y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.L03478.1 |
Family | GH18 |
Protein Properties | Length: 263 Molecular Weight: 27982.4 Isoelectric Point: 5.1317 |
Chromosome | Chromosome/Scaffold: 3325 Start: 1689 End: 2588 |
Description | chitinase A |
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 |
GH18 | 31 | 213 | 5.9e-25 |
IAIYWGQNGNEGTLTSTCATGKYAYVNLAFLYKFGGGQTPQIDLAGHCTSGGCTSISNDIRSCQNQGIKVMLSLGGGAGNYSLVSQADARNVADYLWNNF LGGTSSSRPLGDAVLDGIDFDIELGSPNYWDDLARYLSDYSKQGKKVYLTAAPQCPYPDSYLGAALNTGLFDYVWVQFYNNLP |
Full Sequence |
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Protein Sequence Length: 263 Download |
MPSPPPSTPS LSLLLLLFTS SLIGVSHGGG IAIYWGQNGN EGTLTSTCAT GKYAYVNLAF 60 LYKFGGGQTP QIDLAGHCTS GGCTSISNDI RSCQNQGIKV MLSLGGGAGN YSLVSQADAR 120 NVADYLWNNF LGGTSSSRPL GDAVLDGIDF DIELGSPNYW DDLARYLSDY SKQGKKVYLT 180 AAPQCPYPDS YLGAALNTGL FDYVWVQFYN NLPSGSGYVP PNVLTSQILP VIKMSAKYGG 240 VMLWSKYYDD KNGYSDSIKS SV* 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG3469 | COG3469 | 1.0e-5 | 89 | 239 | 164 | + Chitinase [Carbohydrate transport and metabolism] | ||
cd02871 | GH18_chitinase_D-like | 7.0e-8 | 35 | 211 | 196 | + GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus. | ||
cd00598 | GH18_chitinase-like | 9.0e-9 | 31 | 245 | 237 | + The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model. | ||
pfam00704 | Glyco_hydro_18 | 2.0e-26 | 29 | 209 | 201 | + Glycosyl hydrolases family 18. | ||
cd02877 | GH18_hevamine_XipI_class_III | 1.0e-113 | 29 | 260 | 280 | + This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1HVQ | 0 | 29 | 262 | 1 | 273 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
EMBL | CAA09110.1 | 0 | 28 | 262 | 26 | 299 | chitinase [Hevea brasiliensis] |
EMBL | CBI22573.1 | 0 | 1 | 262 | 1 | 260 | unnamed protein product [Vitis vinifera] |
EMBL | CBI22574.1 | 0 | 1 | 251 | 15 | 263 | unnamed protein product [Vitis vinifera] |
Swiss-Prot | P23472 | 0 | 28 | 262 | 26 | 299 | CHLY_HEVBR RecName: Full=Hevamine-A; Includes: RecName: Full=Chitinase; Includes: RecName: Full=Lysozyme; Flags: Precursor |
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 | 2hvm_A | 0 | 29 | 262 | 1 | 273 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1llo_A | 0 | 29 | 262 | 1 | 273 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1hvq_A | 0 | 29 | 262 | 1 | 273 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
PDB | 1kr0_A | 0 | 29 | 262 | 1 | 273 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
PDB | 1kr1_A | 0 | 29 | 262 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |