Species | Pythium aphanidermatum | |||||||||||
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Lineage | Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum | |||||||||||
CAZyme ID | EPrPAT00000013866-p1 | |||||||||||
CAZy Family | AA17 | |||||||||||
CAZyme Description | UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase. | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT41 | 117 | 788 | 4.5e-104 | 0.6085106382978723 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
226428 | Spy | 1.27e-86 | 178 | 779 | 29 | 610 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
404688 | Glyco_transf_41 | 3.71e-67 | 335 | 776 | 2 | 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 | 1.10e-11 | 146 | 237 | 3 | 93 | 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. |
276809 | TPR | 2.58e-11 | 112 | 206 | 4 | 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 | 3.40e-07 | 115 | 350 | 30 | 290 | Tetratricopeptide (TPR) repeat [General function prediction only]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
5.12e-86 | 331 | 800 | 180 | 631 | |
1.05e-84 | 331 | 800 | 587 | 1038 | |
1.77e-84 | 151 | 789 | 25 | 657 | |
4.86e-84 | 331 | 800 | 607 | 1058 | |
4.94e-83 | 411 | 779 | 16 | 366 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.72e-51 | 281 | 768 | 97 | 544 | 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] |
|
5.06e-51 | 281 | 768 | 97 | 544 | 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] |
|
5.73e-50 | 328 | 777 | 146 | 693 | The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens] |
|
5.79e-50 | 328 | 777 | 147 | 694 | The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens] |
|
6.12e-50 | 328 | 777 | 152 | 699 | Chain A, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_B Chain B, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_C Chain C, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_D Chain D, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE4_A Structure of human O-GlcNAc transferase and its complex with a peptide substrate [Homo sapiens],3PE4_C Structure of human O-GlcNAc transferase and its complex with a peptide substrate [Homo sapiens],3TAX_A A Neutral Diphosphate Mimic Crosslinks the Active Site of Human O-GlcNAc Transferase [Homo sapiens],3TAX_C A Neutral Diphosphate Mimic Crosslinks the Active Site of Human O-GlcNAc Transferase [Homo sapiens],4AY5_A Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_B Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_C Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_D Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY6_A Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_B Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_C Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_D Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4CDR_A Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_B Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_C Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_D Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4GYW_A Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide [Homo sapiens],4GYW_C Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide [Homo sapiens],4GYY_A Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate [Homo sapiens],4GYY_C Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate [Homo sapiens],4GZ3_A Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide [Homo sapiens],4GZ3_C Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide [Homo sapiens],4GZ5_A Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_B Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_C Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_D Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ6_A Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_B Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_C Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_D Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4N39_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) [Homo sapiens],4N3A_A Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (1-26)E10A [Homo sapiens],4N3B_A Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc [Homo sapiens],4N3C_A Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26) and UDP-GlcNAc [Homo sapiens],4XI9_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_B Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_C Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_D Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XIF_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_B Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_C Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_D Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],5BNW_A The active site of O-GlcNAc transferase imposes constraints on substrate sequence [Homo sapiens],5C1D_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RB2L) [Homo sapiens],5VIE_A Chain A, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],5VIE_C Chain C, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],5VIF_A Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase [Homo sapiens],6E37_A O-GlcNAc Transferase in complex with covalent inhibitor [Homo sapiens],6MA1_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 4a [Homo sapiens],6MA2_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor ent-1a [Homo sapiens],6MA3_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 2a [Homo sapiens],6MA4_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 3a [Homo sapiens],6MA5_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 1a [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.84e-63 | 335 | 779 | 509 | 947 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1 |
|
5.10e-49 | 328 | 777 | 470 | 1017 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2 |
|
6.81e-49 | 328 | 777 | 470 | 1017 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Sus scrofa OX=9823 GN=OGT PE=2 SV=1 |
|
1.62e-48 | 328 | 777 | 470 | 1017 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2 |
|
2.17e-48 | 328 | 777 | 470 | 1017 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000044 | 0.000000 |
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