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CAZyme Information: MGYG000000111_00143
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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 | Cutibacterium acnes | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Cutibacterium; Cutibacterium acnes | |||||||||||
| CAZyme ID | MGYG000000111_00143 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 144153; End: 146468 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 334 | 749 | 3.3e-84 | 0.9327485380116959 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 4.03e-78 | 333 | 752 | 1 | 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 | 8.09e-16 | 268 | 678 | 202 | 632 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam13088 | BNR_2 | 1.13e-14 | 473 | 718 | 40 | 251 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam13385 | Laminin_G_3 | 7.61e-06 | 198 | 322 | 26 | 151 | Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. |
| cd00110 | LamG | 6.41e-05 | 218 | 294 | 49 | 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 |
|---|---|---|---|---|---|
| ALD69359.1 | 0.0 | 1 | 771 | 1 | 771 |
| ALU23131.1 | 0.0 | 1 | 771 | 1 | 771 |
| AER06660.1 | 0.0 | 1 | 771 | 1 | 771 |
| AYZ25079.1 | 0.0 | 1 | 771 | 1 | 771 |
| AAT82441.1 | 0.0 | 1 | 771 | 1 | 771 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5TSP_A | 5.11e-87 | 335 | 771 | 13 | 455 | 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 | 3.80e-86 | 335 | 747 | 12 | 429 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 2VK5_A | 4.14e-86 | 335 | 747 | 12 | 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] |
| 2YA4_A | 5.10e-59 | 342 | 752 | 43 | 474 | Crystalstructure of Streptococcus pneumoniae NanA (TIGR4) [Streptococcus pneumoniae TIGR4],2YA4_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) [Streptococcus pneumoniae TIGR4],2YA5_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with sialic acid [Streptococcus pneumoniae TIGR4],2YA5_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with sialic acid [Streptococcus pneumoniae TIGR4],2YA6_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with DANA [Streptococcus pneumoniae TIGR4],2YA6_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with DANA [Streptococcus pneumoniae TIGR4],2YA7_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA7_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA7_C Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA7_D Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA8_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Oseltamivir carboxylate [Streptococcus pneumoniae TIGR4],2YA8_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Oseltamivir carboxylate [Streptococcus pneumoniae TIGR4] |
| 5KKY_A | 5.46e-59 | 342 | 752 | 46 | 477 | Structureof Streptococcus pneumonia NanA bound with inhibitor 9N3Neu5Ac2en [Streptococcus pneumoniae],5KKY_B Structure of Streptococcus pneumonia NanA bound with inhibitor 9N3Neu5Ac2en [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 | 5.95e-70 | 335 | 747 | 384 | 809 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| P62575 | 8.42e-58 | 243 | 752 | 211 | 773 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
| P62576 | 8.42e-58 | 243 | 752 | 211 | 773 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| Q27701 | 2.12e-36 | 266 | 663 | 206 | 631 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| Q02834 | 5.64e-21 | 329 | 763 | 49 | 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 |
|---|---|---|---|---|---|
| 1.000029 | 0.000003 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |