Species | Alistipes provencensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes provencensis | |||||||||||
CAZyme ID | MGYG000001546_00947 | |||||||||||
CAZy Family | GT80 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 1172116; End: 1173621 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT80 | 338 | 479 | 4.7e-36 | 0.39841688654353563 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14948 | BACON | 4.85e-13 | 34 | 116 | 6 | 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. |
pfam11477 | PM0188 | 3.86e-04 | 405 | 476 | 284 | 355 | Sialyltransferase PMO188. PMO188 is a sialyltransferase from P.multocida. It transfers sialic acid from cytidine 5'-monophosphonuraminic acid to an acceptor sugar. It has important catalytic residues such as Asp141, His311, Glu338, Ser355 and Ser356. |
pfam13004 | BACON | 6.04e-04 | 62 | 116 | 4 | 61 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBL01105.1 | 7.60e-245 | 1 | 499 | 1 | 498 |
BBL09010.1 | 1.21e-90 | 311 | 499 | 1 | 189 |
BBL11802.1 | 1.21e-90 | 311 | 499 | 1 | 189 |
AWK81336.1 | 1.27e-08 | 239 | 481 | 224 | 467 |
BAA25316.1 | 6.18e-08 | 339 | 481 | 315 | 467 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4R9V_A | 1.48e-09 | 339 | 481 | 224 | 376 | Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae] |
4R83_A | 1.86e-09 | 339 | 481 | 321 | 473 | Crystalstructure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R83_B Crystal structure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R83_C Crystal structure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R83_D Crystal structure of Sialyltransferase from Photobacterium damsela [Photobacterium damselae],4R84_A Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae],4R84_B Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae],4R84_C Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae],4R84_D Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound [Photobacterium damselae] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000115 | 0.045308 | 0.954526 | 0.000025 | 0.000029 | 0.000023 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.