| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_020_00079.1 |
| Family | GH18 |
| Protein Properties | Length: 409 Molecular Weight: 43627.8 Isoelectric Point: 5.2961 |
| Chromosome | Chromosome/Scaffold: 20 Start: 664508 End: 667685 |
| 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 | 176 | 359 | 6.7e-24 |
| IAIYWGQNGNEGTLAETCNTGNYDFVNLAFLATFGNGQTPMINLAGHCDPYSNGCTSLSDDIKTCQSQGIKVILSIGGGAGSYSLASSDDARQVATYLWN NYLGGQSSSRPLGDAILDGVDFDIEGGTNQHWDDLARYLSGYSKKGKKVYLTAAPQCPFPDAWVGGALNTGLFDNVWVQFYNNP | |||
| Full Sequence |
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| Protein Sequence Length: 409 Download |
| MFQLILNTHG GGIAIYWGQN GNEGTLAETC NTGNYAYVNL AFLSTFGNGQ TPMINLAGHC 60 DPYSNGCTGL SKDIKTCQRK GVKVILSIGG AAGKKVYLTA APQCPFPDAW VGGALKTGLF 120 DNVWVQFYNN PPCHGFIPTG DLTSTILPAI KGSDKYGGVM LWSKYYDDQS GYSGGIAIYW 180 GQNGNEGTLA ETCNTGNYDF VNLAFLATFG NGQTPMINLA GHCDPYSNGC TSLSDDIKTC 240 QSQGIKVILS IGGGAGSYSL ASSDDARQVA TYLWNNYLGG QSSSRPLGDA ILDGVDFDIE 300 GGTNQHWDDL ARYLSGYSKK GKKVYLTAAP QCPFPDAWVG GALNTGLFDN VWVQFYNNPP 360 CHGFIPTSDL TSTILPAIKG SDKYGGVMLW SKYYDDQTGY SKAIKSDV* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00704 | Glyco_hydro_18 | 3.0e-14 | 11 | 101 | 93 | + Glycosyl hydrolases family 18. | ||
| pfam00704 | Glyco_hydro_18 | 2.0e-18 | 174 | 356 | 202 | + Glycosyl hydrolases family 18. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 1.0e-27 | 89 | 176 | 130 | + 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. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 2.0e-36 | 11 | 93 | 84 | + 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. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 1.0e-100 | 174 | 406 | 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 |
| EMBL | CBI40448.1 | 0 | 1 | 408 | 16 | 457 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002279147.1 | 6e-40 | 8 | 100 | 23 | 114 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002279147.1 | 3e-36 | 93 | 176 | 173 | 294 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002279147.1 | 0 | 173 | 408 | 25 | 298 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002530928.1 | 0 | 173 | 408 | 25 | 298 | hevamine-A 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 | 2hvm_A | 0 | 174 | 408 | 1 | 273 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 2hvm_A | 1e-31 | 11 | 205 | 1 | 182 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 2hvm_A | 5e-29 | 86 | 176 | 141 | 269 | 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 | 174 | 408 | 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 | 1e-31 | 11 | 205 | 1 | 182 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| JK988873 | 274 | 173 | 408 | 0 |
| FQ316915 | 250 | 188 | 399 | 0 |
| JK988873 | 91 | 11 | 101 | 1.99993e-41 |
| JK988873 | 129 | 86 | 176 | 2e-36 |
| FQ316915 | 117 | 93 | 171 | 4e-31 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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