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Conserved domains on  [gi|1631921356|ref|YP_009599231|]
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endolysin [Acinetobacter phage vB_AbaP_AS12]

Protein Classification

lysozyme family protein( domain architecture ID 63)

lysozyme family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_hydro_19 super family cl46694
Chitinase class I;
37-164 1.86e-16

Chitinase class I;


The actual alignment was detected with superfamily member COG3179:

Pssm-ID: 481034  Cd Length: 193  Bit Score: 73.42  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631921356  37 EYGLTYP-EAAYLLATIYHETGlpnGYRTMRpikEAGSDSYLRSKKYYP----------------------------YIG 87
Cdd:COG3179    34 EFGITTPlRLAHFLAQIAHESG---GLRYLE---ENLNYSALQVFGRYPdgapeaianrvyggrkdlgntapgdgwrYRG 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631921356  88 YGYVQLTWEENYGRIGKLIGIDLVKNPEKALEPLIAIQIAikgmlnGWFtglgFRRKRPVSKYNKQQYVAARNIING 164
Cdd:COG3179   108 RGLIQLTGRANYRAAGDALGLDLVNNPDLLADPEVAARSA------AWF----WATRGLNALADAGDFGEVTRRING 174
 
Name Accession Description Interval E-value
GH19 COG3179
Chitinase, GH19 family [Carbohydrate transport and metabolism];
37-164 1.86e-16

Chitinase, GH19 family [Carbohydrate transport and metabolism];


Pssm-ID: 442412  Cd Length: 193  Bit Score: 73.42  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631921356  37 EYGLTYP-EAAYLLATIYHETGlpnGYRTMRpikEAGSDSYLRSKKYYP----------------------------YIG 87
Cdd:COG3179    34 EFGITTPlRLAHFLAQIAHESG---GLRYLE---ENLNYSALQVFGRYPdgapeaianrvyggrkdlgntapgdgwrYRG 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631921356  88 YGYVQLTWEENYGRIGKLIGIDLVKNPEKALEPLIAIQIAikgmlnGWFtglgFRRKRPVSKYNKQQYVAARNIING 164
Cdd:COG3179   108 RGLIQLTGRANYRAAGDALGLDLVNNPDLLADPEVAARSA------AWF----WATRGLNALADAGDFGEVTRRING 174
Glyco_hydro_19 pfam00182
Chitinase class I;
79-136 6.18e-08

Chitinase class I;


Pssm-ID: 459702  Cd Length: 232  Bit Score: 50.62  E-value: 6.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631921356  79 SKKYYpyiGYGYVQLTWEENYGRIGKLIGIDLVKNPE-KALEPLIAIQIAIkgmlngWF 136
Cdd:pfam00182 104 GKKYY---GRGPIQLSYNYNYGPAGQAIGQDLLNNPDlVATDAVVSFKTAI------WF 153
chitinase_GH19 cd00325
Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the ...
 44-136 2.12e-07

Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Glycoside hydrolase family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases, but they are smaller in size due to certain deletions. Despite lacking any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the prokaryotic/eukaryotic divergence.


Pssm-ID: 381595 [Multi-domain]  Cd Length: 224  Bit Score: 48.97  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631921356  44 EAAYLLATIYHETG---------LPNGYRTMRPIKEAGSDSYLRSKKYYP-----YIGYGYVQLTWEENYGRIGKLIGI- 108
Cdd:cd00325    48 ELAAFLAHIAHETGggwaaaggpYAWGLCYIEEIGCASDDCCSSSTGYPCapgksYYGRGPIQLSWNYNYGAASEALGGk 127

                          90       100       110
                  ....*....|....*....|....*....|
gi 1631921356 109 -DLVKNPEK-ALEPLIAIQIAIkgmlngWF 136
Cdd:cd00325   128 dDLLNNPDLvATDPTLAFKTAI------WF 151
 
Name Accession Description Interval E-value
GH19 COG3179
Chitinase, GH19 family [Carbohydrate transport and metabolism];
37-164 1.86e-16

Chitinase, GH19 family [Carbohydrate transport and metabolism];


Pssm-ID: 442412  Cd Length: 193  Bit Score: 73.42  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631921356  37 EYGLTYP-EAAYLLATIYHETGlpnGYRTMRpikEAGSDSYLRSKKYYP----------------------------YIG 87
Cdd:COG3179    34 EFGITTPlRLAHFLAQIAHESG---GLRYLE---ENLNYSALQVFGRYPdgapeaianrvyggrkdlgntapgdgwrYRG 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631921356  88 YGYVQLTWEENYGRIGKLIGIDLVKNPEKALEPLIAIQIAikgmlnGWFtglgFRRKRPVSKYNKQQYVAARNIING 164
Cdd:COG3179   108 RGLIQLTGRANYRAAGDALGLDLVNNPDLLADPEVAARSA------AWF----WATRGLNALADAGDFGEVTRRING 174
Glyco_hydro_19 pfam00182
Chitinase class I;
79-136 6.18e-08

Chitinase class I;


Pssm-ID: 459702  Cd Length: 232  Bit Score: 50.62  E-value: 6.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631921356  79 SKKYYpyiGYGYVQLTWEENYGRIGKLIGIDLVKNPE-KALEPLIAIQIAIkgmlngWF 136
Cdd:pfam00182 104 GKKYY---GRGPIQLSYNYNYGPAGQAIGQDLLNNPDlVATDAVVSFKTAI------WF 153
chitinase_GH19 cd00325
Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the ...
 44-136 2.12e-07

Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Glycoside hydrolase family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases, but they are smaller in size due to certain deletions. Despite lacking any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the prokaryotic/eukaryotic divergence.


Pssm-ID: 381595 [Multi-domain]  Cd Length: 224  Bit Score: 48.97  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631921356  44 EAAYLLATIYHETG---------LPNGYRTMRPIKEAGSDSYLRSKKYYP-----YIGYGYVQLTWEENYGRIGKLIGI- 108
Cdd:cd00325    48 ELAAFLAHIAHETGggwaaaggpYAWGLCYIEEIGCASDDCCSSSTGYPCapgksYYGRGPIQLSWNYNYGAASEALGGk 127

                          90       100       110
                  ....*....|....*....|....*....|
gi 1631921356 109 -DLVKNPEK-ALEPLIAIQIAIkgmlngWF 136
Cdd:cd00325   128 dDLLNNPDLvATDPTLAFKTAI------WF 151
 
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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