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CAZyme Information: MGYG000002057_00797
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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 | Dysosmobacter sp001916835 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Dysosmobacter; Dysosmobacter sp001916835 | |||||||||||
| CAZyme ID | MGYG000002057_00797 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 24827; End: 27007 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG0737 | UshA | 5.52e-94 | 6 | 532 | 1 | 514 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
| PRK09558 | ushA | 2.42e-87 | 1 | 529 | 1 | 549 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
| PRK09419 | PRK09419 | 1.07e-83 | 24 | 516 | 649 | 1135 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
| cd00845 | MPP_UshA_N_like | 6.07e-56 | 34 | 274 | 1 | 236 | Escherichia coli UshA-like family, N-terminal metallophosphatase domain. This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. 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. |
| cd07408 | MPP_SA0022_N | 1.37e-52 | 34 | 277 | 1 | 242 | Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain. SA0022 is an uncharacterized Staphylococcus aureus UshA-like protein with two putative domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. SA0022 also contains a putative C-terminal cell wall anchor domain. 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCJ95849.1 | 2.30e-107 | 1 | 533 | 1 | 510 |
| QZY54554.1 | 1.59e-97 | 1 | 525 | 1 | 502 |
| ABW18467.1 | 8.52e-93 | 34 | 510 | 60 | 515 |
| AOT71215.1 | 1.58e-92 | 2 | 542 | 10 | 522 |
| QQY79959.1 | 1.61e-92 | 2 | 533 | 6 | 512 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2Z1A_A | 6.09e-49 | 36 | 516 | 32 | 520 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
| 5H7W_A | 1.97e-43 | 36 | 510 | 7 | 509 | Crystalstructure of 5'-nucleotidase from venom of Naja atra [Naja atra],5H7W_B Crystal structure of 5'-nucleotidase from venom of Naja atra [Naja atra] |
| 7D0V_A | 8.02e-42 | 36 | 510 | 7 | 509 | ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra] |
| 3IVD_A | 1.07e-41 | 34 | 510 | 7 | 482 | 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] |
| 4H2I_A | 9.55e-41 | 36 | 509 | 6 | 507 | Humanecto-5'-nucleotidase (CD73): crystal form III (closed) in complex with AMPCP [Homo sapiens],6TVX_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12676 (an AOPCP derivative, compound 9 in paper) in the closed state [Homo sapiens],6TW0_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12690 (an AOPCP derivative, compound 10 in publication) in the closed state [Homo sapiens],6TWA_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12646 (an AOPCP derivative, compound 20 in publication) in the closed state [Homo sapiens],6TWF_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12604 (an AOPCP derivative, compound 21 in publication) in the closed state [Homo sapiens],6YE1_A Chain A, 5'-nucleotidase [Homo sapiens],6YE1_B Chain B, 5'-nucleotidase [Homo sapiens],6YE2_A Chain A, 5'-nucleotidase [Homo sapiens],6YE2_B Chain B, 5'-nucleotidase [Homo sapiens],6Z9B_A Human Ecto-5'-nucleotidase (CD73) in complex with AOPCP derivative A830 (compound 16 in publication) in the closed form (crystal form III) [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 | 1.04e-54 | 36 | 510 | 671 | 1160 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
| A9BJC1 | 2.59e-48 | 1 | 485 | 1 | 458 | Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1 |
| B6EWW8 | 2.98e-43 | 36 | 510 | 46 | 548 | Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1 |
| A0A2I4HXH5 | 1.08e-42 | 36 | 510 | 7 | 509 | Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1 |
| F8S0Z7 | 1.87e-42 | 36 | 510 | 46 | 548 | Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000301 | 0.998920 | 0.000197 | 0.000204 | 0.000201 | 0.000175 |