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CAZyme Information: MGYG000003016_00013
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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 | Salinicola tamaricis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Halomonadaceae; Salinicola; Salinicola tamaricis | |||||||||||
| CAZyme ID | MGYG000003016_00013 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 15443; End: 16495 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam12038 | DUF3524 | 6.47e-66 | 2 | 169 | 1 | 165 | Domain of unknown function (DUF3524). This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important. |
| cd03801 | GT4_PimA-like | 2.06e-10 | 5 | 325 | 23 | 337 | phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. The members of this family are found mainly in certain bacteria and archaea. |
| COG0438 | RfaB | 5.55e-09 | 191 | 347 | 207 | 374 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd01635 | Glycosyltransferase_GTB-type | 3.78e-06 | 191 | 300 | 118 | 228 | glycosyltransferase family 1 and related proteins with GTB topology. 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. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ABE59474.1 | 1.91e-165 | 1 | 347 | 1 | 347 |
| AJY50875.1 | 1.77e-146 | 1 | 349 | 1 | 355 |
| ATH78968.1 | 1.50e-145 | 1 | 348 | 1 | 349 |
| BCB70053.1 | 1.41e-143 | 1 | 347 | 1 | 348 |
| QGQ70403.1 | 3.02e-142 | 1 | 347 | 1 | 373 |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q568B7 | 1.56e-45 | 1 | 347 | 1 | 419 | Glycosyltransferase-like domain-containing protein 1 OS=Danio rerio OX=7955 GN=gtdc1 PE=2 SV=2 |
| Q9VXN0 | 1.83e-45 | 4 | 320 | 9 | 334 | Glycosyltransferase-like domain-containing protein 1-like OS=Drosophila melanogaster OX=7227 GN=CG15914 PE=2 SV=1 |
| Q4V7R4 | 1.32e-42 | 4 | 348 | 5 | 423 | Glycosyltransferase-like domain-containing protein 1 OS=Xenopus laevis OX=8355 GN=gtdc1 PE=2 SV=1 |
| Q66K99 | 2.66e-40 | 1 | 347 | 1 | 429 | Glycosyltransferase-like domain-containing protein 1 OS=Xenopus tropicalis OX=8364 GN=gtdc1 PE=2 SV=1 |
| Q8BW56 | 4.12e-35 | 1 | 323 | 1 | 410 | Glycosyltransferase-like domain-containing protein 1 OS=Mus musculus OX=10090 GN=Gtdc1 PE=2 SV=2 |
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 |
|---|---|---|---|---|---|
| 0.876046 | 0.123572 | 0.000123 | 0.000100 | 0.000078 | 0.000092 |