| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_035_00024.1 |
| Family | PL1 |
| Protein Properties | Length: 387 Molecular Weight: 43327.5 Isoelectric Point: 11.6463 |
| Chromosome | Chromosome/Scaffold: 35 Start: 142613 End: 144082 |
| Description | Pectin lyase-like superfamily protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| PL1 | 110 | 309 | 0 |
| WITFQRDMHIKLQRKLMVSSFTTIDGRGANIHIADGAGFLLNQVHNVIIHGLHFHHLRSLAPGSVIAPGSTVAQIQQTDGDAIRLVGASKVWIDHNTLNG GQDGLLDVTVGSTDITISNNWFKDHDKVMLLGHDDGFVQDRNMRVTIVFNRFGPNCNQRMPRIRHGYAHIANNFYQGWGDYAIGGTMNPTVRSEANLFIA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 387 Download |
| MARSSLNRIL LHIIVLSVFL FVLAPPSLAR RPRRRTTNFN TIDRCWRRNR NCSINRQQLA 60 TCSVGFAGKM TNNIGKGLTH YTVTDPSDDP MNPRFGTLRY GATKIGGKVW ITFQRDMHIK 120 LQRKLMVSSF TTIDGRGANI HIADGAGFLL NQVHNVIIHG LHFHHLRSLA PGSVIAPGST 180 VAQIQQTDGD AIRLVGASKV WIDHNTLNGG QDGLLDVTVG STDITISNNW FKDHDKVMLL 240 GHDDGFVQDR NMRVTIVFNR FGPNCNQRMP RIRHGYAHIA NNFYQGWGDY AIGGTMNPTV 300 RSEANLFIAP KTGNKEVTWK PGNSRLGNWR SVHDMFLNGA HFSQTGKGIA RPHYNRQQRF 360 RVARARDVRL LTRSAGALRC SNRSRC* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG3866 | PelB | 2.0e-29 | 123 | 307 | 197 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
| pfam00544 | Pec_lyase_C | 8.0e-54 | 129 | 307 | 187 | + 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 | 3.0e-64 | 116 | 311 | 207 | + Amb_all domain. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI26401.1 | 0 | 70 | 386 | 1 | 320 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002267384.1 | 0 | 17 | 386 | 5 | 369 | PREDICTED: similar to putative Cup s 1 pollen allergen [Vitis vinifera] |
| RefSeq | XP_002299118.1 | 0 | 39 | 386 | 1 | 354 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002304865.1 | 0 | 39 | 386 | 1 | 352 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002458626.1 | 0 | 40 | 386 | 25 | 373 | hypothetical protein SORBIDRAFT_03g036930 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1pxz_B | 0 | 40 | 378 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1pxz_A | 0 | 40 | 378 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
| PDB | 1vbl_A | 1e-20 | 125 | 285 | 128 | 302 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 3zsc_A | 2e-17 | 103 | 309 | 42 | 248 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 3vmw_A | 3e-16 | 144 | 379 | 93 | 317 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
