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Conserved domains on  [gi|392898462|ref|NP_500208|]
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lysozyme [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Destabilase super family cl05189
Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves ...
 21-68 2.81e-10

Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves isopeptide bonds formed by transglutaminase (Factor XIIIa) between glutamine gamma-carboxamide and the epsilon-amino group of lysine.


The actual alignment was detected with superfamily member pfam05497:

Pssm-ID: 461666  Cd Length: 118  Bit Score: 51.53  E-value: 2.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392898462   21 ENYYHRYKSQCDGLGMGECEVFARNHNGGPTGCRNPGT-LEYWQSIQKC 68
Cdd:pfam05497  70 QNYMNKYAQDCNGDGVIDCEDYARIHKLGPNGCRKGELpSGYWNRFKKC 118
 
Name Accession Description Interval E-value
Destabilase pfam05497
Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves ...
 21-68 2.81e-10

Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves isopeptide bonds formed by transglutaminase (Factor XIIIa) between glutamine gamma-carboxamide and the epsilon-amino group of lysine.


Pssm-ID: 461666  Cd Length: 118  Bit Score: 51.53  E-value: 2.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392898462   21 ENYYHRYKSQCDGLGMGECEVFARNHNGGPTGCRNPGT-LEYWQSIQKC 68
Cdd:pfam05497  70 QNYMNKYAQDCNGDGVIDCEDYARIHKLGPNGCRKGELpSGYWNRFKKC 118
lyz_i cd16890
I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and ...
 21-69 4.90e-07

I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and marine bivalves, are found in various invertebrate phyla and are apparently ubiquitous in insects. Lysozymes cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. I-type enzymes share structural similarity and the conserved glutamate catalytic residue of the lysozyme family.


Pssm-ID: 381611  Cd Length: 117  Bit Score: 43.49  E-value: 4.90e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 392898462  21 ENYYHRYKSQCDGLGMGECEVFARNHNGGPTGCRNPGTLEYWQSIQKCC 69
Cdd:cd16890   69 RNYMARYGQDCNGDGVIDCEDYARIHYLGPNGCKNQETLGYWNRRFKGC 117
 
Name Accession Description Interval E-value
Destabilase pfam05497
Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves ...
 21-68 2.81e-10

Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves isopeptide bonds formed by transglutaminase (Factor XIIIa) between glutamine gamma-carboxamide and the epsilon-amino group of lysine.


Pssm-ID: 461666  Cd Length: 118  Bit Score: 51.53  E-value: 2.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392898462   21 ENYYHRYKSQCDGLGMGECEVFARNHNGGPTGCRNPGT-LEYWQSIQKC 68
Cdd:pfam05497  70 QNYMNKYAQDCNGDGVIDCEDYARIHKLGPNGCRKGELpSGYWNRFKKC 118
lyz_i cd16890
I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and ...
 21-69 4.90e-07

I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and marine bivalves, are found in various invertebrate phyla and are apparently ubiquitous in insects. Lysozymes cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. I-type enzymes share structural similarity and the conserved glutamate catalytic residue of the lysozyme family.


Pssm-ID: 381611  Cd Length: 117  Bit Score: 43.49  E-value: 4.90e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 392898462  21 ENYYHRYKSQCDGLGMGECEVFARNHNGGPTGCRNPGTLEYWQSIQKCC 69
Cdd:cd16890   69 RNYMARYGQDCNGDGVIDCEDYARIHYLGPNGCKNQETLGYWNRRFKGC 117
 
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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