Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_074_00067.1 |
Family | PL1 |
Protein Properties | Length: 375 Molecular Weight: 41911.1 Isoelectric Point: 9.9198 |
Chromosome | Chromosome/Scaffold: 74 Start: 733358 End: 735536 |
Description | Pectate lyase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL1 | 158 | 351 | 0 |
IIFGRSMMIRLSEELIVTSNKTIDARGFNIHIAHGAGITVQFVDNVIIHGLHIHDIHAGNGGMIRDSVGHVGVRTASDGDGISIFGSTNIWVDHISMSNC KDGLVDIVQGSTAITVSNCHMTNHNEVMLFGASDSYSEDSIMQITVAFNHFGKGLVQRMPRCRWGFVHVVNNDYTHWQMYAIGGSMHPTIISQG |
Full Sequence |
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Protein Sequence Length: 375 Download |
MEAIMPKLLF VFFLAIMAQM VRANIGHFDE VWQQRAKEAR KNALKAYHPN PENVTEHLNN 60 HVRMALEGSN NTRRGLQGKM KNLPCRATNP IDRCWRCRKH WAADRKRLAS CVLGFGRKTT 120 GGKNGTYYMV TDSSDTDLVN PKPGTLRHAV IQPGPLWIIF GRSMMIRLSE ELIVTSNKTI 180 DARGFNIHIA HGAGITVQFV DNVIIHGLHI HDIHAGNGGM IRDSVGHVGV RTASDGDGIS 240 IFGSTNIWVD HISMSNCKDG LVDIVQGSTA ITVSNCHMTN HNEVMLFGAS DSYSEDSIMQ 300 ITVAFNHFGK GLVQRMPRCR WGFVHVVNND YTHWQMYAIG GSMHPTIISQ GKPLYRSSKS 360 FCQRDYKEGL RSRK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR04247 | NosD_copper_fam | 0.0001 | 183 | 308 | 140 | + nitrous oxide reductase family maturation protein NosD. Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase. | ||
pfam04431 | Pec_lyase_N | 8.0e-21 | 24 | 76 | 54 | + Pectate lyase, N terminus. This region is found N terminal to the pectate lyase domain (pfam00544) in some plant pectate lyase enzymes. | ||
COG3866 | PelB | 7.0e-31 | 119 | 343 | 241 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 2.0e-63 | 170 | 351 | 204 | + 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-73 | 164 | 351 | 199 | + Amb_all domain. |
Gene Ontology | |
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GO Term | Description |
GO:0030570 | pectate lyase activity |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAN79927.1 | 0 | 16 | 366 | 19 | 371 | hypothetical protein [Vitis vinifera] |
EMBL | CBI22159.1 | 0 | 16 | 366 | 48 | 400 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270089.1 | 0 | 15 | 351 | 18 | 352 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002330086.1 | 0 | 1 | 366 | 1 | 369 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520133.1 | 0 | 3 | 366 | 2 | 373 | Pectate lyase precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1pxz_B | 0 | 89 | 361 | 2 | 275 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 89 | 361 | 2 | 275 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 9e-20 | 146 | 345 | 38 | 227 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1vbl_A | 0.00000000000003 | 172 | 331 | 128 | 301 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
PDB | 3krg_A | 0.000000000002 | 174 | 331 | 125 | 295 | A Chain A, Structural Insights Into Substrate Specificity And The Anti Beta-Elimination Mechanism Of Pectate Lyase |