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CAZyme Information: MGYG000004469_01930
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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 | Alistipes_A sp900545315 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900545315 | |||||||||||
| CAZyme ID | MGYG000004469_01930 | |||||||||||
| CAZy Family | GH106 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 231; End: 1559 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH106 | 1 | 428 | 1.2e-119 | 0.5169902912621359 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17132 | Glyco_hydro_106 | 3.39e-72 | 1 | 213 | 660 | 867 | alpha-L-rhamnosidase. |
| PRK10150 | PRK10150 | 2.36e-07 | 276 | 387 | 15 | 141 | beta-D-glucuronidase; Provisional |
| PRK10340 | ebgA | 3.19e-05 | 317 | 383 | 110 | 178 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
| pfam02837 | Glyco_hydro_2_N | 1.84e-04 | 275 | 393 | 35 | 144 | Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. |
| cd03143 | A4_beta-galactosidase_middle_domain | 2.77e-04 | 33 | 140 | 39 | 129 | A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCG53972.1 | 2.40e-201 | 1 | 433 | 656 | 1080 |
| SCM59077.1 | 4.31e-164 | 1 | 433 | 661 | 1083 |
| SCD21026.1 | 8.54e-163 | 1 | 432 | 660 | 1081 |
| BBD46131.1 | 1.71e-155 | 1 | 432 | 660 | 1081 |
| QRQ58444.1 | 2.67e-153 | 1 | 432 | 658 | 1080 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6Q2F_A | 1.64e-65 | 1 | 427 | 724 | 1138 | Structureof Rhamnosidase from Novosphingobium sp. PP1Y [Novosphingobium sp. PP1Y] |
| 5MQM_A | 4.96e-44 | 1 | 425 | 674 | 1096 | Glycosidehydrolase BT_0986 [Bacteroides thetaiotaomicron],5MQN_A Glycoside hydrolase BT_0986 [Bacteroides thetaiotaomicron] |
| 5MWK_A | 4.96e-44 | 1 | 425 | 674 | 1096 | Glycosidehydrolase BT_0986 [Bacteroides thetaiotaomicron] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| T2KNA8 | 9.30e-43 | 1 | 435 | 510 | 1163 | Putative beta-glucuronidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22040 PE=2 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.999982 | 0.000054 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |