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Conserved domains on  [gi|1818131881|ref|XP_032573423|]
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uncharacterized protein LOC6604768 isoform X1 [Drosophila sechellia]

Protein Classification

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 ...
 596-723 2.68e-62

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: 207.85  E-value: 2.68e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  596 KIYNRCELAKELyHRHKFPMREIPTWVCIAEHESSFNTAAVGKLNTDGSEDHGLFQISDIYWCTHDQTSGKACHIECDRL 675
Cdd:cd16899      1 KIFTRCELAREL-RKLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881  676 LDSDISDDVQCIRTIHEEHtrlsgdGFNAWTVYNGHCRNQNLAQLSDC 723
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 439-566 1.17e-61

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: 205.92  E-value: 1.17e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  439 KVYNRCELAQELYfSHKFPMQDLATWVCIAEHESSFNTAAVGRLNADGSADHGLFQISDLYWCAHNDGGGKGCHIDCNRL 518
Cdd:cd16899      1 KIFTRCELARELR-KLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881  519 LDSDISDDVKCVRTIHEEHtrisgdGFTAWTVYNGHCRQKTRADIASC 566
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 185-301 1.04e-55

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: 188.97  E-value: 1.04e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  185 KIYSRCELAQELYYQHkLPMRQIPTWVCIAQHESSFNTAAVGRLNADGSADHGLFQISDLFWCTHDQRAGKGCHATCNQF 264
Cdd:cd16899      1 KIFTRCELARELRKLG-VPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1818131881  265 LDSSISDDVQCIRRIHQEHtqisgdGFNAWTVYKRNC 301
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKC 110
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 18-144 2.13e-42

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: 150.84  E-value: 2.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   18 KIFDRCELANLLqHRFGLPAAQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHGLFQISDVYWCSPP-GQGKGCALSCSRL 96
Cdd:cd16899      1 KIFTRCELAREL-RKLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGgGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881   97 RDDDIADDVLCVRKIYAEHqrisgdGFTAWQAYDAYCRQDANSYVAGC 144
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
PHA03255 super family cl31530
BDLF3; Provisional
 939-1042 1.18e-04

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 45.28  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  939 TTTTRKPQTASTTKPVSTTAKTTSLPLWSWQTSTTAKPTISESGNRYTTS---TTRSVITNKPSTRPTIAAASRPTtrAT 1015
Cdd:PHA03255    76 TNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTsnvTTRSSSTTSATTRITNATTLAPT--LS 153

                           90       100
                   ....*....|....*....|....*..
gi 1818131881 1016 TRSTNGPIRTTSQpgtyLNTPPTTRSP 1042
Cdd:PHA03255   154 SKGTSNATKTTAE----LPTVPDERQP 176
PRK13914 super family cl36314
invasion associated endopeptidase;
817-1052 7.75e-04

invasion associated endopeptidase;


The actual alignment was detected with superfamily member PRK13914:

Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 43.64  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  817 KPSSTQGAPGYSTQKpnYDHNPFLKAPGSVTPSVKPSHASQEIKPHDNTSYAQnpflsllgKPIVPAQAPI-KPQPKPSS 895
Cdd:PRK13914   123 KITYNDGKTGFVNGK--YLTDKVTSTPVAPTQEVKKETTTQQAAPAAETKTEV--------KQTTQATTPApKVAETKET 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  896 PSKSTQLVSRPYVSSDSFRNELIKFTATSAAVATTSSFTKQSVTTTTRKP--QTASTTKPVSTTakTTSLPLWSWQTStt 973
Cdd:PRK13914   193 PVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAikQTANTATPKAEV--KTEAPAAEKQAA-- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  974 akPTISESGNRYTTSTTRSVITN-------------KPSTRPTIAAASRPTTRATTRSTNGPIRTTSQPGTYLNTPPTTR 1040
Cdd:PRK13914   269 --PVVKENTNTNTATTEKKETTTqqqtapkapteaaKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTN 346

                          250
                   ....*....|..
gi 1818131881 1041 SPIRSSTIRSST 1052
Cdd:PRK13914   347 TNSNTNANQGSS 358
 
Name Accession Description Interval E-value
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 596-723 2.68e-62

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: 207.85  E-value: 2.68e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  596 KIYNRCELAKELyHRHKFPMREIPTWVCIAEHESSFNTAAVGKLNTDGSEDHGLFQISDIYWCTHDQTSGKACHIECDRL 675
Cdd:cd16899      1 KIFTRCELAREL-RKLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881  676 LDSDISDDVQCIRTIHEEHtrlsgdGFNAWTVYNGHCRNQNLAQLSDC 723
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 439-566 1.17e-61

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: 205.92  E-value: 1.17e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  439 KVYNRCELAQELYfSHKFPMQDLATWVCIAEHESSFNTAAVGRLNADGSADHGLFQISDLYWCAHNDGGGKGCHIDCNRL 518
Cdd:cd16899      1 KIFTRCELARELR-KLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881  519 LDSDISDDVKCVRTIHEEHtrisgdGFTAWTVYNGHCRQKTRADIASC 566
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 185-301 1.04e-55

