Species | Pythium aphanidermatum | |||||||||||
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Lineage | Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum | |||||||||||
CAZyme ID | EPrPAT00000017276-p1 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase 110 kDa subunit. | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT41 | 66 | 742 | 1.5e-116 | 0.6638297872340425 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
226428 | Spy | 4.62e-99 | 251 | 733 | 149 | 614 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
404688 | Glyco_transf_41 | 1.61e-74 | 291 | 726 | 1 | 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. |
276809 | TPR | 2.47e-13 | 157 | 235 | 19 | 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. |
223533 | TPR | 4.51e-13 | 51 | 264 | 87 | 291 | Tetratricopeptide (TPR) repeat [General function prediction only]. |
276809 | TPR | 1.23e-12 | 778 | 867 | 8 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.38e-112 | 49 | 572 | 30 | 559 | |
9.88e-97 | 366 | 733 | 17 | 370 | |
3.10e-95 | 174 | 744 | 87 | 664 | |
2.08e-94 | 55 | 733 | 14 | 654 | |
8.45e-94 | 366 | 736 | 24 | 380 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.16e-63 | 171 | 707 | 22 | 533 | Structure and 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] |
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2.16e-63 | 171 | 707 | 22 | 533 | Xanthomonas campestris 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] |
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5.72e-57 | 291 | 730 | 158 | 702 | Crystal structure of the O-GlcNAc transferase Asn648Tyr mutation [Homo sapiens] |
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9.43e-57 | 291 | 730 | 152 | 696 | The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens] |
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9.57e-57 | 291 | 730 | 153 | 697 | The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.17e-70 | 291 | 730 | 508 | 948 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1 |
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3.88e-55 | 291 | 730 | 476 | 1020 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2 |
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9.04e-55 | 291 | 730 | 476 | 1020 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2 |
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1.20e-54 | 291 | 730 | 476 | 1020 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3 |
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2.79e-54 | 291 | 730 | 476 | 1020 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Sus scrofa OX=9823 GN=OGT PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.829125 | 0.170873 |
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