Species | Bacteroides ovatus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides ovatus | |||||||||||
CAZyme ID | MGYG000001378_02968 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 79544; End: 81931 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 372 | 577 | 2.7e-64 | 0.994535519125683 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14948 | BACON | 1.19e-17 | 31 | 117 | 2 | 82 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. |
pfam19190 | BACON_2 | 1.18e-07 | 31 | 109 | 2 | 84 | Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions. |
cd14948 | BACON | 3.32e-07 | 129 | 213 | 5 | 83 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. |
pfam13004 | BACON | 1.31e-05 | 57 | 117 | 1 | 60 | Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain. |
pfam18884 | TSP3_bac | 5.05e-04 | 730 | 751 | 1 | 22 | Bacterial TSP3 repeat. This entry contains a novel bacterial thrombospondin type 3 repeat which differs from the typical consensus by containing a glutamate in place of one of the calcium binding aspartate residues. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGT73513.1 | 0.0 | 1 | 795 | 1 | 795 |
QNL41094.1 | 0.0 | 1 | 795 | 1 | 795 |
QUT78065.1 | 0.0 | 1 | 795 | 1 | 795 |
ALJ48967.1 | 0.0 | 1 | 795 | 1 | 795 |
SCV08385.1 | 0.0 | 1 | 795 | 1 | 795 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q0CLG7 | 2.42e-39 | 305 | 778 | 11 | 414 | Probable pectate lyase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyC PE=3 SV=1 |
B8NQQ7 | 2.06e-38 | 309 | 778 | 15 | 414 | Probable pectate lyase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyC PE=3 SV=1 |
B0XMA2 | 7.13e-38 | 311 | 778 | 19 | 415 | Probable pectate lyase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyC PE=3 SV=1 |
Q5B297 | 9.85e-38 | 310 | 778 | 17 | 411 | Probable pectate lyase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyC PE=3 SV=1 |
Q4WL88 | 1.78e-37 | 311 | 778 | 19 | 415 | Probable pectate lyase C OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=plyC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000000 | 1.000051 | 0.000000 | 0.000000 | 0.000000 |
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