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CAZyme Information: MGYG000003711_02999
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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 | Stenotrophomonas maltophilia_AQ | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia_AQ | |||||||||||
| CAZyme ID | MGYG000003711_02999 | |||||||||||
| CAZy Family | GT41 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 15589; End: 17295 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT41 | 6 | 557 | 8.3e-121 | 0.6354609929078014 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3914 | Spy | 9.27e-105 | 25 | 559 | 75 | 617 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
| pfam13844 | Glyco_transf_41 | 2.38e-64 | 202 | 549 | 79 | 543 | 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 | 9.03e-11 | 23 | 115 | 3 | 95 | 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. |
| sd00006 | TPR | 3.41e-07 | 13 | 81 | 27 | 95 | 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. |
| TIGR02917 | PEP_TPR_lipo | 1.75e-06 | 13 | 175 | 559 | 724 | putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBO50411.1 | 0.0 | 1 | 564 | 1 | 564 |
| QGL74794.1 | 0.0 | 1 | 564 | 1 | 564 |
| ACF50425.1 | 0.0 | 1 | 564 | 1 | 564 |
| ALA81283.1 | 0.0 | 1 | 566 | 1 | 566 |
| QDY47811.1 | 0.0 | 1 | 568 | 1 | 568 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2JLB_A | 6.11e-261 | 9 | 565 | 11 | 568 | 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] |
| 2VSN_A | 4.98e-260 | 9 | 565 | 11 | 568 | 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] |
| 5HGV_A | 5.50e-46 | 202 | 552 | 232 | 697 | 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] |
| 6IBO_A | 5.69e-46 | 202 | 552 | 236 | 701 | Catalyticdeficiency of O-GlcNAc transferase leads to X-linked intellectual disability [Homo sapiens] |
| 5NPR_A | 7.36e-46 | 202 | 552 | 230 | 695 | Thehuman O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9M8Y0 | 4.12e-55 | 136 | 541 | 508 | 936 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1 |
| O18158 | 2.02e-45 | 204 | 556 | 663 | 1128 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase OS=Caenorhabditis elegans OX=6239 GN=ogt-1 PE=1 SV=2 |
| Q27HV0 | 4.51e-45 | 202 | 552 | 554 | 1019 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Sus scrofa OX=9823 GN=OGT PE=2 SV=1 |
| P56558 | 6.00e-45 | 202 | 552 | 544 | 1009 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Rattus norvegicus OX=10116 GN=Ogt PE=1 SV=1 |
| Q8CGY8 | 8.18e-45 | 202 | 552 | 554 | 1019 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 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 |
|---|---|---|---|---|---|
| 1.000028 | 0.000012 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |