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Conserved domains on  [gi|47117245|sp|Q8N1E2|]
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RecName: Full=Lysozyme g-like protein 1; Flags: Precursor

Protein Classification

lyz_G-like_1 domain-containing protein( domain architecture ID 13013923)

lyz_G-like_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lyz_G-like_1 cd16888
lysozyme G-like protein 1; Eukaryotic goose-type or G-type lysozymes (goose egg-white lysozyme; ...
 38-194 6.65e-117

lysozyme G-like protein 1; Eukaryotic goose-type or G-type lysozymes (goose egg-white lysozyme; GEWL) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozyme G-like proteins, and this family corresponds to human and mouse lysozyme G-like protein 1. In humans and some other species, the canonical catalytic glutamate residue is absent, suggesting a loss of muramidase activity.


:

Pssm-ID: 381609  Cd Length: 160  Bit Score: 328.41  E-value: 6.65e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245  38 CGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILV---NMGDRTSMVQDPG 114
Cdd:cd16888   1 CRIGRRHGLNYCGVRASERLAEIDMPYLLRYQPMMRTVGQKYCMDPAVIAGVLSRESPGGNYLVdlgNVGDGLGMVQDTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245 115 SQAPTSWISESQVSQTTEVLTTRIKEIQRRFPTWTPDQYLRGGLCAYSGGAGYVRSSQDLSCDFCNDVLARAKYLKRHGF 194
Cdd:cd16888  81 FYAPTSWISESQVSQKTEVLTSRIKEIQRRFPTWTPDQCLRGGLCAYSGGPGYVRSNQDLSCDFCNDVLARAKYFKRHGF 160
 
Name Accession Description Interval E-value
lyz_G-like_1 cd16888
lysozyme G-like protein 1; Eukaryotic goose-type or G-type lysozymes (goose egg-white lysozyme; ...
 38-194 6.65e-117

lysozyme G-like protein 1; Eukaryotic goose-type or G-type lysozymes (goose egg-white lysozyme; GEWL) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozyme G-like proteins, and this family corresponds to human and mouse lysozyme G-like protein 1. In humans and some other species, the canonical catalytic glutamate residue is absent, suggesting a loss of muramidase activity.


Pssm-ID: 381609  Cd Length: 160  Bit Score: 328.41  E-value: 6.65e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245  38 CGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILV---NMGDRTSMVQDPG 114
Cdd:cd16888   1 CRIGRRHGLNYCGVRASERLAEIDMPYLLRYQPMMRTVGQKYCMDPAVIAGVLSRESPGGNYLVdlgNVGDGLGMVQDTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245 115 SQAPTSWISESQVSQTTEVLTTRIKEIQRRFPTWTPDQYLRGGLCAYSGGAGYVRSSQDLSCDFCNDVLARAKYLKRHGF 194
Cdd:cd16888  81 FYAPTSWISESQVSQKTEVLTSRIKEIQRRFPTWTPDQCLRGGLCAYSGGPGYVRSNQDLSCDFCNDVLARAKYFKRHGF 160
 
Name Accession Description Interval E-value
lyz_G-like_1 cd16888
lysozyme G-like protein 1; Eukaryotic goose-type or G-type lysozymes (goose egg-white lysozyme; ...
 38-194 6.65e-117

lysozyme G-like protein 1; Eukaryotic goose-type or G-type lysozymes (goose egg-white lysozyme; GEWL) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozyme G-like proteins, and this family corresponds to human and mouse lysozyme G-like protein 1. In humans and some other species, the canonical catalytic glutamate residue is absent, suggesting a loss of muramidase activity.


Pssm-ID: 381609  Cd Length: 160  Bit Score: 328.41  E-value: 6.65e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245  38 CGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILV---NMGDRTSMVQDPG 114
Cdd:cd16888   1 CRIGRRHGLNYCGVRASERLAEIDMPYLLRYQPMMRTVGQKYCMDPAVIAGVLSRESPGGNYLVdlgNVGDGLGMVQDTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245 115 SQAPTSWISESQVSQTTEVLTTRIKEIQRRFPTWTPDQYLRGGLCAYSGGAGYVRSSQDLSCDFCNDVLARAKYLKRHGF 194
Cdd:cd16888  81 FYAPTSWISESQVSQKTEVLTSRIKEIQRRFPTWTPDQCLRGGLCAYSGGPGYVRSNQDLSCDFCNDVLARAKYFKRHGF 160
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 32-193 4.99e-48

Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2.


Pssm-ID: 381601 [Multi-domain]  Cd Length: 174  Bit Score: 154.68  E-value: 4.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245  32 DTPGASCGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILVNMG------- 104
Cdd:cd01021   1 ETTGASAATAKQDGLLYGGVAASEKMAETDLNRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAGAALDKNGwgdhgng 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47117245 105 -------DRTSMVQDPgsqaptsWISESQVSQTTEVLTTRIKEIQRRFPTWTPDQYLRGGLCAYSGGAGYVRSSQDL--- 174
Cdd:cd01021  81 fglmqvdKRYHPPKGA-------WDSEEHIEQATGILIDFIKTVQRKHPSWSPEQQLKGGIAAYNAGVGNVQSYAGMdig 153

                       170       180
                ....*....|....*....|.
gi 47117245 175 --SCDFCNDVLARAKYLKRHG 193
Cdd:cd01021 154 ttGNDYSNDVIARAQWYKNNG 174
 
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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