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Conserved domains on  [gi|24586607|ref|NP_610388|]
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uncharacterized protein Dmel_CG12780 [Drosophila melanogaster]

Protein Classification

CBM39 domain-containing protein( domain architecture ID 11239544)

CBM39 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM39 pfam15886
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
 6-97 2.88e-31

Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1,3-glucan-binding proteins involved in recognition of invading micro-organizms. It often co-occurs with pfam00722 (Glycosyl hydrolases family 16). It recognizes and binds to a triple-helical beta-1,3-glucan structure.


:

Pssm-ID: 464924  Cd Length: 106  Bit Score: 105.81  E-value: 2.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586607     6 VPLARVTSSERRGFEVSIDDEPGISLFGFHGRLNEPIVDLGNQTWAADIIgKDKDGRWTYTNRDVELKDGDVLYYWTTVR 85
Cdd:pfam15886   2 VPSVTFEVLEPKGLRVSIPDEPGIKLFAFHLNINKPFTGLEAGQFACDVT-EVTNGKWIFEDDDAILKAGDVLYYWTYVQ 80

                          90
                  ....*....|..
gi 24586607    86 YNGRDYHRMNQS 97
Cdd:pfam15886  81 YNGLGYRLDDQR 92
 
Name Accession Description Interval E-value
CBM39 pfam15886
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
 6-97 2.88e-31

Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1,3-glucan-binding proteins involved in recognition of invading micro-organizms. It often co-occurs with pfam00722 (Glycosyl hydrolases family 16). It recognizes and binds to a triple-helical beta-1,3-glucan structure.


Pssm-ID: 464924  Cd Length: 106  Bit Score: 105.81  E-value: 2.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586607     6 VPLARVTSSERRGFEVSIDDEPGISLFGFHGRLNEPIVDLGNQTWAADIIgKDKDGRWTYTNRDVELKDGDVLYYWTTVR 85
Cdd:pfam15886   2 VPSVTFEVLEPKGLRVSIPDEPGIKLFAFHLNINKPFTGLEAGQFACDVT-EVTNGKWIFEDDDAILKAGDVLYYWTYVQ 80

                          90
                  ....*....|..
gi 24586607    86 YNGRDYHRMNQS 97
Cdd:pfam15886  81 YNGLGYRLDDQR 92
 
Name Accession Description Interval E-value
CBM39 pfam15886
Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1, ...
 6-97 2.88e-31

Carbohydrate binding domain (family 32); This domain is found at the N-terminus of beta-1,3-glucan-binding proteins involved in recognition of invading micro-organizms. It often co-occurs with pfam00722 (Glycosyl hydrolases family 16). It recognizes and binds to a triple-helical beta-1,3-glucan structure.


Pssm-ID: 464924  Cd Length: 106  Bit Score: 105.81  E-value: 2.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586607     6 VPLARVTSSERRGFEVSIDDEPGISLFGFHGRLNEPIVDLGNQTWAADIIgKDKDGRWTYTNRDVELKDGDVLYYWTTVR 85
Cdd:pfam15886   2 VPSVTFEVLEPKGLRVSIPDEPGIKLFAFHLNINKPFTGLEAGQFACDVT-EVTNGKWIFEDDDAILKAGDVLYYWTYVQ 80

                          90
                  ....*....|..
gi 24586607    86 YNGRDYHRMNQS 97
Cdd:pfam15886  81 YNGLGYRLDDQR 92
 
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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