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CAZyme Information: MGYG000000112_00960
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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 | Actinomyces sp900323545 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces sp900323545 | |||||||||||
| CAZyme ID | MGYG000000112_00960 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1140222; End: 1142627 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 345 | 779 | 9.1e-87 | 0.9298245614035088 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 2.80e-79 | 345 | 782 | 3 | 328 | 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. |
| COG4409 | NanH | 3.68e-17 | 309 | 777 | 226 | 700 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam13088 | BNR_2 | 6.96e-14 | 535 | 748 | 80 | 251 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam13385 | Laminin_G_3 | 6.37e-07 | 202 | 332 | 25 | 151 | Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. |
| cd00110 | LamG | 3.64e-06 | 202 | 304 | 28 | 124 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QQC21411.1 | 0.0 | 1 | 801 | 1 | 799 |
| VEI16013.1 | 0.0 | 1 | 801 | 1 | 797 |
| QLF54682.1 | 0.0 | 1 | 801 | 1 | 810 |
| AMD99362.1 | 0.0 | 1 | 801 | 1 | 810 |
| QCT33734.1 | 0.0 | 1 | 801 | 1 | 807 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5TSP_A | 1.80e-72 | 336 | 777 | 4 | 430 | Crystalstructure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124],5TSP_B Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124] |
| 2BF6_A | 1.31e-71 | 336 | 777 | 3 | 429 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 2VK5_A | 1.42e-71 | 336 | 777 | 3 | 429 | TheStructure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK6_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_B The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens] |
| 3H72_A | 8.24e-62 | 336 | 782 | 4 | 457 | Crystalstructure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H72_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H73_A Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6],3H73_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6] |
| 7A54_A | 1.35e-61 | 336 | 782 | 27 | 480 | ChainA, Sialidase A [Streptococcus pneumoniae],7A54_B Chain B, Sialidase A [Streptococcus pneumoniae],7A5X_A Chain A, Sialidase A [Streptococcus pneumoniae],7A5X_B Chain B, Sialidase A [Streptococcus pneumoniae] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P29767 | 7.81e-66 | 314 | 777 | 341 | 809 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| P62575 | 2.10e-61 | 254 | 782 | 217 | 773 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
| P62576 | 2.10e-61 | 254 | 782 | 217 | 773 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| Q27701 | 1.82e-40 | 291 | 778 | 223 | 730 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| Q02834 | 9.64e-24 | 336 | 793 | 46 | 401 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 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 |
|---|---|---|---|---|---|
| 0.999932 | 0.000107 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |