NCBI Conserved Domain Search

The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.

Pssm-ID: 119376 Cd Length: 191 Bit Score: 190.09 E-value: 2.02e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 162 KGVVDVSEHNGTIDWQAAKNAGVEGAIIRLSYGWYNRY--DYQALRNISECKRLGIPFGVYIYSYAYDSNCAWGEGDDTA 239
Cdd:cd06414     1 KKGIDVSEWQGDIDWKKVKASGVDFAIIRAGYGGYGELqeDKYFEENIKGAKAAGIPVGVYFYSYAVTVAEAREEAEFVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 240 KKLyyagvSPGDLSYPVFYDLENWTWTGHtpPTNPGVYDDIVNKWWSRMQQSGYnNLSVYSYTSYLNGPLNSYNIRSSTR 319
Cdd:cd06414    81 RLI-----KGYKLSYPVYYDLEDETQLGA--GLSKDQRTDIANAFCETIEAAGY-YPGIYANLSWLTNKLDDERLSKYDV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2467975801 320 WVASYGARTGFGFstNDRGWQYSDNGWVNGI-GNVDHNAF 358
Cdd:cd06414   153 WVAQYGNSPTYPG--NYGMWQYTSSGSVPGIsGNVDLNYC 190

Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442971 Cd Length: 208 Bit Score: 133.48 E-value: 1.35e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 165 VDVSEHNGTIDWQAAKNAGVEGAIIRLSYGWYNRyDYQALRNISECKRLGIPFGVYIYSYaydsncAWGEGDDTAkKLYY 244
Cdd:COG3757    14 IDVSHYQGDIDWAAVKAAGIDFAYIKATEGTDYV-DPKFARNWAGARAAGLPRGAYHFFR------PCSDAAAQA-DNFI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 245 AGVSPGDLSYPVFYDLENWTWTGhtppTNPGVYDDIVNKWWSRMQQSGYNNLSVYSYTSYLNGPLNSYNIRSSTRWVASY 324
Cdd:COG3757    86 STVPRDPGDLPPVLDLEENGYYG----LSPAQLRAWLKAFLDEVEAHTGRKPIIYTSPSFYNDYLGNSDFSDYPLWIARY 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2467975801 325 GARTGFGFSTNDRGWQYSDNGWVNGI-GNVDHNAF-GNY 361
Cdd:COG3757   162 GSSPGYLPGRNWTFWQYTSSGRVPGIsGNVDLNVFnGSR 200

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 117.47 E-value: 8.22e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRSEGARLI--TCilNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYR 471
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTANGAPVQqwTC--NGGANQQWTLTPVGDGYYTIRNVASGKCLDVAGGSTANGANVQQWT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 472 GNGGGNQRWRFYRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVWSADGGPNQQF 530
Cdd:cd00161    79 CNGGDNQQWRLEPVGDGYYRIVNKHSG---KCLDVSGGSTANGANVQQWTCNGGANQQW 134

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 117.47 E-value: 8.22e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSGLYLDVNGASRSEGARLI--TCilNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYR 632
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTANGAPVQqwTC--NGGANQQWTLTPVGDGYYTIRNVASGKCLDVAGGSTANGANVQQWT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 633 GNGGGNQRWRFYRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVWSADGGPNQQF 691
Cdd:cd00161    79 CNGGDNQQWRLEPVGDGYYRIVNKHSG---KCLDVSGGSTANGANVQQWTCNGGANQQW 134

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 106.30 E-value: 5.60e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 501 NKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLELVDfdgtplsslgtqvrdirEGDYRIASAYSGLYLDVNGASRSEGAR 580
Cdd:cd00161    11 GKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVG-----------------DGYYTIRNVASGKCLDVAGGSTANGAN 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 581 LITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRW 641
Cdd:cd00161    74 VQQWTCNGGDNQQWRLEPVGDGYYRIVNKHSGKCLDVSGGSTANGANVQQWTCNGGANQQW 134

Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.

Pssm-ID: 119373 [Multi-domain] Cd Length: 186 Bit Score: 96.26 E-value: 8.53e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 164 VVDVSEHNGTIDWQAAKNAGVEGAIIRLSYGWYNRYDYQAlRNISECKRLGIPFGVYIYSYAYDSncawgeGDDTAkKLY 243
Cdd:cd00599     2 GIDVSSWQGSIDWNAVKAAGIDFVFIKATEGTTYVDPKFA-TNRARARAAGLLVGAYHFARPCAN------AEAQA-DNF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 244 YAGVSPGDLSYPVFYDLEnwtWTGHTPPTNpgVYDDIVNKWWSRMQQSGYNNLSVYSYTSYLNGPLNSYNIRSSTRWVAS 323
Cdd:cd00599    74 VNTVPRDPGSLPLVLDVE---DTGGGCSAA--ALAAWLNAFLNEVEALTGKKPIIYTSPSFWDDYLASSQLSDYPLWIAH 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2467975801 324 YGARTGFGFSTND--RGWQYSDNGWVNGI-GNVDHNAF 358
Cdd:cd00599   149 YRGEPPPAPGAWRpwTLWQYTSSGRVPGIsGPVDLNVF 186

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 92.05 E-value: 5.95e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 387 QVRDIREGDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTV 466
Cdd:cd00161    41 TLTPVGDGYYTIRNVASGKCLDVAGGSTANGANVQQWTCNGGDNQQWRLEPVGDGYYRIVNKHSGKCLDVSGGSTANGAN 120

                          90
                  ....*....|....
gi 2467975801 467 VAQYRGNGGGNQRW 480
Cdd:cd00161   121 VQQWTCNGGANQQW 134

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 91.23 E-value: 1.23e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGN 473
Cdd:cd23458     1 GTYRIRNRNSGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEIDNGYYRIKASHSGKCLDVAGGSTANGANIQQWDCV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 474 GGGNQRWRFYRNGQGRMLIESvyggSH-NKVLQIHGLNPNPLGQIDVWSADGGPNQQF 530
Cdd:cd23458    81 GGANQQWKLQDLGNGYFELKA----RHsGKCLDVAGGSTANGASIQQWTCNGNDNQRF 134

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 91.23 E-value: 1.23e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGN 634
Cdd:cd23458     1 GTYRIRNRNSGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEIDNGYYRIKASHSGKCLDVAGGSTANGANIQQWDCV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 635 GGGNQRWRFYRNGQGRMLIESvyggSH-NKVLQIHGLNPNPLGQIDVWSADGGPNQQF 691
Cdd:cd23458    81 GGANQQWKLQDLGNGYFELKA----RHsGKCLDVAGGSTANGASIQQWTCNGNDNQRF 134

Glycosyl hydrolases family 25;

Pssm-ID: 426105 Cd Length: 180 Bit Score: 87.42 E-value: 8.87e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 165 VDVSEHNGTIDWQAAKNAGVEGAIIRLSYG-WYNRYDYQalRNISECKRLGIPFGVYIYSYAYDSNCAWGEGDDTAKKLY 243
Cdd:pfam01183   1 IDVSSYQGDIDWQKVKASGVSFVFIKATEGtDYVDPYFT--TQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNVQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 244 YAGVSPGDLsyPVFYDLENwtwtgHTPPTNPGVYDDIvNKWWSRMQQS-GYNNLsVYSYTS-YLNGPLNSYNIRSSTRWV 321
Cdd:pfam01183  79 GLGLDAGTL--PPVLDVEV-----TTGLTKAAATSNI-LRFLDRVKKQtGYKPV-IYTGTSfWTNNLLYGQFIADYPLWI 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2467975801 322 ASYGAR--TGFGFSTNDRGWQYSDNGWVNGI 350
Cdd:pfam01183 150 ASYAVTppKDYPGWTKWTFWQYTSSGSIPGV 180

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 83.20 E-value: 8.57e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 557 YRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGG 636
Cdd:cd23446     3 YKLVNRNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVGGGYYKIVNRNSGKALDVNGASTADGAAIIQWTSNGG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801 637 GNQRWRFYRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVWSADGGPNQQFSL 693
Cdd:cd23446    83 DNQQWQIVDTGDGYYKIVNRNSG---KLLDVNGWSTADGADIIQWSDNGGTNQQWQL 136

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 83.20 E-value: 8.57e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 396 YRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGG 475
Cdd:cd23446     3 YKLVNRNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVGGGYYKIVNRNSGKALDVNGASTADGAAIIQWTSNGG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801 476 GNQRWRFYRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVWSADGGPNQQFSL 532
Cdd:cd23446    83 DNQQWQIVDTGDGYYKIVNRNSG---KLLDVNGWSTADGADIIQWSDNGGTNQQWQL 136

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 82.76 E-value: 1.19e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 500 HNKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLELVDfdgtplsslgtqvrdirEGDYRIASAYSGLYLDVNGASRSEGA 579
Cdd:cd23458    10 SGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEID-----------------NGYYRIKASHSGKCLDVAGGSTANGA 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467975801 580 RLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWR 642
Cdd:cd23458    73 NIQQWDCVGGANQQWKLQDLGNGYFELKARHSGKCLDVAGGSTANGASIQQWTCNGNDNQRFK 135

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 81.66 E-value: 2.64e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 501 NKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLElvdfdgtplsslgtqvrDIREGDYRIASAYSGLYLDVNGASRSEGAR 580
Cdd:cd23446    11 GKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFT-----------------DVGGGYYKIVNRNSGKALDVNGASTADGAA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467975801 581 LITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRF 643
Cdd:cd23446    74 IIQWTSNGGDNQQWQIVDTGDGYYKIVNRNSGKLLDVNGWSTADGADIIQWSDNGGTNQQWQL 136

AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.

Pssm-ID: 119382 Cd Length: 192 Bit Score: 83.19 E-value: 3.52e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 164 VVDVSEHNGTI---DWQAAKNAGVEGAIIRLSYGWYNRYDYqALRNISECKRLGIPFGVYIYSYAYDSNCAWGEGDDTAK 240
Cdd:cd06522     3 VVDVSSNNGIMsvaDYNKLKNYGVKAVIVKLTEGTTYRNPY-AASQIANAKAAGLKVSAYHYAHYTSAADAQAEARYFAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 241 KLYYAGVSPgdlSYPVFYDLENwtwtghtpptnPGVYDDI---VNKWWSRMQQSGYNNLSVYSYTSYLNGPLNSYNIRSS 317
Cdd:cd06522    82 TAKSLGLSK---NTVMVADMED-----------SSSSGNAtanVNAFWQTMKAAGYKNTDVYTSASWLNSRADTSTLGAK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2467975801 318 TRWVASY--GARTGFGFSTNDRGWQYSDNGWVNGI-GNVDHN 356
Cdd:cd06522   148 RVWVAQYpyNPSSNNLWNTNYGAWQWTSQAHFPGRsGGFDVS 189

PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

Pssm-ID: 119383 Cd Length: 177 Bit Score: 79.71 E-value: 4.33e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 164 VVDVSEHNGTIDWQAAK-NAGVEGAIIRLSYGwYNRYDYQALRNISECKRLGIPFGVYIYSYAYDSNCAWGEGDDtakkl 242
Cdd:cd06523     2 IVDISEWQGPINWDYDTlSKQLDLVIIRVQYG-SNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARD----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 243 YYAGVSPgdlsYPVFY--DLENwtwtghtppTNPGVYDDIVNKWWSRMQQSGYNNLSVYSYTSYLNGpLNSYNIRSSTRW 320
Cdd:cd06523    76 FYNRANK----KPTFYvlDVEV---------TSMSDMNAGVQAFISELRRLGAKKVGLYIGHHFYTT-FNLAVSKFDAIW 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2467975801 321 VASYGARTGfgfSTNDRGWQYSDNGWVNGI-GNVDHNA 357
Cdd:cd06523   142 IPAYGSNPG---TYPYDLWQYTDSGYLPGIsGNVDLNR 176

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 73.18 E-value: 7.36e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 526 PNQQFSLELVDFDGTplsslgtqvrdiregdYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYT 605
Cdd:pfam14200   1 ANQQWRFGGTVGDGY----------------YTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDGYYR 64

                          90       100
                  ....*....|....*....|....*.
gi 2467975801 606 ISPTHSGLMVDASGpSFVNGTVVAQY 631
Cdd:pfam14200  65 IVNKASGKVLDVAG-STANGTNVQQW 89

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 72.80 E-value: 8.95e-16

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGpSFVNGTVVAQY 470
Cdd:pfam14200  14 GYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDGYYRIVNKASGKVLDVAG-STANGTNVQQW 89

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 74.28 E-value: 9.40e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 387 QVRDIREGDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTV 466
Cdd:cd23458    41 TLVEIDNGYYRIKASHSGKCLDVAGGSTANGANIQQWDCVGGANQQWKLQDLGNGYFELKARHSGKCLDVAGGSTANGAS 120

                          90
                  ....*....|....*
gi 2467975801 467 VAQYRGNGGGNQRWR 481
Cdd:cd23458   121 IQQWTCNGNDNQRFK 135

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 73.96 E-value: 1.32e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 390 DIREGDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQ 469
Cdd:cd23446    44 DVGGGYYKIVNRNSGKALDVNGASTADGAAIIQWTSNGGDNQQWQIVDTGDGYYKIVNRNSGKLLDVNGWSTADGADIIQ 123

                          90
                  ....*....|...
gi 2467975801 470 YRGNGGGNQRWRF 482
Cdd:cd23446   124 WSDNGGTNQQWQL 136

Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

Pssm-ID: 119385 Cd Length: 184 Bit Score: 74.64 E-value: 2.43e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 162 KGVvDVSEHNGTIDWQAAKNAGVEGAIIRLSYGWYNRyDYQALRNISECKRLGIPFGVYiySYAYDSNCAWGEGDDtakk 241
Cdd:cd06525     1 KGI-DISNWQGNINFNAVKDSGVEVVYIKATEGTTFV-DSYFNENYNGAKAAGLKVGFY--HFLVGTSNPEEQAEN---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 242 lYYAGVSPGDLSYPVFYDLENwtwtghTPPTNPGVYDDIVNKWWSRMQQ-SGYNnLSVYSYTSYLNGPLNSYnIRSSTRW 320
Cdd:cd06525    73 -FYNTIKGKKMDLKPALDVEV------NFGLSKDELNDYVLRFIEEFEKlSGLK-VGIYTYTSFINNNLDSR-LSSYPLW 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2467975801 321 VASYGART--GFGFSTNDRGWQYSDNGWVNGI-GNVDHNAF 358
Cdd:cd06525   144 IANYGVSPpsSNGIWNSWVGFQYSETGRVNGVsGSVDLDEF 184

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 73.17 E-value: 2.65e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 602 GSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVW 681
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVGDGYYTIRNVASG---KCLDVAGGSTANGANVQQW 77

                          90
                  ....*....|....
gi 2467975801 682 SADGGPNQQFSLER 695
Cdd:cd00161    78 TCNGGDNQQWRLEP 91

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 72.00 E-value: 5.31e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 393 EGDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHirpvGDGSYTISpTHSGLMVDASGPSFVNGTVVAQYRG 472
Cdd:cd23418     3 AGGGQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFT----FTSAGELR-VGGDKCLDAAGGGTTNGTPVVIWPC 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467975801 473 NGGGNQRWRFYRNGQGR-----MLIESVYGGSHNKVLQIhglnpnplgqidVWSADGGPNQQF 530
Cdd:cd23418    78 NGGANQKWRFNSDGTIRnvnsgLCLDVAGGGTANGTRLI------------LWSCNGGSNQRW 128

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 72.00 E-value: 5.31e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 554 EGDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHirpvGDGSYTISpTHSGLMVDASGPSFVNGTVVAQYRG 633
Cdd:cd23418     3 AGGGQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFT----FTSAGELR-VGGDKCLDAAGGGTTNGTPVVIWPC 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467975801 634 NGGGNQRWRFYRNGQGR-----MLIESVYGGSHNKVLQIhglnpnplgqidVWSADGGPNQQF 691
Cdd:cd23418    78 NGGANQKWRFNSDGTIRnvnsgLCLDVAGGGTANGTRLI------------LWSCNGGSNQRW 128

ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467295 [Multi-domain] Cd Length: 145 Bit Score: 68.53 E-value: 1.30e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSGLYLDVNGASRSEGARLIT---CILNGGANQVFHIRPVGDGS--YTISPTHSGLMVDASGPSFVNGTVVA 629
Cdd:cd23416     1 GVYHIRNAGTGTVLDLSGGSSANGTPIQGwqkTGDTGSFNQLWLLEPVPNGSdtYTIQNVRSGTYLDLAGGSSANGTAIV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 630 QYRGNGGGNQRWRFYRNGQGRM-LIESVYGGShnkVLQIHGLNPNPLGQIDVWS-ADGGPNQQFSLER 695
Cdd:cd23416    81 GWQSTNNPNQQWVIKPANGGTYyKIQNKGTGT---FLDLYGGDSANGTKIVGWTgHWGNPNQLWLFER 145

ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467295 [Multi-domain] Cd Length: 145 Bit Score: 66.99 E-value: 5.06e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRSEGARLIT---CILNGGANQVFHIRPVGDGS--YTISPTHSGLMVDASGPSFVNGTVVA 468
Cdd:cd23416     1 GVYHIRNAGTGTVLDLSGGSSANGTPIQGwqkTGDTGSFNQLWLLEPVPNGSdtYTIQNVRSGTYLDLAGGSSANGTAIV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801 469 QYRGNGGGNQRWRFYRNGQGRM-LIESVYGGShnkVLQIHGLNPNPLGQIDVWS-ADGGPNQQFSLE 533
Cdd:cd23416    81 GWQSTNNPNQQWVIKPANGGTYyKIQNKGTGT---FLDLYGGDSANGTKIVGWTgHWGNPNQLWLFE 144

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 64.68 E-value: 1.88e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 439 GDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRmliesVYGgshNKVLQIHGLNPNPLGQID 518
Cdd:cd23418     2 GAGGGQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELR-----VGG---DKCLDAAGGGTTNGTPVV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 519 VWSADGGPNQQFSLelvdfdgtplsslgtqvrdirEGDYRIASAYSGLYLDVNGASRSEGARLI--TCilNGGANQVF 594
Cdd:cd23418    74 IWPCNGGANQKWRF---------------------NSDGTIRNVNSGLCLDVAGGGTANGTRLIlwSC--NGGSNQRW 128

YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.

Pssm-ID: 119384 Cd Length: 194 Bit Score: 63.13 E-value: 3.23e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 165 VDVSEHNGTIDWQAA----KNAGVEGAIIRLSYGwYNRYDYQALRNISECKRLGIPFGVYIYsYAYDSNCAWgEGD---D 237
Cdd:cd06524     3 IDVSHYQGKIDWQKVkakvKDSPVAFVFIKATEG-VDIVDPDFPTNWEGAKEAGIIRGAYHF-YRPNSDPKQ-QADnflN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 238 TAKKLyyagvSPGDLSyPVFyDLEnwtWTGHTppTNPGVYDDIVNKWWSRMQQSG------YNNLSVysYTSYLNGP-LN 310
Cdd:cd06524    80 TVKLL-----GPGDLP-PVL-DVE---WDGRK--SSAKQIQEGVLEWLDAVEKATgvkpiiYTNPSF--WTDYLTDSsFS 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2467975801 311 SYNIrsstrWVASYGARTG---FGFSTNDRGWQYSDNGWVNGI-GNVDHNAF 358
Cdd:cd06524   146 EYPL-----WIADYNPRRKkvpPNESKKWLLWQYSDSGKVPGIsGAVDLNVF 192

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 59.65 E-value: 1.02e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 559 IASAYSGLYLDVNGASRSEG--ARLITCilNGGANQVFHIRPvgDGSYTISpthsGLMVDASGPSFVNGTVVAQYRGNGG 636
Cdd:cd23451     5 VRLANAGKCLDVPGSSTADGnpVQIYTC--NGTAAQKWTLGT--DGTLRVL----GKCLDVSGGGTANGTLVQLWDCNGT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2467975801 637 GNQRWRFYRNGqgrmlieSVYGGSHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFS 692
Cdd:cd23451    77 GAQKWVPRADG-------TLYNPQSGKCLDAPGGSTTDGTQLQLYTCNGTAAQQWT 125

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 59.65 E-value: 1.02e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 398 IASAYSGLYLDVNGASRSEG--ARLITCilNGGANQVFHIRPvgDGSYTISpthsGLMVDASGPSFVNGTVVAQYRGNGG 475
Cdd:cd23451     5 VRLANAGKCLDVPGSSTADGnpVQIYTC--NGTAAQKWTLGT--DGTLRVL----GKCLDVSGGGTANGTLVQLWDCNGT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2467975801 476 GNQRWRFYRNGqgrmlieSVYGGSHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFS 531
Cdd:cd23451    77 GAQKWVPRADG-------TLYNPQSGKCLDAPGGSTTDGTQLQLYTCNGTAAQQWT 125

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 59.67 E-value: 1.19e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 497 GGSHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFSlelvdFDGTplsslgtqvRDIRegdyriasAYSGLYLDVNGASRS 576
Cdd:cd23418    10 GYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFT-----FTSA---------GELR--------VGGDKCLDAAGGGTT 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801 577 EGARLITCILNGGANQVFHIRPVGdgsyTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRF 643
Cdd:cd23418    68 NGTPVVIWPCNGGANQKWRFNSDG----TIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWRR 130

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 58.49 E-value: 2.97e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 602 GSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMLIESvygGSHNKVLQIHGLNPNPLGQIDVW 681
Cdd:cd23458     1 GTYRIRNRNSGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEIDNGYYRIKA---SHSGKCLDVAGGSTANGANIQQW 77

                          90
                  ....*....|...
gi 2467975801 682 SADGGPNQQFSLE 694
Cdd:cd23458    78 DCVGGANQQWKLQ 90

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 58.31 E-value: 3.25e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 557 YRIASAYSGLYLDVNGASrSEGARLI--TCiLNGGANQVFHIRPVGdgsyTISPTHSGLMVDASGPSfvNGTVVAQYR-G 633
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGS-SAGGPVGlyPC-HGSNGNQLWTLTGDG----TIRSVASDLCLDVGSTA--DGAKVVLWPcH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 634 NGGGNQRWRFYRNGQGrmliesVYGGSHNKVLQIHGLNpNPLGQIDVWSAD-GGPNQQF 691
Cdd:pfam00652  75 PGNGNQRWRYDEDGTQ------IRNPQSGKCLDVSGAG-TSNGKVILWTCDsGNPNQQW 126

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 58.31 E-value: 3.25e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 396 YRIASAYSGLYLDVNGASrSEGARLI--TCiLNGGANQVFHIRPVGdgsyTISPTHSGLMVDASGPSfvNGTVVAQYR-G 472
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGS-SAGGPVGlyPC-HGSNGNQLWTLTGDG----TIRSVASDLCLDVGSTA--DGAKVVLWPcH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 473 NGGGNQRWRFYRNGQGrmliesVYGGSHNKVLQIHGLNpNPLGQIDVWSAD-GGPNQQF 530
Cdd:pfam00652  75 PGNGNQRWRYDEDGTQ------IRNPQSGKCLDVSGAG-TSNGKVILWTCDsGNPNQQW 126

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 54.31 E-value: 3.17e-09

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 590 ANQVFHIR-PVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMLIESVYGG 659
Cdd:pfam14200   1 ANQQWRFGgTVGDGYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDGYYRIVNKASG 71

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 54.31 E-value: 3.17e-09

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 429 ANQVFHIR-PVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMLIESVYGG 498
Cdd:pfam14200   1 ANQQWRFGgTVGDGYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDGYYRIVNKASG 71

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 51.23 E-value: 3.30e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 477 NQRWRF-YRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLElvdfdgtplsslgtqvrDIREG 555
Cdd:pfam14200   2 NQQWRFgGTVGDGYYTIVNVASG---KYLDVAGGSTANGANVQQWTDNGNDNQQWRIV-----------------DAGDG 61

                          90       100
                  ....*....|....*....|....*...
gi 2467975801 556 DYRIASAYSGLYLDVNGASrSEGARLIT 583
Cdd:pfam14200  62 YYRIVNKASGKVLDVAGST-ANGTNVQQ 88

ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end.

Pssm-ID: 467300 [Multi-domain] Cd Length: 135 Bit Score: 51.94 E-value: 5.75e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 520 WSADGGPNQQFSLElvdfdgtplsslgtqvrDIREGDYRIASAYSGLYLDVNGASRsEGARLITcilnGGANQVFHIRPV 599
Cdd:cd23422    29 WPFHGGENQQWTLE-----------------PTPGGGYTIQSVSTGKYLGIEGGPR-DGTRLVG----SDQPFVWDIEPD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2467975801 600 G--DGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRF 643
Cdd:cd23422    87 EgdSGAFRIFVPGTNLVLDLDDGGSAPGTPVQLWERSEGPNQLWRF 132

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 51.58 E-value: 8.59e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 402 YSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGdgsyTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWR 481
Cdd:cd23418    54 GGDKCLDAAGGGTTNGTPVVIWPCNGGANQKWRFNSDG----TIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWR 129


                  .
gi 2467975801 482 F 482
Cdd:cd23418   130 R 130

ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end.

Pssm-ID: 467300 [Multi-domain] Cd Length: 135 Bit Score: 50.78 E-value: 1.52e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRsEGARLITcilnGGANQVFHIRPVG--DGSYTISPTHSGLMVDASGPSFVNGTVVAQYR 471
Cdd:cd23422    47 GGYTIQSVSTGKYLGIEGGPR-DGTRLVG----SDQPFVWDIEPDEgdSGAFRIFVPGTNLVLDLDDGGSAPGTPVQLWE 121

                          90
                  ....*....|.
gi 2467975801 472 GNGGGNQRWRF 482
Cdd:cd23422   122 RSEGPNQLWRF 132

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.

Pssm-ID: 467327 [Multi-domain] Cd Length: 128 Bit Score: 50.37 E-value: 1.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 559 IASAYSGLYLDVNGASRSEGARLITCILNGGA--NQVFHIRPVgdgSYTISPTHSGLMVDASGPsfvNGTVVAQYRGNGG 636
Cdd:cd23449     5 IKSKLNGKVLDVEGANAKPGAKVIMWEKKGGAedNQLWYEDEV---TGTIRSKLNDFCLDASGD---KGLILNPYDPSNP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 637 gNQRWRFYRNgqgrmLIESvyGGSHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLE 694
Cdd:cd23449    79 -KQQWKISGN-----KIQN--RSNPDNVLDIKGGSKDDGARLCAWEYNGGPNQLWDFE 128

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.

Pssm-ID: 467327 [Multi-domain] Cd Length: 128 Bit Score: 50.37 E-value: 1.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 398 IASAYSGLYLDVNGASRSEGARLITCILNGGA--NQVFHIRPVgdgSYTISPTHSGLMVDASGPsfvNGTVVAQYRGNGG 475
Cdd:cd23449     5 IKSKLNGKVLDVEGANAKPGAKVIMWEKKGGAedNQLWYEDEV---TGTIRSKLNDFCLDASGD---KGLILNPYDPSNP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 476 gNQRWRFYRNgqgrmLIESvyGGSHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLE 533
Cdd:cd23449    79 -KQQWKISGN-----KIQN--RSNPDNVLDIKGGSKDDGARLCAWEYNGGPNQLWDFE 128

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.

Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 50.94 E-value: 7.26e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 565 GLYLDVNGASRSeGARLITCILNGGANQVFHIRPVGDGSYtispthSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRfY 644
Cdd:NF035930  127 GLCLDVSGGLRP-GNGLIVYNCNGGENQRFTWGRGGELRV------GDLCLDVADGNTRDGARVIAWSCSGGPNQRWR-W 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2467975801 645 RNGQgrmlIESVYGGshnKVLQIHGLNPNPLGQIDVWSADGGPNQQF 691
Cdd:NF035930  199 RGGQ----IRSRLSG---KCLDIEGGRARPGQPVIVWSCNGGPNQRW 238

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 48.53 E-value: 1.13e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 602 GSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVW 681
Cdd:cd23446     1 TYYKLVNRNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVGGGYYKIVNRNSG---KALDVNGASTADGAAIIQW 77

                          90
                  ....*....|...
gi 2467975801 682 SADGGPNQQFSLE 694
Cdd:cd23446    78 TSNGGDNQQWQIV 90

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 47.89 E-value: 1.34e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801  559 IASAYSGLYLDVNGasRSEGARLITCIlNGGANQVFHIRPVGdgsyTISPTHSGLMVDASGPsfvNGTVVAQYRGNGG-G 637
Cdd:smart00458   1 IISGNTGKCLDVNG--NKNPVGLFDCH-GTGGNQLWKLTSDG----AIRIKDTDLCLTANGN---TGSTVTLYSCDGTnD 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801  638 NQRWRFYRNGQgrmliesVYGGSHNKVLQIhgLNPNPLGQIDVWSADGGPNQQFSLE 694
Cdd:smart00458  71 NQYWEVNKDGT-------IRNPDSGKCLDV--KDGNTGTKVILWTCSGNPNQKWIFE 118

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 47.14 E-value: 2.20e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 393 EGDYRIASAYSGLYLDVNGASRSEGARLITCIlNGGANQVFHIRPVGDgsyTISPTHSGLMVDASGPSFVNGTVVAQYRG 472
Cdd:pfam00652  43 TGDGTIRSVASDLCLDVGSTADGAKVVLWPCH-PGNGNQRWRYDEDGT---QIRNPQSGKCLDVSGAGTSNGKVILWTCD 118


                  ....*...
gi 2467975801 473 NGGGNQRW 480
Cdd:pfam00652 119 SGNPNQQW 126

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 47.14 E-value: 2.20e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 554 EGDYRIASAYSGLYLDVNGASRSEGARLITCIlNGGANQVFHIRPVGDgsyTISPTHSGLMVDASGPSFVNGTVVAQYRG 633
Cdd:pfam00652  43 TGDGTIRSVASDLCLDVGSTADGAKVVLWPCH-PGNGNQRWRYDEDGT---QIRNPQSGKCLDVSGAGTSNGKVILWTCD 118


                  ....*...
gi 2467975801 634 NGGGNQRW 641
Cdd:pfam00652 119 SGNPNQQW 126

Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

Pssm-ID: 119375 Cd Length: 191 Bit Score: 48.43 E-value: 2.71e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 165 VDVSEHNGTIDWQAAKNAGVEGAIIRLSYGwYNRYDYQALRNISECKRLGIPFGVYIYsYAYDSNcawgeGDDTAKKlYY 244
Cdd:cd06413     6 IDVSHHQGDIDWARVRAQGVSFAYIKATEG-GDHVDKRFAENWRGARAAGLPRGAYHF-FTFCRS-----GAEQAAN-FI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 245 AGV--SPGDLsyPVFYDLEnwtWTGHTP--PTNPGVYDDIvnKWWSRMQQSGYNN-----LSVYSYTSYLNGPLNSYNIr 315
Cdd:cd06413    78 RNVpkDPGAL--PPVVDVE---WNGNSAtcPSAEEVLAEL--QVFLDALEAHYGKrpiiyTTYDFYDDYLKGEFPDYPL- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2467975801 316 sstrWVASYgARTGFGFSTND-RGWQYSDNGWVNGI-GNVDHNAF 358
Cdd:cd06413   150 ----WIRSV-AGHPRLYEDRPwTFWQYTNRGRVPGIeGDVDLNVF 189

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 45.99 E-value: 7.09e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 442 SYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQgrmlIESVYGgshNKVLQIHGLNPNplGQIDVWS 521
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGT----IRSVAS---DLCLDVGSTADG--AKVVLWP 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467975801 522 -ADGGPNQQFSLelvdfdgtplsslgtqvrdiREGDYRIASAYSGLYLDVNGASRSEGA-RLITCiLNGGANQVF 594
Cdd:pfam00652  73 cHPGNGNQRWRY--------------------DEDGTQIRNPQSGKCLDVSGAGTSNGKvILWTC-DSGNPNQQW 126

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 45.42 E-value: 9.99e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 600 GDGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRmliesVYGgshNKVLQIHGLNPNPLGQID 679
Cdd:cd23418     2 GAGGGQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELR-----VGG---DKCLDAAGGGTTNGTPVV 73

                          90
                  ....*....|..
gi 2467975801 680 VWSADGGPNQQF 691
Cdd:cd23418    74 IWPCNGGANQKW 85

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.

Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 45.12 E-value: 1.15e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSGLYLDVNGasrSEGARLITCilNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGpsfvNGTVVAqYRGN 634
Cdd:cd23415     1 GTVRLRNVATGRCLDSNA---GGNVYTGPC--NGGPYQRWTWSGVGDGTVTLRNAATGRCLDSNG----NGGVYT-LPCN 70

                          90       100
                  ....*....|....*....|....*
gi 2467975801 635 GGGNQRWRFYRNGQGRMLIESVYGG 659
Cdd:cd23415    71 GGSYQRWRVTSTSGGGVTLRNVATG 95

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.

Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 45.12 E-value: 1.15e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGasrSEGARLITCilNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGpsfvNGTVVAqYRGN 473
Cdd:cd23415     1 GTVRLRNVATGRCLDSNA---GGNVYTGPC--NGGPYQRWTWSGVGDGTVTLRNAATGRCLDSNG----NGGVYT-LPCN 70

                          90       100
                  ....*....|....*....|....*
gi 2467975801 474 GGGNQRWRFYRNGQGRMLIESVYGG 498
Cdd:cd23415    71 GGSYQRWRVTSTSGGGVTLRNVATG 95

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 45.02 E-value: 1.44e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 517 IDVWSADGGPNQQFSLELvdfDGTplsslgtqvrdIRegdyriasaYSGLYLDVNGASRSEGARLITCILNGGANQVFHI 596
Cdd:cd23451    27 VQIYTCNGTAAQKWTLGT---DGT-----------LR---------VLGKCLDVSGGGTANGTLVQLWDCNGTGAQKWVP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2467975801 597 RPVGdgsyTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWR 642
Cdd:cd23451    84 RADG----TLYNPQSGKCLDAPGGSTTDGTQLQLYTCNGTAAQQWT 125

ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) and similar proteins; RSA is a 15.5-kDa lectin accumulated in the mycelium and sclerotia of the soil born plant pathogenic fungus R. solani. It may act as a storage protein implicated in fungal insecticidal activity. It displays high selectivity towards terminal non-reducing N-acetylgalactosamine residues. RSA reveals a domain-swapping dimeric assembly. Each monomer contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467333 [Multi-domain] Cd Length: 131 Bit Score: 45.01 E-value: 1.51e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVG---------------------------------- 600
Cdd:cd23455     1 GTYRIKNVATGTVLDLYLGSSAEGTPVQGYQPNGGDNQKWQLEWVGsgngvtlrnvasgtyagfpahadggqvvgsnnpv 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 601 -------DGSYTISPT-HSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRF 643
Cdd:cd23455    81 lftivaaDGGYQIQPVdDPDLVLDLAGSNDEDGTPVILYNNDGGDNQKWYF 131

ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) and similar proteins; RSA is a 15.5-kDa lectin accumulated in the mycelium and sclerotia of the soil born plant pathogenic fungus R. solani. It may act as a storage protein implicated in fungal insecticidal activity. It displays high selectivity towards terminal non-reducing N-acetylgalactosamine residues. RSA reveals a domain-swapping dimeric assembly. Each monomer contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467333 [Multi-domain] Cd Length: 131 Bit Score: 45.01 E-value: 1.51e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVG---------------------------------- 439
Cdd:cd23455     1 GTYRIKNVATGTVLDLYLGSSAEGTPVQGYQPNGGDNQKWQLEWVGsgngvtlrnvasgtyagfpahadggqvvgsnnpv 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 440 -------DGSYTISPT-HSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRF 482
Cdd:cd23455    81 lftivaaDGGYQIQPVdDPDLVLDLAGSNDEDGTPVILYNNDGGDNQKWYF 131

second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. The model corresponds to the second lectin domain.

Pssm-ID: 467378 [Multi-domain] Cd Length: 128 Bit Score: 44.76 E-value: 1.90e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 450 SGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFyRNGQGRMliesVYGGSHNKVLQIHGLNPNPLGQIDVWSADG-GPNQ 528
Cdd:cd23500    10 SGKCLSAANGSQLNGSLVQLDACHASAGQLWYF-DPKKGTI----RSALDGNKCLAIPGGNTGNHTQLQLADCDAsNPAQ 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801 529 QFslelvDFDGTPLSSlgtqvrdiregdyRIASAYSglyLDVNGAsrSEGARLITCILNGGANQVFH 595
Cdd:cd23500    85 QF-----NYDGGVFRS-------------RLNSNQV---IDASGG--SDGSELILYDYHGGSNQRWR 128

ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 44.33 E-value: 2.75e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 502 KVLQIHGLNPNPLGQIDVWSADGGPNQQFSLELVDfdgtplsslgtqvrdirEGDYRIASAY-SGLYLDVNGASRSEGAR 580
Cdd:cd23457    14 KVLSAEGCSTATGTNVEQQSWTGSACQKWQFTPTD-----------------NGFYQLRPASnASLCLAVEGGSLAAGAN 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2467975801 581 LI--TCilnGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQY 631
Cdd:cd23457    77 LVlgAC---SADSSQWRLEPLADGALRLVSRHSGLVLDLDNCSLADGANLQQY 126

