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Conserved domains on  [gi|1683571013|ref|WP_139159151|]
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MULTISPECIES: carbohydrate porin, partial [Klebsiella]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OM_channels super family cl21487
Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in ...
1-50 3.05e-07

Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in strand and shear number. Classical (gram-negative ) porins are non-specific channels for small hydrophillic molecules and form 16 beta-stranded barrels (16,20), which associate as trimers. Maltoporin-like channels have specificities for various sugars and form 18 beta-stranded barrels (18,22), which associate as trimers. Ligand-gated protein channels cooperate with a TonB associated inner membrane complex to actively transport ligands via the proton motive force and they form monomeric, (22,24) barrels. The 150-200 N-terminal residues form a plug that blocks the channel from the periplasmic end.


The actual alignment was detected with superfamily member pfam02264:

Pssm-ID: 473880  Cd Length: 385  Bit Score: 44.21  E-value: 3.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1683571013   1 AIGMGPEFRPMLRFYVTGGQVDNE--HTAKVNGTQDQQLDSLNVGGMFEAWF 50
Cdd:pfam02264 334 KAGSGFWSRPELRLFATYANWNDAadGALAGGGGFGGDTSGWNFGVQAEAWW 385
 
Name Accession Description Interval E-value
LamB pfam02264
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
1-50 3.05e-07

LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel.


Pssm-ID: 426687  Cd Length: 385  Bit Score: 44.21  E-value: 3.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1683571013   1 AIGMGPEFRPMLRFYVTGGQVDNE--HTAKVNGTQDQQLDSLNVGGMFEAWF 50
Cdd:pfam02264 334 KAGSGFWSRPELRLFATYANWNDAadGALAGGGGFGGDTSGWNFGVQAEAWW 385
LamB COG4580
Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];
1-50 4.49e-04

Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];


Pssm-ID: 443637  Cd Length: 408  Bit Score: 35.29  E-value: 4.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1683571013   1 AIGMGPEF--RPMLRFYVTGGQVDNEHTAKVNGTQDQQLDSLNVGGMFEAWF 50
Cdd:COG4580   357 TWSAGPGFwsRPELRLFATYAKWNEAAQGAATGTFGGDTSGVTFGVQVEAWW 408
 
Name Accession Description Interval E-value
LamB pfam02264
LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the ...
1-50 3.05e-07

LamB porin; Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel.


Pssm-ID: 426687  Cd Length: 385  Bit Score: 44.21  E-value: 3.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1683571013   1 AIGMGPEFRPMLRFYVTGGQVDNE--HTAKVNGTQDQQLDSLNVGGMFEAWF 50
Cdd:pfam02264 334 KAGSGFWSRPELRLFATYANWNDAadGALAGGGGFGGDTSGWNFGVQAEAWW 385
LamB COG4580
Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];
1-50 4.49e-04

Maltoporin (phage lambda and maltose receptor) [Carbohydrate transport and metabolism];


Pssm-ID: 443637  Cd Length: 408  Bit Score: 35.29  E-value: 4.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1683571013   1 AIGMGPEF--RPMLRFYVTGGQVDNEHTAKVNGTQDQQLDSLNVGGMFEAWF 50
Cdd:COG4580   357 TWSAGPGFwsRPELRLFATYAKWNEAAQGAATGTFGGDTSGVTFGVQVEAWW 408
 
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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