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: 188.97  E-value: 1.04e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  185 KIYSRCELAQELYYQHkLPMRQIPTWVCIAQHESSFNTAAVGRLNADGSADHGLFQISDLFWCTHDQRAGKGCHATCNQF 264
Cdd:cd16899      1 KIFTRCELARELRKLG-VPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1818131881  265 LDSSISDDVQCIRRIHQEHtqisgdGFNAWTVYKRNC 301
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKC 110
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 18-144 2.13e-42

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: 150.84  E-value: 2.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   18 KIFDRCELANLLqHRFGLPAAQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHGLFQISDVYWCSPP-GQGKGCALSCSRL 96
Cdd:cd16899      1 KIFTRCELAREL-RKLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGgGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881   97 RDDDIADDVLCVRKIYAEHqrisgdGFTAWQAYDAYCRQDANSYVAGC 144
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
596-724 1.23e-39

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 143.20  E-value: 1.23e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   596 KIYNRCELAKELYHRHKFPMREI--PTWVCIAEHESSFNTAAVGKlNTDGSEDHGLFQISDIYWCTHDQT--SGKACHIE 671
Cdd:smart00263    1 KVFTRCELARELKRLGLDGYRGIslANWVCLAFHESGYNTQATNY-NNGGSTDYGIFQINSKYWCNDGKTpgSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881   672 CDRLLDSDISDDVQCIRTIHEEHtrlsgdGFNAWTVYNGHCRNQNLAQ-LSDCF 724
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQGEDLSQwIRGCG 127
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
439-567 1.01e-37

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 137.81  E-value: 1.01e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   439 KVYNRCELAQELYFSHK--FPMQDLATWVCIAEHESSFNTAAVGRlNADGSADHGLFQISDLYWCAHN--DGGGKGCHID 514
Cdd:smart00263    1 KVFTRCELARELKRLGLdgYRGISLANWVCLAFHESGYNTQATNY-NNGGSTDYGIFQINSKYWCNDGktPGSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881   515 CNRLLDSDISDDVKCVRTIHEEHtrisgdGFTAWTVYNGHCR-QKTRADIASCF 567
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQgEDLSQWIRGCG 127
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
185-313 1.13e-35

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 132.03  E-value: 1.13e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   185 KIYSRCELAQELYYQHKLPMRQI--PTWVCIAQHESSFNTAAVGRlNADGSADHGLFQISDLFWCTHDQ--RAGKGCHAT 260
Cdd:smart00263    1 KVFTRCELARELKRLGLDGYRGIslANWVCLAFHESGYNTQATNY-NNGGSTDYGIFQINSKYWCNDGKtpGSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881   261 CNQFLDSSISDDVQCIRRIHQEHtqisgdGFNAWTVYKRNCLNQHYEQ-VAACF 313
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQGEDLSQwIRGCG 127
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 596-723 8.49e-32

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: 120.60  E-value: 8.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  596 KIYNRCELAKELYHRHKFPMREI--PTWVCIAEHESSFNTAAVGklNTDGSEDHGLFQISDIYWCTHDQT--SGKACHIE 671
Cdd:pfam00062    1 KQFTRCELARELKKLGMDGYRGIslAEWVCLAFHESGYDTQAIV--YNNGSTDYGIFQINDKYWCKDGKTpqSVNICGIS 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1818131881  672 CDRLLDSDISDDVQCIRTIheehtrLSGDGFNAWTVYNGHCRnQNLAQLSDC 723
Cdd:pfam00062   79 CDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHCS-EDLEQWIGC 123
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 439-558 1.30e-30

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: 117.52  E-value: 1.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  439 KVYNRCELAQELyfsHKFPMQD-----LATWVCIAEHESSFNTAAVGrlNADGSADHGLFQISDLYWCahNDGGGK---- 509
Cdd:pfam00062    1 KQFTRCELAREL---KKLGMDGyrgisLAEWVCLAFHESGYDTQAIV--YNNGSTDYGIFQINDKYWC--KDGKTPqsvn 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1818131881  510 GCHIDCNRLLDSDISDDVKCVRTIheehtrISGDGFTAWTVYNGHCRQK 558
Cdd:pfam00062   74 ICGISCDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHCSED 116
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
18-145 7.77e-29

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 112.38  E-value: 7.77e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881    18 KIFDRCELANLL--QHRFGLPAAQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHGlFQISDVYWCSP---PGQGKGCALS 92
Cdd:smart00263    1 KVFTRCELARELkrLGLDGYRGISLANWVCLAFHESGYNTQATNYNNGGSTDYGI-FQINSKYWCNDgktPGSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881    93 CSRLRDDDIADDVLCVRKIYAEHqrisgdGFTAWQAYDAYCR-QDANSYVAGCG 145
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQgEDLSQWIRGCG 127
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 185-312 8.87e-28

