You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000000074_02232
You are here: Home > Sequence: MGYG000000074_02232
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Alistipes onderdonkii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes onderdonkii | |||||||||||
| CAZyme ID | MGYG000000074_02232 | |||||||||||
| CAZy Family | GT80 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 449391; End: 450887 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT80 | 335 | 480 | 1.1e-36 | 0.40897097625329815 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14948 | BACON | 3.99e-08 | 39 | 114 | 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. |
| pfam11477 | PM0188 | 0.002 | 404 | 473 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBL01105.1 | 0.0 | 1 | 498 | 1 | 498 |
| BBL09010.1 | 6.51e-132 | 310 | 498 | 1 | 189 |
| BBL11802.1 | 6.51e-132 | 310 | 498 | 1 | 189 |
| AWK81336.1 | 5.13e-15 | 238 | 480 | 224 | 467 |
| BAA25316.1 | 1.57e-13 | 232 | 480 | 215 | 467 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4R9V_A | 2.82e-15 | 232 | 480 | 124 | 376 | Crystalstructure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain [Photobacterium damselae] |
| 4R83_A | 4.21e-15 | 232 | 480 | 221 | 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] |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000184 | 0.110681 | 0.888991 | 0.000055 | 0.000054 | 0.000043 |