y
Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa015812m |
Family | GH18 |
Protein Properties | Length: 299 Molecular Weight: 32425.9 Isoelectric Point: 10.0125 |
Chromosome | Chromosome/Scaffold: 2 Start: 18865327 End: 18866523 |
Description | chitinase A |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH18 | 30 | 249 | 1.2e-28 |
IVVYWGQNGGEGTLTETCNTGRYQIVNIGFLSKFGRGQAPEINLAGHCNPKSNGCHRASIGIKNCQRKGIKVLLSIGGGFGSYGLSSENDAKNVANYIWN NFLGGRSNSRPLGDAILDGVDFDIEKGGPHYVTLARMLAAHSTRGRKVYLSAAPQCPFPDQHLNAALSTGLFDYVWVQFYNNPQCEFSSRNANAFKRSWN RWSSSIRAKIFVGLPASRAV |
Full Sequence |
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Protein Sequence Length: 299 Download |
MAPSQFCSQA AIVFLLVLPS LVSKSDAGSI VVYWGQNGGE GTLTETCNTG RYQIVNIGFL 60 SKFGRGQAPE INLAGHCNPK SNGCHRASIG IKNCQRKGIK VLLSIGGGFG SYGLSSENDA 120 KNVANYIWNN FLGGRSNSRP LGDAILDGVD FDIEKGGPHY VTLARMLAAH STRGRKVYLS 180 AAPQCPFPDQ HLNAALSTGL FDYVWVQFYN NPQCEFSSRN ANAFKRSWNR WSSSIRAKIF 240 VGLPASRAVV VSGFVPANDL INEVLPFVKR SPKYGGVMLY NKFNDDKSGY SPKIRGRV* 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06542 | GH18_EndoS-like | 2.0e-5 | 95 | 291 | 219 | + 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. | ||
cd02871 | GH18_chitinase_D-like | 1.0e-6 | 30 | 264 | 278 | + 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 | 2.0e-10 | 30 | 210 | 197 | + 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 | 7.0e-29 | 28 | 246 | 248 | + Glycosyl hydrolases family 18. | ||
cd02877 | GH18_hevamine_XipI_class_III | 2.0e-130 | 28 | 296 | 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 | 2GSJ | 0 | 28 | 298 | 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 |
GenBank | ACH54087.1 | 0 | 12 | 287 | 10 | 286 | class III chitinase [Vitis vinifera] |
DDBJ | BAC65326.1 | 0 | 12 | 287 | 10 | 286 | chitinase III [Vitis vinifera] |
EMBL | CAO78600.1 | 0 | 33 | 298 | 1 | 266 | endochitinase and N-acetylglucosamine-binding hemagglutinin precursor [Parkia platycephala] |
RefSeq | XP_002264744.1 | 0 | 12 | 287 | 10 | 286 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 2gsj_A | 0 | 28 | 298 | 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 | 28 | 298 | 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 | 28 | 298 | 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 | 28 | 298 | 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 | 28 | 298 | 1 | 273 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |