NCBI Conserved Domain Search

first ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the first ricin B-type lectin domain.

Pssm-ID: 467298 Cd Length: 148 Bit Score: 284.83 E-value: 3.56e-96

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424   2 VLCTNPLDIGELRSFKSKQCVDIVGNQGSGNIATYDCDGLSDQQIIICGDGTIRNEARNYCFTPDGSGNANVMSSPCTLY 81
Cdd:cd23419   2 VLCTNPLDIGELRSFKSKQCVDIVGNQGSGNVATYDCDGLDDQQIIICGDGTIRNEARNYCFTPDGSGNANVMSSPCTLY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55670424  82 PEIPSSQRWRQGRRKTFTDNGGIEQVATEIINLASGKCLDIEGSDGTGDIGVYDCQNLDDQYFYVRS 148
Cdd:cd23419  82 PEIPSSQKWRQGRRKTFTDNGGIEQVAREIINLASGKCLDVEGSDGTGNIGVYDCQNLDDQYFYFRS 148

second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467299 [Multi-domain] Cd Length: 133 Bit Score: 256.71 E-value: 3.00e-85

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 151 PELFYGRLRNEKSDLCLDVEGSDGKGNVLMYSCEDNLDQWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQ 230
Cdd:cd23420   1 PELFYGRLRNEKSDLCLDVEGSDGKGNVLMYSCEDNLDQWFRYYENGEIVNAKSRMCLDVSGSDGSGNVGIYRCEDLRDQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 55670424 231 MWSRPNAYCNGDYCSFLNKESNKCLDVSGDQGTGDVGTWQCDGLPDQRFKWVF 283
Cdd:cd23420  81 MWSRPNQYCNGDYCSFLNKESNKCLDVSGDQGTGDVGTYQCDGLPDQRFKWVF 133

pore-forming module of hemolytic lectin Cucumaria echinate CEL-III and similar aerolysin-type beta-barrel pore-forming proteins; Cucumaria echinate CEL-III is a Ca(2+)-dependent and galactose-specific lectin, which is cytotoxic to some cultured cell lines, has strong hemolytic activity toward human and rabbit erythrocytes, and anti-malarial activity. Hemolysis results from ion-permeable pores formed from CEL-III oligomers in the target cell membrane. Members of this group includes CEL-III isoforms: CEL-III-L1, CEL-III-L2, CEL-III-S1, CEL-III-S2, and CEL-III-LS1. Many proteins belonging to this group have two N-terminal ricin-type carbohydrate-binding domains which adopt beta-trefoil folds. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). The CEL-III oligomer in the membrane may be composed of six monomers.

Pssm-ID: 380784 Cd Length: 124 Bit Score: 238.78 E-value: 1.89e-78

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 284 DDWEVPTATWNMVGCDQNGKVSQQISNTISFSSTVTAGVAVEVSSTIEKGVIFAKATVSVKVTASLSKAWTNSQSGTTAI 363
Cdd:cd20214   1 DDWEVPTATWNMVGCNQNGKVSQQISNTISFSSTVTAGVAVEVSSTIEKGVIFAKASVSVKVSASLSKAWTNSQSGTTAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 55670424 364 TYTCDNYDSDEEFTRGCMWQLAIETTEVKSGDLLVWNPQIVKCT 407
Cdd:cd20214  81 TYTCDNYDSDEEFTRGCMWQLAIETTEVKSGDLLVWNPQIVKCT 124

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 94.14 E-value: 3.89e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424   109 TEIINLASGKCLDIEGSDGTG-DIGVYDCQNLDD-QYFYVRSRgpelfyGRLRNEKSDLCLDVEGSDGKGNVLMYSCE-- 184
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSAGgPVGLYPCHGSNGnQLWTLTGD------GTIRSVASDLCLDVGSTADGAKVVLWPCHpg 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 55670424   185 DNLDQWFRYYENGEIVNAKSGMCLDVEGSDGS-GNVGIYRCDDLRD-QMW 232
Cdd:pfam00652  77 NGNQRWRYDEDGTQIRNPQSGKCLDVSGAGTSnGKVILWTCDSGNPnQQW 126

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: 2.30e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 155 YGRLRNEKSDLCLDVEGSDGK--GNVLMYSCEDNLDQWFRYYENG----EIVNAKSGMCLDVEGSDGS--GNVGIYRCDD 226
Cdd:cd00161   2 TYRIVNAASGKCLDVAGGSTAngAPVQQWTCNGGANQQWTLTPVGdgyyTIRNVASGKCLDVAGGSTAngANVQQWTCNG 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55670424 227 LRDQMWsRPNAYCNGDYcSFLNKESNKCLDVSGDQGT--GDVGTWQCDGLPDQRF 279
Cdd:cd00161  82 GDNQQW-RLEPVGDGYY-RIVNKHSGKCLDVSGGSTAngANVQQWTCNGGANQQW 134

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 91.82 E-value: 2.35e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424   154 FYGRLRNEKSDLCLDVEGSDGKG-NVLMYSCEDNLD-QWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRD-Q 230
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPGGSSAGgPVGLYPCHGSNGnQLWTLTGDGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGnQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 55670424   231 MWSRPNaycNGDYcsFLNKESNKCLDVSG-DQGTGDVGTWQCD-GLPDQRF 279
Cdd:pfam00652  81 RWRYDE---DGTQ--IRNPQSGKCLDVSGaGTSNGKVILWTCDsGNPNQQW 126

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: 80.17 E-value: 3.08e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 111 IINLASGKCLDiegSDGTGDIGVYDCQNLDDQYFYVRSRGPElfYGRLRNEKSDLCLDvegSDGKGNVLMYSCEDNLDQW 190
Cdd:cd23415   5 LRNVATGRCLD---SNAGGNVYTGPCNGGPYQRWTWSGVGDG--TVTLRNAATGRCLD---SNGNGGVYTLPCNGGSYQR 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 55670424 191 FRYY----ENGEIVNAKSGMCLDvegSDGSGNVGIYRCDDLRDQMWS 233
Cdd:cd23415  77 WRVTstsgGGVTLRNVATGRCLD---SNGSGGVYTRPCNGGSYQRWR 120

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

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 79.48 E-value: 5.63e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424    111 IINLASGKCLDIEGSDGTgdIGVYDC-QNLDDQYFYVRSRGpelfygRLRNEKSDLCLDVeGSDGKGNVLMYSCE-DNLD 188
Cdd:smart00458   1 IISGNTGKCLDVNGNKNP--VGLFDChGTGGNQLWKLTSDG------AIRIKDTDLCLTA-NGNTGSTVTLYSCDgTNDN 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 55670424    189 QWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQMW 232
Cdd:smart00458  72 QYWEVNKDGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKW 115

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: 75.48 E-value: 2.36e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  50 GDGTIRNEARNYCFTPDGSG---NANVMSSPCTLYPeipsSQRWrqgrrkTFTDNGGieqVATEIINLASGKCLDIEGSD 126
Cdd:cd00161   1 GTYRIVNAASGKCLDVAGGStanGAPVQQWTCNGGA----NQQW------TLTPVGD---GYYTIRNVASGKCLDVAGGS 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55670424 127 GT--GDIGVYDCQNLDDQYFYVRSRGPElfYGRLRNEKSDLCLDVEGSDGK--GNVLMYSCEDNLDQWF 191
Cdd:cd00161  68 TAngANVQQWTCNGGDNQQWRLEPVGDG--YYRIVNKHSGKCLDVSGGSTAngANVQQWTCNGGANQQW 134

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

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 74.47 E-value: 3.11e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424    160 NEKSDLCLDVEGsdGKGNVLMYSC-EDNLDQWFRYYENGEIVNAKSGMCLDVeGSDGSGNVGIYRCD-DLRDQMWsrpna 237
Cdd:smart00458   3 SGNTGKCLDVNG--NKNPVGLFDChGTGGNQLWKLTSDGAIRIKDTDLCLTA-NGNTGSTVTLYSCDgTNDNQYW----- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 55670424    238 YCNGDYcSFLNKESNKCLDVSGDQGTGDVGTWQCDGLPDQRFKWV 282
Cdd:smart00458  75 EVNKDG-TIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 118

first ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the first ricin B-type lectin domain.

