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CAZyme Information: MGYG000004340_01369
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; | |||||||||||
| CAZyme ID | MGYG000004340_01369 | |||||||||||
| 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: 4344; End: 6086 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK09419 | PRK09419 | 4.65e-141 | 21 | 577 | 42 | 647 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
| cd07410 | MPP_CpdB_N | 9.31e-81 | 21 | 285 | 1 | 280 | 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. |
| COG0737 | UshA | 3.56e-79 | 2 | 492 | 8 | 513 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
| PRK09420 | cpdB | 2.12e-63 | 2 | 553 | 16 | 624 | bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase. |
| PRK11907 | PRK11907 | 2.13e-60 | 1 | 532 | 94 | 677 | bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CDI50173.1 | 3.25e-190 | 19 | 577 | 36 | 605 |
| AAO36497.1 | 1.69e-187 | 19 | 577 | 36 | 605 |
| QBD85406.1 | 1.69e-187 | 19 | 577 | 36 | 605 |
| AVP54978.1 | 3.39e-187 | 19 | 577 | 36 | 605 |
| SNV84369.1 | 6.42e-182 | 19 | 580 | 36 | 608 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3GVE_A | 8.93e-35 | 18 | 275 | 9 | 303 | 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] |
| 5EQV_A | 3.79e-26 | 19 | 296 | 8 | 318 | 1.45Angstrom Crystal Structure of Bifunctional 2',3'-cyclic Nucleotide 2'-phosphodiesterase/3'-Nucleotidase Periplasmic Precursor Protein from Yersinia pestis with Phosphate bound to the Active site [Yersinia pestis CO92] |
| 3JYF_A | 2.32e-25 | 19 | 308 | 7 | 329 | 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] |
| 3IVD_A | 6.88e-19 | 20 | 534 | 6 | 497 | 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] |
| 7JV9_A | 4.03e-08 | 15 | 453 | 1 | 448 | HumanCD73 (ecto 5'-nucleotidase) in complex with compound 12 [Homo sapiens],7JV9_B Human CD73 (ecto 5'-nucleotidase) in complex with compound 12 [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O34313 | 9.55e-49 | 18 | 534 | 42 | 609 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
| P44764 | 6.32e-47 | 19 | 553 | 32 | 632 | 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 |
| P08331 | 7.96e-42 | 19 | 534 | 22 | 595 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2 |
| P53052 | 9.85e-41 | 19 | 538 | 27 | 604 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1 |
| P26265 | 2.75e-39 | 19 | 534 | 22 | 595 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000047 | 0.000016 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |