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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s144_96V6.1 |
Family | GH18 |
Protein Properties | Length: 373 Molecular Weight: 40512 Isoelectric Point: 3.9846 |
Chromosome | Chromosome/Scaffold: 144 Start: 753604 End: 755506 |
Description | Glycosyl hydrolase family protein with chitinase insertion domain |
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 | 43 | 362 | 0 |
PLVNINFNYETHVYYAFAGLDPSSYQVVAPTTDNGQYATFVATAKSSNPSVVTLLSIGGGAANFTTFGEMVSTSTRRQAFIDSSISLARQYSYEGLDLDW ESPQSQTEMENLALLLQEWRAAAHTEAQSSGNTELLLTAAVSYQSILLYTGVGNQVWPITAFNTYLDWVNVMTYDYHGSWEPTTTGEHTALYDPNSDVDT DYGINNWLSAGMQADKMCLGLAFYGKQWVLASLANTGVGAPATSGGDPITYADIVTYNNAGGATVEQDSTTVSMYSYKSDLTWIGYDNPDTIAAKVQYAQ SKSLLGYFAWALHQDDANFS |
Full Sequence |
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Protein Sequence Length: 373 Download |
MAPRISLFGI LLVQILSFQL LVSPDFFLAG AVVRGGYWLQ DLPLVNINFN YETHVYYAFA 60 GLDPSSYQVV APTTDNGQYA TFVATAKSSN PSVVTLLSIG GGAANFTTFG EMVSTSTRRQ 120 AFIDSSISLA RQYSYEGLDL DWESPQSQTE MENLALLLQE WRAAAHTEAQ SSGNTELLLT 180 AAVSYQSILL YTGVGNQVWP ITAFNTYLDW VNVMTYDYHG SWEPTTTGEH TALYDPNSDV 240 DTDYGINNWL SAGMQADKMC LGLAFYGKQW VLASLANTGV GAPATSGGDP ITYADIVTYN 300 NAGGATVEQD STTVSMYSYK SDLTWIGYDN PDTIAAKVQY AQSKSLLGYF AWALHQDDAN 360 FSLASAAQNA WT* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06548 | GH18_chitinase | 2.0e-56 | 35 | 357 | 355 | + The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. | ||
pfam00704 | Glyco_hydro_18 | 4.0e-69 | 35 | 357 | 337 | + Glycosyl hydrolases family 18. | ||
smart00636 | Glyco_18 | 2.0e-80 | 33 | 357 | 343 | + Glyco_18 domain. | ||
cd02872 | GH18_chitolectin_chitotriosidase | 8.0e-81 | 46 | 358 | 346 | + This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens. | ||
cd02879 | GH18_plant_chitinase_class_V | 4.0e-148 | 30 | 363 | 337 | + The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity. |
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 |
RefSeq | XP_001771980.1 | 0 | 1 | 369 | 1 | 369 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784103.1 | 0 | 32 | 366 | 22 | 357 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002309324.1 | 0 | 7 | 371 | 9 | 368 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002336275.1 | 0 | 33 | 358 | 27 | 352 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523517.1 | 0 | 1 | 371 | 1 | 369 | chitinase, 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 | 3alf_A | 0 | 33 | 371 | 4 | 345 | A Chain A, Crystal Structure Of Class V Chitinase From Nicotiana Tobaccum |
PDB | 3aqu_D | 0 | 32 | 371 | 4 | 343 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_C | 0 | 32 | 371 | 4 | 343 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_B | 0 | 32 | 371 | 4 | 343 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_A | 0 | 32 | 371 | 4 | 343 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
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 |