Species | Actinobaculum massiliense | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinobaculum; Actinobaculum massiliense | |||||||||||
CAZyme ID | MGYG000003314_00323 | |||||||||||
CAZy Family | GH111 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 202365; End: 206180 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH111 | 202 | 1023 | 1.9e-276 | 0.7965116279069767 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam12733 | Cadherin-like | 2.92e-09 | 228 | 302 | 9 | 87 | 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. |
pfam04886 | PT | 5.44e-07 | 972 | 1006 | 1 | 35 | PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat. |
pfam04886 | PT | 1.44e-06 | 968 | 1002 | 1 | 35 | PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat. |
pfam04886 | PT | 2.94e-06 | 981 | 1015 | 2 | 36 | PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat. |
pfam04886 | PT | 4.22e-06 | 977 | 1010 | 2 | 35 | PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
SDU00779.1 | 0.0 | 14 | 972 | 37 | 1003 |
EDN79875.1 | 0.0 | 6 | 974 | 25 | 1016 |
AKU64455.1 | 0.0 | 8 | 970 | 27 | 1010 |
QQC43335.1 | 0.0 | 8 | 970 | 27 | 1010 |
QCT36061.1 | 0.0 | 6 | 970 | 25 | 1012 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999982 | 0.000083 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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