Species | Ascosphaera apis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Ascosphaeraceae; Ascosphaera; Ascosphaera apis | |||||||||||
CAZyme ID | KZZ89866.1 | |||||||||||
CAZy Family | GT90 | |||||||||||
CAZyme Description | TPR Domain containing protein [Source:UniProtKB/TrEMBL;Acc:A0A167XBC6] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
404688 | Glyco_transf_41 | 1.86e-102 | 1457 | 1918 | 28 | 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. |
226428 | Spy | 7.57e-61 | 1510 | 1927 | 260 | 616 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
276809 | TPR | 7.93e-14 | 801 | 883 | 8 | 90 | 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 | 1.91e-13 | 1197 | 1274 | 20 | 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. |
276809 | TPR | 3.88e-13 | 1212 | 1290 | 1 | 79 | 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 |
---|---|---|---|---|---|
0.0 | 340 | 1939 | 217 | 1646 | |
0.0 | 656 | 1939 | 362 | 1607 | |
0.0 | 119 | 1939 | 78 | 1642 | |
0.0 | 266 | 1939 | 131 | 1696 | |
0.0 | 266 | 1939 | 131 | 1696 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.52e-76 | 1457 | 1946 | 184 | 724 | Chain AAA, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens] |
|
3.93e-76 | 1457 | 1946 | 206 | 746 | Human OGT in complex with UDP and fused substrate peptide (HCF1) [Homo sapiens] |
|
3.93e-76 | 1457 | 1946 | 206 | 746 | Human OGT in complex with UDP and fused substrate peptide (Tab1) [Homo sapiens] |
|
5.04e-76 | 1457 | 1936 | 179 | 710 | The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens] |
|
5.14e-76 | 1457 | 1936 | 180 | 711 | 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 |
---|---|---|---|---|---|---|
6.05e-88 | 1457 | 1934 | 535 | 960 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1 |
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4.90e-74 | 1457 | 1946 | 503 | 1043 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2 |
|
1.56e-73 | 1457 | 1946 | 503 | 1043 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2 |
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2.08e-73 | 1457 | 1946 | 503 | 1043 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3 |
|
4.95e-73 | 1457 | 1946 | 503 | 1043 | 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 |
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1.000033 | 0.000000 |
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