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CAZyme Information: jhhlp_003097-t41_1-p1

You are here: Home > Sequence: jhhlp_003097-t41_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 Lomentospora prolificans
Lineage Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
CAZyme ID jhhlp_003097-t41_1-p1
CAZy Family CE2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
837 NLAX01000008|CGC34 87883.56 4.9922
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_LprolificansJHH5317 8768 N/A 208 8560
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.151:27 3.2.1.150:4 3.2.1.151:5

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH74 79 186 1.3e-24 0.44635193133047213

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
197593 fCBD 2.40e-17 804 837 1 34
Fungal-type cellulose-binding domain. Small four-cysteine cellulose-binding domain of fungi
395595 CBM_1 3.76e-15 805 833 1 29
Fungal cellulose binding domain.
406353 Sortilin-Vps10 7.85e-08 86 266 25 211
Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
271234 Sialidase_non-viral 1.05e-05 99 288 158 332
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.
406353 Sortilin-Vps10 2.08e-05 119 251 5 110
Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 837 1 840
0.0 6 837 7 838
0.0 6 837 7 838
0.0 19 837 345 1167
0.0 21 837 1 818

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.89e-191 21 736 2 721
Crystal structure of Streptomyces rapamycinicus GH74 in complex with xyloglucan fragments XLLG and XXXG [Streptomyces rapamycinicus NRRL 5491],6P2O_B Crystal structure of Streptomyces rapamycinicus GH74 in complex with xyloglucan fragments XLLG and XXXG [Streptomyces rapamycinicus NRRL 5491]
1.93e-188 22 740 6 745
Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, D60A mutant in complex with XXLG and XGXXLG xyloglucan [Paenibacillus odorifer]
6.50e-187 22 740 7 734
The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase [Acidothermus cellulolyticus 11B]
3.40e-183 22 740 6 745
Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_B Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_C Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_D Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_E Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_F Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_G Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGJ_H Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme [Paenibacillus odorifer],6MGK_A Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer],6MGK_B Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer],6MGK_C Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer],6MGK_D Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, in complex with XLX xyloglucan [Paenibacillus odorifer]
6.46e-182 22 637 5 621
Unraveling the first step of xyloglucan degradation by the soil saprophyte Cellvibrio japonicus through the functional and structural characterization of a potent GH74 endo-xyloglucanase [Cellvibrio japonicus Ueda107],5FKS_A Unraveling the first step of xyloglucan degradation by the soil saprophyte Cellvibrio japonicus through the functional and structural characterization of a potent GH74 endo-xyloglucanase [Cellvibrio japonicus Ueda107]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 6 837 7 838
Xyloglucanase OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=cel74a PE=1 SV=1
9.38e-196 22 740 38 765
Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
3.05e-168 22 740 38 757
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xghA PE=3 SV=1
1.20e-167 22 740 38 757
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
1.78e-92 8 740 17 784
Oligoxyloglucan reducing end-specific cellobiohydrolase OS=Geotrichum sp. (strain M128) OX=203496 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000334 0.999622 CS pos: 20-21. Pr: 0.9734

TMHMM  Annotations      help

There is no transmembrane helices in jhhlp_003097-t41_1-p1.