y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma15g01820.3 |
Family | GH18 |
Protein Properties | Length: 625 Molecular Weight: 68801.8 Isoelectric Point: 8.0494 |
Chromosome | Chromosome/Scaffold: 15 Start: 1200171 End: 1204142 |
Description | chitinase A |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH18 | 27 | 255 | 2.1e-25 |
NVAIYWGQNADEGTLNETCATGTYSHVIIAFLSTFGNGQTPQLSLADHCDPSTNGCTKIGREIKNCQEQGITVMLSIGGGSGNYSITSDEDANNVSNYLW DNFFGGFSSSRPFGDAVLDGLDFDIALGDNTSFMANLAQYLKSNSDSQTIQQKQLPASLYLSAAPQCPFPDARLGSAIGTGIFDYVWVQFYNNPSCSYSQ NNLDNFLKSWREWATSLKVGKLFLGLPAD |
Full Sequence |
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Protein Sequence Length: 625 Download |
MSTSVLPSLL FFLVLILLLL DPSEPENVAI YWGQNADEGT LNETCATGTY SHVIIAFLST 60 FGNGQTPQLS LADHCDPSTN GCTKIGREIK NCQEQGITVM LSIGGGSGNY SITSDEDANN 120 VSNYLWDNFF GGFSSSRPFG DAVLDGLDFD IALGDNTSFM ANLAQYLKSN SDSQTIQQKQ 180 LPASLYLSAA PQCPFPDARL GSAIGTGIFD YVWVQFYNNP SCSYSQNNLD NFLKSWREWA 240 TSLKVGKLFL GLPADEAAAP AGGYVPADVL MSKILPEINK STNYGGLMLW SRYYDKISGY 300 STRIQNPLRN GTANPLCTRK SQACRSHEGG FAELLGYMST LGIKVYEDDN NGTQCCEIIC 360 RNNCSCDAFA PLNHINNTST GCQIWLKGTK FVRASGNIAL PINVSVALLE HKVNSWWIWL 420 IVGVGAAFVI PVIFYLSRAF LRKYKAKVER KKMQKKLLHD IGGNAMLAMV YGKTIKSNNK 480 GKTNNEVELF AFDTIVVATN NFSAANKLGE GGFGPVYKGN LSDQQEVAIK RLSKSSGQGL 540 IEFTNEAKLM AKLQHTNLVK LLGFCIQRDE RILVYEYMSN KSLDFYLFGR LSFILTKVRM 600 CQMLACSILT SNLTLKQIRL ERIC* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 5.0e-21 | 507 | 606 | 109 | + Protein tyrosine kinase. | ||
cd00192 | PTKc | 4.0e-21 | 506 | 587 | 87 | + Catalytic domain of Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers. | ||
smart00219 | TyrKc | 2.0e-21 | 507 | 606 | 108 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam00704 | Glyco_hydro_18 | 2.0e-28 | 27 | 295 | 348 | + Glycosyl hydrolases family 18. | ||
cd02877 | GH18_hevamine_XipI_class_III | 1.0e-113 | 27 | 306 | 287 | + 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:0004672 | protein kinase activity |
GO:0005524 | ATP binding |
GO:0005975 | carbohydrate metabolic process |
GO:0006468 | protein phosphorylation |
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 | AAQ07267.1 | 0 | 9 | 304 | 3 | 288 | acidic chitinase [Ficus pumila var. awkeotsang] |
GenBank | ABF82271.1 | 0 | 1 | 306 | 1 | 296 | class III chitinase [Panax ginseng] |
GenBank | ABN03967.1 | 0 | 9 | 306 | 10 | 296 | acidic chitinase [Gossypium hirsutum] |
Swiss-Prot | P51614 | 0 | 1 | 295 | 1 | 288 | CHIT3_VITVI RecName: Full=Acidic endochitinase; Flags: Precursor |
RefSeq | XP_002513612.1 | 0 | 28 | 304 | 27 | 293 | 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 | 28 | 304 | 3 | 269 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1llo_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1hvq_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
PDB | 1kr1_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1kqz_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
chitin degradation II | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12623 | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12624 | EC-3.2.1.14 | chitinase |
chitin degradation III (carnivorous plants) | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |