dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Rhizopus delemar

Lineage

Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus delemar

CAZyme ID

RO3G_11756-t26_1-p1

CAZy Family

GT17

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
218	CH476740\|CGC1	23695.90	8.2500

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RdelemarRA99-880	17703	246409	244	17459

Gene Location

Enzyme Prediction help

No EC number prediction in RO3G_11756-t26_1-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH152	42	218	4.3e-42	0.8796296296296297

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	1.90e-56	46	218	28	210	Thaumatin family.
185757	TLP-PA	5.79e-50	46	218	34	219	allergenic/antifungal thaumatin-like proteins: plant and animal homologs. This subfamily is represented by the thaumatin-like proteins (TLPs), Cherry Allergen Pru Av 2 TLP, Peach PpAZ44 TLP (a propylene-induced TLP in abscission), the Caenorhabditis elegans thaumatin family member (thn-6), and other plant and animal homologs. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Due to their inducible expression by environmental stresses such as pathogen/pest attack, drought and cold, plant TLPs are classified as the pathogenesis-related (PR) protein family 5 (PR5). Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. TLPs within this subfamily contain 16 conserved Cys residues.
128501	THN	1.37e-39	19	218	3	217	Thaumatin family. The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism.
185758	TLP-F	1.78e-23	17	218	1	228	thaumatin-like proteins: basidiomycete homologs. This subfamily is represented by Lentinula edodes TLG1, a thaumatin-like protein (TLP), as well as, other basidiomycete homologs. In general, TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. TLG1 TLP is involved in lentinan degradation and fruiting body senescence. TLG1 expressed in Escherichia coli and Aspergillus oryzae exhibited beta-1,3-glucanase activity and demonstrated lentinan degrading activity. TLG1 is proposed to be involved in lentinan and cell wall degradation during senescence following harvest and spore diffusion. TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. TLG1 from Lentinula edodes contains the required acidic amino acids conserved in the appropriate positions to possess an electronegative cleft. TLPs within this subfamily contain 13 conserved Cys residues; the number of total Cys residues in these TLPs varies from 16 in L. edodes TLG1 to 18 in other basidiomycete homologs.
185754	Thaumatin-like	3.90e-23	17	218	1	157	the sweet-tasting protein, thaumatin, and thaumatin-like proteins involved in host defense. This family is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii and thaumatin-like proteins (TLPs) involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs included in this family are such proteins as zeamatin, found in high concentrations in cereal seeds; osmotin, a salt-induced protein in osmotically stressed plants; and PpAZ44, a propylene-induced TLP in abscission of young fruit. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.01e-39	42	218	4	190
1.98e-38	16	218	55	272
2.12e-38	19	218	80	292
2.93e-38	4	218	15	233
3.56e-38	21	218	31	235

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.82e-35	16	218	2	221	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
3.94e-28	44	218	33	221	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
4.88e-23	16	209	2	190	Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]
4.66e-20	16	218	2	204	Structure K137A thaumatin [Thaumatococcus daniellii]
8.91e-20	16	218	2	204	Thaumatin Before A High Dose X-Ray 'Burn' [Thaumatococcus daniellii],2BLU_A Thaumatin After A High Dose X-Ray 'Burn' [Thaumatococcus daniellii],2VHK_A Atomic resolution (0.94 A) structure of purified thaumatin I grown in sodium L-tartrate at 22C [Thaumatococcus daniellii],2WBZ_A 1.6 A Structure of Thaumatin Crystallized without Tartrate at 4 C [Thaumatococcus daniellii],3N02_A Thaumatic crystals grown in loops/micromounts [Thaumatococcus daniellii],3N03_A Thaumatin crystals grown from drops [Thaumatococcus daniellii],4AXU_A CRYSTAL STRUCTURE OF THAUMATIN FROM AN AUTO-HARVESTED CRYSTAL, control experiment [Thaumatococcus daniellii],5AMZ_A Crystal Structure of Thaumatin processed with the CrystalDirect automated mounting and cryo-cooling technology [Thaumatococcus daniellii],5AVG_A The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel [Thaumatococcus daniellii]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.35e-34	16	218	25	244	Glucan endo-1,3-beta-glucosidase OS=Prunus avium OX=42229 PE=1 SV=1
6.66e-34	58	218	69	237	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
9.16e-34	44	218	61	248	Thaumatin-like protein OS=Oryza sativa subsp. japonica OX=39947 GN=Os11g0706600 PE=2 SV=1
2.82e-33	16	218	22	238	Thaumatin-like protein OS=Arabidopsis thaliana OX=3702 GN=At1g18250 PE=2 SV=2
1.41e-32	44	218	55	238	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.992193	0.007839

TMHMM Annotations help

There is no transmembrane helices in RO3G_11756-t26_1-p1.

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