Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10009026m |
Family | GH19 |
Protein Properties | Length: 476 Molecular Weight: 52016.9 Isoelectric Point: 7.6822 |
Chromosome | Chromosome/Scaffold: 1 Start: 12077959 End: 12080200 |
Description | pathogenesis-related gene 5 |
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 |
GH19 | 58 | 250 | 0 |
RITKIVTQKFFDGIISNASNGCAGKKFYTRDSFIEAARTNLEFNTSVTRLEIATMFAHFTYETQHFCKIEEVNGSSYDYCDENNLQYPCAQGKKYYGRGP MQLSWNYNYGSCGQSLGLDLLREPELVGSNPTVAFRASLWFWMNNVRPVLDQGFVATIKAINSLELSSEDQSAVSARVEYYTNYCKQLGVDPG |
Full Sequence |
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Protein Sequence Length: 476 Download |
MPLKKISSVS LLLIFGFYYE TAKSQFCGCS PVLCCSMYGY CGFTEGYCGS GCKEGPCRIT 60 KIVTQKFFDG IISNASNGCA GKKFYTRDSF IEAARTNLEF NTSVTRLEIA TMFAHFTYET 120 QHFCKIEEVN GSSYDYCDEN NLQYPCAQGK KYYGRGPMQL SWNYNYGSCG QSLGLDLLRE 180 PELVGSNPTV AFRASLWFWM NNVRPVLDQG FVATIKAINS LELSSEDQSA VSARVEYYTN 240 YCKQLGVDPG IIDLPSRLTV FTLKNKCSHT VWAATLAGRG PRLGGGGFKL TSGASQKLQA 300 PAGWSGRFWA RTGCKFDASG NGRCITGDCG GLRCNGGAVP PVTLAEFTLV GDGGKDFYDV 360 SLVDGYNVKL GIRPYGGYGD CRYAGCITDL NANCPNELKV MGPQNNVVAC KSACAVFNTD 420 QYCCRGAFNT PETCPPTNYS RIFKEACPIA YSYAYDDQTN TFTCSRANYE ITFCP* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00182 | Glyco_hydro_19 | 1.0e-68 | 62 | 250 | 227 | + Chitinase class I. | ||
cd00325 | chitinase_glyco_hydro_19 | 5.0e-72 | 63 | 250 | 225 | + Glycoside hydrolase family 19 chitinase domain. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases but they are smaller in size due to certain deletions. Despite any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the procaryotic/eucaryotic divergence. | ||
smart00205 | THN | 1.0e-102 | 261 | 475 | 219 | + Thaumatin family. The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism. | ||
pfam00314 | Thaumatin | 2.0e-104 | 265 | 475 | 214 | + Thaumatin family. | ||
cd09218 | TLP-PA | 3.0e-113 | 260 | 474 | 219 | + allergenic/antifungal thaumatin-like proteins: plant and animal homologs. This subfamily is represented by the thaumatin-like proteins (TLPs), Cherry Allergen Pru Av 2 TLP, Peach PpAZ44 TLP (a propylene-induced TLP in abscission), the Caenorhabditis elegans thaumatin family member (thn-6), and other plant and animal homologs. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Due to their inducible expression by environmental stresses such as pathogen/pest attack, drought and cold, plant TLPs are classified as the pathogenesis-related (PR) protein family 5 (PR5). Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. TLPs within this subfamily contain 16 conserved Cys residues. |
Gene Ontology | |
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GO Term | Description |
GO:0004568 | chitinase activity |
GO:0006032 | chitin catabolic process |
GO:0008061 | chitin binding |
GO:0016998 | cell wall macromolecule catabolic 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 |
GenBank | ABV89613.1 | 0 | 1 | 250 | 1 | 263 | chitinase [Brassica rapa] |
DDBJ | BAF35569.1 | 0 | 1 | 250 | 1 | 263 | chitinase [Brassica rapa subsp. pekinensis] |
RefSeq | NP_177641.1 | 0 | 259 | 475 | 24 | 239 | PR5 (PATHOGENESIS-RELATED GENE 5) [Arabidopsis thaliana] |
RefSeq | NP_181887.1 | 0 | 1 | 250 | 1 | 259 | chitinase, putative [Arabidopsis thaliana] |
Swiss-Prot | Q06209 | 0 | 1 | 250 | 1 | 263 | CHI4_BRANA RecName: Full=Basic endochitinase CHB4; 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 | 2ahn_A | 0 | 260 | 475 | 2 | 222 | A Chain A, High Resolution Structure Of A Cherry Allergen Pru Av 2 |
PDB | 3zs3_A | 0 | 261 | 475 | 3 | 222 | A Chain A, High Resolution Structure Of Mal D 2, The Thaumatin Like Food Allergen From Apple |
PDB | 1du5_B | 0 | 260 | 475 | 2 | 206 | A Chain A, The Crystal Structure Of Zeamatin. |
PDB | 1du5_A | 0 | 260 | 475 | 2 | 206 | A Chain A, The Crystal Structure Of Zeamatin. |
PDB | 1z3q_A | 0 | 260 | 475 | 2 | 200 | A Chain A, Resolution Of The Structure Of The Allergenic And Antifungal Banana Fruit Thaumatin-like Protein At 1.7a |