Species | Aspergillus tubingensis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis | |||||||||||
CAZyme ID | ASPTUDRAFT_933791-t33_1-p1 | |||||||||||
CAZy Family | GT69 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH35 | 46 | 316 | 1.3e-49 | 0.758957654723127 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
402180 | BetaGal_dom2 | 2.73e-63 | 344 | 519 | 1 | 180 | Beta-galactosidase, domain 2. This is the second domain of the five-domain beta-galactosidase enzyme that altogether catalyzes the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel beta-strands and an alpha-helix at its C-terminus. The fold of this domain appears to be unique. In addition, the last seven strands of the domain form a subdomain with an immunoglobulin-like (I-type Ig) fold in which the first strand is divided between the two beta-sheets. In penicillin spp this strand is interrupted by a 12-residue insertion which forms an additional edge-strand to the second beta-sheet of the sub-domain. The remainder of the second domain forms a series of beta-hairpins at its N-terminus, four strands of which are contiguous with part of the Ig-like sub-domain, forming in total a seven-stranded antiparallel beta-sheet. This domain is associated with family Glyco_hydro_35, pfam01301, which is N-terminal to it, but itself has no metazoan members. |
198097 | BetaGal_dom2 | 4.44e-42 | 343 | 520 | 1 | 182 | Beta-galactosidase, domain 2. This is the second domain of the five-domain beta-galactosidase enzyme that altogether catalyses the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel beta-strands and an alpha-helix at its C terminus. The fold of this domain appears to be unique. In addition, the last seven strands of the domain form a subdomain with an immunoglobulin-like (I-type Ig) fold in which the first strand is divided between the two beta-sheets. In penicillin spp this strand is interrupted by a 12-residue insertion which forms an additional edge-strand to the second beta-sheet of the sub-domain. The remainder of the second domain forms a series of beta-hairpins at its N terminus, four strands of which are contiguous with part of the Ig-like sub-domain, forming in total a seven-stranded antiparallel beta-sheet. This domain is associated with family Glyco_hydro_35, which is N-terminal to it, but itself has no metazoan members. |
396048 | Glyco_hydro_35 | 1.44e-40 | 46 | 322 | 41 | 302 | Glycosyl hydrolases family 35. |
404274 | BetaGal_dom4_5 | 8.82e-37 | 799 | 913 | 1 | 111 | Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold. |
404274 | BetaGal_dom4_5 | 1.31e-26 | 629 | 741 | 1 | 111 | Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 952 | 1 | 993 | |
0.0 | 77 | 952 | 1 | 886 | |
0.0 | 1 | 952 | 32 | 1009 | |
0.0 | 19 | 952 | 18 | 982 | |
0.0 | 13 | 943 | 7 | 973 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.94e-140 | 30 | 922 | 6 | 943 | Native structure of beta-galactosidase from Penicillium sp. [Penicillium sp.],1XC6_A Native Structure Of Beta-Galactosidase from Penicillium sp. in complex with Galactose [Penicillium sp.] |
|
1.48e-135 | 30 | 922 | 46 | 979 | Structure Of Beta-galactosidase From Aspergillus Niger [Aspergillus niger CBS 513.88] |
|
4.05e-135 | 30 | 922 | 46 | 979 | STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 3-b-Galactopyranosyl glucose [Aspergillus niger CBS 513.88],5IHR_A Structure Of E298q-beta-galactosidase From Aspergillus Niger In Complex With Allolactose [Aspergillus niger CBS 513.88],5JUV_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 6-b-Galactopyranosyl galactose [Aspergillus niger CBS 513.88],5MGC_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 4-Galactosyl-lactose [Aspergillus niger CBS 513.88],5MGD_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 6-Galactosyl-lactose [Aspergillus niger CBS 513.88] |
|
6.27e-125 | 30 | 922 | 26 | 975 | Chain A, Beta-galactosidase [Trichoderma reesei],3OGR_A Chain A, Beta-galactosidase [Trichoderma reesei],3OGS_A Chain A, Beta-galactosidase [Trichoderma reesei],3OGV_A Chain A, Beta-galactosidase [Trichoderma reesei] |
|
9.13e-125 | 30 | 922 | 46 | 977 | Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose [Aspergillus oryzae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 30 | 947 | 32 | 979 | Probable beta-galactosidase C OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=lacC PE=3 SV=1 |
|
0.0 | 15 | 943 | 9 | 974 | Probable beta-galactosidase C OS=Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) OX=665079 GN=lacC PE=3 SV=1 |
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0.0 | 24 | 952 | 26 | 983 | Probable beta-galactosidase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=lacC PE=3 SV=1 |
|
0.0 | 18 | 952 | 20 | 984 | Probable beta-galactosidase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=lacC PE=3 SV=1 |
|
0.0 | 1 | 947 | 1 | 976 | Probable beta-galactosidase C OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=lacC PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000207 | 0.999764 | CS pos: 19-20. Pr: 0.9795 |
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