y
Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si003958m |
Family | GH18 |
Protein Properties | Length: 672 Molecular Weight: 72533.2 Isoelectric Point: 6.1458 |
Chromosome | Chromosome/Scaffold: 5 Start: 33919481 End: 33921829 |
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 | 27 | 253 | 9.9e-27 |
VKIAVYWGQNASEGTLRDTCSTGLYAYVNIAFLSTFGDGRAPVLNLADHCDPPSGGCASLATDIASCQSVGVKVLLSIGGGALGGYNLSSPSDAQGVAAY LWDNFLGGTGVAGAPRPLGGAVLDGIDFDIEAPSQYYDDLARNLTSLYRGDARGRAYMLTAAPQCPFPDASLATALGTGLFDHVWVQFYNNPPCQYAPGD DAALRSSWRQWTAGLPSATVFLGLPAS |
Full Sequence |
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Protein Sequence Length: 672 Download |
MSGKLRFYAS LLFAVSSVLA AAASDDVKIA VYWGQNASEG TLRDTCSTGL YAYVNIAFLS 60 TFGDGRAPVL NLADHCDPPS GGCASLATDI ASCQSVGVKV LLSIGGGALG GYNLSSPSDA 120 QGVAAYLWDN FLGGTGVAGA PRPLGGAVLD GIDFDIEAPS QYYDDLARNL TSLYRGDARG 180 RAYMLTAAPQ CPFPDASLAT ALGTGLFDHV WVQFYNNPPC QYAPGDDAAL RSSWRQWTAG 240 LPSATVFLGL PASLDAAGSG FVDADTLASQ VLPAVEGAPN YGGIMLWSRS YDKDTGFSVK 300 LQGILQNRND QTDIIVGVAV AGVLLLFLLI CSCFLCHRKY RGTPPPVEGS TTPPAPKTEP 360 SQPKQRPQRL KRYTYSEVER MTKAYAHKLG HGSNGDVYRG NLRDGCQVAV KVLKNSKGDD 420 KEFMSEVASI GRISHVNVVP LLGFCLQGPT RALIYEYMHN GSLESYAFSN NDSVEDNYSL 480 WLYWEKLFDI AIGVARGLEY LHGQGNANIL HLNVKPCNVM LDQELCPKIS DVGVANLCHG 540 KENKRSTGDA RGRDGYDAPE VVSRKFGAIS SKSDVYSYGV MVLEMVRAKR NISVGADTTS 600 KYFAQWLYEH LDQFCNSISD ISTETRDLVK KMIIVGLWCI QTVQTNRPSM CRVVEMLESS 660 STDLELPVRI S* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00219 | TyrKc | 9.0e-37 | 387 | 585 | 210 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam07714 | Pkinase_Tyr | 3.0e-38 | 388 | 585 | 205 | + Protein tyrosine kinase. | ||
pfam00069 | Pkinase | 5.0e-39 | 388 | 655 | 274 | + Protein kinase domain. | ||
cd00180 | PKc | 4.0e-40 | 389 | 589 | 205 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
cd02877 | GH18_hevamine_XipI_class_III | 3.0e-132 | 28 | 301 | 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: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 | EEC71310.1 | 0 | 1 | 312 | 1 | 320 | hypothetical protein OsI_03342 [Oryza sativa Indica Group] |
GenBank | EEC71310.1 | 2e-22 | 606 | 669 | 338 | 401 | hypothetical protein OsI_03342 [Oryza sativa Indica Group] |
GenBank | EEE55216.1 | 0 | 1 | 669 | 1 | 657 | hypothetical protein OsJ_03081 [Oryza sativa Japonica Group] |
RefSeq | NP_001043931.1 | 0 | 1 | 312 | 1 | 317 | Os01g0691000 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002456179.1 | 0 | 1 | 362 | 1 | 371 | hypothetical protein SORBIDRAFT_03g031710 [Sorghum bicolor] |
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 | 29 | 302 | 3 | 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 | 29 | 301 | 3 | 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 | 29 | 301 | 3 | 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 | 29 | 301 | 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 | 1kr0_A | 0 | 29 | 301 | 3 | 269 | A Chain A, Hevamine Mutant D125aY183F 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 |