Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10030791 |
Family | PL1 |
Protein Properties | Length: 438 Molecular Weight: 48769.6 Isoelectric Point: 7.9268 |
Chromosome | Chromosome/Scaffold: 373 Start: 560064 End: 561765 |
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 | 152 | 355 | 0 |
KGPLWIIFARSMIIRLTQELMVSCDKTIDGRGANVHIANGGGITLQFVKNVIIHGLHIHDIVPKPGGMIRDAVDHYGLRTRSDGDGISLYGATNVWIDHV SMSNCADGIVDAIMESTGITISNCHITDHNEVMLFGASGSYSKDSVMQITLAFNHFGHGLVQRMPRCRWGFFHVVNNDYTHWLMYAMGGSNHPTIISQGN RFIA |
Full Sequence |
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Protein Sequence Length: 438 Download |
MDFRFTKLVF FIVLIVALVP YLEAHIAHFD EYWQQRADEA SRAAQETYHP EPFNVTEHFN 60 TLVDTHLFGS NDTRRSMMNH KGKCEATNPI DSCWRCDPNG EKTRQRLAAC VQGFGFKTTG 120 GKGGRIYVVT DASDCDMVNP KPGTLRHAVI QKGPLWIIFA RSMIIRLTQE LMVSCDKTID 180 GRGANVHIAN GGGITLQFVK NVIIHGLHIH DIVPKPGGMI RDAVDHYGLR TRSDGDGISL 240 YGATNVWIDH VSMSNCADGI VDAIMESTGI TISNCHITDH NEVMLFGASG SYSKDSVMQI 300 TLAFNHFGHG LVQRMPRCRW GFFHVVNNDY THWLMYAMGG SNHPTIISQG NRFIAPQNIA 360 AKEVTKREYA QPSEWKHWDW ISQGDLMMNG AFFVPSGNPQ VVNKITKQQR INEKAGTHVT 420 TLSRFSGALN CCAGKPC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00295 | Glyco_hydro_28 | 0.0007 | 152 | 277 | 137 | + Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism. | ||
pfam04431 | Pec_lyase_N | 3.0e-16 | 25 | 77 | 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 | 9.0e-26 | 170 | 353 | 196 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 7.0e-65 | 168 | 353 | 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 | 3.0e-75 | 163 | 356 | 205 | + 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 | 18 | 437 | 20 | 439 | hypothetical protein [Vitis vinifera] |
EMBL | CBI22159.1 | 0 | 18 | 437 | 49 | 468 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270089.1 | 0 | 18 | 437 | 20 | 443 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002311599.1 | 0 | 11 | 437 | 1 | 429 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520133.1 | 0 | 7 | 437 | 6 | 440 | 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 | 88 | 429 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 88 | 429 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 2e-19 | 118 | 344 | 21 | 227 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1vbl_A | 0.0000000000005 | 152 | 353 | 108 | 330 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
PDB | 1bn8_A | 0.000000000005 | 173 | 365 | 146 | 358 | A Chain A, Bacillus Subtilis Pectate Lyase |