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Conserved domains on  [gi|85726436|ref|NP_611165|]
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uncharacterized protein Dmel_CG6435 [Drosophila melanogaster]

Protein Classification

lyz_i domain-containing protein( domain architecture ID 10527524)

lyz_i domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Destabilase pfam05497
Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves ...
 26-142 1.01e-54

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: 168.25  E-value: 1.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726436    26 TEDCLDCLCETMSGCNASAICVNG--ACGIFRITWGYWVEAGKLTlpTDTALSEDAFTNCVNQPHCAANTVQNYMFKHGQ 103
Cdd:pfam05497   1 TEDCLGCICEASSGCNATAGCHNDslSCGPFRITWAYWQDAGKPV--GDKPSLEGAFENCANDPYCAADTVQNYMNKYAQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 85726436   104 DCNGDEHIDCLDFGALHKLGNLKC-QEELPYIFAKVFNRC 142
Cdd:pfam05497  79 DCNGDGVIDCEDYARIHKLGPNGCrKGELPSGYWNRFKKC 118
 
Name Accession Description Interval E-value
Destabilase pfam05497
Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves ...
 26-142 1.01e-54

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: 168.25  E-value: 1.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726436    26 TEDCLDCLCETMSGCNASAICVNG--ACGIFRITWGYWVEAGKLTlpTDTALSEDAFTNCVNQPHCAANTVQNYMFKHGQ 103
Cdd:pfam05497   1 TEDCLGCICEASSGCNATAGCHNDslSCGPFRITWAYWQDAGKPV--GDKPSLEGAFENCANDPYCAADTVQNYMNKYAQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 85726436   104 DCNGDEHIDCLDFGALHKLGNLKC-QEELPYIFAKVFNRC 142
Cdd:pfam05497  79 DCNGDGVIDCEDYARIHKLGPNGCrKGELPSGYWNRFKKC 118
lyz_i cd16890
I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and ...
 28-142 2.39e-48

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: 152.11  E-value: 2.39e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726436  28 DCLDCLCETMSGCNASAICVN-GACGIFRITWGYWVEAGKLTLPTDTALSEDAFTNCVNQPHCAANTVQNYMFKHGQDCN 106
Cdd:cd16890   1 DCLGCLCEAASGCNPTAGCSMgGVCGPFRISKPYWQDAGKPVLPGDDPNRGGAFERCANDPYCAARTVRNYMARYGQDCN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 85726436 107 GDEHIDCLDFGALHKLGNLKCQE-ELPYIFAKVFNRC 142
Cdd:cd16890  81 GDGVIDCEDYARIHYLGPNGCKNqETLGYWNRRFKGC 117
 
Name Accession Description Interval E-value
Destabilase pfam05497
Destabilase; Destabilase is an endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves ...
 26-142 1.01e-54

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: 168.25  E-value: 1.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726436    26 TEDCLDCLCETMSGCNASAICVNG--ACGIFRITWGYWVEAGKLTlpTDTALSEDAFTNCVNQPHCAANTVQNYMFKHGQ 103
Cdd:pfam05497   1 TEDCLGCICEASSGCNATAGCHNDslSCGPFRITWAYWQDAGKPV--GDKPSLEGAFENCANDPYCAADTVQNYMNKYAQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 85726436   104 DCNGDEHIDCLDFGALHKLGNLKC-QEELPYIFAKVFNRC 142
Cdd:pfam05497  79 DCNGDGVIDCEDYARIHKLGPNGCrKGELPSGYWNRFKKC 118
lyz_i cd16890
I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and ...
 28-142 2.39e-48

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: 152.11  E-value: 2.39e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726436  28 DCLDCLCETMSGCNASAICVN-GACGIFRITWGYWVEAGKLTLPTDTALSEDAFTNCVNQPHCAANTVQNYMFKHGQDCN 106
Cdd:cd16890   1 DCLGCLCEAASGCNPTAGCSMgGVCGPFRISKPYWQDAGKPVLPGDDPNRGGAFERCANDPYCAARTVRNYMARYGQDCN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 85726436 107 GDEHIDCLDFGALHKLGNLKCQE-ELPYIFAKVFNRC 142
Cdd:cd16890  81 GDGVIDCEDYARIHYLGPNGCKNqETLGYWNRRFKGC 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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