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CAZyme Information: MGYG000004752_00124
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; | |||||||||||
| CAZyme ID | MGYG000004752_00124 | |||||||||||
| CAZy Family | GH123 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 12445; End: 14313 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam13385 | Laminin_G_3 | 7.95e-16 | 72 | 210 | 3 | 146 | Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. |
| cd15482 | Sialidase_non-viral | 1.46e-12 | 279 | 574 | 47 | 318 | 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. |
| pfam13088 | BNR_2 | 1.27e-05 | 337 | 498 | 75 | 233 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| smart00560 | LamGL | 5.00e-05 | 86 | 210 | 1 | 131 | LamG-like jellyroll fold domain. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QWT17714.1 | 5.79e-195 | 30 | 615 | 929 | 1602 |
| ADO53743.1 | 3.21e-194 | 35 | 615 | 944 | 1609 |
| AXM91086.1 | 3.42e-194 | 35 | 615 | 923 | 1588 |
| QTQ18982.1 | 1.09e-193 | 35 | 615 | 944 | 1609 |
| BBA47625.1 | 1.31e-193 | 35 | 615 | 923 | 1588 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5HON_A | 3.32e-09 | 31 | 210 | 4 | 197 | Structureof Domain 4 of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinotriose [Geobacillus stearothermophilus],5HON_B Structure of Domain 4 of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinotriose [Geobacillus stearothermophilus] |
| 5HO0_A | 2.51e-08 | 31 | 210 | 643 | 836 | Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus] |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000752 | 0.942905 | 0.055460 | 0.000387 | 0.000254 | 0.000207 |