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 44.25 E-value: 2.80e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 444 TISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMLiesvyggshNKVLQIHGLNPNPLGQIDVWSAD 523
Cdd:cd23451     4 PVRLANAGKCLDVPGSSTADGNPVQIYTCNGTAAQKWTLGTDGTLRVL---------GKCLDVSGGGTANGTLVQLWDCN 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467975801 524 GGPNQQFSlelVDFDGTplsslgtqvrdiregdyrIASAYSGLYLDVNGASRSEGARLI--TCilNGGANQVF 594
Cdd:cd23451    75 GTGAQKWV---PRADGT------------------LYNPQSGKCLDAPGGSTTDGTQLQlyTC--NGTAAQQW 124

ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 43.95 E-value: 4.66e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 440 DGSYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMLIESVYGGshNKVLQIHGlNPNPLGQIDV 519
Cdd:cd23457     2 VGSVAIVSAQSGKVLSAEGCSTATGTNVEQQSWTGSACQKWQFTPTDNGFYQLRPASNA--SLCLAVEG-GSLAAGANLV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 520 WSADGGPNQQFSLElvdfdgtPLSslgtqvrdirEGDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIR 597
Cdd:cd23457    79 LGACSADSSQWRLE-------PLA----------DGALRLVSRHSGLVLDLDNCSLADGANLQQYPWLDNICQRFYLR 139

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 42.88 E-value: 6.89e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801  497 GGSHNKVLQIHGlNPNPLGqidVWSADG-GPNQQFSLelvdfdgtplsslgtqvrdIREGDYRIASaySGLYLDVNGaSR 575
Cdd:smart00458   3 SGNTGKCLDVNG-NKNPVG---LFDCHGtGGNQLWKL-------------------TSDGAIRIKD--TDLCLTANG-NT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801  576 SEGARLITCiLNGGANQVFHIRPvgdgSYTISPTHSGLMVDASGPSFvnGTVVAQYRGNGGGNQRWRFY 644
Cdd:smart00458  57 GSTVTLYSC-DGTNDNQYWEVNK----DGTIRNPDSGKCLDVKDGNT--GTKVILWTCSGNPNQKWIFE 118

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.

Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 44.39 E-value: 8.99e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 470 YRGNGGGNQRWRFYRnGQGRMLIEsVYGGSHnkvlqihglnpnPLGQIDVWSADGGPNQQFSLElvdfdgtplsslgtqv 549
Cdd:NF035930  109 YPGQGGGGWGGREIR-GKGGLCLD-VSGGLR------------PGNGLIVYNCNGGENQRFTWG---------------- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 550 rdiREGDYRIasaySGLYLDVNGASRSEGARLITCILNGGANQVFHIRpvgdGSyTISPTHSGLMVDASGPSFVNGTVVA 629
Cdd:NF035930  159 ---RGGELRV----GDLCLDVADGNTRDGARVIAWSCSGGPNQRWRWR----GG-QIRSRLSGKCLDIEGGRARPGQPVI 226

                         170
                  ....*....|..
gi 2467975801 630 QYRGNGGGNQRW 641
Cdd:NF035930  227 VWSCNGGPNQRW 238

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.

Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 42.42 E-value: 9.11e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 387 QVRDIREGDYRIASAYSGLYLDVNGASrseGARLITCilNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGpsfvNGTV 466
Cdd:cd23415    36 TWSGVGDGTVTLRNAATGRCLDSNGNG---GVYTLPC--NGGSYQRWRVTSTSGGGVTLRNVATGRCLDSNG----SGGV 106

                          90
                  ....*....|....*
gi 2467975801 467 VAqYRGNGGGNQRWR 481
Cdd:cd23415   107 YT-RPCNGGSYQRWR 120

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.

Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 42.42 E-value: 9.11e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 548 QVRDIREGDYRIASAYSGLYLDVNGASrseGARLITCilNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGpsfvNGTV 627
Cdd:cd23415    36 TWSGVGDGTVTLRNAATGRCLDSNGNG---GVYTLPC--NGGSYQRWRVTSTSGGGVTLRNVATGRCLDSNG----SGGV 106

                          90
                  ....*....|....*
gi 2467975801 628 VAqYRGNGGGNQRWR 642
Cdd:cd23415   107 YT-RPCNGGSYQRWR 120

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.

Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 44.39 E-value: 1.01e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 451 GLMVDASGpSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRMliesvyggsHNKVLQIHGLNPNPLGQIDVWSADGGPNQQF 530
Cdd:NF035930  127 GLCLDVSG-GLRPGNGLIVYNCNGGENQRFTWGRGGELRV---------GDLCLDVADGNTRDGARVIAWSCSGGPNQRW 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2467975801 531 SLElvdfdgtplsslGTQVRdiregdyriaSAYSGLYLDVNGASRSEGARLITCILNGGANQ 592
Cdd:NF035930  197 RWR------------GGQIR----------SRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQ 236

ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467295 [Multi-domain] Cd Length: 145 Bit Score: 42.33 E-value: 1.87e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRP-VGDGSYTISPTHSGLMVDASGPSFVNGTVVAQY-R 471
Cdd:cd23416    53 DTYTIQNVRSGTYLDLAGGSSANGTAIVGWQSTNNPNQQWVIKPaNGGTYYKIQNKGTGTFLDLYGGDSANGTKIVGWtG 132

                          90
                  ....*....|...
gi 2467975801 472 GNGGGNQRWRFYR 484
Cdd:cd23416   133 HWGNPNQLWLFER 145

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating proteins, HA17 and HA33, and similar proteins; The subfamily includes Clostridium botulinum hemagglutinating proteins HA17 and HA33, Lysinibacillus sphaericus mosquitocidal toxin (MTX) and Pieris brassicae pierisin. The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin. It may increase internalization of the neurotoxin into the bloodstream of the host. The hemagglutinin complex, composed of HA-70 (also known as HA3), HA-33 (also known as HA1) and HA-17 (also known as HA2), agglutinates erythrocytes, whereas the individual components do not. HA-33 is involved in recognition of cell-surface carbohydrates. HA-17 and HA-70 are involved in paracellular barrier disruption by E-cadherin binding. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this subfamily contain at least one ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467323 [Multi-domain] Cd Length: 133 Bit Score: 41.15 E-value: 3.10e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSG-LYLDVNGASRSegARLITciLNGGANQVFHIRP-VGDGSYTI--SPTHSGLMvdaSGPSFVNGTVVAq 630
Cdd:cd23445     1 GIYKIVTALNSnKVLDMNSNSNN--VVLWD--NNGGNNQKWRFEYdSGKNAYQIknLDNTNLVL---AWNSSSSNNVFA- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467975801 631 YRGNGGGNQRWRFYRNGQGRMLIESVYGgsHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFSL 693
Cdd:cd23445    73 STNTSKDEQYWKLEEAGDGYYIIKNYAD--PNLVLDVEGSNTANGTNIIVYPRNGSNNQKFKL 133

ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 41.25 E-value: 3.29e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 393 EGDYRIASAY-SGLYLDVNGASRSEGARLI--TCilnGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSFVNGTVVAQ 469
Cdd:cd23457    49 NGFYQLRPASnASLCLAVEGGSLAAGANLVlgAC---SADSSQWRLEPLADGALRLVSRHSGLVLDLDNCSLADGANLQQ 125


                  .
gi 2467975801 470 Y 470
Cdd:cd23457   126 Y 126

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.

Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 42.08 E-value: 5.37e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 392 REGDYRIasaySGLYLDVNGASRSEGARLITCILNGGANQVFHIRpvgdGSyTISPTHSGLMVDASGPSFVNGTVVAQYR 471
Cdd:NF035930  159 RGGELRV----GDLCLDVADGNTRDGARVIAWSCSGGPNQRWRWR----GG-QIRSRLSGKCLDIEGGRARPGQPVIVWS 229


                  ....*....
gi 2467975801 472 GNGGGNQRW 480
Cdd:NF035930  230 CNGGPNQRW 238

ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 40.48 E-value: 5.89e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPVGDGSYTISPTH-SGLMVDASGPSFVNGTVVAQyrG 472
Cdd:cd23457     3 GSVAIVSAQSGKVLSAEGCSTATGTNVEQQSWTGSACQKWQFTPTDNGFYQLRPASnASLCLAVEGGSLAAGANLVL--G 80

                          90
                  ....*....|....*..
gi 2467975801 473 N-GGGNQRWRFYRNGQG 488
Cdd:cd23457    81 AcSADSSQWRLEPLADG 97

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467330 [Multi-domain] Cd Length: 125 Bit Score: 40.19 E-value: 6.73e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 449 HSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQGRML---IESVYGGSHNKVlqihglnpnplgQIDVWSADGG 525
Cdd:cd23452     9 LANKCIDVPNSSTTDGAPLQLWDCNGTNAQKWTFASDGTLRALgkcLDVAWGGTDNGT------------AVQLWTCSGN 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467975801 526 PNQQFSLelvdfdgtplsslgTQVRDiregdyrIASAYSGLYLDVNGASRSEGARLITCILNGGANQ 592
Cdd:cd23452    77 PAQQFVL--------------SGAGD-------LVNPQANKCVDVSGGNSGNGTRLQLWECSGNANQ 122

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467334 [Multi-domain] Cd Length: 122 Bit Score: 39.65 E-value: 8.68e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 449 HSGLMVDASGPSFVNGTVVAqYRGNGGGNQRWrfYRNGQGRMliesvyggsHNKV-----LQIHGLNPNPlGQIDVWSAD 523
Cdd:cd23456     9 ASGLCLDVSGGATNGANVVV-YDCNNSNSQKW--YYDATGRL---------HSKAnpgkcLDAGGENSNG-ANVVLWACN 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 524 GGPNQQFslelvDFDGTPLSSlgtqvrdiregdyriaSAYSGLYLDVNGasrSEGARLITCILNGGANQ 592
Cdd:cd23456    76 DSANQRW-----DFDGNFIRS----------------RNNTNLALDAYG---SQGSNVGLWQFHGGANQ 120

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467334 [Multi-domain] Cd Length: 122 Bit Score: 39.26 E-value: 1.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 396 YRIASAYSGLYLDVNGaSRSEGARLI--TCilNGGANQvfhiRPVGDGSYTI-SPTHSGLMVDASGPSFVNGTVVAqYRG 472
Cdd:cd23456     3 FQLKSQASGLCLDVSG-GATNGANVVvyDC--NNSNSQ----KWYYDATGRLhSKANPGKCLDAGGENSNGANVVL-WAC 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 473 NGGGNQRWRFYrNGQGRMLIesvyggSHNKVLQIHGLNPnplGQIDVWSADGGPNQQF 530
Cdd:cd23456    75 NDSANQRWDFD-GNFIRSRN------NTNLALDAYGSQG---SNVGLWQFHGGANQQW 122

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467334 [Multi-domain] Cd Length: 122 Bit Score: 39.26 E-value: 1.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 557 YRIASAYSGLYLDVNGaSRSEGARLI--TCilNGGANQvfhiRPVGDGSYTI-SPTHSGLMVDASGPSFVNGTVVAqYRG 633
Cdd:cd23456     3 FQLKSQASGLCLDVSG-GATNGANVVvyDC--NNSNSQ----KWYYDATGRLhSKANPGKCLDAGGENSNGANVVL-WAC 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 634 NGGGNQRWRFYrNGQGRMLIesvyggSHNKVLQIHGLNPnplGQIDVWSADGGPNQQF 691
Cdd:cd23456    75 NDSANQRWDFD-GNFIRSRN------NTNLALDAYGSQG---SNVGLWQFHGGANQQW 122

ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end.

Pssm-ID: 467300 [Multi-domain] Cd Length: 135 Bit Score: 39.22 E-value: 1.46e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 602 GSYTISPTHSGLMVDASGPSfvNGTVVAqYRGNGGGNQRWRFYRNGQGRMLIESVYGGS 660
Cdd:cd23422     3 GTYKIVNVKSGTVLDLSGDD--NTSVVG-WPFHGGENQQWTLEPTPGGGYTIQSVSTGK 58

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating proteins, HA17 and HA33, and similar proteins; The subfamily includes Clostridium botulinum hemagglutinating proteins HA17 and HA33, Lysinibacillus sphaericus mosquitocidal toxin (MTX) and Pieris brassicae pierisin. The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin. It may increase internalization of the neurotoxin into the bloodstream of the host. The hemagglutinin complex, composed of HA-70 (also known as HA3), HA-33 (also known as HA1) and HA-17 (also known as HA2), agglutinates erythrocytes, whereas the individual components do not. HA-33 is involved in recognition of cell-surface carbohydrates. HA-17 and HA-70 are involved in paracellular barrier disruption by E-cadherin binding. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this subfamily contain at least one ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467323 [Multi-domain] Cd Length: 133 Bit Score: 39.22 E-value: 1.47e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 441 GSYTISPTHSGLMVDASGPSFVNGTVvaqYRGNGGGNQRWRF-YRNGQGRMLIESVYggSHNKVLQIhglNPNPLGQIDV 519
Cdd:cd23445     1 GIYKIVTALNSNKVLDMNSNSNNVVL---WDNNGGNNQKWRFeYDSGKNAYQIKNLD--NTNLVLAW---NSSSSNNVFA 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2467975801 520 WSADGGPNQQFSLElvdfdgtplsslgtqvrDIREGDYRIAS-AYSGLYLDVNGASRSEGARLITCILNGGANQVFHI 596
Cdd:cd23445    73 STNTSKDEQYWKLE-----------------EAGDGYYIIKNyADPNLVLDVEGSNTANGTNIIVYPRNGSNNQKFKL 133

ricin B-type lectin domain, beta-trefoil fold, found in Mushroom tyrosinase-associated lectin-like protein (MtaL) and similar proteins; Mushroom tyrosinase-associated lectin-like protein (MtaL) binds to mature Agaricus bisporus tyrosinase in vivo, but the exact physiological function of MtaL is poorly understood. MtaL contains a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. The tyrosinase enzyme complex is comprised of a H(2)L(2) tetramer. The L subunit has a lectin-like fold, whereas the H subunit contains a binuclear copper-binding site in the deoxy-state, in which three histidine residues coordinate each copper ion. Comparison of the structures of MtaL and a ricin-B-like lectin with a bound disaccharide shows that MtaL may have a similar carbohydrate-binding site that may be involved in glycoreceptor activity.