Pssm-ID: 467298 Cd Length: 148 Bit Score: 74.89 E-value: 4.15e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 156 GRLRNEKSDLCLDVEGSDGKGNVLMYSCEDNLDQWFRYYENGEIVNAKSGMCLDVEGSdGSGNVGIYRCDDL----RDQM 231
Cdd:cd23419  11 GELRSFKSKQCVDIVGNQGSGNVATYDCDGLDDQQIIICGDGTIRNEARNYCFTPDGS-GNANVMSSPCTLYpeipSSQK 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55670424 232 W--SRPNAYCNG-----DYCSFLNKESNKCLDVSGDQGTGDVGTWQCDGLPDQRF 279
Cdd:cd23419  90 WrqGRRKTFTDNggieqVAREIINLASGKCLDVEGSDGTGNIGVYDCQNLDDQYF 144

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467337 [Multi-domain] Cd Length: 132 Bit Score: 72.35 E-value: 2.48e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 113 NLASGKCLD--IEGSDGTGDIGVYDCQN--LDDQYF-YVRSrgpelfyGRLRNEKSdlCLDVEGsDGKGNVLMYSCEDNL 187
Cdd:cd23459  12 NPGTNLCLDtlQRDEDKGYNLGLYPCQGglSSNQLFsLSKK-------GELRREES--CADVQG-TEESKVILITCHGLE 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 55670424 188 --DQWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQMWS 233
Cdd:cd23459  82 kfNQKWKHTKGGQIVHLASGKCLDAEGLKSGDDVTLAKCDGSLSQKWT 129

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: 71.23 E-value: 5.72e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 108 ATEIINLASGKCLDIEGSDGT--GDIGVYDCQNLDDQYFYVRSRGPELFYGrlrneksDLCLDVEGSDGKGN--VLMYSC 183
Cdd:cd23418   5 GGQIRGYGSGRCLDVPGGSTTngTRLILWDCHGGANQQFTFTSAGELRVGG-------DKCLDAAGGGTTNGtpVVIWPC 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 55670424 184 EDNLDQWFRYYENGEIVNAKSGMCLDVEGSDGSGN--VGIYRCDDLRDQMWSR 234
Cdd:cd23418  78 NGGANQKWRFNSDGTIRNVNSGLCLDVAGGGTANGtrLILWSCNGGSNQRWRR 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: 70.04 E-value: 1.82e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 155 YGRLRNEKSDLCLDVE-GSDGKGNVLM-YSCEDNLDQWFRYYENG----EIVNAKSGMCLDVEG---SDGSgNVGIYRCD 225
Cdd:cd23458   2 TYRIRNRNSGKCIDVAgGSTANGANIQqWDCGSGSNQQWTLVEIDngyyRIKASHSGKCLDVAGgstANGA-NIQQWDCV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55670424 226 DLRDQMWSRPNAycNGDYCSFLNKESNKCLDVSG-DQGTG-DVGTWQCDGLPDQRFK 280
Cdd:cd23458  81 GGANQQWKLQDL--GNGYFELKARHSGKCLDVAGgSTANGaSIQQWTCNGNDNQRFK 135

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 68.71 E-value: 4.74e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424    11 GELRSFKSKQCVDIVG-NQGSGNIATYDCDG-LSDQQIIICGDGTIRNEARNYCFT-PDGSGNANVMSSPCTlypEIPSS 87
Cdd:pfam00652   3 GRIRNRASGKCLDVPGgSSAGGPVGLYPCHGsNGNQLWTLTGDGTIRSVASDLCLDvGSTADGAKVVLWPCH---PGNGN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 55670424    88 QRWRqgrrktFTDNGgieqvaTEIINLASGKCLDI-EGSDGTGDIGVYDCQNLDD 141
Cdd:pfam00652  80 QRWR------YDEDG------TQIRNPQSGKCLDVsGAGTSNGKVILWTCDSGNP 122

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: 67.84 E-value: 7.18e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 155 YGRLRNEKSDLCLDvegSDGKGNVLMYSCEDNLDQWFRY----YENGEIVNAKSGMCLDvegSDGSGNVGIYRCDDLRDQ 230
Cdd:cd23415   2 TVRLRNVATGRCLD---SNAGGNVYTGPCNGGPYQRWTWsgvgDGTVTLRNAATGRCLD---SNGNGGVYTLPCNGGSYQ 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 55670424 231 MWsRPNAYCNGDYcSFLNKESNKCLDVSGDqgtGDVGTWQCDGLPDQR 278
Cdd:cd23415  76 RW-RVTSTSGGGV-TLRNVATGRCLDSNGS---GGVYTRPCNGGSYQR 118

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: 65.47 E-value: 6.77e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 197 GEIVNAKSGMCLDVEGSDGS--GNVGIYRCDDLRDQMWSRPNAycNGDYCSFLNKESNKCLDVSGDQGT--GDVGTWQCD 272
Cdd:cd00161   3 YRIVNAASGKCLDVAGGSTAngAPVQQWTCNGGANQQWTLTPV--GDGYYTIRNVASGKCLDVAGGSTAngANVQQWTCN 80

                        90
                ....*....|
gi 55670424 273 GLPDQRFKWV 282
Cdd:cd00161  81 GGDNQQWRLE 90

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: 65.08 E-value: 8.47e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  10 IGELRSFKSKQCVDIVGNQGS--GNIATYDCDGLSDQQIII----CGDGTIRNEARNYCFTPDGSG---NANVMSSPCTL 80
Cdd:cd00161   2 TYRIVNAASGKCLDVAGGSTAngAPVQQWTCNGGANQQWTLtpvgDGYYTIRNVASGKCLDVAGGStanGANVQQWTCNG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55670424  81 YPeipsSQRWRqgrrktFTDNGGieqVATEIINLASGKCLDIEGSDGT--GDIGVYDCQNLDDQYF 144
Cdd:cd00161  82 GD----NQQWR------LEPVGD---GYYRIVNKHSGKCLDVSGGSTAngANVQQWTCNGGANQQW 134

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: 63.92 E-value: 1.63e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 155 YGRLRNEKSDLCLDVEGSDGKG-NVLMYSCEDNLDQWFRYYENGEIVNAK-SGMCLDVEGSDGSG-NVGIYRCDDLRDQM 231
Cdd:cd23456   2 YFQLKSQASGLCLDVSGGATNGaNVVVYDCNNSNSQKWYYDATGRLHSKAnPGKCLDAGGENSNGaNVVLWACNDSANQR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 55670424 232 WSRpnaycNGDYCSfLNKESNKCLDVSGDQGtGDVGTWQCDGLPDQRF 279
Cdd:cd23456  82 WDF-----DGNFIR-SRNNTNLALDAYGSQG-SNVGLWQFHGGANQQW 122

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3)-like subfamily; The GALNT3-like subfamily includes GALNT3, GALNT4, GALNT6 and GALNT12. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which are 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 binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467313 [Multi-domain] Cd Length: 128 Bit Score: 62.73 E-value: 4.86e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 153 LFYGRLRNEKSDLCLDVEGSDGKG--NVLMYSCEdNLD--QWFRYYENGEI-VNAKSGMCLDVEGSDgsgNVGIYRC--- 224
Cdd:cd23435   2 GYYGALRNKGSELCLDVNNPNGQGgkPVIMYGCH-GLGgnQYFEYTSKGEIrHNIGKELCLHASGSD---EVILQHCtsk 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55670424 225 --DDLRDQMWS-RPNAycngdycSFLNKESNKCLDVSGDqgtgDVGTWQCDGLpDQRFKWVFD 284
Cdd:cd23435  78 gkDVPPEQKWLfTQDG-------TIRNPASGLCLHASGY----KVLLRTCNPS-DDSQKWTFI 128

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467337 [Multi-domain] Cd Length: 132 Bit Score: 62.72 E-value: 5.38e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 153 LFYGRLRNEKSDLCLDV--EGSDGKGNVLMYSCEDNL--DQWFRYYENGEIVNAKSgmCLDVEGSDGSgNVGIYRCDDL- 227
Cdd:cd23459   5 LAYGQVRNPGTNLCLDTlqRDEDKGYNLGLYPCQGGLssNQLFSLSKKGELRREES--CADVQGTEES-KVILITCHGLe 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55670424 228 -RDQMWSRPNaycNGdycSFLNKESNKCLDVSGDQGTGDVGTWQCDGLPDQrfKWVFDD 285
Cdd:cd23459  82 kFNQKWKHTK---GG---QIVHLASGKCLDAEGLKSGDDVTLAKCDGSLSQ--KWTFEH 132

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

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 62.14 E-value: 6.16e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424     18 SKQCVDIVGNqgSGNIATYDCDGLSD-QQIIICGDGTIRNEARNYCFTPDGSGNANVMSSPCTlypEIPSSQRWRQGRRK 96
Cdd:smart00458   6 TGKCLDVNGN--KNPVGLFDCHGTGGnQLWKLTSDGAIRIKDTDLCLTANGNTGSTVTLYSCD---GTNDNQYWEVNKDG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 55670424     97 TftdnggieqvateIINLASGKCLDIEGSDGTGDIGVYDCQNLDDQ 142
Cdd:smart00458  81 T-------------IRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQ 113

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467340 [Multi-domain] Cd Length: 126 Bit Score: 60.84 E-value: 2.62e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 155 YGRLRNEKSDLCLDVEGSDGKGN--VLMYSCED-NLDQWFRYYENGEIvnAKSGMCLDVegSDGSGNVGIYRCDDLR-DQ 230
Cdd:cd23462   5 YGEIRNLAGKLCLDAPGRKKELNkpVGLYPCHGqGGNQYWMLTKDGEI--RRDDLCLDY--AGGSGDVTLYPCHGMKgNQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 55670424 231 MWSrpnaYCNGDYcSFLNKESNKCLDVSGDqgTGDVGTWQCDG-LPDQRFKW 281
Cdd:cd23462  81 FWI----YDEETK-QIVHGTSKKCLELSDD--SSKLVMEPCNGsSPRQQWEF 125

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: 60.41 E-value: 3.70e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 108 ATEIINLASGKCLDIEG---SDGTGdIGVYDCQNLDDQYFYVRSRGPElfYGRLRNEKSDLCLDVEG---SDGKgNVLMY 181
Cdd:cd23458   2 TYRIRNRNSGKCIDVAGgstANGAN-IQQWDCGSGSNQQWTLVEIDNG--YYRIKASHSGKCLDVAGgstANGA-NIQQW 77

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 55670424 182 SCEDNLDQWFRYYENG----EIVNAKSGMCLDVEGSD 214
Cdd:cd23458  78 DCVGGANQQWKLQDLGngyfELKARHSGKCLDVAGGS 114

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: 60.04 E-value: 3.79e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 115 ASGKCLDIEGS---DGTGdIGVYDCQNLDDQYFYVRSRGPELFYGRlrneksdlCLDVEGSdGKGN---VLMYSCEDNLD 188
Cdd:cd23451   9 NAGKCLDVPGSstaDGNP-VQIYTCNGTAAQKWTLGTDGTLRVLGK--------CLDVSGG-GTANgtlVQLWDCNGTGA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 55670424 189 QWFRYYENGEIVNAKSGMCLDVEGSDGS--GNVGIYRCDDLRDQMWS 233
Cdd:cd23451  79 QKWVPRADGTLYNPQSGKCLDAPGGSTTdgTQLQLYTCNGTAAQQWT 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: 60.06 E-value: 5.41e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  11 GELRSFKSKQCVDIVGNQGS--GNIATYDCDGLSDQQIIICGDGTIRNEArNYCFTPDGSGNAN---VMSSPCTLYPEip 85
Cdd:cd23418   6 GQIRGYGSGRCLDVPGGSTTngTRLILWDCHGGANQQFTFTSAGELRVGG-DKCLDAAGGGTTNgtpVVIWPCNGGAN-- 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55670424  86 ssQRWRqgrrktFTDNGgieqvatEIINLASGKCLDIEG---SDGTgDIGVYDCQNLDDQYFYV 146
Cdd:cd23418  83 --QKWR------FNSDG-------TIRNVNSGLCLDVAGggtANGT-RLILWSCNGGSNQRWRR 130

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: 59.37 E-value: 6.38e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  50 GDGTIRNEARNYCFtpDGSGNANVMSSPCTLYPeipsSQRWRqgrrKTFTDNGGIEqvateIINLASGKCLDiegSDGTG 129
Cdd:cd23415   1 GTVRLRNVATGRCL--DSNAGGNVYTGPCNGGP----YQRWT----WSGVGDGTVT-----LRNAATGRCLD---SNGNG 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 130 DIGVYDCQNLDDQYFYVRSRGPELFygRLRNEKSDLCLDvegSDGKGNVLMYSCEDNLDQ 189
Cdd:cd23415  63 GVYTLPCNGGSYQRWRVTSTSGGGV--TLRNVATGRCLD---SNGSGGVYTRPCNGGSYQ 117

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467315 [Multi-domain] Cd Length: 124 Bit Score: 58.85 E-value: 1.02e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 153 LFYGRLRNEKSDLCLDVEGSDGKGNVLMYSCE---DNldQWFRYYENGEIvnAKSGMCLDVEGSDGSgnVGIYRCDDLRD 229
Cdd:cd23437   3 LAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHgmgGN--QLFRLNEAGQL--AVGEQCLTASGSGGK--VKLRKCNLGET 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 55670424 230 QMWSrpnaYCNGDYcSFLNKESNKCLDVSGDQGTGDVGTwqCDG-LPDQRFKW 281
Cdd:cd23437  77 GKWE----YDEATG-QIRHKGTGKCLDLNEGTNKLILQP--CDSsSPSQKWEF 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: 58.52 E-value: 1.59e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 110 EIINLASGKCLDIEGSDGTG-DIGVYDCQNLDDQYFYVRSRGpelfygRLRN-EKSDLCLDVEGSDGKG-NVLMYSCEDN 186
Cdd:cd23456   4 QLKSQASGLCLDVSGGATNGaNVVVYDCNNSNSQKWYYDATG------RLHSkANPGKCLDAGGENSNGaNVVLWACNDS 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 55670424 187 LDQWFRYYENGEIVNAKSGMCLDVEGSDGSgNVGIY 222
Cdd:cd23456  78 ANQRWDFDGNFIRSRNNTNLALDAYGSQGS-NVGLW 112

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467311 [Multi-domain] Cd Length: 127 Bit Score: 58.48 E-value: 1.68e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 156 GRLRNEKSDLCLDVEGSDGKGNVLMYSCEdNL--DQWFRYYENGEIVNakSGMCLDVegSDGSGNVGIYRCDDLRD-QMW 232
Cdd:cd23433   7 GEIRNVETNLCLDTMGRKAGEKVGLSSCH-GQggNQVFSYTAKGEIRS--DDLCLDA--SRKGGPVKLEKCHGMGGnQEW 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55670424 233 srpnaycngDY----CSFLNKESNKCLDVSGDQGTGDVGTWQCDGLPDQRfkWVFDD 285
Cdd:cd23433  82 ---------EYdketKQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGPSQK--WELEG 127

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: 57.34 E-value: 4.16e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  11 GELRSFKSKQCVDIVGNQGS-GN-IATYDCDGLSDQQIIICGDGTIRneARNYCFTPDGSGNANvmSSPCTLYPEIPS-S 87
Cdd:cd23451   3 GPVRLANAGKCLDVPGSSTAdGNpVQIYTCNGTAAQKWTLGTDGTLR--VLGKCLDVSGGGTAN--GTLVQLWDCNGTgA 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 55670424  88 QRWRQGRRKTftdnggieqvateIINLASGKCLDIEGS---DGTgDIGVYDCQNLDDQ 142
Cdd:cd23451  79 QKWVPRADGT-------------LYNPQSGKCLDAPGGsttDGT-QLQLYTCNGTAAQ 122

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: 59.03 E-value: 7.71e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  117 GKCLDIEGS--DGTGDIgVYDCQNLDDQYFYVrSRGPELFYGrlrneksDLCLDVEGSDGK--GNVLMYSCEDNLDQWFR 192
Cdd:NF035930 127 GLCLDVSGGlrPGNGLI-VYNCNGGENQRFTW-GRGGELRVG-------DLCLDVADGNTRdgARVIAWSCSGGPNQRWR 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 55670424  193 YyENGEIVNAKSGMCLDVEGSDG--SGNVGIYRCDDLRDQMW 232
Cdd:NF035930 198 W-RGGQIRSRLSGKCLDIEGGRArpGQPVIVWSCNGGPNQRW 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: 52.77 E-value: 1.94e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 111 IINLASGKCLDIEGSDGT--GDIGVYDCQNLDDQYFYVRSRGPelFYGRLRNEKSDLCLDVEGS---DGKGNVLMYSCED 185
Cdd:cd23446   5 LVNRNSGKALDVLSGSTTdgAQIEQWTDNGGTSQQWYFTDVGG--GYYKIVNRNSGKALDVNGAstaDGAAIIQWTSNGG 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 55670424 186 NLDQW------FRYYEngeIVNAKSGMCLDVEG--SDGSGNVGIYRCDDLRDQMWS 233
Cdd:cd23446  83 DNQQWqivdtgDGYYK---IVNRNSGKLLDVNGwsTADGADIIQWSDNGGTNQQWQ 135

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: 52.33 E-value: 2.14e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 156 GRLRNEKSDLCLDVEGSDGK-GN-VLMYSCEDNLDQWFRYYENGEIVNakSGMCLDVEGSdGSGN---VGIYRCDDLRDQ 230
Cdd:cd23451   3 GPVRLANAGKCLDVPGSSTAdGNpVQIYTCNGTAAQKWTLGTDGTLRV--LGKCLDVSGG-GTANgtlVQLWDCNGTGAQ 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 55670424 231 MWS-RPNAycngdycSFLNKESNKCLDVSGD---QGTgDVGTWQCDGLPDQRFK 280
Cdd:cd23451  80 KWVpRADG-------TLYNPQSGKCLDAPGGsttDGT-QLQLYTCNGTAAQQWT 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: 51.95 E-value: 3.31e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 196 NGEIVNAKSGMCLDVEGSDGS-GN-VGIYRCDDLRDQMWSRPNaycNGDYcsflnKESNKCLDVSGDqGTGD---VGTWQ 270
Cdd:cd23451   2 TGPVRLANAGKCLDVPGSSTAdGNpVQIYTCNGTAAQKWTLGT---DGTL-----RVLGKCLDVSGG-GTANgtlVQLWD 72

                        90
                ....*....|....*
gi 55670424 271 CDGLPDQrfKWVFDD 285
Cdd:cd23451  73 CNGTGAQ--KWVPRA 85

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 50.46 E-value: 3.84e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424    86 SSQRWRqgrrktFTDNGGIEQVatEIINLASGKCLDIEGSDGTG--DIGVYDCQNLDDQYFYVRSRGPELFygRLRNEKS 163
Cdd:pfam14200   1 ANQQWR------FGGTVGDGYY--TIVNVASGKYLDVAGGSTANgaNVQQWTDNGNDNQQWRIVDAGDGYY--RIVNKAS 70

                          90
                  ....*....|....*....
gi 55670424   164 DLCLDVEGSDGKG-NVLMY 181
Cdd:pfam14200  71 GKVLDVAGSTANGtNVQQW 89

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467318 [Multi-domain] Cd Length: 127 Bit Score: 51.22 E-value: 5.54e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 153 LFYGRLRNEKSDLCLDVEG--SDGKGNVLMYSCEDNLDQ--WfRYYENGEIVNAKSgMCLDVEGSDGSGnVGIYRCDDLR 228
Cdd:cd23440   3 IRKGQLKHAGSGLCLVAEDevSQKGSLLVLRPCSRNDKKqlW-YYTEDGELRLANL-LCLDSSETSSDF-PRLMKCHGSG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55670424 229 -DQMWSRPNA---YcngdycsflNKESNKCLDVSGDQGTGDVGTWQCDGLPDQrfKWVF 283
Cdd:cd23440  80 gSQQWRFKKDnrlY---------NPASGQCLAASKNGTSGYVTMDICSDSPSQ--KWVF 127

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 50.07 E-value: 5.79e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55670424   199 IVNAKSGMCLDVEGS--DGSGNVGIYRCDDLRDQMWSRPNAycNGDYCSFLNKESNKCLDVSGDQGTG-DVGTW 269
Cdd:pfam14200  18 IVNVASGKYLDVAGGstANGANVQQWTDNGNDNQQWRIVDA--GDGYYRIVNKASGKVLDVAGSTANGtNVQQW 89

