Species | Pseudoflavonifractor capillosus | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Pseudoflavonifractor; Pseudoflavonifractor capillosus | |||||||||||
CAZyme ID | MGYG000000071_00130 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | Trifunctional nucleotide phosphoesterase protein YfkN | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 157079; End: 159202 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK09419 | PRK09419 | 1.20e-116 | 22 | 570 | 26 | 631 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
COG0737 | UshA | 1.10e-79 | 22 | 501 | 10 | 501 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
cd07410 | MPP_CpdB_N | 3.88e-74 | 38 | 301 | 1 | 276 | Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain. CpdB is a bacterial periplasmic protein with an N-terminal metallophosphatase domain and a C-terminal 3'-nucleotidase domain. This alignment model represents the N-terminal metallophosphatase domain, which has 2',3'-cyclic phosphodiesterase activity, hydrolyzing the 2',3'-cyclic phosphates of adenosine, guanosine, cytosine and uridine to yield nucleoside and phosphate. CpdB also hydrolyzes the chromogenic substrates p-nitrophenyl phosphate (PNPP), bis(PNPP) and p-nitrophenyl phosphorylcholine (NPPC). CpdB is thought to play a scavenging role during RNA hydrolysis by converting the non-transportable nucleotides produced by RNaseI to nucleosides which can easily enter a cell for use as a carbon source. This family also includes YfkN, a Bacillus subtilis nucleotide phosphoesterase with two copies of each of the metallophosphatase and 3'-nucleotidase domains. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. |
PRK09418 | PRK09418 | 3.39e-69 | 24 | 560 | 22 | 631 | bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase. |
PRK09420 | cpdB | 8.39e-62 | 27 | 543 | 15 | 598 | bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AGB41602.1 | 6.22e-134 | 38 | 560 | 37 | 559 |
BAL01252.1 | 5.41e-111 | 9 | 569 | 4 | 559 |
BBE30724.1 | 3.15e-95 | 35 | 566 | 20 | 595 |
CDI50173.1 | 8.80e-92 | 20 | 572 | 19 | 590 |
QBD85406.1 | 2.40e-91 | 15 | 572 | 14 | 590 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3QFK_A | 1.01e-38 | 36 | 499 | 18 | 481 | ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325] |
4Q7F_A | 1.01e-38 | 36 | 499 | 18 | 481 | ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL] |
3GVE_A | 2.78e-36 | 35 | 261 | 9 | 251 | Crystalstructure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3GVE_B Crystal structure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168] |
3IVD_A | 4.57e-27 | 38 | 499 | 7 | 452 | Putative5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVD_B Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVE_A Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Cytidine [Escherichia coli O6] |
3JYF_A | 4.31e-26 | 38 | 268 | 9 | 251 | ChainA, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578],3JYF_B Chain B, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O34313 | 6.01e-54 | 2 | 545 | 4 | 612 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
P08331 | 3.65e-49 | 18 | 545 | 6 | 598 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2 |
P26265 | 1.79e-46 | 18 | 545 | 6 | 598 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2 |
P44764 | 3.20e-45 | 28 | 546 | 24 | 612 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=cpdB PE=3 SV=1 |
P53052 | 5.58e-45 | 9 | 549 | 4 | 607 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.000434 | 0.998599 | 0.000224 | 0.000280 | 0.000232 | 0.000187 |
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