Species | UBA5905 sp900764115 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA5905; UBA5905 sp900764115 | |||||||||||
CAZyme ID | MGYG000002128_01166 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 606; End: 2522 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4193 | LytD | 8.35e-27 | 161 | 392 | 24 | 245 | Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]. |
cd14256 | Dockerin_I | 3.04e-15 | 575 | 631 | 1 | 57 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
pfam00404 | Dockerin_1 | 1.37e-14 | 576 | 630 | 1 | 55 | Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. |
pfam12733 | Cadherin-like | 1.23e-12 | 421 | 493 | 5 | 89 | Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain. |
pfam08239 | SH3_3 | 6.31e-11 | 46 | 99 | 1 | 54 | Bacterial SH3 domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CCO04280.1 | 1.52e-123 | 46 | 508 | 37 | 531 |
AEN96074.1 | 5.63e-114 | 26 | 611 | 110 | 734 |
QRV21758.1 | 1.63e-98 | 10 | 602 | 6 | 749 |
ADL03932.1 | 1.63e-98 | 10 | 602 | 6 | 749 |
CBK91761.1 | 2.03e-98 | 38 | 611 | 150 | 761 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2KRS_A | 4.10e-09 | 40 | 100 | 3 | 61 | SolutionNMR structure of SH3 domain from CPF_0587 (fragment 415-479) from Clostridium perfringens. Northeast Structural Genomics Consortium (NESG) Target CpR74A. [Clostridium perfringens] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.382877 | 0.610827 | 0.004683 | 0.000784 | 0.000366 | 0.000464 |
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