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CAZyme Information: RVD90431.1

You are here: Home > Sequence: RVD90431.1

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 Arthrobotrys flagrans
Lineage Ascomycota; Orbiliomycetes; ; Orbiliaceae; Arthrobotrys; Arthrobotrys flagrans
CAZyme ID RVD90431.1
CAZy Family PL1
CAZyme Description CBM1 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A437AH22]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
847 90017.65 5.0121
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AflagransCBSH-5679 9927 N/A 30 9897
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.151:27 3.2.1.150:4 - 3.2.1.151:27 3.2.1.150:4 3.2.1.4:10

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH74 78 188 1.7e-24 0.4592274678111588

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
197593 fCBD 7.48e-15 814 847 1 34
Fungal-type cellulose-binding domain. Small four-cysteine cellulose-binding domain of fungi
395595 CBM_1 3.55e-14 815 843 1 29
Fungal cellulose binding domain.
406353 Sortilin-Vps10 1.97e-05 69 188 12 117
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.
214740 VPS10 1.02e-04 116 180 55 112
VPS10 domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 847 1 861
0.0 5 847 6 855
0.0 5 847 4 838
0.0 5 847 4 838
0.0 10 847 11 833

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.90e-239 22 738 3 746
Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, D60A mutant in complex with XXLG and XGXXLG xyloglucan [Paenibacillus odorifer]
2.05e-233 22 738 3 746
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]
1.24e-229 20 738 1 747
Crystal structure of Paenibacillus graminis GH74 (PgGH74) [Paenibacillus graminis]
2.66e-226 20 737 2 734
The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase [Acidothermus cellulolyticus 11B]
6.36e-217 21 737 1 729
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
2.97e-269 25 847 21 838
Xyloglucanase OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=cel74a PE=1 SV=1
3.12e-243 11 738 24 766
Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
3.87e-207 19 743 32 763
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
1.54e-206 19 743 32 763
Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
1.58e-108 15 739 25 809
Oligoxyloglucan-reducing end-specific xyloglucanase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgcA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000334 0.999646 CS pos: 19-20. Pr: 0.9697

TMHMM  Annotations      help

There is no transmembrane helices in RVD90431.1.