Species | Paenibacillus_A phocaensis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A phocaensis | |||||||||||
CAZyme ID | MGYG000001535_03235 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 175707; End: 177884 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK09419 | PRK09419 | 4.24e-144 | 38 | 573 | 653 | 1157 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
COG0737 | UshA | 4.23e-103 | 42 | 538 | 23 | 488 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
cd07409 | MPP_CD73_N | 3.92e-102 | 46 | 302 | 1 | 277 | CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain. CD73 is a mammalian ecto-5'-nucleotidase expressed in endothelial cells and lymphocytes that catalyzes the conversion of 5'-AMP to adenosine in the final step of a pathway that generates adenosine from ATP. This pathway also includes a CD39 nucleoside triphosphate dephosphorylase that mediates the dephosphorylation of ATP to ADP and then to 5'-AMP. These enzymes all have an N-terminal metallophosphatase domain and a C-terminal 5'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. |
PRK09558 | ushA | 8.72e-97 | 32 | 549 | 21 | 538 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
cd00845 | MPP_UshA_N_like | 6.28e-71 | 46 | 304 | 1 | 255 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AYG73682.1 | 3.56e-111 | 43 | 594 | 25 | 578 |
AYG67288.1 | 3.56e-111 | 43 | 594 | 25 | 578 |
ASW07599.1 | 4.27e-111 | 43 | 585 | 25 | 566 |
AYG60397.1 | 3.15e-109 | 22 | 567 | 10 | 542 |
QYA14314.1 | 4.65e-109 | 43 | 573 | 25 | 548 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2Z1A_A | 2.51e-122 | 44 | 556 | 28 | 528 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
5H7W_A | 1.63e-79 | 44 | 556 | 3 | 522 | 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 | 3.27e-79 | 44 | 562 | 3 | 528 | ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra] |
6XUQ_A | 2.66e-69 | 39 | 533 | 15 | 521 | HumanEcto-5'-nucleotidase (CD73) in complex with A1618 (compound 1b in publication) in the closed state in crystal form III [Homo sapiens],6Z9D_A Human Ecto-5'-nucleotidase (CD73) in complex with AOPCP derivative AB680 (compound 55 in publication) in the closed form (crystal form III) [Homo sapiens] |
6S7F_A | 2.88e-68 | 44 | 533 | 2 | 503 | HumanCD73 (5'-nucleotidase) in complex with PSB12379 (an AOPCP derivative) in the closed state [Homo sapiens],6S7H_A Human CD73 (5'-nucleotidase) in complex with PSB12489 (an AOPCP derivative) in the closed state [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O34313 | 4.44e-119 | 44 | 559 | 667 | 1177 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
A0A2I4HXH5 | 8.95e-79 | 44 | 556 | 3 | 522 | Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1 |
P29240 | 3.06e-76 | 44 | 556 | 30 | 546 | 5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1 |
B6EWW8 | 3.97e-76 | 44 | 567 | 42 | 572 | Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1 |
F8S0Z7 | 3.97e-76 | 44 | 567 | 42 | 572 | Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000328 | 0.998982 | 0.000173 | 0.000194 | 0.000163 | 0.000139 |
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