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Conserved domains on  [gi|2315513858|dbj|GIU69603|]
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MAG: hypothetical protein KatS3mg002_0839 [Candidatus Woesearchaeota archaeon]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2129 super family cl43613
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
34-57 2.03e-03

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


The actual alignment was detected with superfamily member COG2129:

Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 33.83  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|....*.
gi 2315513858  34 KLILVTHAPPYDTNLDNM--GPFGGS 57
Cdd:COG2129   129 VDILLTHAPPYGTTLDRVedGPHVGS 154
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
34-57 2.03e-03

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 33.83  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|....*.
gi 2315513858  34 KLILVTHAPPYDTNLDNM--GPFGGS 57
Cdd:COG2129   129 VDILLTHAPPYGTTLDRVedGPHVGS 154
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 18-49 2.64e-03

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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.


Pssm-ID: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 33.44  E-value: 2.64e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2315513858  18 ENFIKEYDRLCSNNDMKLILVTHAPPYDTNLD 49
Cdd:cd07392   111 EEIYSKLGLLNVKLPGRLILVTHAPPYGTAVD 142
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
34-57 2.03e-03

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 33.83  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|....*.
gi 2315513858  34 KLILVTHAPPYDTNLDNM--GPFGGS 57
Cdd:COG2129   129 VDILLTHAPPYGTTLDRVedGPHVGS 154
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 18-49 2.64e-03

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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.


Pssm-ID: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 33.44  E-value: 2.64e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2315513858  18 ENFIKEYDRLCSNNDMKLILVTHAPPYDTNLD 49
Cdd:cd07392   111 EEIYSKLGLLNVKLPGRLILVTHAPPYGTAVD 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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