Species | Batrachochytrium salamandrivorans | |||||||||||
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Lineage | Chytridiomycota; Chytridiomycetes; ; NA; Batrachochytrium; Batrachochytrium salamandrivorans | |||||||||||
CAZyme ID | OON05970.1 | |||||||||||
CAZy Family | GH76 | |||||||||||
CAZyme Description | Glyco_trans_2-like domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1S8VUG0] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 440 | 634 | 3.1e-23 | 0.9187817258883249 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
404513 | Glyco_trans_2_3 | 3.76e-23 | 440 | 616 | 1 | 173 | Glycosyl transferase family group 2. Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis. |
224136 | BcsA | 1.50e-09 | 311 | 671 | 11 | 390 | Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility]. |
236669 | PRK10263 | 2.79e-06 | 89 | 191 | 739 | 843 | DNA translocase FtsK; Provisional |
367362 | Glutenin_hmw | 3.33e-06 | 86 | 257 | 535 | 706 | High molecular weight glutenin subunit. Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. |
367362 | Glutenin_hmw | 4.80e-05 | 83 | 256 | 374 | 549 | High molecular weight glutenin subunit. Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
5.46e-94 | 273 | 699 | 797 | 1229 | |
9.76e-85 | 273 | 699 | 629 | 1070 | |
2.34e-83 | 273 | 699 | 626 | 1067 | |
2.09e-81 | 273 | 699 | 627 | 1068 | |
2.09e-81 | 273 | 699 | 627 | 1068 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.74e-30 | 323 | 699 | 60 | 449 | Beta-1,4-mannosyltransferase egh OS=Drosophila melanogaster OX=7227 GN=egh PE=2 SV=1 |
|
1.55e-24 | 415 | 699 | 157 | 450 | Beta-1,4-mannosyltransferase bre-3 OS=Caenorhabditis elegans OX=6239 GN=bre-3 PE=2 SV=2 |
|
2.79e-24 | 415 | 699 | 157 | 450 | Beta-1,4-mannosyltransferase bre-3 OS=Caenorhabditis briggsae OX=6238 GN=bre-3 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000061 | 0.000000 |
Start | End |
---|---|
276 | 298 |
318 | 340 |
595 | 617 |
627 | 649 |
656 | 678 |
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