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: 50.89 E-value: 5.89e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 199 IVNAKSGMCLDvegSDGSGNVGIYRCDDLRDQMWSRPNAYCNGDycSFLNKESNKCLDVSGDqgtGDVGTWQCDGLPDQR 278
Cdd:cd23415   5 LRNVATGRCLD---SNAGGNVYTGPCNGGPYQRWTWSGVGDGTV--TLRNAATGRCLDSNGN---GGVYTLPCNGGSYQR 76


                ....*...
gi 55670424 279 FKWVFDDW 286
Cdd:cd23415  77 WRVTSTSG 84

ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and similar proteins; AglA (EC 3.2.1.22), also called melibiase A, hydrolyzes a variety of simple alpha-D-galactosides as well as more complex molecules such as oligosaccharides and polysaccharides. It belongs to the glycosyl hydrolase 27 (GH27) family. AglA contains an N-terminal GH27 catalytic domain, an alpha galactosidase C-terminal beta sandwich domain in the middle region, and a carbohydrate-binding domain at the C-terminus. The carbohydrate-binding domain is also known as 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 may contain a potential sugar-binding pocket.

Pssm-ID: 467303 [Multi-domain] Cd Length: 116 Bit Score: 50.91 E-value: 6.24e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 107 VATEII-NLASGKCLdiegSDGTGDIGVYDCQNLDDQYFYVRSrgpelfYGRLRN-EKSDLCLDVEGsdgkGNVLMYSCE 184
Cdd:cd23425   2 VATGIIfNTASGNCL----TADAAEVKFQTCDGSDSQIWQVRK------SGILRNlSNTGQCLTADG----ANVSLSPCD 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 55670424 185 DNLDQWFRYYENGEIVNAKSGMCLDVegsDGSGNVGIYRCDDLRD-QMWSRP 235
Cdd:cd23425  68 TSTSQNWSYEISGNLVNKKTGLCLTE---GNDAQVTVTDCGNELDsQVFGLP 116

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467337 [Multi-domain] Cd Length: 132 Bit Score: 51.17 E-value: 7.06e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424   6 NPLDIGELRSFKSKQCVD--IVGNQGSGNIATYDC--DGLSDQQIIICGDGTIRNEarNYCFTPDGSGNANVMSSPCTly 81
Cdd:cd23459   3 DVLAYGQVRNPGTNLCLDtlQRDEDKGYNLGLYPCqgGLSSNQLFSLSKKGELRRE--ESCADVQGTEESKVILITCH-- 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55670424  82 PEIPSSQRWrqgrrkTFTDNGgieqvatEIINLASGKCLDIEGSDGTGDIGVYDCQNLDDQ 142
Cdd:cd23459  79 GLEKFNQKW------KHTKGG-------QIVHLASGKCLDAEGLKSGDDVTLAKCDGSLSQ 126

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 49.30 E-value: 1.15e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424   140 DDQYFYVRSRGPELFYgRLRNEKSDLCLDVEGS--DGKGNVLMYSCEDNLDQWFRYYENGE----IVNAKSGMCLDVEGS 213
Cdd:pfam14200   1 ANQQWRFGGTVGDGYY-TIVNVASGKYLDVAGGstANGANVQQWTDNGNDNQQWRIVDAGDgyyrIVNKASGKVLDVAGS 79

                          90
                  ....*....|
gi 55670424   214 DGSG-NVGIY 222
Cdd:pfam14200  80 TANGtNVQQW 89

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467312 [Multi-domain] Cd Length: 121 Bit Score: 49.24 E-value: 2.14e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 117 GKCLDIEGSDGTGDIGVYDCQNLD-DQYF-YVRSrgpelfyGRLRNekSDLCLDVEGSDGKGNVLMYSCE--DNLDQWFR 192
Cdd:cd23434   9 NLCLDTLGHKAGGTVGLYPCHGTGgNQEWsFTKD-------GQIKH--DDLCLTVVDRAPGSLVTLQPCRedDSNQKWEQ 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 55670424 193 YYENGEIVNAKSGMCLDVEGSDgSGNVGIYRCDDLRD-QMWS 233
Cdd:cd23434  80 IENNSKLRHVGSNLCLDSRNAK-SGGLTVETCDPSSGsQQWK 120

first 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 first lectin domain.

Pssm-ID: 467377 [Multi-domain] Cd Length: 131 Bit Score: 49.75 E-value: 2.24e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 110 EIINLASGKCLDIEGSDGT----GDIGVYDCQN--LDDQYFYVRSRgpelfyGRLRNEKS-DLCLDVEG--SDGkGNVLM 180
Cdd:cd23499   4 RIVNRASGKCLDIPGNDNDvvngANVILWDCADksADQRWIYDAAS------GMLRNKANpSYCLDNRGqaYNG-GEVVL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55670424 181 YSCEDNLDQ-WfrYYENGEIVNA-KSGMCLDVEGSDGSGNVGIYRCDDLRDQMWS 233
Cdd:cd23499  77 WQCEDSDNLrW--TYDNGVLRSKhNPNIVLDAYGRDNNSQVGQWEYHGGANQQWE 129

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467338 [Multi-domain] Cd Length: 121 Bit Score: 48.98 E-value: 3.14e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 110 EIINLASGKCLDIEGSDGTGD-IGVYDCQ-NLDDQYFYVRSRgpelfyGRLRNekSDLCLDVEgsdgKGNVLMY-SCEDN 186
Cdd:cd23460   4 QIKHTESGLCLDWAGESNGDKtVALKPCHgGGGNQFWMYTGD------GQIRQ--DHLCLTAD----EGNKVTLrECADQ 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 55670424 187 LD--QWFrYYEN-GEIVNAKSGMCLDVegSDGSGNVGIYRCDDLRD-QMW 232
Cdd:cd23460  72 LPsqEWS-YDEKtGTIRHRSTGLCLTL--DANNDVVILKECDSNSLwQKW 118

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467317 [Multi-domain] Cd Length: 126 Bit Score: 48.88 E-value: 3.26e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 110 EIINLASGKCLDIEGSDGTGDIGVYDC---QNLDDQYFyvrsrgpELFYGR-LRNEKSDLCLDVEGSDGKGNVLMYSCED 185
Cdd:cd23439   4 EIRNVGSGLCIDTKHGGENDEVRLSKCvkdGGGGEQQF-------ELTWHEdIRPKKRKVCFDVSSHTPGAPVILYACHG 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 55670424 186 NL-DQWFRYYEN-GEIVNAKSGMCLDveGSDGSGNVGIYRCD-DLRDQMW 232
Cdd:cd23439  77 MKgNQLWKYRPNtKQLYHPVSGLCLD--ADPGSGKVFMNHCDeSSDTQKW 124

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: 48.89 E-value: 3.60e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 198 EIVNAKSGMCLDVEGSDGSG-NVGIYRCDDLRDQMWSRpnaycngDYCSFL--NKESNKCLDVSGDQGTG-DVGTWQCDG 273
Cdd:cd23456   4 QLKSQASGLCLDVSGGATNGaNVVVYDCNNSNSQKWYY-------DATGRLhsKANPGKCLDAGGENSNGaNVVLWACND 76

                        90
                ....*....|..
gi 55670424 274 LPDQRfkWVFDD 285
Cdd:cd23456  77 SANQR--WDFDG 86

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-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. One member of this family, MRC1, is missing the gamma subdomain.

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 48.36 E-value: 4.17e-07

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55670424 158 LRNEKSDLCLDVEGSDGKgnVLMYSC-EDNLDQWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRD-QMWS 233
Cdd:cd23385   5 IYNEDLGKCLAARSSSSK--VSLSTCnPNSPNQQWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEDElQKWK 80

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467315 [Multi-domain] Cd Length: 124 Bit Score: 48.45 E-value: 4.58e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  11 GELRSFKSKQCVDIVGNQGSGNIATYDCDGLSDQQII-ICGDGTIRNEarNYCFTPDGSGNAnVMSSPCTLypeiPSSQR 89
Cdd:cd23437   6 GEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFrLNEAGQLAVG--EQCLTASGSGGK-VKLRKCNL----GETGK 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 55670424  90 WrqgrrkTFTDNGGieqvatEIINLASGKCLDIegSDGTGDIGVYDCQNLDD 141
Cdd:cd23437  79 W------EYDEATG------QIRHKGTGKCLDL--NEGTNKLILQPCDSSSP 116

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467311 [Multi-domain] Cd Length: 127 Bit Score: 48.08 E-value: 6.44e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  10 IGELRSFKSKQCVDIVGNQGSGNIATYDCDGLSDQQII-ICGDGTIRNEARnyCFTPdGSGNANVMSSPCTlypEIPSSQ 88
Cdd:cd23433   6 LGEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFsYTAKGEIRSDDL--CLDA-SRKGGPVKLEKCH---GMGGNQ 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55670424  89 RWRqgrrktftdnggIEQVATEIINLASGKCLDIEGSDGTGDIGVYDCQNLDDQY 143
Cdd:cd23433  80 EWE------------YDKETKQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGPSQK 122

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: 47.43 E-value: 1.05e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  13 LRSFKSKQCVDivgNQGSGNIATYDCDGLSDQQ----IIICGDGTIRNEARNYCFtpDGSGNANVMSSPCTlypeIPSSQ 88
Cdd:cd23415   5 LRNVATGRCLD---SNAGGNVYTGPCNGGPYQRwtwsGVGDGTVTLRNAATGRCL--DSNGNGGVYTLPCN----GGSYQ 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 55670424  89 RWRQGRrktfTDNGGIeqvatEIINLASGKCLDiegSDGTGDIGVYDCQNLDDQ 142
Cdd:cd23415  76 RWRVTS----TSGGGV-----TLRNVATGRCLD---SNGSGGVYTRPCNGGSYQ 117

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: 46.35 E-value: 2.62e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 107 VATEIINLAsGKCLDIEGSDGTGDIGV--YDCQNLDDQYFYVRSRGPELFYGRlrneksdlCLDVE--GSDGKGNVLMYS 182
Cdd:cd23452   2 TGTPIIGLA-NKCIDVPNSSTTDGAPLqlWDCNGTNAQKWTFASDGTLRALGK--------CLDVAwgGTDNGTAVQLWT 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 55670424 183 CEDNLDQWFRYYENGEIVNAKSGMCLDVEGSD-GSGN-VGIYRCDDLRDQMWS 233
Cdd:cd23452  73 CSGNPAQQFVLSGAGDLVNPQANKCVDVSGGNsGNGTrLQLWECSGNANQKWR 125

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467338 [Multi-domain] Cd Length: 121 Bit Score: 45.90 E-value: 3.56e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 154 FYGRLRNEKSDLCLDVEGSDGKGNVL-MYSCEDN-LDQWFRYYENGEIVNakSGMCLDVegsDGSGNVGIYRCDDLRD-Q 230
Cdd:cd23460   1 GLGQIKHTESGLCLDWAGESNGDKTVaLKPCHGGgGNQFWMYTGDGQIRQ--DHLCLTA---DEGNKVTLRECADQLPsQ 75

                        90       100
                ....*....|....*....|....*...
gi 55670424 231 MWSrpnaYCNGDYcSFLNKESNKCLDVS 258
Cdd:cd23460  76 EWS----YDEKTG-TIRHRSTGLCLTLD 98

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467318 [Multi-domain] Cd Length: 127 Bit Score: 45.45 E-value: 6.49e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 111 IINLASGKCLDIEGSDGT--GDIGVYDCQNLDD-QYFYVRSRGpELfygRLRNEksdLCLDVEGSDGKGNVLMYSCEDNL 187
Cdd:cd23440   8 LKHAGSGLCLVAEDEVSQkgSLLVLRPCSRNDKkQLWYYTEDG-EL---RLANL---LCLDSSETSSDFPRLMKCHGSGG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 55670424 188 DQWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQMW 232
Cdd:cd23440  81 SQQWRFKKDNRLYNPASGQCLAASKNGTSGYVTMDICSDSPSQKW 125

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

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 45.19 E-value: 6.79e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424     11 GELRSFKSKQCVDIVGNQGSgNIATYDCDGLSD-QQIIICGDGTIRNEARNYCFT-PDGSGNANVMSSPCTLYPeipsSQ 88
Cdd:smart00458  39 GAIRIKDTDLCLTANGNTGS-TVTLYSCDGTNDnQYWEVNKDGTIRNPDSGKCLDvKDGNTGTKVILWTCSGNP----NQ 113


                   ....
gi 55670424     89 RWRQ 92
Cdd:smart00458 114 KWIF 117

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: 44.97 E-value: 8.45e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 111 IINLASGKCLDIEGSDG--TGDIGVYDcqnlddqyfyvRSRGPE---LFY-----GRLRNEKSDLCLDVegSDGKGNVLM 180
Cdd:cd23449   5 IKSKLNGKVLDVEGANAkpGAKVIMWE-----------KKGGAEdnqLWYedevtGTIRSKLNDFCLDA--SGDKGLILN 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 55670424 181 -YSCEDNLDQWfrYYENGEIVNAK-SGMCLDVEGS--DGSGNVGIYRCDDLRDQMW 232
Cdd:cd23449  72 pYDPSNPKQQW--KISGNKIQNRSnPDNVLDIKGGskDDGARLCAWEYNGGPNQLW 125

second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467299 [Multi-domain] Cd Length: 133 Bit Score: 44.08 E-value: 1.92e-05

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 55670424  11 GELRSF---KSKQCVDIVGNQGSGNIATYDCDGLSDQQ 45
Cdd:cd23420  91 GDYCSFlnkESNKCLDVSGDQGTGDVGTYQCDGLPDQR 128

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: 43.61 E-value: 2.20e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 155 YGRLRNEKSDLCLDV-EGSDGKGNVL-MYSCEDNLDQWFRY-YENGEIVNA-KSGMCLDVEGsdgsGNVG------IYRC 224
Cdd:cd23500   2 WTTYRSKRSGKCLSAaNGSQLNGSLVqLDACHASAGQLWYFdPKKGTIRSAlDGNKCLAIPG----GNTGnhtqlqLADC 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55670424 225 DDLRD-QMWSRPNAYcngdYCSFLNkeSNKCLDVSGDQGTGDVGTWQCDGLPDQRFK 280
Cdd:cd23500  78 DASNPaQQFNYDGGV----FRSRLN--SNQVIDASGGSDGSELILYDYHGGSNQRWR 128

first 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 first lectin domain.