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: 109.43  E-value: 8.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  185 KIYSRCELAQELyyqHKLPMR-----QIPTWVCIAQHESSFNTAAVGrlNADGSADHGLFQISDLFWCTHDQ--RAGKGC 257
Cdd:pfam00062    1 KQFTRCELAREL---KKLGMDgyrgiSLAEWVCLAFHESGYDTQAIV--YNNGSTDYGIFQINDKYWCKDGKtpQSVNIC 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1818131881  258 HATCNQFLDSSISDDVQCIRRIhqehtqISGDGFNAWTVYKRNClNQHYEQVAAC 312
Cdd:pfam00062   76 GISCDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHC-SEDLEQWIGC 123
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 18-144 4.27e-24

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: 98.65  E-value: 4.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   18 KIFDRCELANLLQhRFGLPA---AQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHglFQISDVYWCSP---PGQGKGCAL 91
Cdd:pfam00062    1 KQFTRCELARELK-KLGMDGyrgISLAEWVCLAFHESGYDTQAIVYNNGSTDYGI--FQINDKYWCKDgktPQSVNICGI 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1818131881   92 SCSRLRDDDIADDVLCVRKIyaehqrISGDGFTAWQAYDAYCRQDANSYVaGC 144
Cdd:pfam00062   78 SCDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHCSEDLEQWI-GC 123
PHA03255 PHA03255
BDLF3; Provisional
 939-1042 1.18e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 45.28  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  939 TTTTRKPQTASTTKPVSTTAKTTSLPLWSWQTSTTAKPTISESGNRYTTS---TTRSVITNKPSTRPTIAAASRPTtrAT 1015
Cdd:PHA03255    76 TNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTsnvTTRSSSTTSATTRITNATTLAPT--LS 153

                           90       100
                   ....*....|....*....|....*..
gi 1818131881 1016 TRSTNGPIRTTSQpgtyLNTPPTTRSP 1042
Cdd:PHA03255   154 SKGTSNATKTTAE----LPTVPDERQP 176
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
935-1064 1.22e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 46.19  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  935 KQSVTTTTRKPQ-TASTTKPVSTTAKTTSLPLWSWQTSTTAKPTISESGNRYTTSTTRSVI-----TNKPSTR-PTIAAA 1007
Cdd:pfam05539  169 KTAVTTSKTTSWpTEVSHPTYPSQVTPQSQPATQGHQTATANQRLSSTEPVGTQGTTTSSNpepqtEPPPSQRgPSGSPQ 248

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1818131881 1008 SRPTTRATTRSTNGPIRTTSQPGTYLNTPPTTRSPIRSSTIRSSTFPVFTTRSTTRP 1064
Cdd:pfam05539  249 HPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRPTPRP 305
PRK13914 PRK13914
invasion associated endopeptidase;
817-1052 7.75e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 43.64  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  817 KPSSTQGAPGYSTQKpnYDHNPFLKAPGSVTPSVKPSHASQEIKPHDNTSYAQnpflsllgKPIVPAQAPI-KPQPKPSS 895
Cdd:PRK13914   123 KITYNDGKTGFVNGK--YLTDKVTSTPVAPTQEVKKETTTQQAAPAAETKTEV--------KQTTQATTPApKVAETKET 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  896 PSKSTQLVSRPYVSSDSFRNELIKFTATSAAVATTSSFTKQSVTTTTRKP--QTASTTKPVSTTakTTSLPLWSWQTStt 973
Cdd:PRK13914   193 PVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAikQTANTATPKAEV--KTEAPAAEKQAA-- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  974 akPTISESGNRYTTSTTRSVITN-------------KPSTRPTIAAASRPTTRATTRSTNGPIRTTSQPGTYLNTPPTTR 1040
Cdd:PRK13914   269 --PVVKENTNTNTATTEKKETTTqqqtapkapteaaKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTN 346

                          250
                   ....*....|..
gi 1818131881 1041 SPIRSSTIRSST 1052
Cdd:PRK13914   347 TNSNTNANQGSS 358
 
Name Accession Description Interval E-value
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 596-723 2.68e-62

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: 207.85  E-value: 2.68e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  596 KIYNRCELAKELyHRHKFPMREIPTWVCIAEHESSFNTAAVGKLNTDGSEDHGLFQISDIYWCTHDQTSGKACHIECDRL 675
Cdd:cd16899      1 KIFTRCELAREL-RKLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881  676 LDSDISDDVQCIRTIHEEHtrlsgdGFNAWTVYNGHCRNQNLAQLSDC 723
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 439-566 1.17e-61

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: 205.92  E-value: 1.17e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  439 KVYNRCELAQELYfSHKFPMQDLATWVCIAEHESSFNTAAVGRLNADGSADHGLFQISDLYWCAHNDGGGKGCHIDCNRL 518
Cdd:cd16899      1 KIFTRCELARELR-KLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881  519 LDSDISDDVKCVRTIHEEHtrisgdGFTAWTVYNGHCRQKTRADIASC 566
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 185-301 1.04e-55

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: 188.97  E-value: 1.04e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  185 KIYSRCELAQELYYQHkLPMRQIPTWVCIAQHESSFNTAAVGRLNADGSADHGLFQISDLFWCTHDQRAGKGCHATCNQF 264
Cdd:cd16899      1 KIFTRCELARELRKLG-VPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGGGSGNGCNVKCEDL 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1818131881  265 LDSSISDDVQCIRRIHQEHtqisgdGFNAWTVYKRNC 301
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKC 110
LYZ_C_invert cd16899
C-type invertebrate lysozyme; C-type lysozyme proteins of invertebrates, including digestive ...
 18-144 2.13e-42

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: 150.84  E-value: 2.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   18 KIFDRCELANLLqHRFGLPAAQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHGLFQISDVYWCSPP-GQGKGCALSCSRL 96
Cdd:cd16899      1 KIFTRCELAREL-RKLGVPRSQLANWVCLAEHESSFNTTAVGGPNSDGSGDYGLFQINDKYWCSPGgGSGNGCNVKCEDL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881   97 RDDDIADDVLCVRKIYAEHqrisgdGFTAWQAYDAYCRQDANSYVAGC 144
Cdd:cd16899     80 LDDDISDDVKCAKKIYKEQ------GFNAWVGWKNKCKGKNLPSYSDC 121
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
596-724 1.23e-39

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 143.20  E-value: 1.23e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   596 KIYNRCELAKELYHRHKFPMREI--PTWVCIAEHESSFNTAAVGKlNTDGSEDHGLFQISDIYWCTHDQT--SGKACHIE 671
Cdd:smart00263    1 KVFTRCELARELKRLGLDGYRGIslANWVCLAFHESGYNTQATNY-NNGGSTDYGIFQINSKYWCNDGKTpgSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881   672 CDRLLDSDISDDVQCIRTIHEEHtrlsgdGFNAWTVYNGHCRNQNLAQ-LSDCF 724
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQGEDLSQwIRGCG 127
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
439-567 1.01e-37

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 137.81  E-value: 1.01e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   439 KVYNRCELAQELYFSHK--FPMQDLATWVCIAEHESSFNTAAVGRlNADGSADHGLFQISDLYWCAHN--DGGGKGCHID 514
Cdd:smart00263    1 KVFTRCELARELKRLGLdgYRGISLANWVCLAFHESGYNTQATNY-NNGGSTDYGIFQINSKYWCNDGktPGSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881   515 CNRLLDSDISDDVKCVRTIHEEHtrisgdGFTAWTVYNGHCR-QKTRADIASCF 567
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQgEDLSQWIRGCG 127
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
185-313 1.13e-35

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 132.03  E-value: 1.13e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   185 KIYSRCELAQELYYQHKLPMRQI--PTWVCIAQHESSFNTAAVGRlNADGSADHGLFQISDLFWCTHDQ--RAGKGCHAT 260
Cdd:smart00263    1 KVFTRCELARELKRLGLDGYRGIslANWVCLAFHESGYNTQATNY-NNGGSTDYGIFQINSKYWCNDGKtpGSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881   261 CNQFLDSSISDDVQCIRRIHQEHtqisgdGFNAWTVYKRNCLNQHYEQ-VAACF 313
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQGEDLSQwIRGCG 127
LYZ_C cd16897
C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). ...
 439-556 3.98e-33

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: 124.69  E-value: 3.98e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  439 KVYNRCELAQELyfsHKFPMqD------LATWVCIAEHESSFNTAAVGRlNADGSADHGLFQISDLYWCahNDGGGK--- 509
Cdd:cd16897      1 KIFSRCELARIL---KRGGL-DgyrgysLANWVCLAYYESGFNTRATNE-NPDGSTDYGIFQINSRYWC--NDGKTPskn 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1818131881  510 GCHIDCNRLLDSDISDDVKCVRTIHEEHtrisgDGFTAWTVYNGHCR 556
Cdd:cd16897     74 LCHISCSDLLNDDITDDIKCAKKIVKDP-----QGMGAWVAWRLHCE 115
LYZ_C cd16897
C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). ...
 596-723 4.68e-32

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: 121.60  E-value: 4.68e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  596 KIYNRCELAKELYHRH--KFPMREIPTWVCIAEHESSFNTAAVGKlNTDGSEDHGLFQISDIYWCTHDQTSGK-ACHIEC 672
Cdd:cd16897      1 KIFSRCELARILKRGGldGYRGYSLANWVCLAYYESGFNTRATNE-NPDGSTDYGIFQINSRYWCNDGKTPSKnLCHISC 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1818131881  673 DRLLDSDISDDVQCIRTIHEEHtrlsgDGFNAWTVYNGHCRNQNLAQ-LSDC 723
Cdd:cd16897     80 SDLLNDDITDDIKCAKKIVKDP-----QGMGAWVAWRLHCEGRDLSRwLDGC 126
LYZ cd00119
C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1, ...
 596-723 8.26e-32

