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CAZyme Information: MGYG000004140_00889
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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 | UMGS1375 sp900551235 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UMGS1375; UMGS1375 sp900551235 | |||||||||||
| CAZyme ID | MGYG000004140_00889 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 81671; End: 86518 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 394 | 808 | 3.4e-93 | 0.935672514619883 |
| CBM32 | 970 | 1099 | 1.2e-23 | 0.9516129032258065 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 9.46e-77 | 394 | 819 | 3 | 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. |
| pfam00754 | F5_F8_type_C | 4.63e-23 | 967 | 1099 | 1 | 127 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
| pfam13088 | BNR_2 | 2.15e-20 | 585 | 801 | 84 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| COG4409 | NanH | 1.84e-19 | 289 | 804 | 170 | 700 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| cd00057 | FA58C | 4.08e-13 | 968 | 1101 | 14 | 139 | Substituted updates: Jan 31, 2002 |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QJA08933.1 | 1.61e-96 | 274 | 892 | 109 | 743 |
| VEH64880.1 | 2.56e-95 | 356 | 856 | 37 | 566 |
| APZ74275.1 | 7.66e-93 | 354 | 804 | 177 | 630 |
| QIM67783.1 | 8.35e-93 | 274 | 884 | 113 | 766 |
| QQA11681.1 | 2.14e-92 | 354 | 804 | 218 | 671 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2BF6_A | 1.33e-94 | 385 | 804 | 3 | 429 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 5TSP_A | 1.40e-94 | 385 | 804 | 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] |
| 2VK5_A | 1.46e-94 | 385 | 804 | 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] |
| 2VVZ_A | 9.05e-85 | 389 | 841 | 6 | 486 | Structureof the catalytic domain of Streptococcus pneumoniae sialidase NanA [Streptococcus pneumoniae],2VVZ_B Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA [Streptococcus pneumoniae] |
| 2W20_A | 1.22e-84 | 389 | 823 | 4 | 469 | Structureof the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6],2W20_B Structure of the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [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 |
|---|---|---|---|---|---|---|
| P62576 | 5.21e-82 | 335 | 936 | 272 | 877 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| P62575 | 5.21e-82 | 335 | 936 | 272 | 877 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
| P29767 | 3.53e-78 | 317 | 920 | 299 | 929 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| Q27701 | 1.37e-39 | 302 | 805 | 186 | 730 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| Q02834 | 3.29e-24 | 392 | 1103 | 54 | 645 | 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 |
|---|---|---|---|---|---|
| 0.000350 | 0.998867 | 0.000229 | 0.000198 | 0.000164 | 0.000144 |
