Species | Bacteroides sp900553815 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900553815 | |||||||||||
CAZyme ID | MGYG000004185_01381 | |||||||||||
CAZy Family | GT80 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 19934; End: 21409 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT80 | 313 | 480 | 6.7e-32 | 0.46174142480211083 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam11477 | PM0188 | 3.03e-05 | 398 | 467 | 284 | 353 | 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. |
cd14948 | BACON | 2.13e-04 | 44 | 120 | 9 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBL01105.1 | 7.78e-138 | 37 | 490 | 32 | 497 |
BBL09010.1 | 2.50e-53 | 304 | 490 | 1 | 188 |
BBL11802.1 | 2.50e-53 | 304 | 490 | 1 | 188 |
BAF92026.1 | 1.07e-11 | 235 | 474 | 229 | 471 |
AWK81336.1 | 3.29e-11 | 233 | 474 | 224 | 467 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2Z4T_A | 3.91e-13 | 235 | 474 | 229 | 471 | CrystalStructure of Vibrionaceae Photobacterium sp. JT-ISH-224 2,6-sialyltransferase in a Ternary Complex with Donor Product CMP and Accepter Substrate Lactose [Photobacterium sp. JT-ISH-224] |
4R9V_A | 1.15e-12 | 233 | 474 | 133 | 376 | Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae] |
4R83_A | 1.57e-12 | 233 | 474 | 230 | 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 |
---|---|---|---|---|---|
1.000051 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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