NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767916595|ref|XP_011508882|]
View 

lysozyme g-like protein 1 isoform X1 [Homo sapiens]

Protein Classification

lysozyme family protein; bifunctional lytic transglycosylase/C40 family peptidase( domain architecture ID 13013923)

lysozyme family protein| bifunctional lytic transglycosylase/C40 family peptidase may catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and/or cleave peptide cross-bridges between glycan chains

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 767916595  38 CGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILV---NMGDRTSMVQDPG 114
Cdd:cd16888    1 CRIGRRHGLNYCGVRASERLAEIDMPYLLRYQPMMRTVGQKYCMDPAVIAGVLSRESPGGNYLVdlgNVGDGLGMVQDTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916595 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 767916595  38 CGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILV---NMGDRTSMVQDPG 114
Cdd:cd16888    1 CRIGRRHGLNYCGVRASERLAEIDMPYLLRYQPMMRTVGQKYCMDPAVIAGVLSRESPGGNYLVdlgNVGDGLGMVQDTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916595 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 767916595  38 CGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILV---NMGDRTSMVQDPG 114
Cdd:cd16888    1 CRIGRRHGLNYCGVRASERLAEIDMPYLLRYQPMMRTVGQKYCMDPAVIAGVLSRESPGGNYLVdlgNVGDGLGMVQDTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916595 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 767916595  32 DTPGASCGIGRRHGLNYCGVRASERLAEIDMPYLLKYQPMMQTIGQKYCMDPAVIAGVLSRKSPGDKILVNMG------- 104
Cdd:cd01021    1 ETTGASAATAKQDGLLYGGVAASEKMAETDLNRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAGAALDKNGwgdhgng 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916595 105 -------DRTSMVQDPgsqaptsWISESQVSQTTEVLTTRIKEIQRRFPTWTPDQYLRGGLCAYSGGAGYVRSSQDL--- 174
Cdd:cd01021   81 fglmqvdKRYHPPKGA-------WDSEEHIEQATGILIDFIKTVQRKHPSWSPEQQLKGGIAAYNAGVGNVQSYAGMdig 153

                        170       180
                 ....*....|....*....|.
gi 767916595 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH