Species | Faecalibacterium prausnitzii_D | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_D | |||||||||||
CAZyme ID | MGYG000002272_02497 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 45525; End: 46526 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 5 | 178 | 7e-32 | 0.9941176470588236 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04186 | GT_2_like_c | 1.86e-58 | 6 | 214 | 1 | 164 | Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families. |
COG1216 | GT2 | 2.35e-56 | 1 | 301 | 2 | 303 | Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]. |
pfam00535 | Glycos_transf_2 | 3.03e-31 | 5 | 174 | 1 | 164 | Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. |
cd00761 | Glyco_tranf_GTA_type | 6.58e-30 | 6 | 203 | 1 | 153 | Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities. |
cd02525 | Succinoglycan_BP_ExoA | 6.86e-24 | 3 | 214 | 1 | 207 | ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ATP00751.1 | 2.15e-234 | 3 | 333 | 2 | 332 |
QIA43524.1 | 2.15e-234 | 3 | 333 | 2 | 332 |
ATL90949.1 | 4.33e-234 | 3 | 333 | 2 | 332 |
AXA81626.1 | 1.14e-229 | 3 | 333 | 2 | 332 |
AXB29301.1 | 1.68e-229 | 1 | 333 | 1 | 333 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5HEA_A | 7.93e-12 | 5 | 104 | 8 | 107 | CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213] |
1H7L_A | 7.88e-08 | 3 | 202 | 2 | 193 | dTDP-MAGNESIUMCOMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1H7Q_A dTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1QG8_A Native (Magnesium-Containing) Spsa From Bacillus Subtilis [Bacillus subtilis],1QGQ_A Udp-manganese Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis],1QGS_A Udp-Magnesium Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis] |
6P61_A | 6.75e-07 | 5 | 196 | 16 | 182 | Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197] |
3L7I_A | 7.78e-06 | 1 | 91 | 1 | 93 | Structureof the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_B Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_C Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_D Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A] |
3L7J_A | 7.78e-06 | 1 | 91 | 1 | 93 | ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P9WMY3 | 7.82e-12 | 17 | 221 | 18 | 242 | N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2 |
P9WMY2 | 7.82e-12 | 17 | 221 | 18 | 242 | N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2 |
Q8NUI7 | 9.90e-12 | 5 | 239 | 50 | 276 | Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain MW2) OX=196620 GN=icaA PE=3 SV=1 |
Q6G608 | 9.90e-12 | 5 | 239 | 50 | 276 | Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=icaA PE=3 SV=1 |
Q6GDD8 | 1.33e-11 | 5 | 239 | 50 | 276 | Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=icaA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000047 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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