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CAZyme Information: MGYG000002275_00190
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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 | Paraprevotella sp003477995 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp003477995 | |||||||||||
| CAZyme ID | MGYG000002275_00190 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 231657; End: 236603 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 1014 | 1381 | 1.3e-48 | 0.9239766081871345 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 1.96e-61 | 1001 | 1386 | 1 | 339 | 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. |
| cd01828 | sialate_O-acetylesterase_like2 | 6.53e-42 | 42 | 202 | 1 | 164 | sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| cd01841 | NnaC_like | 2.86e-29 | 41 | 206 | 1 | 174 | NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis. |
| cd01828 | sialate_O-acetylesterase_like2 | 4.17e-22 | 243 | 413 | 1 | 164 | sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| pfam13472 | Lipase_GDSL_2 | 6.18e-19 | 45 | 197 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUB73272.1 | 5.74e-103 | 893 | 1646 | 282 | 1059 |
| QUB85277.1 | 2.20e-102 | 914 | 1646 | 273 | 1032 |
| QUB76590.1 | 3.57e-101 | 893 | 1646 | 274 | 1051 |
| AUI56353.1 | 9.64e-99 | 875 | 1646 | 330 | 1132 |
| ALO48969.1 | 4.58e-98 | 990 | 1398 | 16 | 402 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6XPM_A | 3.69e-26 | 25 | 206 | 10 | 201 | ChainA, Lysophospholipase L1 [Phocaeicola vulgatus] |
| 6NJC_A | 6.83e-26 | 25 | 206 | 10 | 201 | ChainA, Sialate O-acetylesterase [Phocaeicola vulgatus ATCC 8482],6NJC_B Chain B, Sialate O-acetylesterase [Phocaeicola vulgatus ATCC 8482],6XPG_A Chain A, Lysophospholipase L1 [Phocaeicola vulgatus] |
| 1EUR_A | 1.19e-11 | 1014 | 1387 | 25 | 356 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
| 1W8N_A | 2.72e-11 | 1014 | 1387 | 21 | 352 | Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens] |
| 1EUT_A | 2.74e-11 | 1014 | 1387 | 25 | 356 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q02834 | 1.59e-10 | 1014 | 1387 | 67 | 398 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
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 |
|---|---|---|---|---|---|
| 0.000274 | 0.999028 | 0.000214 | 0.000165 | 0.000147 | 0.000135 |