You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000001318_03793
You are here: Home > Sequence: MGYG000001318_03793
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 | Enterobacter cancerogenus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter cancerogenus | |||||||||||
| CAZyme ID | MGYG000001318_03793 | |||||||||||
| CAZy Family | GT41 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 1625524; End: 1629696 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT41 | 42 | 616 | 3.4e-113 | 0.7063829787234043 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3914 | Spy | 2.42e-77 | 14 | 599 | 23 | 618 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
| pfam13844 | Glyco_transf_41 | 2.60e-23 | 234 | 585 | 73 | 540 | Glycosyl transferase family 41. This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyzes the addition of O-GlcNAc to serine and threonine residues. In addition to its function as an O-GlcNAc transferase, human OGT also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1. |
| sd00006 | TPR | 4.58e-09 | 60 | 148 | 8 | 94 | 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. |
| COG0457 | TPR | 6.25e-09 | 45 | 189 | 122 | 268 | Tetratricopeptide (TPR) repeat [General function prediction only]. |
| sd00006 | TPR | 1.43e-08 | 87 | 185 | 1 | 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 |
|---|---|---|---|---|---|
| QZY35339.1 | 0.0 | 1 | 1390 | 1 | 1390 |
| CAD5356562.1 | 0.0 | 1 | 1390 | 1 | 1390 |
| QGG07655.1 | 0.0 | 1 | 1390 | 1 | 1390 |
| BCL43458.1 | 0.0 | 46 | 1390 | 1 | 1345 |
| QGP84426.1 | 0.0 | 1 | 1158 | 1 | 1158 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5DJS_A | 1.46e-80 | 83 | 601 | 5 | 521 | Thermobaculumterrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_B Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_C Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_D Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum] |
| 2VSN_A | 8.07e-40 | 234 | 599 | 201 | 563 | Structureand topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004],2VSN_B Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004] |
| 2JLB_A | 1.95e-39 | 234 | 599 | 201 | 563 | Xanthomonascampestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2JLB_B Xanthomonas campestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2VSY_A Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2VSY_B Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2XGM_A Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGM_B Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGO_A XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGO_B XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGS_A XcOGT in complex with C-UDP [Xanthomonas campestris],2XGS_B XcOGT in complex with C-UDP [Xanthomonas campestris] |
| 5A01_A | 3.55e-25 | 242 | 609 | 235 | 708 | O-GlcNActransferase from Drososphila melanogaster [Drosophila melanogaster],5A01_B O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster],5A01_C O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster] |
| 5HGV_A | 1.46e-24 | 236 | 606 | 228 | 712 | Structureof an O-GlcNAc transferase point mutant, D554N in complex with peptide [Homo sapiens],5HGV_C Structure of an O-GlcNAc transferase point mutant, D554N in complex with peptide [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O82422 | 9.98e-69 | 185 | 605 | 416 | 841 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Hordeum vulgare OX=4513 GN=SPY PE=2 SV=1 |
| Q6YZI0 | 1.95e-68 | 178 | 642 | 409 | 880 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Oryza sativa subsp. japonica OX=39947 GN=SPY PE=2 SV=1 |
| Q8RVB2 | 2.05e-68 | 185 | 605 | 430 | 855 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Solanum lycopersicum OX=4081 GN=SPY PE=2 SV=1 |
| O82039 | 6.70e-68 | 185 | 605 | 430 | 855 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Petunia hybrida OX=4102 GN=SPY PE=2 SV=1 |
| Q96301 | 7.18e-68 | 185 | 638 | 425 | 888 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Arabidopsis thaliana OX=3702 GN=SPY PE=1 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 |
|---|---|---|---|---|---|
| 1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |