| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT3G53190.1 |
| Family | PL1 |
| Protein Properties | Length: 484 Molecular Weight: 53593.5 Isoelectric Point: 6.4483 |
| Chromosome | Chromosome/Scaffold: 3 Start: 19713928 End: 19717595 |
| Description | pectate lyase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL1 | 143 | 341 | 0 |
| IVFPSNMMIKLKQELIFNSYKTLDGRGANVHIVGGGCITLQYVSNIIIHNIHIHHCYQSGNTNVRSSPTHYGFRTKSDGDGISIFGSKDIWIDHCSLSRC KDGLIDAVMGSTGITISNNFFSHHNEVMLLGHSDHYEPDSGMQVTIAFNHFGEKLIQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGNPTINSQGNRYTA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 484 Download |
| MMLQRSCIVL FFSLFLLVPQ MVFSMLNRTL LLIPHPDPEL VAYQVQWKVN ASITRRQALD 60 TTDQAGSTPC ITGNPIDDCW KCDPNWPNNR QGLADCGIGF GQYALGGKGG QFYFVTDSSD 120 DDAVNPKPGT LRYGVIQEEP LWIVFPSNMM IKLKQELIFN SYKTLDGRGA NVHIVGGGCI 180 TLQYVSNIII HNIHIHHCYQ SGNTNVRSSP THYGFRTKSD GDGISIFGSK DIWIDHCSLS 240 RCKDGLIDAV MGSTGITISN NFFSHHNEVM LLGHSDHYEP DSGMQVTIAF NHFGEKLIQR 300 MPRCRRGYIH VVNNDFTQWE MYAIGGSGNP TINSQGNRYT APTNPFAKEV TKRVETPDGD 360 WKGWNWRSEG DILVNGAFFV ASGEGAEMRY EKAYSVEPKS ASFITQITFH SGVLGVGGRN 420 NNLGMWTTTG SEGTSGLDSY NDYTDEMSGA GSTNRLSFSV LVFLLSSISY LVVFTSSTQM 480 FML* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG3866 | PelB | 6.0e-22 | 83 | 354 | 291 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
| pfam00544 | Pec_lyase_C | 3.0e-61 | 154 | 339 | 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-70 | 148 | 342 | 206 | + Amb_all domain. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008150 | biological_process |
| GO:0016829 | lyase activity |
| GO:0030570 | pectate lyase activity |
| GO:0031225 | anchored to membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAM61400.1 | 0 | 2 | 483 | 1 | 482 | pectate lyase-like protein [Arabidopsis thaliana] |
| EMBL | CAB64222.1 | 0 | 21 | 483 | 1 | 463 | pectate lyase-like protein [Arabidopsis thaliana] |
| RefSeq | NP_566979.1 | 0 | 1 | 483 | 1 | 483 | pectate lyase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002265853.1 | 0 | 2 | 431 | 115 | 540 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002519460.1 | 0 | 34 | 483 | 31 | 483 | 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 | 74 | 414 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1pxz_A | 0 | 74 | 414 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 3zsc_A | 7e-20 | 105 | 339 | 22 | 246 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1pe9_B | 0.0000000000001 | 152 | 412 | 78 | 357 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 1pe9_A | 0.0000000000001 | 152 | 412 | 78 | 357 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
