You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000003359_03490
You are here: Home > Sequence: MGYG000003359_03490
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 | Paenibacillus_A sp900766135 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900766135 | |||||||||||
| CAZyme ID | MGYG000003359_03490 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 233618; End: 237133 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd04950 | GT4_TuaH-like | 2.53e-34 | 134 | 471 | 8 | 337 | teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. |
| pfam04464 | Glyphos_transf | 3.46e-30 | 800 | 1153 | 5 | 358 | CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase. Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid. |
| COG1887 | TagB | 7.23e-28 | 854 | 1153 | 96 | 384 | CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]. |
| cd03794 | GT4_WbuB-like | 6.54e-10 | 309 | 440 | 185 | 324 | Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase. |
| sd00006 | TPR | 2.83e-09 | 11 | 97 | 11 | 97 | Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AJS60369.1 | 0.0 | 4 | 1166 | 3 | 1155 |
| BAQ14354.1 | 0.0 | 36 | 1156 | 97 | 1221 |
| ADQ45924.1 | 8.45e-172 | 71 | 697 | 245 | 862 |
| AKC63521.1 | 8.37e-170 | 49 | 708 | 111 | 792 |
| AVP60134.1 | 8.37e-170 | 49 | 708 | 111 | 792 |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q2G1B8 | 1.20e-13 | 922 | 1148 | 347 | 554 | Teichoic acid ribitol-phosphate polymerase TarL OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=tarL PE=1 SV=1 |
| Q2G1C2 | 5.52e-13 | 797 | 1148 | 179 | 505 | Teichoic acid ribitol-phosphate polymerase TarK OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=tarK PE=1 SV=1 |
| P27621 | 4.69e-10 | 867 | 1093 | 117 | 322 | Teichoic acid glycerol-phosphate primase OS=Bacillus subtilis (strain 168) OX=224308 GN=tagB PE=1 SV=1 |
| Q8RKJ2 | 3.54e-09 | 902 | 1153 | 373 | 603 | Teichoic acid poly(ribitol-phosphate) polymerase OS=Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) OX=655816 GN=tarL PE=1 SV=1 |
| Q8RKI8 | 1.88e-08 | 872 | 1126 | 120 | 365 | Teichoic acid glycerol-phosphate primase OS=Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) OX=655816 GN=tarB PE=3 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 |
|---|---|---|---|---|---|
| 1.000068 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |