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CAZyme Information: MELLADRAFT_104278-t26_1-p1

You are here: Home > Sequence: MELLADRAFT_104278-t26_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Melampsora larici-populina
Lineage Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
CAZyme ID MELLADRAFT_104278-t26_1-p1
CAZy Family AA1
CAZyme Description family 18 glycoside hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
522 57470.55 8.4115
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Mlarici-populina98AG31 16380 747676 8 16372
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 113 486 2e-45 0.9324324324324325

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 8.78e-58 114 486 1 333
Glyco_18 domain.
119365 GH18_chitinase 2.68e-50 115 481 1 316
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.
395573 Glyco_hydro_18 5.27e-50 114 486 1 306
Glycosyl hydrolases family 18.
225862 ChiA 1.33e-44 113 495 38 431
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351 GH18_chitolectin_chitotriosidase 9.70e-37 167 481 59 335
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.69e-81 114 501 36 420
1.20e-70 118 486 29 392
2.25e-58 129 493 49 407
4.25e-58 130 496 59 399
5.17e-58 140 479 3 335

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.46e-30 172 486 152 447
Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
3.03e-27 170 486 116 405
Chain A, Glycosyl Hydrolase [Niallia circulans]
1.19e-23 172 483 104 373
Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
1.38e-23 172 483 355 624
Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
1.25e-22 178 483 76 353
Crystal structure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXM_B Crystal structure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.69e-26 170 486 148 437
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
1.46e-20 178 478 90 348
Chitinase-3-like protein 1 OS=Sus scrofa OX=9823 GN=CHI3L1 PE=1 SV=2
3.18e-20 172 478 84 356
Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
7.44e-20 172 478 84 356
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
2.08e-19 178 478 88 346
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.001104 0.998879 CS pos: 25-26. Pr: 0.7473

TMHMM  Annotations      help

There is no transmembrane helices in MELLADRAFT_104278-t26_1-p1.