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CAZyme Information: MGYG000000104_02393
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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 | Clostridium cuniculi | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium cuniculi | |||||||||||
| CAZyme ID | MGYG000000104_02393 | |||||||||||
| CAZy Family | CBM32 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 33951; End: 37421 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 379 | 809 | 5.7e-99 | 0.9619883040935673 |
| CBM40 | 192 | 358 | 7.4e-43 | 0.9664804469273743 |
| CBM32 | 54 | 175 | 4.4e-18 | 0.9112903225806451 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 1.37e-85 | 380 | 808 | 2 | 333 | 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 | 3.49e-31 | 227 | 801 | 86 | 703 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam02973 | Sialidase | 3.38e-27 | 184 | 361 | 1 | 188 | Sialidase, N-terminal domain. |
| pfam13088 | BNR_2 | 2.99e-17 | 556 | 795 | 79 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam00754 | F5_F8_type_C | 5.72e-16 | 51 | 175 | 1 | 127 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AYE33273.1 | 0.0 | 2 | 1069 | 3 | 1087 |
| QAS61444.1 | 0.0 | 2 | 1069 | 3 | 1087 |
| ATD57534.1 | 0.0 | 1 | 1156 | 1 | 1299 |
| QBJ75069.1 | 0.0 | 1 | 1156 | 1 | 1299 |
| ATD54786.1 | 0.0 | 1 | 1156 | 1 | 1299 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5TSP_A | 1.30e-194 | 374 | 816 | 6 | 448 | 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 | 6.69e-194 | 374 | 816 | 5 | 447 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 2VK5_A | 7.44e-194 | 374 | 816 | 5 | 447 | 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] |
| 1SLI_A | 1.01e-94 | 201 | 817 | 22 | 667 | LeechIntramolecular Trans-Sialidase Complexed With Dana [Macrobdella decora],1SLL_A Sialidase L From Leech Macrobdella Decora [Macrobdella decora],2SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac, The Reaction Product [Macrobdella decora],3SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac Prepared By Soaking With 3'-Sialyllactose [Macrobdella decora],4SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2- Propenyl-Neu5ac, An Inactive Substrate Analogue [Macrobdella decora] |
| 3H72_A | 1.08e-85 | 370 | 820 | 1 | 471 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P29767 | 2.11e-316 | 2 | 1006 | 3 | 1013 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| Q27701 | 5.70e-94 | 125 | 817 | 28 | 747 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| P62576 | 3.24e-93 | 182 | 829 | 116 | 796 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| P62575 | 3.24e-93 | 182 | 829 | 116 | 796 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
| Q54727 | 7.73e-37 | 197 | 811 | 51 | 682 | Sialidase B OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=nanB PE=1 SV=2 |
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 |
|---|---|---|---|---|---|
| 0.000301 | 0.999050 | 0.000169 | 0.000172 | 0.000153 | 0.000137 |
