| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | Medtr7g116850.1 |
| Family | GH18 |
| Protein Properties | Length: 456 Molecular Weight: 50275.9 Isoelectric Point: 8.8656 |
| Chromosome | Chromosome/Scaffold: 7 Start: 38003779 End: 38006389 |
| Description | chitinase A |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH18 | 53 | 272 | 1e-27 |
| IVVYWGQNEREGSLTETCNTGLYEIVNIAFLSIFGSGRKPQLNLAGHCDPTSNNGCKSLSIDIKNCQKKGIKIILSIGGGVNGYSLSSNEDARNVGDYIL NNFLGGTSKSRPLGDVVLDGVDFDIEVGGGEVFYSELARRLSQHRGTKKVYLTAAPQCPFPDQHLKGALSTGLFDYVWVQFYNNGPCQIEASNLNKFQKS WNQWVSTIKVSKIYVGVPAS | |||
| Full Sequence |
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| Protein Sequence Length: 456 Download |
| MEAGGSNPNL SQQDKHQADN SIAMGNETRR LSNSIIFLLI FLTLVSSTNG GDIVVYWGQN 60 EREGSLTETC NTGLYEIVNI AFLSIFGSGR KPQLNLAGHC DPTSNNGCKS LSIDIKNCQK 120 KGIKIILSIG GGVNGYSLSS NEDARNVGDY ILNNFLGGTS KSRPLGDVVL DGVDFDIEVG 180 GGEVFYSELA RRLSQHRGTK KVYLTAAPQC PFPDQHLKGA LSTGLFDYVW VQFYNNGPCQ 240 IEASNLNKFQ KSWNQWVSTI KVSKIYVGVP ASPSAATASS GYVPTQVLIS KVLPFVKRSR 300 KYGGVMLWDR FADKQNGYSR DIKHAFKKSH HMLRILLITQ IIPKVNVQNT PTFEATAGWI 360 DVHAEFNGGK PQRLKVRYLD VTLRGLNDEL TEFNQGVNPR DARRVEYVRY KRPTLDEGRV 420 SFTLVELKND ENVTSMLGAQ HVPVDQYAGD GAEIN* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00704 | Glyco_hydro_18 | 2.0e-14 | 53 | 269 | 246 | + Glycosyl hydrolases family 18. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 5.0e-110 | 51 | 323 | 282 | + 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 - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2GSJ | 0 | 51 | 323 | 1 | 268 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| GenBank | ABF82271.1 | 0 | 28 | 323 | 2 | 295 | class III chitinase [Panax ginseng] |
| EMBL | CAO78600.1 | 0 | 56 | 323 | 1 | 263 | endochitinase and N-acetylglucosamine-binding hemagglutinin precursor [Parkia platycephala] |
| RefSeq | XP_002276387.1 | 0 | 30 | 323 | 4 | 295 | PREDICTED: similar to chitinase [Vitis vinifera] |
| RefSeq | XP_002320838.1 | 0 | 41 | 325 | 1 | 281 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2gsj_A | 0 | 51 | 323 | 1 | 268 | 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 | 51 | 322 | 1 | 269 | 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 | 51 | 322 | 1 | 269 | 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 | 51 | 322 | 1 | 269 | 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 | 51 | 322 | 1 | 269 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| JZ123100 | 276 | 50 | 323 | 0 |
| JK988873 | 277 | 49 | 323 | 0 |
| DW497436 | 273 | 51 | 322 | 0 |
| CD809335 | 273 | 51 | 322 | 0 |
| DY829451 | 273 | 53 | 325 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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