Species | Citrobacter youngae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter youngae | |||||||||||
CAZyme ID | MGYG000000124_01516 | |||||||||||
CAZy Family | GH105 | |||||||||||
CAZyme Description | Unsaturated rhamnogalacturonyl hydrolase YesR | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1525547; End: 1526686 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH105 | 60 | 376 | 1.1e-115 | 0.9698795180722891 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4225 | YesR | 1.16e-143 | 29 | 378 | 2 | 353 | Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism]. |
pfam07470 | Glyco_hydro_88 | 4.02e-127 | 37 | 378 | 1 | 343 | Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases. |
cd21828 | gammaCoV_Nsp7 | 0.007 | 236 | 292 | 10 | 70 | gammacoronavirus non-structural protein 7. This model represents the non-structural protein 7 (Nsp7) of gammacoronaviruses that include Avian infectious bronchitis virus (IBV) and Canada goose coronavirus (CGCoV), among others. CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Upon processing of the Nsp7-10 region by protease M (Mpro), the released four small proteins Nsp7, Nsp8, Nsp9 and Nsp10 form functional complexes with CoV core enzymes and stimulate replication. Most importantly, a complex of Nsp7 with Nsp8 has been shown to activate and confer processivity to the RNA-synthesizing activity of Nsp12, the RNA-dependent RNA-polymerase (RdRp); in SARS-CoV, point mutations in the NSP7- or NSP8-coding region have been shown to delay virus growth. Nsp7 and Nsp8 cooperate in activating the primer-dependent activity of the Nsp12 RdRp such that the level of their association may constitute a limiting factor for obtaining a high RNA polymerase activity. The subsequent Nsp7/Nsp8/Nsp12 polymerase complex is then able to associate with an active bifunctional Nsp14, which includes N-terminal 3' to 5' exoribonuclease (ExoN) and C-terminal N7-guanine cap methyltransferase (N7-MTase) activities, thus representing a unique coronavirus Nsp assembly that incorporates RdRp, exoribonuclease, and N7-MTase activities. Interaction of Nsp7 with Nsp8 appears to be conserved across the coronavirus family, making these proteins interesting drug targets. Nsp7 has a 4-helical bundle conformation which is strongly affected by its interaction with Nsp8, especially where it concerns alpha-helix 4. SARS-CoV Nsp7 forms a 8:8 hexadecameric supercomplex with Nsp8 that adopts a hollow cylinder-like structure with a large central channel and positive electrostatic properties in the cylinder, while Feline infectious peritonitis virus Nsp7 forms a 2:1 heterotrimer with Nsp8. Regardless of their oligomeric structure, the Nsp7/Nsp8 complex functions as a noncanonical RNA polymerase capable of synthesizing RNA of up to template length. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AMH14932.1 | 2.42e-284 | 1 | 379 | 1 | 379 |
AYL61933.1 | 2.82e-283 | 1 | 379 | 1 | 379 |
QMR50634.1 | 2.32e-282 | 1 | 379 | 1 | 379 |
QGG14278.1 | 6.65e-282 | 1 | 379 | 1 | 379 |
AUV25939.1 | 6.65e-282 | 1 | 379 | 1 | 379 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3QWT_A | 7.96e-253 | 3 | 379 | 5 | 381 | ChainA, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_B Chain B, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_C Chain C, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_D Chain D, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A] |
3PMM_A | 2.46e-238 | 3 | 379 | 6 | 382 | ChainA, Putative cytoplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578] |
4XUV_A | 2.31e-159 | 23 | 378 | 7 | 372 | Crystalstructure of a glycoside hydrolase family 105 (GH105) enzyme from Thielavia terrestris [Thermothielavioides terrestris NRRL 8126],4XUV_B Crystal structure of a glycoside hydrolase family 105 (GH105) enzyme from Thielavia terrestris [Thermothielavioides terrestris NRRL 8126] |
4WU0_A | 2.43e-20 | 63 | 327 | 23 | 299 | StructuralAnalysis of C. acetobutylicum ATCC 824 Glycoside Hydrolase From Family 105 [Clostridium acetobutylicum ATCC 824],4WU0_B Structural Analysis of C. acetobutylicum ATCC 824 Glycoside Hydrolase From Family 105 [Clostridium acetobutylicum ATCC 824] |
3K11_A | 1.47e-16 | 187 | 357 | 224 | 392 | Crystalstructure of Putative glycosyl hydrolase (NP_813087.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.80 A resolution [Bacteroides thetaiotaomicron VPI-5482] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O31521 | 2.58e-50 | 63 | 376 | 29 | 337 | Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR PE=1 SV=1 |
P0A3U6 | 2.77e-09 | 180 | 324 | 10 | 160 | Protein Atu3128 OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=Atu3128 PE=3 SV=1 |
P0A3U7 | 2.77e-09 | 180 | 324 | 10 | 160 | 24.9 kDa protein in picA locus OS=Rhizobium radiobacter OX=358 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000046 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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