Species | Haemophilus_D sp900756155 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Pasteurellaceae; Haemophilus_D; Haemophilus_D sp900756155 | |||||||||||
CAZyme ID | MGYG000000993_00441 | |||||||||||
CAZy Family | GT41 | |||||||||||
CAZyme Description | UDP-glucose:protein N-beta-glucosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 63767; End: 65785 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT41 | 268 | 645 | 1.4e-36 | 0.49361702127659574 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam18254 | HMw1_D2 | 4.65e-59 | 158 | 245 | 1 | 88 | HMW1 domain 2. This domain is found in Actinobacillus pleuropneumoniae HMW1C (ApHMW1C). HMW1 adhesin is an N-linked glycoprotein that mediates adherence to respiratory epithelium through N-glycosylation of protein acceptor sites and O-glycosylation of sugar acceptor sites. This domain forms an all alpha domain (AAD) when combined with the N-terminal domain. The AAD interacts extensively with the C-terminal GT-B fold in order to create a unique groove with the potential to accommodate the acceptor protein. |
pfam18071 | HMW1C_N | 7.11e-48 | 8 | 153 | 2 | 143 | HMW1C N-terminal. This is the N-terminal domain found in Actinobacillus pleuropneumoniae HMW1C (ApHMW1C). HMW1 adhesin is an N-linked glycoprotein that mediates adherence to respiratory epithelium through N-glycosylation of protein acceptor sites an O-glycosylation of sugar acceptor sites. The N-terminal domain forms an all alpha domain (AAD) when combined with the domain spanning from residue 154 to residue 245. The AAD interacts extensively with the C-terminal GT-B fold in order to create unique groove with potential to accommodate the acceptor protein. |
COG3914 | Spy | 1.23e-14 | 348 | 619 | 338 | 620 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QAT96181.1 | 0.0 | 1 | 631 | 1 | 631 |
QOR15805.1 | 0.0 | 1 | 631 | 1 | 631 |
QOR13984.1 | 0.0 | 1 | 631 | 1 | 631 |
CBW14699.1 | 0.0 | 1 | 631 | 1 | 631 |
QOR23145.1 | 0.0 | 1 | 631 | 1 | 631 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3Q3E_A | 0.0 | 3 | 621 | 13 | 631 | Crystalstructure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3E_B Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3H_A Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in complex with UDP-GLC [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3H_B Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in complex with UDP-GLC [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3I_A Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in the presence of peptide N1131 [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3I_B Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in the presence of peptide N1131 [Actinobacillus pleuropneumoniae serovar 1 str. 4074] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A3N2T3 | 0.0 | 3 | 621 | 2 | 620 | UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 5b (strain L20) OX=416269 GN=APL_1635 PE=1 SV=1 |
B3H2N2 | 0.0 | 3 | 621 | 2 | 620 | UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 7 (strain AP76) OX=537457 GN=APP7_1697 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000075 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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