Species | Bacteroides gallinarum | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides gallinarum | |||||||||||
CAZyme ID | MGYG000001661_02360 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 47853; End: 50300 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 380 | 584 | 4.8e-63 | 0.9890710382513661 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14948 | BACON | 7.50e-17 | 31 | 122 | 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. |
pfam13004 | BACON | 1.19e-06 | 65 | 122 | 4 | 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. |
cd14948 | BACON | 3.16e-06 | 131 | 218 | 2 | 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. |
pfam19190 | BACON_2 | 3.34e-06 | 31 | 125 | 2 | 91 | 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 | 3.90e-04 | 242 | 304 | 9 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT78065.1 | 0.0 | 1 | 814 | 1 | 794 |
ALJ48967.1 | 0.0 | 1 | 814 | 1 | 794 |
SCV08385.1 | 0.0 | 1 | 814 | 1 | 794 |
QRQ55777.1 | 0.0 | 1 | 814 | 1 | 794 |
QGT73513.1 | 0.0 | 1 | 814 | 1 | 794 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B8NQQ7 | 5.56e-38 | 318 | 798 | 17 | 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 |
Q2UB83 | 5.56e-38 | 318 | 798 | 17 | 414 | Probable pectate lyase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyC PE=3 SV=1 |
Q5B297 | 1.95e-37 | 317 | 798 | 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 |
Q0CLG7 | 1.57e-36 | 312 | 798 | 11 | 414 | Probable pectate lyase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyC PE=3 SV=1 |
Q4WL88 | 6.02e-35 | 316 | 798 | 16 | 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 | 1.000044 | 0.000000 | 0.000000 | 0.000000 |
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