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Conserved domains on  [gi|62997712|gb|AAY24700|]
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lysozyme c-4 [Anopheles gambiae]

Protein Classification

LYZ_C_invert domain-containing protein( domain architecture ID 13014106)

LYZ_C_invert domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
32-151 1.39e-53

C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive lysozymes 1 and 2 from Musca domestica, which aid in the use of bacteria as a food source. These lysozymes have high expression in the gut and optimal lytic activity at a lower pH. Other lysozymes in this subfamily have immunological roles. e.g. Anopheles gambiae has eight lysozymes, most of which seem to have immunological roles, those some may function as digestive enzymes in larvae. C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase) has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins.


:

Pssm-ID: 381618 [Multi-domain]  Cd Length: 121  Bit Score: 165.09  E-value: 1.39e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712  32 KVYEKCSLARTFDRQKISsRTLISNWVCLVMAESGADTSKVTKLPND-SANYGIFQINSKTWCREGRK-GGHCDKKCEDF 109
Cdd:cd16899   1 KIFTRCELARELRKLGVP-RSQLANWVCLAEHESSFNTTAVGGPNSDgSGDYGLFQINDKYWCSPGGGsGNGCNVKCEDL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 62997712 110 LNDDLTDDIECAKQIYNDSGFAAWKGWVNRCKQKTLPDLSSC 151
Cdd:cd16899  80 LDDDISDDVKCAKKIYKEQGFNAWVGWKNKCKGKNLPSYSDC 121
 
Name Accession Description Interval E-value
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
32-151 1.39e-53

C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive lysozymes 1 and 2 from Musca domestica, which aid in the use of bacteria as a food source. These lysozymes have high expression in the gut and optimal lytic activity at a lower pH. Other lysozymes in this subfamily have immunological roles. e.g. Anopheles gambiae has eight lysozymes, most of which seem to have immunological roles, those some may function as digestive enzymes in larvae. C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase) has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins.


Pssm-ID: 381618 [Multi-domain]  Cd Length: 121  Bit Score: 165.09  E-value: 1.39e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712  32 KVYEKCSLARTFDRQKISsRTLISNWVCLVMAESGADTSKVTKLPND-SANYGIFQINSKTWCREGRK-GGHCDKKCEDF 109
Cdd:cd16899   1 KIFTRCELARELRKLGVP-RSQLANWVCLAEHESSFNTTAVGGPNSDgSGDYGLFQINDKYWCSPGGGsGNGCNVKCEDL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 62997712 110 LNDDLTDDIECAKQIYNDSGFAAWKGWVNRCKQKTLPDLSSC 151
Cdd:cd16899  80 LDDDISDDVKCAKKIYKEQGFNAWVGWKNKCKGKNLPSYSDC 121
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
32-151 4.04e-39

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 128.56  E-value: 4.04e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712     32 KVYEKCSLARTFDRQKISS--RTLISNWVCLVMAESGADTSKVTKLPNDSANYGIFQINSKTWCREGRKGGH---CDKKC 106
Cdd:smart00263   1 KVFTRCELARELKRLGLDGyrGISLANWVCLAFHESGYNTQATNYNNGGSTDYGIFQINSKYWCNDGKTPGSvnaCGISC 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 62997712    107 EDFLNDDLTDDIECAKQIYNDSGFAAWKGWVNRCK-QKTLPDLSSC 151
Cdd:smart00263  81 SKLLDDDITDDVKCAKKIVSDQGIDAWVAWKNHCQgEDLSQWIRGC 126
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
32-151 1.67e-29

C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of lactose synthase, changing the substrate specificity of galactosyltransferase from N-acetylglucosamine to glucose. C-type lysozymes are secreted bacteriolytic enzymes that cleave the peptidoglycan of bacterial cell walls. Structure is a multi-domain, mixed alpha and beta fold, containing four conserved disulfide bonds.