Pssm-ID: 467380 [Multi-domain] Cd Length: 129 Bit Score: 38.97 E-value: 2.11e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSGLYL-DVNGASRSEGARLITCILNGGANQVFHIRPVGDGsYTISPTHSGLMVDASGPsfvnGTVVAqyrG 633
Cdd:cd23714     1 GTYRIVNVGSGLWLgSFPDPPPPFGTPIVFDNNFASVFEVWEVTPFDDG-YTIQNVGTGLFATAKPR----GEVVV---S 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2467975801 634 NGGGNQRWRFYRNGQGRMLIESVYGgshNKVLQIHGlnPNPLGQIDVWSADGGPNQQFSLER 695
Cdd:cd23714    73 EEFQPTKWAIEPAGGGEYRIKVPNQ---DLVWTLDP--AGYDSTVVLEPADGSPNQRWKFVR 129

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467330 [Multi-domain] Cd Length: 125 Bit Score: 38.27 E-value: 2.77e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 401 AYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPvgDGSYTISpthsGLMVDASGPSFVNGTVVAQYRGNGGGNQRW 480
Cdd:cd23452     8 GLANKCIDVPNSSTTDGAPLQLWDCNGTNAQKWTFAS--DGTLRAL----GKCLDVAWGGTDNGTAVQLWTCSGNPAQQF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 481 RFyrNGQGrmlieSVYGGSHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFS 531
Cdd:cd23452    82 VL--SGAG-----DLVNPQANKCVDVSGGNSGNGTRLQLWECSGNANQKWR 125

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467330 [Multi-domain] Cd Length: 125 Bit Score: 38.27 E-value: 2.77e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 562 AYSGLYLDVNGASRSEGARLITCILNGGANQVFHIRPvgDGSYTISpthsGLMVDASGPSFVNGTVVAQYRGNGGGNQRW 641
Cdd:cd23452     8 GLANKCIDVPNSSTTDGAPLQLWDCNGTNAQKWTFAS--DGTLRAL----GKCLDVAWGGTDNGTAVQLWTCSGNPAQQF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 642 RFyrNGQGrmlieSVYGGSHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFS 692
Cdd:cd23452    82 VL--SGAG-----DLVNPQANKCVDVSGGNSGNGTRLQLWECSGNANQKWR 125

ricin B-type lectin domain, beta-trefoil fold, found in Sclerotinia sclerotiorum agglutinin (SSA) and similar proteins; SSA acts as a lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha-over the beta-anomer. It can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. SSA strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. It also strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans. SSA is a homodimeric protein. The monomer contains a ricin B-type lectin domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a putative sugar-binding pocket.

Pssm-ID: 467304 [Multi-domain] Cd Length: 147 Bit Score: 38.87 E-value: 2.87e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAY-SGLYLDVNGASRSEGARLIT---CILNGGANQVFHIRPVGDGS---YTISPTHSGLMVDASGPSfvNGTV 627
Cdd:cd23426     3 GTYEIVPYHaPNKNLNLWGGSKEDGTKVRLysrGTASKNAHWQIVYAGGGGSGkdeYHIINVNSGLYLTATDKG--NGKV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 628 VAQYRGNGGGNQRWRFY--RNGQGRMLIESVygGSHNKVLQIHGLNPNPLGQIDVWS-ADGGPNQQFSL 693
Cdd:cd23426    81 TTNTTSPRNPRARWNIVpaRNGTGTYWINSV--ANKKLQLNVAGYGTADGTPVIIWAgADGAENQQFYL 147

ricin B-type lectin domain, beta-trefoil fold, found in Sclerotinia sclerotiorum agglutinin (SSA) and similar proteins; SSA acts as a lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha-over the beta-anomer. It can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. SSA strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. It also strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans. SSA is a homodimeric protein. The monomer contains a ricin B-type lectin domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a putative sugar-binding pocket.

Pssm-ID: 467304 [Multi-domain] Cd Length: 147 Bit Score: 38.87 E-value: 2.87e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAY-SGLYLDVNGASRSEGARLIT---CILNGGANQVFHIRPVGDGS---YTISPTHSGLMVDASGPSfvNGTV 466
Cdd:cd23426     3 GTYEIVPYHaPNKNLNLWGGSKEDGTKVRLysrGTASKNAHWQIVYAGGGGSGkdeYHIINVNSGLYLTATDKG--NGKV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 467 VAQYRGNGGGNQRWRFY--RNGQGRMLIESVygGSHNKVLQIHGLNPNPLGQIDVWS-ADGGPNQQFSL 532
Cdd:cd23426    81 TTNTTSPRNPRARWNIVpaRNGTGTYWINSV--ANKKLQLNVAGYGTADGTPVIIWAgADGAENQQFYL 147

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 38.28 E-value: 3.01e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 603 SYTISPTHSGLMVDASGPSFVNGTVVAQYRGNGGGNQRWRFYRNGQgrmlIESVYGgshNKVLQIHGLNPNplGQIDVWS 682
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGT----IRSVAS---DLCLDVGSTADG--AKVVLWP 72

                          90
                  ....*....|..
gi 2467975801 683 -ADGGPNQQFSL 693
Cdd:pfam00652  73 cHPGNGNQRWRY 84

ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end.

Pssm-ID: 467300 [Multi-domain] Cd Length: 135 Bit Score: 37.68 E-value: 4.78e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 555 GDYRIASAYSGLYLDVNGASRsegarliTCI----LNGGANQVFHIRPVGDGSYTISPTHSGLMVDASGPSfVNGTVVaq 630
Cdd:cd23422     3 GTYKIVNVKSGTVLDLSGDDN-------TSVvgwpFHGGENQQWTLEPTPGGGYTIQSVSTGKYLGIEGGP-RDGTRL-- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467975801 631 yrgnGGGN--QRWRF--YRNGQGRMLIeSVYGgsHNKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLER 695
Cdd:cd23422    73 ----VGSDqpFVWDIepDEGDSGAFRI-FVPG--TNLVLDLDDGGSAPGTPVQLWERSEGPNQLWRFER 134

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 36.20 E-value: 6.86e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 638 NQRWRF-YRNGQGRMLIESVYGGshnKVLQIHGLNPNPLGQIDVWSADGGPNQQFSLERL 696
Cdd:pfam14200   2 NQQWRFgGTVGDGYYTIVNVASG---KYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDA 58

ricin B-type lectin domain, beta-trefoil fold, found in Mushroom tyrosinase-associated lectin-like protein (MtaL) and similar proteins; Mushroom tyrosinase-associated lectin-like protein (MtaL) binds to mature Agaricus bisporus tyrosinase in vivo, but the exact physiological function of MtaL is poorly understood. MtaL contains a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. The tyrosinase enzyme complex is comprised of a H(2)L(2) tetramer. The L subunit has a lectin-like fold, whereas the H subunit contains a binuclear copper-binding site in the deoxy-state, in which three histidine residues coordinate each copper ion. Comparison of the structures of MtaL and a ricin-B-like lectin with a bound disaccharide shows that MtaL may have a similar carbohydrate-binding site that may be involved in glycoreceptor activity.

Pssm-ID: 467380 [Multi-domain] Cd Length: 129 Bit Score: 37.05 E-value: 9.17e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467975801 394 GDYRIASAYSGLYL-DVNGASRSEGARLITCILNGGANQVFHIRPVGDGsYTISPTHSGLMVDASGPsfvnGTVVAqyrG 472
Cdd:cd23714     1 GTYRIVNVGSGLWLgSFPDPPPPFGTPIVFDNNFASVFEVWEVTPFDDG-YTIQNVGTGLFATAKPR----GEVVV---S 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2467975801 473 NGGGNQRWRFYRNGQGRMLIESVYGgshNKVLQIHGlnPNPLGQIDVWSADGGPNQQFSLE 533
Cdd:cd23714    73 EEFQPTKWAIEPAGGGEYRIKVPNQ---DLVWTLDP--AGYDSTVVLEPADGSPNQRWKFV 128