Species | Prevotellamassilia sp900556465 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900556465 | |||||||||||
CAZyme ID | MGYG000000866_00002 | |||||||||||
CAZy Family | GH29 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 694; End: 2217 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH29 | 46 | 360 | 1.4e-56 | 0.8728323699421965 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3669 | AfuC | 5.65e-39 | 40 | 507 | 4 | 430 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
smart00812 | Alpha_L_fucos | 2.29e-23 | 36 | 359 | 9 | 331 | Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis. |
pfam01120 | Alpha_L_fucos | 2.39e-23 | 85 | 359 | 75 | 329 | Alpha-L-fucosidase. |
pfam00754 | F5_F8_type_C | 8.46e-10 | 382 | 495 | 8 | 115 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
cd08666 | APC10-HECTD3 | 0.009 | 385 | 417 | 18 | 50 | APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination. This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QFQ12382.1 | 6.63e-215 | 28 | 507 | 25 | 492 |
QFQ12303.1 | 1.89e-214 | 28 | 507 | 25 | 492 |
AKU70405.1 | 9.30e-212 | 20 | 507 | 21 | 509 |
QUB86038.1 | 9.30e-212 | 20 | 507 | 21 | 509 |
AUI56213.1 | 8.22e-208 | 21 | 507 | 22 | 509 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5K9H_A | 1.61e-71 | 42 | 507 | 34 | 463 | Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified] |
3UES_A | 1.23e-56 | 47 | 501 | 19 | 470 | Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UES_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088] |
3UET_A | 1.74e-55 | 47 | 501 | 19 | 470 | Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UET_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088] |
3MO4_A | 3.63e-53 | 47 | 469 | 21 | 449 | Thecrystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3MO4_B The crystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088] |
4ZRX_A | 1.85e-52 | 46 | 467 | 31 | 427 | Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8GW72 | 4.62e-54 | 40 | 507 | 31 | 477 | Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2 |
Q7XUR3 | 2.15e-52 | 7 | 507 | 6 | 476 | Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.161282 | 0.830351 | 0.007189 | 0.000455 | 0.000328 | 0.000358 |
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