Pssm-ID: 395016  Cd Length: 123  Bit Score: 104.04  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712    32 KVYEKCSLARTFDRQKISSRTLIS--NWVCLVMAESGADTsKVTKLPNDSANYGIFQINSKTWCREGRKGGH---CDKKC 106
Cdd:pfam00062   1 KQFTRCELARELKKLGMDGYRGISlaEWVCLAFHESGYDT-QAIVYNNGSTDYGIFQINDKYWCKDGKTPQSvniCGISC 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 62997712   107 EDFLNDDLTDDIECAKQIYNDSGFAAWKGWVNRCKQKtLPDLSSC 151
Cdd:pfam00062  80 DKLLDDDITDDIMCAKKILDPQGIDAWLAWKPHCSED-LEQWIGC 123
 
Name Accession Description Interval E-value
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
32-151 1.39e-53

C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive lysozymes 1 and 2 from Musca domestica, which aid in the use of bacteria as a food source. These lysozymes have high expression in the gut and optimal lytic activity at a lower pH. Other lysozymes in this subfamily have immunological roles. e.g. Anopheles gambiae has eight lysozymes, most of which seem to have immunological roles, those some may function as digestive enzymes in larvae. C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase) has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins.


Pssm-ID: 381618 [Multi-domain]  Cd Length: 121  Bit Score: 165.09  E-value: 1.39e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712  32 KVYEKCSLARTFDRQKISsRTLISNWVCLVMAESGADTSKVTKLPND-SANYGIFQINSKTWCREGRK-GGHCDKKCEDF 109
Cdd:cd16899   1 KIFTRCELARELRKLGVP-RSQLANWVCLAEHESSFNTTAVGGPNSDgSGDYGLFQINDKYWCSPGGGsGNGCNVKCEDL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 62997712 110 LNDDLTDDIECAKQIYNDSGFAAWKGWVNRCKQKTLPDLSSC 151
Cdd:cd16899  80 LDDDISDDVKCAKKIYKEQGFNAWVGWKNKCKGKNLPSYSDC 121
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
32-151 4.04e-39

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 128.56  E-value: 4.04e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712     32 KVYEKCSLARTFDRQKISS--RTLISNWVCLVMAESGADTSKVTKLPNDSANYGIFQINSKTWCREGRKGGH---CDKKC 106
Cdd:smart00263   1 KVFTRCELARELKRLGLDGyrGISLANWVCLAFHESGYNTQATNYNNGGSTDYGIFQINSKYWCNDGKTPGSvnaCGISC 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 62997712    107 EDFLNDDLTDDIECAKQIYNDSGFAAWKGWVNRCK-QKTLPDLSSC 151
Cdd:smart00263  81 SKLLDDDITDDVKCAKKIVSDQGIDAWVAWKNHCQgEDLSQWIRGC 126
LYZ cd00119
C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1, ...
32-151 1.36e-35

C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1,4-beta-N-acetylmuramidase) and alpha-lactalbumin (lactose synthase B protein, LA). They have a close evolutionary relationship and similar tertiary structure, however, functionally they are quite different. Lysozymes have primarily bacteriolytic function; hydrolysis of peptidoglycans of prokaryotic cell walls and transglycosylation. LA is a calcium-binding metalloprotein that is expressed exclusively in the mammary gland during lactation. LA is the regulatory subunit of the enzyme lactose synthase. The association of LA with the catalytic component of lactose synthase, galactosyltransferase, alters the acceptor substrate specificity of this glycosyltransferase, facilitating biosynthesis of lactose. Some lysozymes have evolved into digestive enzymes, both in mammals and invertebrates.


Pssm-ID: 340357  Cd Length: 122  Bit Score: 119.60  E-value: 1.36e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712  32 KVYEKCSLARTFDRQKISSRTLISNWVCLVMAESGADTSKVTKLPNDSANYGIFQINSKTWCREGRKGGH---CDKKCED 108
Cdd:cd00119   1 KVFTRCELARLLKDIGGYGGISLPNWVCLMKHESGYDTQATNENNNGSTDYGLFQINSRYWCKDGQTPGArniCDISCSK 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 62997712 109 FLNDDLTDDIECAKQIYNDSGFAAWKGWVNRCkQKTLPDLSSC 151
Cdd:cd00119  81 LLTDDITDAIMCAKKIVDDKGIDAWVAWKNHC-QNKLRQYVSC 122
LYZ_C cd16897
C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). ...
32-145 2.07e-30

C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). In humans, lysozyme is found in a wide variety of tissue types and body fluids. It has bacteriolytic properties through the hydolysis of beta-1,4, glyocosidic linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan, as well as between N-acetyl-D-glucosamine residues in chitodextrins. This family also includes digestive stomach lysozyme, which allow ruminants to digest bacteria in the foregut. The mammalian enzyme is related to lysozyme found hen egg-whites and related species.


