Species | Stenotrophomonas maltophilia_F | |||||||||||
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Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia_F | |||||||||||
CAZyme ID | MGYG000002481_00369 | |||||||||||
CAZy Family | GT41 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 27953; End: 29659 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT41 | 6 | 557 | 1.6e-119 | 0.6354609929078014 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3914 | Spy | 5.56e-103 | 25 | 559 | 75 | 617 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
pfam13844 | Glyco_transf_41 | 8.64e-61 | 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 | 1.68e-09 | 7 | 81 | 21 | 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 | 7.59e-08 | 23 | 99 | 3 | 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. |
NF033920 | C39_PA2778_fam | 1.43e-06 | 7 | 86 | 176 | 255 | PA2778 family cysteine peptidase. Members of this family are MEROPS classification C39 family cysteine peptidases, a group that includes many processing enzyme for peptide natural products such as lantibiotics and other bacteriocins. This family, more specifically, includes PA2778 as found in Pseudomonas aeruginosa. All members of the defining seed alignment are encoded in the vicinity of a homolog of PA2779 (see HMM NF033919). Note that the C-terminal region consists largely of tetratricopeptide repeats (TPR), so classification using this HMM must be based on comparing the top domain score to the second gathering threshold (GA2). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWB77156.1 | 0.0 | 1 | 568 | 1 | 568 |
VEF37334.1 | 0.0 | 1 | 568 | 1 | 568 |
CCH11333.1 | 0.0 | 1 | 568 | 1 | 568 |
QGL83384.1 | 0.0 | 1 | 568 | 1 | 568 |
QCB33232.1 | 0.0 | 1 | 568 | 1 | 568 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2JLB_A | 4.97e-248 | 10 | 565 | 12 | 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 | 4.05e-247 | 10 | 565 | 12 | 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 | 4.15e-44 | 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 | 4.28e-44 | 202 | 552 | 236 | 701 | Catalyticdeficiency of O-GlcNAc transferase leads to X-linked intellectual disability [Homo sapiens] |
5NPR_A | 5.55e-44 | 202 | 552 | 230 | 695 | Thehuman O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9M8Y0 | 1.39e-56 | 204 | 549 | 592 | 944 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1 |
O18158 | 4.58e-46 | 204 | 556 | 663 | 1128 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase OS=Caenorhabditis elegans OX=6239 GN=ogt-1 PE=1 SV=2 |
P56558 | 2.12e-43 | 202 | 552 | 544 | 1009 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Rattus norvegicus OX=10116 GN=Ogt PE=1 SV=1 |
Q27HV0 | 2.88e-43 | 202 | 552 | 554 | 1019 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Sus scrofa OX=9823 GN=OGT PE=2 SV=1 |
P81436 | 7.01e-43 | 202 | 552 | 554 | 1019 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000029 | 0.000012 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |
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