| Species | CAG-217 sp900547275 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-217; CAG-217 sp900547275 | |||||||||||
| CAZyme ID | MGYG000000395_00327 | |||||||||||
| CAZy Family | GH23 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 321676; End: 329442 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG4646 | COG4646 | 3.80e-64 | 1672 | 2212 | 1 | 540 | Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]. |
| pfam18824 | LPD11 | 1.43e-30 | 1248 | 1314 | 1 | 69 | Large polyvalent protein-associated domain 11. This is an alpha-helical domain with conserved hydrophobic residues. It is found in polyvalent proteins of conjugative elements. |
| COG4646 | COG4646 | 2.57e-28 | 2353 | 2544 | 439 | 637 | Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]. |
| pfam02384 | N6_Mtase | 6.81e-11 | 1436 | 1646 | 17 | 247 | N-6 DNA Methylase. Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes. |
| cd18011 | DEXDc_RapA | 2.57e-10 | 2158 | 2217 | 1 | 62 | DEXH-box helicase domain of RapA. In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ASV45029.1 | 4.46e-235 | 1360 | 2580 | 1548 | 2781 |
| AEY69616.1 | 2.27e-234 | 1360 | 2580 | 1689 | 2921 |
| AXF51455.1 | 2.31e-234 | 1360 | 2580 | 1782 | 3014 |
| QIW86704.1 | 6.41e-234 | 1360 | 2580 | 1616 | 2849 |
| QIW86628.1 | 6.41e-234 | 1360 | 2580 | 1616 | 2849 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q71TF8 | 2.42e-33 | 1378 | 2511 | 50 | 1224 | Defense against restriction protein B OS=Escherichia phage P1 OX=2886926 GN=darB PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000045 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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