y
Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00047846m |
Family | GH18 |
Protein Properties | Length: 626 Molecular Weight: 67157.2 Isoelectric Point: 6.9123 |
Chromosome | Chromosome/Scaffold: 0158938 Start: 2 End: 2264 |
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 | 2 | 227 | 1.1e-26 |
KIAVYWGQNASEGTLRDTCNTGLYAYVCIAFLSTFGDGRAPVLNLAGHCDPASGGCASLAADIASCQSAGVKVLLSIGGGALGGYSLSSPSDAQGVAAFL WDTFLGGTGAAGAPRPLGAAVLDGIDFDIEAPSLYYGDLARSLASLYGRDARGRAYMLTAAPQCPFPDASLAAALGTGLFDHVWVQFYNNPRCQYAPGDV AALRGAWQQWTAGLPSAAVFLGLPAS |
Full Sequence |
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Protein Sequence Length: 626 Download |
VKIAVYWGQN ASEGTLRDTC NTGLYAYVCI AFLSTFGDGR APVLNLAGHC DPASGGCASL 60 AADIASCQSA GVKVLLSIGG GALGGYSLSS PSDAQGVAAF LWDTFLGGTG AAGAPRPLGA 120 AVLDGIDFDI EAPSLYYGDL ARSLASLYGR DARGRAYMLT AAPQCPFPDA SLAAALGTGL 180 FDHVWVQFYN NPRCQYAPGD VAALRGAWQQ WTAGLPSAAV FLGLPASLDA AGSGFVDADT 240 LASQVLPAVE GAPNYGGIML WSRAYDKDTG FSVKLQGILR NRNNHTDITV GAAVAGALLL 300 FLLICTCFLC HKKYRSTKPP EEGSKTLPAP KIEPSQPKQR PQRLKRYTDS EVKGMTKSYA 360 HNLGHGSNAD VYRGNLRDGR QVAVKVLKNS TGDDKEFMGD VTSIGRISHV NVVPLLGFCL 420 HGPTRALIYE YMPNGSLESY AFSNNDSVEE NYSLWLYWEK LFDIAIGIAR GLEYLHGQGN 480 ANIVHLNVRP GNILLDKELC PKISDVGVTN LCHGKESKRF MGDARGRDGY DAPEVVSRKF 540 GAVSSKSDVY SYGVMVLEMV RAKRNISVGA DTTSKYFAQW LYEHLDQFCN SISDISTQTN 600 RPLMSRVVEM LESSCIDLEL PVRIS* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00221 | STYKc | 2.0e-35 | 363 | 559 | 216 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
smart00219 | TyrKc | 1.0e-35 | 363 | 559 | 216 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam07714 | Pkinase_Tyr | 2.0e-36 | 363 | 559 | 204 | + Protein tyrosine kinase. | ||
cd00180 | PKc | 7.0e-39 | 363 | 563 | 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 | 4.0e-109 | 2 | 275 | 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 | 290 | 29 | 324 | hypothetical protein OsI_03342 [Oryza sativa Indica Group] |
GenBank | EEC71310.1 | 0.00000003 | 580 | 623 | 338 | 401 | hypothetical protein OsI_03342 [Oryza sativa Indica Group] |
GenBank | EEE55216.1 | 0 | 1 | 623 | 29 | 657 | hypothetical protein OsJ_03081 [Oryza sativa Japonica Group] |
RefSeq | NP_001043931.1 | 0 | 1 | 286 | 29 | 317 | Os01g0691000 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002456179.1 | 0 | 1 | 336 | 26 | 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 | 3 | 276 | 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 | 3 | 275 | 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 | 3 | 275 | 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 | 3 | 275 | 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 | 3 | 275 | 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 |