| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna18987.1-v1.0-hybrid |
| Family | GH18 |
| Protein Properties | Length: 301 Molecular Weight: 32382.4 Isoelectric Point: 8.0248 |
| Chromosome | Chromosome/Scaffold: 7 Start: 2411682 End: 2412587 |
| Description | chitinase A |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH18 | 31 | 256 | 1.6e-30 |
| SIVVYWGQNEGEGSLTAACDSGRYRIVNIAFLSQYGNGQTPQINLAGHCDPRSRGCVNLSTDIKHCQSKGIKVLLSIGGADGNYGLSSDADAGKVADYIW NNFLGGQSSSRPLGDAVLDGVDFDIEKGGSHYDTLARKLSQYSQRGKKVYLGAAPQCPFPDQFVNGALSTGLFDYVWVQFYNNPQCEFTTSNPNAFRNSW NKWTSSIQAGQFFVGLPASKAAAGDG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 301 Download |
| MAAMSTKSCS QALTVLLVIL HVFVSNSYAG SIVVYWGQNE GEGSLTAACD SGRYRIVNIA 60 FLSQYGNGQT PQINLAGHCD PRSRGCVNLS TDIKHCQSKG IKVLLSIGGA DGNYGLSSDA 120 DAGKVADYIW NNFLGGQSSS RPLGDAVLDG VDFDIEKGGS HYDTLARKLS QYSQRGKKVY 180 LGAAPQCPFP DQFVNGALST GLFDYVWVQF YNNPQCEFTT SNPNAFRNSW NKWTSSIQAG 240 QFFVGLPASK AAAGDGYVST GDLINQVLPF VKKSAKYGGI MLYDRFEDIK TGYSSKVIGS 300 V 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06542 | GH18_EndoS-like | 1.0e-6 | 88 | 284 | 211 | + Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B. | ||
| COG3469 | COG3469 | 2.0e-8 | 54 | 281 | 262 | + Chitinase [Carbohydrate transport and metabolism] | ||
| cd02871 | GH18_chitinase_D-like | 6.0e-15 | 54 | 267 | 255 | + 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. | ||
| pfam00704 | Glyco_hydro_18 | 7.0e-30 | 30 | 297 | 292 | + Glycosyl hydrolases family 18. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 2.0e-135 | 30 | 299 | 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 | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2gsj_A | 0 | 30 | 301 | 1 | 271 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| PDB | 2hvm_A | 0 | 30 | 301 | 1 | 273 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| PDB | 1llo_A | 0 | 30 | 301 | 1 | 273 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| PDB | 1hvq_A | 0 | 30 | 301 | 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 | 30 | 301 | 1 | 273 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