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: 120.75  E-value: 8.26e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  596 KIYNRCELAKELYHRHKFPMREIPTWVCIAEHESSFNTAAVGKlNTDGSEDHGLFQISDIYWCTHDQT--SGKACHIECD 673
Cdd:cd00119      1 KVFTRCELARLLKDIGGYGGISLPNWVCLMKHESGYDTQATNE-NNNGSTDYGLFQINSRYWCKDGQTpgARNICDISCS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1818131881  674 RLLDSDISDDVQCIRTIHEEHtrlsgdGFNAWTVYNGHCRNQnLAQLSDC 723
Cdd:cd00119     80 KLLTDDITDAIMCAKKIVDDK------GIDAWVAWKNHCQNK-LRQYVSC 122
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 596-723 8.49e-32

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: 120.60  E-value: 8.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  596 KIYNRCELAKELYHRHKFPMREI--PTWVCIAEHESSFNTAAVGklNTDGSEDHGLFQISDIYWCTHDQT--SGKACHIE 671
Cdd:pfam00062    1 KQFTRCELARELKKLGMDGYRGIslAEWVCLAFHESGYDTQAIV--YNNGSTDYGIFQINDKYWCKDGKTpqSVNICGIS 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1818131881  672 CDRLLDSDISDDVQCIRTIheehtrLSGDGFNAWTVYNGHCRnQNLAQLSDC 723
Cdd:pfam00062   79 CDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHCS-EDLEQWIGC 123
LYZ cd00119
C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1, ...
 439-566 1.25e-30

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: 117.29  E-value: 1.25e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  439 KVYNRCELAQELYFSHKFPMQDLATWVCIAEHESSFNTAAVGRlNADGSADHGLFQISDLYWC--AHNDGGGKGCHIDCN 516
Cdd:cd00119      1 KVFTRCELARLLKDIGGYGGISLPNWVCLMKHESGYDTQATNE-NNNGSTDYGLFQINSRYWCkdGQTPGARNICDISCS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1818131881  517 RLLDSDISDDVKCVRTIHEEHtrisgdGFTAWTVYNGHCRQKTRaDIASC 566
Cdd:cd00119     80 KLLTDDITDAIMCAKKIVDDK------GIDAWVAWKNHCQNKLR-QYVSC 122
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 439-558 1.30e-30

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: 117.52  E-value: 1.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  439 KVYNRCELAQELyfsHKFPMQD-----LATWVCIAEHESSFNTAAVGrlNADGSADHGLFQISDLYWCahNDGGGK---- 509
Cdd:pfam00062    1 KQFTRCELAREL---KKLGMDGyrgisLAEWVCLAFHESGYDTQAIV--YNNGSTDYGIFQINDKYWC--KDGKTPqsvn 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1818131881  510 GCHIDCNRLLDSDISDDVKCVRTIheehtrISGDGFTAWTVYNGHCRQK 558
Cdd:pfam00062   74 ICGISCDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHCSED 116
LYZ1 smart00263
Alpha-lactalbumin / lysozyme C;
18-145 7.77e-29

Alpha-lactalbumin / lysozyme C;


Pssm-ID: 197612  Cd Length: 127  Bit Score: 112.38  E-value: 7.77e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881    18 KIFDRCELANLL--QHRFGLPAAQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHGlFQISDVYWCSP---PGQGKGCALS 92
Cdd:smart00263    1 KVFTRCELARELkrLGLDGYRGISLANWVCLAFHESGYNTQATNYNNGGSTDYGI-FQINSKYWCNDgktPGSVNACGIS 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1818131881    93 CSRLRDDDIADDVLCVRKIYAEHqrisgdGFTAWQAYDAYCR-QDANSYVAGCG 145
Cdd:smart00263   80 CSKLLDDDITDDVKCAKKIVSDQ------GIDAWVAWKNHCQgEDLSQWIRGCG 127
LYZ_C cd16897
C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). ...
 185-305 2.12e-28

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: 111.20  E-value: 2.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  185 KIYSRCELAQELyyqHKLPM---RQI--PTWVCIAQHESSFNTAAVGRlNADGSADHGLFQISDLFWC-THDQRAGKGCH 258
Cdd:cd16897      1 KIFSRCELARIL---KRGGLdgyRGYslANWVCLAYYESGFNTRATNE-NPDGSTDYGIFQINSRYWCnDGKTPSKNLCH 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1818131881  259 ATCNQFLDSSISDDVQCIRRIHQEHtqisgDGFNAWTVYKRNCLNQH 305
Cdd:cd16897     77 ISCSDLLNDDITDDIKCAKKIVKDP-----QGMGAWVAWRLHCEGRD 118
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 185-312 8.87e-28

