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Conserved domains on  [gi|50284813|ref|XP_444834|]
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uncharacterized protein GVI51_A01331 [Nakaseomyces glabratus]

Protein Classification

AGA2 domain-containing protein( domain architecture ID 13879734)

AGA2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AGA2 pfam17366
A-agglutinin-binding subunit Aga2; The wall of Saccharomyces cerevisiae consists of ...
29-83 5.25e-20

A-agglutinin-binding subunit Aga2; The wall of Saccharomyces cerevisiae consists of mannoproteins, beta-glucans, and a small amount of chitin. Mannoproteins include Aga2p where this domain family is found. There are two main display systems for yeast, the agglutinin system and the flocculin system. The S. cerevisiae sexual agglutinins facilitate the mating between two types of cells, a and alpha. A-Agglutinin consists of two subunits, encoded by two unlinked genes, AGA1 and AGA2. The cell surface adhesion protein (Aga2), enhances agglutination between a and alpha cells. Optimal binding includes interactions of the alpha-agglutinin binding pocket with the Aga2p terminal carboxyl group. This O-mannosylated glycopeptide is doubly disulfide linked to Aga1p. The Aga2p half-cystines near the ends of the peptide are linked to two Aga1p Cys residues separated by only two residues. This closeness of the disulfide bonds stabilizes the alpha/beta structure in Aga2p.


:

Pssm-ID: 375157  Cd Length: 58  Bit Score: 75.50  E-value: 5.25e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 50284813   29 TIPPNTLETTPYSSSTTNIVANGKKMIGVFQYYRSIKYISDCE---EKEDVVDTKIIH 83
Cdd:pfam17366  1 TIPTATLETTPYSTSTTTILANGKSMVGVTEYYRSVTYVSNCDtttTKASPTSTITVF 58
 
Name Accession Description Interval E-value
AGA2 pfam17366
A-agglutinin-binding subunit Aga2; The wall of Saccharomyces cerevisiae consists of ...
29-83 5.25e-20

A-agglutinin-binding subunit Aga2; The wall of Saccharomyces cerevisiae consists of mannoproteins, beta-glucans, and a small amount of chitin. Mannoproteins include Aga2p where this domain family is found. There are two main display systems for yeast, the agglutinin system and the flocculin system. The S. cerevisiae sexual agglutinins facilitate the mating between two types of cells, a and alpha. A-Agglutinin consists of two subunits, encoded by two unlinked genes, AGA1 and AGA2. The cell surface adhesion protein (Aga2), enhances agglutination between a and alpha cells. Optimal binding includes interactions of the alpha-agglutinin binding pocket with the Aga2p terminal carboxyl group. This O-mannosylated glycopeptide is doubly disulfide linked to Aga1p. The Aga2p half-cystines near the ends of the peptide are linked to two Aga1p Cys residues separated by only two residues. This closeness of the disulfide bonds stabilizes the alpha/beta structure in Aga2p.


Pssm-ID: 375157  Cd Length: 58  Bit Score: 75.50  E-value: 5.25e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 50284813   29 TIPPNTLETTPYSSSTTNIVANGKKMIGVFQYYRSIKYISDCE---EKEDVVDTKIIH 83
Cdd:pfam17366  1 TIPTATLETTPYSTSTTTILANGKSMVGVTEYYRSVTYVSNCDtttTKASPTSTITVF 58
 
Name Accession Description Interval E-value
AGA2 pfam17366
A-agglutinin-binding subunit Aga2; The wall of Saccharomyces cerevisiae consists of ...
29-83 5.25e-20

A-agglutinin-binding subunit Aga2; The wall of Saccharomyces cerevisiae consists of mannoproteins, beta-glucans, and a small amount of chitin. Mannoproteins include Aga2p where this domain family is found. There are two main display systems for yeast, the agglutinin system and the flocculin system. The S. cerevisiae sexual agglutinins facilitate the mating between two types of cells, a and alpha. A-Agglutinin consists of two subunits, encoded by two unlinked genes, AGA1 and AGA2. The cell surface adhesion protein (Aga2), enhances agglutination between a and alpha cells. Optimal binding includes interactions of the alpha-agglutinin binding pocket with the Aga2p terminal carboxyl group. This O-mannosylated glycopeptide is doubly disulfide linked to Aga1p. The Aga2p half-cystines near the ends of the peptide are linked to two Aga1p Cys residues separated by only two residues. This closeness of the disulfide bonds stabilizes the alpha/beta structure in Aga2p.


Pssm-ID: 375157  Cd Length: 58  Bit Score: 75.50  E-value: 5.25e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 50284813   29 TIPPNTLETTPYSSSTTNIVANGKKMIGVFQYYRSIKYISDCE---EKEDVVDTKIIH 83
Cdd:pfam17366  1 TIPTATLETTPYSTSTTTILANGKSMVGVTEYYRSVTYVSNCDtttTKASPTSTITVF 58
 
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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