | 429 | 77 | 470 | pectate lyase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002297822.1 | 0 | 1 | 429 | 1 | 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 | 81 | 421 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1pxz_A | 0 | 81 | 421 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 3zsc_A | 1e-16 | 150 | 346 | 50 | 246 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1vbl_A | 0.000000000000001 | 159 | 347 | 119 | 331 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 1pcl_A | 0.000000000006 | 159 | 346 | 71 | 276 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