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: 109.43  E-value: 8.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  185 KIYSRCELAQELyyqHKLPMR-----QIPTWVCIAQHESSFNTAAVGrlNADGSADHGLFQISDLFWCTHDQ--RAGKGC 257
Cdd:pfam00062    1 KQFTRCELAREL---KKLGMDgyrgiSLAEWVCLAFHESGYDTQAIV--YNNGSTDYGIFQINDKYWCKDGKtpQSVNIC 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1818131881  258 HATCNQFLDSSISDDVQCIRRIhqehtqISGDGFNAWTVYKRNClNQHYEQVAAC 312
Cdd:pfam00062   76 GISCDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHC-SEDLEQWIGC 123
LYZ cd00119
C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1, ...
 185-312 1.35e-27

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: 108.81  E-value: 1.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  185 KIYSRCELAQELYYQHKLPMRQIPTWVCIAQHESSFNTAAVGRlNADGSADHGLFQISDLFWCTHDQ--RAGKGCHATCN 262
Cdd:cd00119      1 KVFTRCELARLLKDIGGYGGISLPNWVCLMKHESGYDTQATNE-NNNGSTDYGLFQINSRYWCKDGQtpGARNICDISCS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1818131881  263 QFLDSSISDDVQCIRRIHQEHtqisgdGFNAWTVYKRNCLNQhYEQVAAC 312
Cdd:cd00119     80 KLLTDDITDAIMCAKKIVDDK------GIDAWVAWKNHCQNK-LRQYVSC 122
LYZ_LA cd16898
alpha lactalbumin; alpha-lactalbumin (lactose synthase B protein, LA) is a calcium-binding ...
 597-713 1.42e-24

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: 100.20  E-value: 1.42e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  597 IYNRCELAKEL--YHRHKFPMREIPTWVCIAEHESSFNTAAVgkLNTDGSEDHGLFQISDIYWCTHDQT--SGKACHIEC 672
Cdd:cd16898      2 IFTKCELSQILkeHGLDGFNGISLPEWICVTFHTSGYDTQAL--VYNNGSTEYGLFQISNKGWCDDSQEpvSRNICGISC 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1818131881  673 DRLLDSDISDDVQCIRTIHEEhtrlsGDGFNAWTVYNGHCR 713
Cdd:cd16898     80 SKLLDDDITDDIACAKKILAI-----PKGIDYWKAHKPFCR 115
Lys pfam00062
C-type lysozyme/alpha-lactalbumin family; Alpha-lactalbumin is the regulatory subunit of ...
 18-144 4.27e-24

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: 98.65  E-value: 4.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   18 KIFDRCELANLLQhRFGLPA---AQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHglFQISDVYWCSP---PGQGKGCAL 91
Cdd:pfam00062    1 KQFTRCELARELK-KLGMDGyrgISLAEWVCLAFHESGYDTQAIVYNNGSTDYGI--FQINDKYWCKDgktPQSVNICGI 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1818131881   92 SCSRLRDDDIADDVLCVRKIyaehqrISGDGFTAWQAYDAYCRQDANSYVaGC 144
Cdd:pfam00062   78 SCDKLLDDDITDDIMCAKKI------LDPQGIDAWLAWKPHCSEDLEQWI-GC 123
LYZ_C cd16897
C-type lysozyme; C-type lysozyme (chicken or conventional type; 1, 4-beta-N-acetylmuramidase). ...
 18-144 2.58e-23

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: 96.57  E-value: 2.58e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   18 KIFDRCELANLLqHRFGLPAAQVATL---VCIAQHSSDFNTAAFGSGVGLGGGSHGlFQISDVYWCSPpgqGK-----GC 89
Cdd:cd16897      1 KIFSRCELARIL-KRGGLDGYRGYSLanwVCLAYYESGFNTRATNENPDGSTDYGI-FQINSRYWCND---GKtpsknLC 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1818131881   90 ALSCSRLRDDDIADDVLCVRKIYAEHQrisgdGFTAWQAYDAYCR-QDANSYVAGC 144
Cdd:cd16897     76 HISCSDLLNDDITDDIKCAKKIVKDPQ-----GMGAWVAWRLHCEgRDLSRWLDGC 126
LYZ_LA cd16898
alpha lactalbumin; alpha-lactalbumin (lactose synthase B protein, LA) is a calcium-binding ...
 441-558 1.92e-22

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: 94.04  E-value: 1.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  441 YNRCELAQEL--YFSHKFPMQDLATWVCIAEHESSFNTAAVgrLNADGSADHGLFQISDLYWCA--HNDGGGKGCHIDCN 516
Cdd:cd16898      3 FTKCELSQILkeHGLDGFNGISLPEWICVTFHTSGYDTQAL--VYNNGSTEYGLFQISNKGWCDdsQEPVSRNICGISCS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1818131881  517 RLLDSDISDDVKCVRTIHEEhtrisGDGFTAWTVYNGHCRQK 558
Cdd:cd16898     81 KLLDDDITDDIACAKKILAI-----PKGIDYWKAHKPFCRED 117
LYZ cd00119
C-type lysozyme and alpha-lactalbumin; C-type lysozyme (chicken or conventional type, 1, ...
 18-142 2.00e-22