Pssm-ID: 467377 [Multi-domain] Cd Length: 131 Bit Score: 43.59 E-value: 2.57e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 155 YGRLRNEKSDLCLDVEGSDGK----GNVLMYSCED-NLDQWFRYyengeivNAKSGM---------CLDVEGSDGS-GNV 219
Cdd:cd23499   2 FVRIVNRASGKCLDIPGNDNDvvngANVILWDCADkSADQRWIY-------DAASGMlrnkanpsyCLDNRGQAYNgGEV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55670424 220 GIYRCDDLRDQMWSrpnaYCNGDYCSFLNkeSNKCLDVSGDQGTGDVGTWQCDGLPDQRFKW 281
Cdd:cd23499  75 VLWQCEDSDNLRWT----YDNGVLRSKHN--PNIVLDAYGRDNNSQVGQWEYHGGANQQWEL 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: 43.47 E-value: 3.35e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  12 ELRSFKSKQCVDIVGNQ---GSgNIATYDCDGLSDQQIIICGDGT----IRNEARNYCFTPDGSGN---ANVMSSPCtly 81
Cdd:cd23458   4 RIRNRNSGKCIDVAGGStanGA-NIQQWDCGSGSNQQWTLVEIDNgyyrIKASHSGKCLDVAGGSTangANIQQWDC--- 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55670424  82 pEIPSSQRWrqgrRKTFTDNGgieqvATEIINLASGKCLDIEGSDGT--GDIGVYDCQNLDDQYF 144
Cdd:cd23458  80 -VGGANQQW----KLQDLGNG-----YFELKARHSGKCLDVAGGSTAngASIQQWTCNGNDNQRF 134

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

Pssm-ID: 467344 Cd Length: 127 Bit Score: 43.11 E-value: 4.06e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 110 EIINLASGKCLDIEGSDGTGDIGVYDCQNLDDQYFYVRSRGPELfygrlrnEKSDLCLDVegSDGKGNVLMYSCEDNLDQ 189
Cdd:cd23466   8 EIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEI-------RTDDLCLDV--SKLNGPVMMLKCHHLKGN 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 55670424 190 WFRYYENGE--IVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQMW 232
Cdd:cd23466  79 QLWEYDPVKltLLHVNSNQCLDKATEEDSQVPSIRDCNGSRSQQW 123

pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium perfringens epsilon-toxin is responsible for fatal enterotoxemia in ungulates. It forms a heptamer in the lipid rafts of Madin-Darby Canine Kidney (MDCK) cells, leading to cell death; its oligomer formation is induced by activation of neutral sphingomyelinase. This group also includes an insecticidal crystal protein Cry14-4 (encoded on plasmid pBMBt1 of Bacillus thuringiensis serovar darmstadiensis). Also included is pXO2-60 (a protein from the pathogenic pXO2 plasmid of Bacillus anthracis) which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-like domain, and is involved in virulence. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).

Pssm-ID: 380793 [Multi-domain] Cd Length: 144 Bit Score: 42.99 E-value: 5.89e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55670424 305 SQQISNTISFSSTVTAGVAVEVSSTIEKGVIFAkATVSVKVTASLSKAWTNSQSGTTAITY 365
Cdd:cd20223  38 SKTVTDTVTTTTTNGFKLGVSTSAKFKIPFPGG-GSTELSAEYNFSTTNTNTTSETKTYTA 97

first ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the first ricin B-type lectin domain.

Pssm-ID: 467298 Cd Length: 148 Bit Score: 42.92 E-value: 6.06e-05

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 55670424 249 KESNKCLDVSGDQGTGDVGTWQCDGLPDQRFKWVFD 284
Cdd:cd23419  16 FKSKQCVDIVGNQGSGNVATYDCDGLDDQQIIICGD 51

second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the second ricin B-type lectin domain. Members of this family includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).

Pssm-ID: 467322 [Multi-domain] Cd Length: 122 Bit Score: 41.87 E-value: 7.73e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  37 DC-DGLSDQQIIICGDGTIR-NEARNYCFTPDGSGNANVMS-SPCtlypEIPSSQRWrqgrrkTFTDNGGieqvateIIN 113
Cdd:cd23444  26 ECvSNKKEQKWALYPDGTIRpNQNRNLCLTSSSDVQGSIIVvLSC----SGSSGQRW------VFRNDGT-------ILN 88

                        90
                ....*....|...
gi 55670424 114 LASGKCLDIEGSD 126
Cdd:cd23444  89 LYTGLVMDVKESD 101

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467320 [Multi-domain] Cd Length: 124 Bit Score: 42.04 E-value: 8.75e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 110 EIINLASGKCLDI--EGSDGTGDIGVYDCQNLD-DQYFYVRSRGpelfygRLRNEKSDLCLDVEgsdgKGNVLMYSC-ED 185
Cdd:cd23442   7 QLYNTGTGYCADYihGWRLAGGPVELSPCSGQNgNQLFEYTSDK------EIRFGSLQLCLDVR----QEQVVLQNCtKE 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 55670424 186 NLDQWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQMW 232
Cdd:cd23442  77 KTSQKWDFQETGRIVHILSGKCIEAVESENSKLLFLSPCNGQRNQMW 123

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT3 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467346 Cd Length: 129 Bit Score: 42.11 E-value: 9.01e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 153 LFYGRLRNEKSDLCLDV-EGSDGKGNVLMYSCED-NLDQWFRYYENGEIV-NAKSGMCLDveGSDGSgnVGIYRCD---- 225
Cdd:cd23468   3 LIFGAIKNVGKELCLDVgENNHGGKPLIMYNCHGlGGNQYFEYSTHHEIRhNIQKELCLH--GSQGS--VQLKECTykgr 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55670424 226 ---DLRDQMWSRPNAYcngdycSFLNKESNKCLDVSGDQGTgdvgTWQCDglPDQRF-KWVF 283
Cdd:cd23468  79 ntaVLPEEKWELQKDQ------LLYNPALNMCLSANGENPS----LVPCN--PSDPFqQWIF 128

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467340 [Multi-domain] Cd Length: 126 Bit Score: 41.58 E-value: 1.08e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 194 YENGEIVNAKSGMCLDVEGSDGSGN--VGIYRCDDLRD-QMWSRPNaycngdycsflNKE---SNKCLDVSGdqGTGDVG 267
Cdd:cd23462   3 LAYGEIRNLAGKLCLDAPGRKKELNkpVGLYPCHGQGGnQYWMLTK-----------DGEirrDDLCLDYAG--GSGDVT 69

