Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; | |||||||||||
CAZyme ID | MGYG000001219_01795 | |||||||||||
CAZy Family | CBM67 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 2; End: 2896 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam18565 | Glyco_hydro2_C5 | 4.65e-33 | 235 | 339 | 8 | 103 | Glycoside hydrolase family 2 C-terminal domain 5. Domain 5 is found in dimeric beta-D-galactosidase from Paracoccus sp. 32d, which contributes to stabilization of the functional dimer. It is suggested that the location of this domain 5, may be one of the factors responsible for the creation of a functional dimer and cold-adaptation of this enzyme. |
pfam13306 | LRR_5 | 2.43e-10 | 870 | 930 | 44 | 102 | Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis. |
sd00036 | LRR_3 | 2.72e-10 | 870 | 932 | 47 | 108 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
sd00036 | LRR_3 | 1.23e-09 | 871 | 931 | 71 | 130 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
sd00036 | LRR_3 | 7.29e-09 | 870 | 931 | 24 | 84 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AMN35793.1 | 6.13e-144 | 15 | 761 | 573 | 1304 |
QAS60578.1 | 5.82e-142 | 13 | 745 | 571 | 1288 |
AYE35175.1 | 5.82e-142 | 13 | 745 | 571 | 1288 |
AMN32811.1 | 1.15e-141 | 15 | 737 | 573 | 1281 |
AWS26051.1 | 2.22e-141 | 15 | 737 | 573 | 1281 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7NIT_A | 1.90e-102 | 15 | 745 | 558 | 1288 | ChainA, Beta-galactosidase [Bifidobacterium bifidum],7NIT_B Chain B, Beta-galactosidase [Bifidobacterium bifidum],7NIT_C Chain C, Beta-galactosidase [Bifidobacterium bifidum],7NIT_D Chain D, Beta-galactosidase [Bifidobacterium bifidum],7NIT_E Chain E, Beta-galactosidase [Bifidobacterium bifidum],7NIT_F Chain F, Beta-galactosidase [Bifidobacterium bifidum] |
5DMY_A | 1.43e-71 | 15 | 363 | 564 | 904 | Beta-galactosidase- construct 33-930 [Bifidobacterium bifidum],5DMY_B Beta-galactosidase - construct 33-930 [Bifidobacterium bifidum],5DMY_C Beta-galactosidase - construct 33-930 [Bifidobacterium bifidum] |
6QUB_A | 1.15e-69 | 15 | 349 | 558 | 883 | Truncatedbeta-galactosidase III from Bifidobacterium bifidum in complex with galactose [Bifidobacterium bifidum],6QUC_A Truncated beta-galactosidase III from Bifidobacterium bifidum [Bifidobacterium bifidum],6QUC_B Truncated beta-galactosidase III from Bifidobacterium bifidum [Bifidobacterium bifidum],6QUD_A 2-deoxy-galactose reaction intermediate of a Truncated beta-galactosidase III from Bifidobacterium bifidum [Bifidobacterium bifidum] |
6QUB_B | 2.37e-68 | 15 | 345 | 535 | 856 | Truncatedbeta-galactosidase III from Bifidobacterium bifidum in complex with galactose [Bifidobacterium bifidum] |
4CU6_A | 3.91e-48 | 18 | 347 | 542 | 849 | Unravellingthe multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA [Streptococcus pneumoniae TIGR4],4CU7_A Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA [Streptococcus pneumoniae TIGR4],4CU8_A Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA [Streptococcus pneumoniae TIGR4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A7LXS9 | 2.47e-34 | 9 | 345 | 574 | 851 | Beta-galactosidase BoGH2A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02645 PE=1 SV=1 |
T2KM09 | 8.90e-12 | 16 | 145 | 548 | 665 | Putative beta-glucuronidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22050 PE=2 SV=2 |
A0A401ETL2 | 8.86e-09 | 474 | 745 | 1073 | 1366 | Exo-beta-1,6-galactobiohydrolase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=bl1,6Gal PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000050 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.