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: 93.79  E-value: 2.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   18 KIFDRCELANLLQHRFGLPAAQVATLVCIAQHSSDFNTAAfGSGVGLGGGSHGLFQISDVYWCSP---PGQGKGCALSCS 94
Cdd:cd00119      1 KVFTRCELARLLKDIGGYGGISLPNWVCLMKHESGYDTQA-TNENNNGSTDYGLFQINSRYWCKDgqtPGARNICDISCS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1818131881   95 RLRDDDIADDVLCVRKIYAEHqrisgdGFTAWQAYDAYCRQDANSYVA 142
Cdd:cd00119     80 KLLTDDITDAIMCAKKIVDDK------GIDAWVAWKNHCQNKLRQYVS 121
LYZ_LA cd16898
alpha lactalbumin; alpha-lactalbumin (lactose synthase B protein, LA) is a calcium-binding ...
 186-302 3.92e-21

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: 90.19  E-value: 3.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  186 IYSRCELAQELYyQHKLPMRQ---IPTWVCIAQHESSFNTAAVgrLNADGSADHGLFQISDLFWCTHDQ--RAGKGCHAT 260
Cdd:cd16898      2 IFTKCELSQILK-EHGLDGFNgisLPEWICVTFHTSGYDTQAL--VYNNGSTEYGLFQISNKGWCDDSQepVSRNICGIS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1818131881  261 CNQFLDSSISDDVQCIRRIHQEhtqisGDGFNAWTVYKRNCL 302
Cdd:cd16898     79 CSKLLDDDITDDIACAKKILAI-----PKGIDYWKAHKPFCR 115
LYZ_LA cd16898
alpha lactalbumin; alpha-lactalbumin (lactose synthase B protein, LA) is a calcium-binding ...
 19-136 2.81e-19

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: 84.79  E-value: 2.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881   19 IFDRCELANLLQHRF--GLPAAQVATLVCIAQHSSDFNTAAFGSGVGLGGGSHglFQISDVYWC----SPPGQGKgCALS 92
Cdd:cd16898      2 IFTKCELSQILKEHGldGFNGISLPEWICVTFHTSGYDTQALVYNNGSTEYGL--FQISNKGWCddsqEPVSRNI-CGIS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1818131881   93 CSRLRDDDIADDVLCVRKIYAEhqrisGDGFTAWQAYDAYCRQD 136
Cdd:cd16898     79 CSKLLDDDITDDIACAKKILAI-----PKGIDYWKAHKPFCRED 117
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 624-657 9.52e-05

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 42.90  E-value: 9.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1818131881  624 IAEHESSFNTAAVGKlNTDGSEDHGLFQISDIYW 657
Cdd:cd13400     11 IAKVESGFNPNAINR-NKNGSYDIGLMQINSIWL 43
PHA03255 PHA03255
BDLF3; Provisional
 939-1042 1.18e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 45.28  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  939 TTTTRKPQTASTTKPVSTTAKTTSLPLWSWQTSTTAKPTISESGNRYTTS---TTRSVITNKPSTRPTIAAASRPTtrAT 1015
Cdd:PHA03255    76 TNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTsnvTTRSSSTTSATTRITNATTLAPT--LS 153

                           90       100
                   ....*....|....*....|....*..
gi 1818131881 1016 TRSTNGPIRTTSQpgtyLNTPPTTRSP 1042
Cdd:PHA03255   154 SKGTSNATKTTAE----LPTVPDERQP 176
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
935-1064 1.22e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 46.19  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  935 KQSVTTTTRKPQ-TASTTKPVSTTAKTTSLPLWSWQTSTTAKPTISESGNRYTTSTTRSVI-----TNKPSTR-PTIAAA 1007
Cdd:pfam05539  169 KTAVTTSKTTSWpTEVSHPTYPSQVTPQSQPATQGHQTATANQRLSSTEPVGTQGTTTSSNpepqtEPPPSQRgPSGSPQ 248

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1818131881 1008 SRPTTRATTRSTNGPIRTTSQPGTYLNTPPTTRSPIRSSTIRSSTFPVFTTRSTTRP 1064
Cdd:pfam05539  249 HPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRPTPRP 305
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 206-241 1.66e-04

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 42.13  E-value: 1.66e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1818131881  206 QIPTWV--CIAQHESSFNTAAVGRlNADGSADHGLFQI 241
Cdd:cd13400      2 GVPPRLlrAIAKVESGFNPNAINR-NKNGSYDIGLMQI 38
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 467-495 6.38e-04

