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Conserved domains on  [gi|1570043195|gb|RYP41836|]
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hypothetical protein DL767_000737 [Monosporascus sp. MG133]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fungal_lectin super family cl06810
Fungal fucose-specific lectin; Lectins are involved in many recognition events at the ...
 177-285 4.72e-03

Fungal fucose-specific lectin; Lectins are involved in many recognition events at the molecular or cellular level. These fungal lectins, such as Aleuria aurantia lectin (AAL), specifically recognize fucosylated glycans. AAL is a dimeric protein, with each monomer being organized into a six-bladed beta-propeller fold and a small antiparallel two-stranded beta-sheet. The beta-propeller fold is important in fucose recognition; five binding pockets are found between the propeller blades. The small beta-sheet, on the other hand, is involved in the dimerization process.


The actual alignment was detected with superfamily member pfam07938:

Pssm-ID: 429745 [Multi-domain]  Cd Length: 299  Bit Score: 38.00  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043195 177 VYQELLQNHLKEFNVTGGQSTDIESTGNAKPLTSMAVT---YYDG-KAYLYYTDNSNNLCRVIKDgsvdnDDRGW--GDY 250
Cdd:pfam07938 118 VYAQKTDNTIQEYMWNGDGWKKGTNLGVALPGTGIAVTcwkYYDGpSIRVYYQTDNLKLVEKAYD-----PHTGWykGLT 192

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1570043195 251 KIFEGSPK--VATDSQLTVSSSHGInHIFYVSTDDIL 285
Cdd:pfam07938 193 TFDKAPPRcaIAATSFNPSSSSIGI-RVYYVNSDNTI 228
 
Name Accession Description Interval E-value
Fungal_lectin pfam07938
Fungal fucose-specific lectin; Lectins are involved in many recognition events at the ...
 177-285 4.72e-03

Fungal fucose-specific lectin; Lectins are involved in many recognition events at the molecular or cellular level. These fungal lectins, such as Aleuria aurantia lectin (AAL), specifically recognize fucosylated glycans. AAL is a dimeric protein, with each monomer being organized into a six-bladed beta-propeller fold and a small antiparallel two-stranded beta-sheet. The beta-propeller fold is important in fucose recognition; five binding pockets are found between the propeller blades. The small beta-sheet, on the other hand, is involved in the dimerization process.


Pssm-ID: 429745 [Multi-domain]  Cd Length: 299  Bit Score: 38.00  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043195 177 VYQELLQNHLKEFNVTGGQSTDIESTGNAKPLTSMAVT---YYDG-KAYLYYTDNSNNLCRVIKDgsvdnDDRGW--GDY 250
Cdd:pfam07938 118 VYAQKTDNTIQEYMWNGDGWKKGTNLGVALPGTGIAVTcwkYYDGpSIRVYYQTDNLKLVEKAYD-----PHTGWykGLT 192

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1570043195 251 KIFEGSPK--VATDSQLTVSSSHGInHIFYVSTDDIL 285
Cdd:pfam07938 193 TFDKAPPRcaIAATSFNPSSSSIGI-RVYYVNSDNTI 228
 
Name Accession Description Interval E-value
Fungal_lectin pfam07938
Fungal fucose-specific lectin; Lectins are involved in many recognition events at the ...
 177-285 4.72e-03

Fungal fucose-specific lectin; Lectins are involved in many recognition events at the molecular or cellular level. These fungal lectins, such as Aleuria aurantia lectin (AAL), specifically recognize fucosylated glycans. AAL is a dimeric protein, with each monomer being organized into a six-bladed beta-propeller fold and a small antiparallel two-stranded beta-sheet. The beta-propeller fold is important in fucose recognition; five binding pockets are found between the propeller blades. The small beta-sheet, on the other hand, is involved in the dimerization process.


Pssm-ID: 429745 [Multi-domain]  Cd Length: 299  Bit Score: 38.00  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043195 177 VYQELLQNHLKEFNVTGGQSTDIESTGNAKPLTSMAVT---YYDG-KAYLYYTDNSNNLCRVIKDgsvdnDDRGW--GDY 250
Cdd:pfam07938 118 VYAQKTDNTIQEYMWNGDGWKKGTNLGVALPGTGIAVTcwkYYDGpSIRVYYQTDNLKLVEKAYD-----PHTGWykGLT 192

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1570043195 251 KIFEGSPK--VATDSQLTVSSSHGInHIFYVSTDDIL 285
Cdd:pfam07938 193 TFDKAPPRcaIAATSFNPSSSSIGI-RVYYVNSDNTI 228
 
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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