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Conserved domains on  [gi|1101084543|gb|OIO44591|]
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MAG: hypothetical protein AUJ41_02455 [Candidatus Pacebacteria bacterium CG1_02_43_31]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glucodextran_B super family cl07671
Glucodextranase, domain B; Members of this family adopt a structure consisting of seven ...
181-256 1.14e-07

Glucodextranase, domain B; Members of this family adopt a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. They act as cell wall anchors, where they interact with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, Domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface.


The actual alignment was detected with superfamily member pfam09136:

Pssm-ID: 430428 [Multi-domain]  Cd Length: 83  Bit Score: 48.25  E-value: 1.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101084543 181 PSLEILEPADGSsfesRTNQS-INLKGK-TDVGAK-IYINNRVVFPNDEGLFEHSILLVEGENKIEVHAEDKAKNSTKI 256
Cdd:pfam09136   1 PELTITSPADGL----TTNREtVTVTGTvADANLDsVTVNGIAATVYKDGTFSKRILLVEGENVITVIAVDSAGNTVTK 75
Glucodextran_B super family cl07671
Glucodextranase, domain B; Members of this family adopt a structure consisting of seven ...
104-170 2.11e-06

Glucodextranase, domain B; Members of this family adopt a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. They act as cell wall anchors, where they interact with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, Domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface.


The actual alignment was detected with superfamily member pfam09136:

Pssm-ID: 430428 [Multi-domain]  Cd Length: 83  Bit Score: 44.79  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101084543 104 TSSANIKVTG-FGEPESDLILVlNGRKddsIKINEDGSFEIGIILDEGENTIAAYSLDKAENESAATR 170
Cdd:pfam09136  14 TNRETVTVTGtVADANLDSVTV-NGIA---ATVYKDGTFSKRILLVEGENVITVIAVDSAGNTVTKTI 77
 
Name Accession Description Interval E-value
Glucodextran_B pfam09136
Glucodextranase, domain B; Members of this family adopt a structure consisting of seven ...
181-256 1.14e-07

Glucodextranase, domain B; Members of this family adopt a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. They act as cell wall anchors, where they interact with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, Domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface.


Pssm-ID: 430428 [Multi-domain]  Cd Length: 83  Bit Score: 48.25  E-value: 1.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101084543 181 PSLEILEPADGSsfesRTNQS-INLKGK-TDVGAK-IYINNRVVFPNDEGLFEHSILLVEGENKIEVHAEDKAKNSTKI 256
Cdd:pfam09136   1 PELTITSPADGL----TTNREtVTVTGTvADANLDsVTVNGIAATVYKDGTFSKRILLVEGENVITVIAVDSAGNTVTK 75
Glucodextran_B pfam09136
Glucodextranase, domain B; Members of this family adopt a structure consisting of seven ...
104-170 2.11e-06

Glucodextranase, domain B; Members of this family adopt a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. They act as cell wall anchors, where they interact with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, Domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface.


Pssm-ID: 430428 [Multi-domain]  Cd Length: 83  Bit Score: 44.79  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101084543 104 TSSANIKVTG-FGEPESDLILVlNGRKddsIKINEDGSFEIGIILDEGENTIAAYSLDKAENESAATR 170
Cdd:pfam09136  14 TNRETVTVTGtVADANLDSVTV-NGIA---ATVYKDGTFSKRILLVEGENVITVIAVDSAGNTVTKTI 77
 
Name Accession Description Interval E-value
Glucodextran_B pfam09136
Glucodextranase, domain B; Members of this family adopt a structure consisting of seven ...
181-256 1.14e-07

Glucodextranase, domain B; Members of this family adopt a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. They act as cell wall anchors, where they interact with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, Domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface.


Pssm-ID: 430428 [Multi-domain]  Cd Length: 83  Bit Score: 48.25  E-value: 1.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101084543 181 PSLEILEPADGSsfesRTNQS-INLKGK-TDVGAK-IYINNRVVFPNDEGLFEHSILLVEGENKIEVHAEDKAKNSTKI 256
Cdd:pfam09136   1 PELTITSPADGL----TTNREtVTVTGTvADANLDsVTVNGIAATVYKDGTFSKRILLVEGENVITVIAVDSAGNTVTK 75
Glucodextran_B pfam09136
Glucodextranase, domain B; Members of this family adopt a structure consisting of seven ...
104-170 2.11e-06

Glucodextranase, domain B; Members of this family adopt a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. They act as cell wall anchors, where they interact with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, Domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface.


Pssm-ID: 430428 [Multi-domain]  Cd Length: 83  Bit Score: 44.79  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101084543 104 TSSANIKVTG-FGEPESDLILVlNGRKddsIKINEDGSFEIGIILDEGENTIAAYSLDKAENESAATR 170
Cdd:pfam09136  14 TNRETVTVTGtVADANLDSVTV-NGIA---ATVYKDGTFSKRILLVEGENVITVIAVDSAGNTVTKTI 77
 
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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