Species | Paenibacillus polymyxa | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa | |||||||||||
CAZyme ID | MGYG000003687_01276 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 83052; End: 84959 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK09558 | ushA | 1.80e-133 | 5 | 508 | 2 | 536 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
PRK09419 | PRK09419 | 8.88e-132 | 47 | 521 | 659 | 1145 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
COG0737 | UshA | 1.32e-127 | 48 | 521 | 26 | 513 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
cd00845 | MPP_UshA_N_like | 1.97e-77 | 49 | 300 | 1 | 254 | 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 | 3.42e-71 | 49 | 291 | 1 | 246 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AIY10403.1 | 0.0 | 1 | 635 | 1 | 635 |
AHM64790.1 | 0.0 | 1 | 635 | 1 | 635 |
AUS25370.1 | 0.0 | 1 | 635 | 1 | 635 |
QPK51790.1 | 0.0 | 1 | 635 | 1 | 635 |
QPK56876.1 | 0.0 | 1 | 635 | 1 | 635 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2Z1A_A | 6.72e-75 | 46 | 482 | 27 | 491 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
1HP1_A | 7.03e-66 | 49 | 513 | 9 | 506 | 5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli] |
1HO5_A | 1.21e-64 | 49 | 513 | 9 | 515 | 5'-Nucleotidase(E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HO5_B 5'-Nucleotidase (E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HPU_A 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_B 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_C 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_D 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli] |
1USH_A | 2.11e-64 | 49 | 513 | 34 | 540 | 5'-NucleotidaseFrom E. Coli [Escherichia coli K-12],2USH_A 5'-Nucleotidase From E. Coli [Escherichia coli K-12],2USH_B 5'-Nucleotidase From E. Coli [Escherichia coli K-12] |
1OI8_A | 3.82e-64 | 49 | 513 | 9 | 515 | 5'-Nucleotidase(E. coli) with an Engineered Disulfide Bridge (P90C, L424C) [Escherichia coli],1OI8_B 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (P90C, L424C) [Escherichia coli] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A9BJC1 | 2.49e-78 | 48 | 508 | 23 | 486 | Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1 |
O34313 | 3.74e-71 | 49 | 521 | 669 | 1176 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
Q56878 | 7.98e-68 | 49 | 505 | 34 | 532 | Protein UshA OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=ushA PE=3 SV=3 |
P07024 | 1.15e-63 | 49 | 513 | 34 | 540 | Protein UshA OS=Escherichia coli (strain K12) OX=83333 GN=ushA PE=1 SV=2 |
Q9KQ30 | 1.71e-63 | 49 | 508 | 38 | 537 | 5'-nucleotidase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nutA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000388 | 0.502792 | 0.496096 | 0.000281 | 0.000237 | 0.000182 |
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