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CAZyme Information: I302_08444-t42_1-p1

You are here: Home > Sequence: I302_08444-t42_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 Kwoniella bestiolae
Lineage Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella bestiolae
CAZyme ID I302_08444-t42_1-p1
CAZy Family GT58
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
389 KI894026|CGC7 42038.54 8.0654
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_KbestiolaeCBS10118 9270 1296100 137 9133
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in I302_08444-t42_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH93 51 364 1.1e-90 0.9869706840390879

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
350098 GH43-like 1.24e-04 148 259 46 150
Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
271234 Sialidase_non-viral 0.007 155 372 52 275
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
271234 Sialidase_non-viral 0.009 88 211 227 330
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.92e-115 11 388 10 383
1.10e-107 6 384 21 395
3.84e-105 8 384 24 396
5.27e-105 34 384 52 395
2.85e-104 9 384 24 394

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.00e-90 22 367 3 341
Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum]
1.13e-89 22 367 3 341
Chain A, Alpha-l-arabinofuranosidase [Fusarium graminearum]
1.60e-89 22 367 3 341
Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_B Chain B, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_C Chain C, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum]
5.09e-88 22 367 3 341
Chain A, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum]
5.65e-84 44 355 15 320
High resolution structure of Penicillium chrysogenum alpha-L-arabinanase [Penicillium chrysogenum],3A72_A High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose [Penicillium chrysogenum]

Swiss-Prot Hits      help

I302_08444-t42_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000689 0.999294 CS pos: 27-28. Pr: 0.9230

TMHMM  Annotations      help

There is no transmembrane helices in I302_08444-t42_1-p1.