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Conserved domains on  [gi|14318468|ref|NP_116576|]
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uncharacterized protein YFL051C [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PA14 super family cl08459
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
125-151 2.26e-03

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


The actual alignment was detected with superfamily member pfam07691:

Pssm-ID: 471833 [Multi-domain]  Cd Length: 141  Bit Score: 36.19  E-value: 2.26e-03
                          10        20
                  ....*....|....*....|....*..
gi 14318468   125 NTAYWSSDLFGFYTTPTNVTVEMTGYL 151
Cdd:pfam07691  28 NTFYWDTDVPGFGEAPGDFSARWTGYL 54
 
Name Accession Description Interval E-value
PA14 pfam07691
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
125-151 2.26e-03

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


Pssm-ID: 400161 [Multi-domain]  Cd Length: 141  Bit Score: 36.19  E-value: 2.26e-03
                          10        20
                  ....*....|....*....|....*..
gi 14318468   125 NTAYWSSDLFGFYTTPTNVTVEMTGYL 151
Cdd:pfam07691  28 NTFYWDTDVPGFGEAPGDFSARWTGYL 54
 
Name Accession Description Interval E-value
PA14 pfam07691
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
125-151 2.26e-03

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


Pssm-ID: 400161 [Multi-domain]  Cd Length: 141  Bit Score: 36.19  E-value: 2.26e-03
                          10        20
                  ....*....|....*....|....*..
gi 14318468   125 NTAYWSSDLFGFYTTPTNVTVEMTGYL 151
Cdd:pfam07691  28 NTFYWDTDVPGFGEAPGDFSARWTGYL 54
 
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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