Species | ||||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-698; DUOT01; | |||||||||||
CAZyme ID | MGYG000004423_00603 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 84556; End: 93765 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4646 | COG4646 | 5.00e-73 | 812 | 1345 | 1 | 540 | Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]. |
COG4983 | COG4983 | 5.76e-30 | 2769 | 3049 | 9 | 292 | Uncharacterized protein, contains Primase-polymerase (Primpol) domain [Function unknown]. |
COG4646 | COG4646 | 1.20e-28 | 1421 | 1679 | 382 | 637 | Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]. |
cd18011 | DEXDc_RapA | 2.67e-10 | 1291 | 1556 | 1 | 188 | 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. |
cd17919 | DEXHc_Snf | 1.32e-09 | 1291 | 1550 | 1 | 177 | DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins. Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases 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 | 4.33e-290 | 521 | 2040 | 1558 | 3141 |
QIW86704.1 | 5.83e-290 | 521 | 2040 | 1626 | 3209 |
QIW86628.1 | 5.83e-290 | 521 | 2040 | 1626 | 3209 |
AEY69616.1 | 3.45e-275 | 521 | 2049 | 1699 | 3294 |
AXF51455.1 | 1.19e-274 | 521 | 2078 | 1792 | 3415 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6K9A_A | 2.26e-13 | 2779 | 3024 | 18 | 250 | Thecomplex of NrS-1 N terminal domain (1-305) with dGTP [Nitratiruptor phage NrS-1],6K9B_A Apo structure of NrS-1 N terminal domain N305 [Nitratiruptor phage NrS-1],6K9B_B Apo structure of NrS-1 N terminal domain N305 [Nitratiruptor phage NrS-1] |
6A9W_A | 2.69e-13 | 2779 | 3024 | 37 | 269 | Structureof the bifunctional DNA primase-polymerase from phage NrS-1 [Nitratiruptor phage NrS-1],6JON_A Crystal structures of phage NrS-1 N300-dNTPs-Mg2+ complex provide molecular mechanisms for substrate specificity [Nitratiruptor phage NrS-1],6JOP_A Crystal structures of phage NrS-1 N300-dNTPs-Mg2+ complex provide molecular mechanisms for substrate specificity [Nitratiruptor phage NrS-1],6JOQ_A Crystal structures of phage NrS-1 N300-dNTPs-Mg2+ complex provide molecular mechanisms for substrate specificity [Nitratiruptor phage NrS-1] |
7RR4_A | 4.30e-13 | 2801 | 3024 | 33 | 249 | ChainA, Primase [Nitratiruptor phage NrS-1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q71TF8 | 3.32e-39 | 526 | 1872 | 47 | 1567 | Defense against restriction protein B OS=Escherichia phage P1 OX=2886926 GN=darB PE=3 SV=1 |
P54509 | 4.11e-06 | 1270 | 1870 | 41 | 507 | Uncharacterized ATP-dependent helicase YqhH OS=Bacillus subtilis (strain 168) OX=224308 GN=yqhH PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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