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 40.59  E-value: 6.38e-04
                           10        20
                   ....*....|....*....|....*....
gi 1818131881  467 IAEHESSFNTAAVGRlNADGSADHGLFQI 495
Cdd:cd13400     11 IAKVESGFNPNAINR-NKNGSYDIGLMQI 38
PRK13914 PRK13914
invasion associated endopeptidase;
817-1052 7.75e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 43.64  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  817 KPSSTQGAPGYSTQKpnYDHNPFLKAPGSVTPSVKPSHASQEIKPHDNTSYAQnpflsllgKPIVPAQAPI-KPQPKPSS 895
Cdd:PRK13914   123 KITYNDGKTGFVNGK--YLTDKVTSTPVAPTQEVKKETTTQQAAPAAETKTEV--------KQTTQATTPApKVAETKET 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  896 PSKSTQLVSRPYVSSDSFRNELIKFTATSAAVATTSSFTKQSVTTTTRKP--QTASTTKPVSTTakTTSLPLWSWQTStt 973
Cdd:PRK13914   193 PVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAikQTANTATPKAEV--KTEAPAAEKQAA-- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  974 akPTISESGNRYTTSTTRSVITN-------------KPSTRPTIAAASRPTTRATTRSTNGPIRTTSQPGTYLNTPPTTR 1040
Cdd:PRK13914   269 --PVVKENTNTNTATTEKKETTTqqqtapkapteaaKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTN 346

                          250
                   ....*....|..
gi 1818131881 1041 SPIRSSTIRSST 1052
Cdd:PRK13914   347 TNSNTNANQGSS 358
PHA03255 PHA03255
BDLF3; Provisional
 937-1066 8.22e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.58  E-value: 8.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  937 SVTTTTRKPQTASTTKPVSTTAKTTSLPLWSwqtsttakptiSESGNRYTTSTTrsviTNKPSTrpTIAAASRPTTRAT- 1015
Cdd:PHA03255    21 SLIWTSSGSSTASAGNVTGTTAVTTPSPSAS-----------GPSTNQSTTLTT----TSAPIT--TTAILSTNTTTVTs 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1818131881 1016 TRSTNGPIRTTSQPGTYLNTPPTTRSPIRSSTIRSSTFPVFTTRSTTRPIY 1066
Cdd:PHA03255    84 TGTTVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSS 134
SLT_3 pfam18896
Lysozyme like domain; This entry represents a lysozyme like domain found in candidate phyla ...
 205-262 4.01e-03

Lysozyme like domain; This entry represents a lysozyme like domain found in candidate phyla radiation bacteria. The domain contains several conserved cysteine and histidine residues suggesting that it may bind to zinc.


Pssm-ID: 436815 [Multi-domain]  Cd Length: 89  Bit Score: 37.77  E-value: 4.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1818131881  205 RQIPTWVCIAQHESSFNTAAVGRL-NADGSADHGLFQISDLFWCTHDQRAGKGCHATCN 262
Cdd:pfam18896   12 DDAVTAVAVAMAESGGDPSAVGDLaNTKGSPSRGLWQINSLAHPEVTGPDACAYDPQCN 70
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 939-1062 5.75e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.10  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  939 TTTTRKPQTAST--TKPVSTTAKTTSLPLWSwqTSTTAKPTiSESGNRYTTSTTRSVITNKPSTRPTIAAASRPTTRATT 1016
Cdd:pfam17823   53 KSSEQ*NFCAATaaPAPVTLTKGTSAAHLNS--TEVTAEHT-PHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQS 129

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1818131881 1017 RSTngpirTTSQPGTYLNTPPTTRSPIRSSTIRSSTfPVFTTRSTT 1062
Cdd:pfam17823  130 LPA-----AIAALPSEAFSAPRAAACRANASAAPRA-AIAAASAPH 169
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 463-527 8.39e-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: 35.85  E-value: 8.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1818131881  463 TWVCIAEHESSFNTAAvgrLNADGSADHGLFQISDLYWCAHndggGKGCHIDcnrLLDSDISDDV 527
Cdd:cd00442      1 VLAAIIGQESGGNKPA---NAGSGSGAAGLFQFMPGTWKAY----GKNSSSD---LNDPEASIEA 55
DUF316 pfam03761
Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes ...
 575-664 9.13e-03

Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes that are part of the chymotrypsin family S1, ie a serine peptidase. The C. elegans sequence UniProt:O01566 is trypsin-6: all the active site residues are present (His90, Asp168, Ser267).


Pssm-ID: 367641  Cd Length: 281  Bit Score: 39.72  E-value: 9.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818131881  575 EVAKPSKGNELVKKTSPTPKAKIYNRCELAKELYHRHKFPM-------REIPTW-VCIAEHESSFNTAAVGK---LNTDG 643
Cdd:pfam03761  123 DIMDLSKKKGKNSFRDNITRAYVLNGCANTKSKFDLSAKPMlvelegpLEPNISyPCLADESTSLEKGDAVDvygIDSSG 202

                           90       100
                   ....*....|....*....|.
gi 1818131881  644 SEDHGLFQISDIYWCTHDQTS 664
Cdd:pfam03761  203 ELKHRKLNIVNCYSNDLSIGT 223
 
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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