Species | Clostridium neonatale | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium neonatale | |||||||||||
CAZyme ID | MGYG000000902_03951 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 12488; End: 14257 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0737 | UshA | 1.65e-117 | 11 | 496 | 1 | 502 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
PRK09419 | PRK09419 | 6.57e-107 | 17 | 504 | 640 | 1144 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
PRK09558 | ushA | 1.52e-98 | 1 | 473 | 5 | 513 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
cd07408 | MPP_SA0022_N | 8.69e-75 | 37 | 278 | 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. |
cd00845 | MPP_UshA_N_like | 8.84e-71 | 37 | 286 | 1 | 253 | 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 |
---|---|---|---|---|---|
CDH91764.1 | 9.91e-246 | 1 | 587 | 1 | 580 |
ACD21945.1 | 9.91e-246 | 1 | 587 | 1 | 580 |
ACD51841.1 | 1.14e-244 | 1 | 587 | 1 | 580 |
AJF30422.1 | 1.14e-244 | 1 | 587 | 1 | 580 |
AJF33485.1 | 1.14e-244 | 1 | 587 | 1 | 580 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2Z1A_A | 1.18e-63 | 37 | 505 | 30 | 530 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
3IVD_A | 6.72e-56 | 37 | 470 | 7 | 459 | 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] |
6XUE_A | 1.54e-52 | 36 | 507 | 2 | 524 | HumanEcto-5'-nucleotidase (CD73) in complex with A2396 (compound 74 in publication) in the closed form in crystal form IV [Homo sapiens],6XUE_B Human Ecto-5'-nucleotidase (CD73) in complex with A2396 (compound 74 in publication) in the closed form in crystal form IV [Homo sapiens],6XUG_A Human Ecto-5'-nucleotidase (CD73) in complex with A2410 (compound 53 in publication) in the closed form in crystal form IV [Homo sapiens],6XUG_B Human Ecto-5'-nucleotidase (CD73) in complex with A2410 (compound 53 in publication) in the closed form in crystal form IV [Homo sapiens] |
7QGO_A | 1.62e-52 | 36 | 507 | 2 | 524 | ChainA, 5'-nucleotidase [Homo sapiens] |
7QGA_A | 1.81e-52 | 36 | 507 | 2 | 524 | ChainA, 5'-nucleotidase [Homo sapiens],7QGL_A Chain A, 5'-nucleotidase [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A9BJC1 | 2.73e-67 | 37 | 467 | 24 | 458 | Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1 |
O34313 | 1.16e-61 | 37 | 504 | 669 | 1175 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
Q05927 | 1.20e-52 | 36 | 509 | 28 | 552 | 5'-nucleotidase OS=Bos taurus OX=9913 GN=NT5E PE=1 SV=2 |
P21589 | 5.76e-51 | 36 | 441 | 28 | 474 | 5'-nucleotidase OS=Homo sapiens OX=9606 GN=NT5E PE=1 SV=1 |
F8S0Z7 | 1.38e-50 | 36 | 471 | 43 | 527 | 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 |
---|---|---|---|---|---|
0.000245 | 0.999081 | 0.000169 | 0.000179 | 0.000157 | 0.000141 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.