| Species | Paenibacillus_A rubinfantis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis | |||||||||||
| CAZyme ID | MGYG000001525_02298 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 18973; End: 21153 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK09419 | PRK09419 | 1.50e-143 | 38 | 558 | 654 | 1146 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
| COG0737 | UshA | 2.94e-107 | 21 | 547 | 5 | 501 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
| cd07409 | MPP_CD73_N | 1.73e-103 | 45 | 303 | 1 | 279 | 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 | 1.23e-99 | 4 | 551 | 1 | 541 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
| cd00845 | MPP_UshA_N_like | 1.29e-72 | 45 | 303 | 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 | 8.23e-109 | 26 | 552 | 7 | 542 |
| AYG67288.1 | 8.23e-109 | 26 | 552 | 7 | 542 |
| AUX77867.1 | 1.48e-108 | 42 | 573 | 25 | 560 |
| ASW07599.1 | 2.73e-108 | 26 | 574 | 7 | 550 |
| AWM26442.1 | 2.84e-108 | 42 | 573 | 25 | 559 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2Z1A_A | 4.24e-124 | 43 | 555 | 28 | 528 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
| 5H7W_A | 1.72e-78 | 43 | 555 | 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 | 6.85e-77 | 43 | 555 | 3 | 522 | ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra] |
| 6XUQ_A | 1.41e-71 | 36 | 555 | 13 | 539 | 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] |
| 4H1Y_P | 4.08e-70 | 43 | 555 | 24 | 543 | Humanecto-5'-nucleotidase (CD73): crystal form II (open) in complex with PSB11552 [Homo sapiens],6TVE_P Unliganded human CD73 (5'-nucleotidase) in the open state [Homo sapiens],6TVG_A Human CD73 (ecto 5'-nucleotidase) in complex with AMPCP in the open state [Homo sapiens],7BBJ_A Chain A, 5'-nucleotidase [Homo sapiens],7BBJ_B Chain B, 5'-nucleotidase [Homo sapiens],7P9N_A Chain A, 5'-nucleotidase [Homo sapiens],7P9R_A Chain A, 5'-nucleotidase [Homo sapiens],7P9T_A Chain A, 5'-nucleotidase [Homo sapiens],7PA4_A Chain A, 5'-nucleotidase [Homo sapiens],7PB5_A Chain A, 5'-nucleotidase [Homo sapiens],7PBA_A Chain A, 5'-nucleotidase [Homo sapiens],7PBB_A Chain A, 5'-nucleotidase [Homo sapiens],7PBY_A Chain A, 5'-nucleotidase [Homo sapiens],7PCP_A Chain A, 5'-nucleotidase [Homo sapiens],7PD9_A Chain A, 5'-nucleotidase [Homo sapiens] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O34313 | 3.06e-117 | 34 | 558 | 660 | 1177 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
| A0A2I4HXH5 | 9.41e-78 | 43 | 555 | 3 | 522 | Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1 |
| P29240 | 2.24e-76 | 40 | 555 | 27 | 546 | 5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1 |
| B6EWW8 | 2.91e-76 | 36 | 555 | 35 | 561 | Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1 |
| F8S0Z7 | 1.52e-75 | 36 | 555 | 35 | 561 | 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 |
|---|---|---|---|---|---|
| 0.000290 | 0.998969 | 0.000174 | 0.000208 | 0.000181 | 0.000148 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.