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CAZyme Information: SDRG_06263-t26_1-p1

You are here: Home > Sequence: SDRG_06263-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 Saprolegnia diclina
Lineage Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
CAZyme ID SDRG_06263-t26_1-p1
CAZy Family GH17|CBM13|CBM13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
659 71051.26 6.0678
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SdiclinaVS20 17448 1156394 89 17359
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - - -

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 19 365 2.1e-75 0.9797297297297297

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 2.20e-101 21 353 1 334
Glyco_18 domain.
119365 GH18_chitinase 1.55e-98 22 353 1 322
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 6.65e-85 21 353 1 307
Glycosyl hydrolases family 18.
225862 ChiA 4.77e-71 20 373 38 439
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351 GH18_chitolectin_chitotriosidase 3.19e-70 23 348 2 336
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
1.08e-130 18 393 16 394
2.64e-100 9 399 13 427
1.06e-99 11 399 15 425
7.38e-95 6 399 9 420
1.20e-94 5 398 11 426

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.99e-73 20 394 38 420
Structure of Chitinase 42 from Trichoderma harzianum [Trichoderma harzianum]
5.43e-71 20 394 38 420
Chain A, Endochitinase 42 [Trichoderma harzianum],6YN4_A Chain A, Endochitinase 42 [Trichoderma harzianum],7AKQ_A Chain A, Endochitinase 42 [Trichoderma harzianum]
1.55e-66 16 394 1 391
Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus],1WNO_B Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus]
1.16e-65 16 394 39 429
Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9P_B Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9U_A Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9U_B Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9V_A Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],1W9V_B Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],2A3A_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3A_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3B_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3B_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3C_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3C_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3E_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2A3E_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2IUZ_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],2IUZ_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],3CH9_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CH9_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CHC_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHC_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHD_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHD_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHE_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHE_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHF_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus],3CHF_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus]
1.29e-63 11 393 7 400
Crystal structure of Aspergillus niger chitinase B [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.77e-74 20 394 39 427
Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
2.68e-71 20 394 38 420
Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
2.79e-70 20 393 38 419
Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
5.94e-65 16 394 39 429
Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1
5.94e-65 16 394 39 429
Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000323 0.999637 CS pos: 18-19. Pr: 0.7502

TMHMM  Annotations      help

There is no transmembrane helices in SDRG_06263-t26_1-p1.