Pssm-ID: 340383  Cd Length: 126  Bit Score: 106.58  E-value: 2.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712  32 KVYEKCSLARTFDRQKISSRTLIS--NWVCLVMAESGADTSKVTKLPNDSANYGIFQINSKTWCREGRKGG--HCDKKCE 107
Cdd:cd16897   1 KIFSRCELARILKRGGLDGYRGYSlaNWVCLAYYESGFNTRATNENPDGSTDYGIFQINSRYWCNDGKTPSknLCHISCS 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 62997712 108 DFLNDDLTDDIECAKQIYND-SGFAAWKGWVNRCKQKTL 145
Cdd:cd16897  81 DLLNDDITDDIKCAKKIVKDpQGMGAWVAWRLHCEGRDL 119
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
32-151 1.67e-29

C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of lactose synthase, changing the substrate specificity of galactosyltransferase from N-acetylglucosamine to glucose. C-type lysozymes are secreted bacteriolytic enzymes that cleave the peptidoglycan of bacterial cell walls. Structure is a multi-domain, mixed alpha and beta fold, containing four conserved disulfide bonds.


Pssm-ID: 395016  Cd Length: 123  Bit Score: 104.04  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712    32 KVYEKCSLARTFDRQKISSRTLIS--NWVCLVMAESGADTsKVTKLPNDSANYGIFQINSKTWCREGRKGGH---CDKKC 106
Cdd:pfam00062   1 KQFTRCELARELKKLGMDGYRGISlaEWVCLAFHESGYDT-QAIVYNNGSTDYGIFQINDKYWCKDGKTPQSvniCGISC 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 62997712   107 EDFLNDDLTDDIECAKQIYNDSGFAAWKGWVNRCKQKtLPDLSSC 151
Cdd:pfam00062  80 DKLLDDDITDDIMCAKKILDPQGIDAWLAWKPHCSED-LEQWIGC 123
LYZ_LA cd16898
alpha lactalbumin; alpha-lactalbumin (lactose synthase B protein, LA) is a calcium-binding ...
34-143 2.27e-20

alpha lactalbumin; alpha-lactalbumin (lactose synthase B protein, LA) is a calcium-binding metalloprotein that is expressed exclusively in the mammary gland during lactation. LA is the regulatory subunit of the enzyme lactose synthase. The association of LA with the catalytic component of lactose synthase, galactosyltransferase, alters the acceptor substrate specificity of this glycosyltransferase, facilitating biosynthesis of lactose.


Pssm-ID: 340384  Cd Length: 123  Bit Score: 80.94  E-value: 2.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712  34 YEKCSLARTFDRQKIS--SRTLISNWVCLVMAESGADTSKVTKlPNDSANYGIFQINSKTWCREGR---KGGHCDKKCED 108
Cdd:cd16898   3 FTKCELSQILKEHGLDgfNGISLPEWICVTFHTSGYDTQALVY-NNGSTEYGLFQISNKGWCDDSQepvSRNICGISCSK 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 62997712 109 FLNDDLTDDIECAKQIYNDS-GFAAWKGWVNRCKQK 143
Cdd:cd16898  82 LLDDDITDDIACAKKILAIPkGIDYWKAHKPFCRED 117
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
56-124 1.82e-03

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 34.69  E-value: 1.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62997712  56 NWVCLVMAESGADtsKVTKLPNDSANYGIFQINSKTWCregrkggHCDKKCEDFLNDDlTDDIECAKQI 124
Cdd:cd00442   1 VLAAIIGQESGGN--KPANAGSGSGAAGLFQFMPGTWK-------AYGKNSSSDLNDP-EASIEAAAKY 59
mannanase_GH134 cd19610
glycosyl hydrolase family 134 inverting endo-beta-1,4-mannanase; glycosyl hydrolase family 134 ...
77-133 3.07e-03

glycosyl hydrolase family 134 inverting endo-beta-1,4-mannanase; glycosyl hydrolase family 134 beta-mannanase (E.C. 3.2.1.78) differs from other mannanases in as it has a hen egg white lysozyme fold and cleaves beta-1,4-mannans with inversion of sterochemistry. Beta-mannosidases are enzymes involved in seed germination and the degradation of the hemicellulose fraction of soft- and hardwoods.


Pssm-ID: 381622  Cd Length: 162  Bit Score: 36.24  E-value: 3.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62997712  77 NDSANYGIFQIN---SKTWCREGRKGGHCDKKCEDFLNDDLTDDIECAKQIYNDSGFAAW 133
Cdd:cd19610  50 GDAANFGIFKQNwgmLRTCCSQFKGQTAGDYNNGAVLNSNLAQDIKCLHESQSYYGGDKW 109
 
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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