                        90
                ....*....|....*..
gi 55670424 268 TWQCDGLPDQRFkWVFD 284
Cdd:cd23462  70 LYPCHGMKGNQF-WIYD 85

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: 41.51 E-value: 1.52e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 142 QYFYVRSRgpelfygrlrneKSDLCLDVEGSDGK--GNVLMYSCEDNLD---QWFRYYENGEIVNAKSGMCLDVEGsDGS 216
Cdd:cd23449   1 KYFYIKSK------------LNGKVLDVEGANAKpgAKVIMWEKKGGAEdnqLWYEDEVTGTIRSKLNDFCLDASG-DKG 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55670424 217 GNVGIYRCDDlRDQMWsrpnaYCNGDY-CSFLNkeSNKCLDVSGdqGTGDVGT----WQCDGLPDQRfkWVFD 284
Cdd:cd23449  68 LILNPYDPSN-PKQQW-----KISGNKiQNRSN--PDNVLDIKG--GSKDDGArlcaWEYNGGPNQL--WDFE 128

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467340 [Multi-domain] Cd Length: 126 Bit Score: 41.20 E-value: 1.55e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  11 GELRSFKSKQCVDIVGNQGSGN--IATYDCDGLSD-QQIIICGDGTIRNEarNYCFTPDGsGNANVMSSPCTLypeIPSS 87
Cdd:cd23462   6 GEIRNLAGKLCLDAPGRKKELNkpVGLYPCHGQGGnQYWMLTKDGEIRRD--DLCLDYAG-GSGDVTLYPCHG---MKGN 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55670424  88 QRWRQgRRKTFTdnggieqvateIINLASGKCLDIegSDGTGDIGVYDCQNLDDQ 142
Cdd:cd23462  80 QFWIY-DEETKQ-----------IVHGTSKKCLEL--SDDSSKLVMEPCNGSSPR 120

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).

Pssm-ID: 380810 [Multi-domain] Cd Length: 145 Bit Score: 41.09 E-value: 2.28e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 275 PDQRFKWVFDDWEVPTATWNMVgcdqngkVSQQISNTISFSSTVtaGVAVEVSSTIEKGV-IFAKATVSVKVTASLSKAW 353
Cdd:cd20240   5 PDFIVTWTYTNNTSIEQTMTTN-------FSETATETSSFSETE--GVSTTVSTSLKVGIpFIAGGEITTTTTTSQSWTY 75

                        90
                ....*....|...
gi 55670424 354 TNSQSGTTAITYT 366
Cdd:cd20240  76 GKSETKTDTISYT 88

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467317 [Multi-domain] Cd Length: 126 Bit Score: 40.79 E-value: 2.50e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 156 GRLRNEKSDLCLDVEGSDGKGNVLMYSCED---NLDQWFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLR-DQM 231
Cdd:cd23439   3 GEIRNVGSGLCIDTKHGGENDEVRLSKCVKdggGGEQQFELTWHEDIRPKKRKVCFDVSSHTPGAPVILYACHGMKgNQL 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 55670424 232 WS-RPNAYcngdycSFLNKESNKCLDvsGDQGTGDVGTWQCD-GLPDQRFKW 281
Cdd:cd23439  83 WKyRPNTK------QLYHPVSGLCLD--ADPGSGKVFMNHCDeSSDTQKWTW 126

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467345 Cd Length: 127 Bit Score: 40.78 E-value: 2.51e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 110 EIINLASGKCLDIEGSDGTGDIGVYDCQNLDDQYFYVRSRGPELfygrlrnEKSDLCLDVegSDGKGNVLMYSCED-NLD 188
Cdd:cd23467   8 EIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEI-------RTDDLCLDV--SRLNGPVVMLKCHHmRGN 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 55670424 189 QWFRY-YENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQMW 232
Cdd:cd23467  79 QLWEYdAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQW 123

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: 41.18 E-value: 2.65e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 157 RLRNEKSDLCLDVEGSDGKGNVLMYSCEDNLDQWFR--------------YYEngeIVNAKSGMCLDVEGSDGSGNVGI- 221
Cdd:cd23416   4 HIRNAGTGTVLDLSGGSSANGTPIQGWQKTGDTGSFnqlwllepvpngsdTYT---IQNVRSGTYLDLAGGSSANGTAIv 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55670424 222 -YRCDDLRDQMW--SRPNAycnGDYCSFLNKESNKCLDVSG--DQGTGDVGTWQ-CDGLPDQRfkWVFD 284
Cdd:cd23416  81 gWQSTNNPNQQWviKPANG---GTYYKIQNKGTGTFLDLYGgdSANGTKIVGWTgHWGNPNQL--WLFE 144

GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are 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. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain.

Pssm-ID: 467332 [Multi-domain] Cd Length: 136 Bit Score: 40.38 E-value: 3.54e-04

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55670424 143 YFYVRSRGpelfygrlrnekSDLCLDVEGSDGK--GNVLM-----YSCEDNLdqWfrYYENGEIVNAKSGMCLDVEGSD 214
Cdd:cd23454   2 WFFIKSSS------------NGLVLDVEHGSLKsgAKVVLaplktKDYESQL--W--RYDDGYLVNKASGLVLDIQGGV 64

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467345 Cd Length: 127 Bit Score: 40.01 E-value: 4.75e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 156 GRLRNEKSDLCLDVEGSDGKGNVLMYSCED-NLDQWFRYYENGEIvnAKSGMCLDVegSDGSGNVGIYRCDDLR-DQMWS 233
Cdd:cd23467   7 GEIRNVETNQCLDNMGRKENEKVGIFNCHGmGGNQVFSYTADKEI--RTDDLCLDV--SRLNGPVVMLKCHHMRgNQLWE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 55670424 234 RpnaycNGDYCSFLNKESNKCLDVSGDQGTGDVGTWQCDGLPDQRF 279
Cdd:cd23467  83 Y-----DAERLTLRHVNSNQCLDEPSEEDKMVPTMKDCSGSRSQQW 123

second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the second ricin B-type lectin domain. Members of this family includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).

Pssm-ID: 467322 [Multi-domain] Cd Length: 122 Bit Score: 39.56 E-value: 5.48e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 107 VATEIINLaSGKCLDiegSDGTGDIGVYDC-QNLDDQYFYvrsrgpelFY--GRLR-NEKSDLCLDVEGSDGKGNVLMYS 182
Cdd:cd23444   2 IVTSIVGL-NDLCLQ---ANGGNNVWLEECvSNKKEQKWA--------LYpdGTIRpNQNRNLCLTSSSDVQGSIIVVLS 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 55670424 183 CEDNLDQ-W-FRYyeNGEIVNAKSGMCLDVEGSDGSGNVGI-YRCDDLRDQMW 232
Cdd:cd23444  70 CSGSSGQrWvFRN--DGTILNLYTGLVMDVKESDPSLKQIIlWPATGGPNQQW 120

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-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. One member of this family, MRC1, is missing the gamma subdomain.

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 39.12 E-value: 6.90e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 111 IINLASGKCLdiEGSDGTGDIGVYDC-QNLDDQYFYVRSRGpelfygRLRNEKSDLCLDVEGSDGKGNVLMYSC-EDNLD 188
Cdd:cd23385   5 IYNEDLGKCL--AARSSSSKVSLSTCnPNSPNQQWKWTSGH------RLFNVGTGKCLGVSSSSPSSPLRLFECdSEDEL 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 55670424 189 QWFRYYENGEIVNakSGMCLDVEGSDGSGNVGIYR 223
Cdd:cd23385  77 QKWKCSKDGLLLL--KGLGLLLLYDKSGKNVVVSK 109

ricin B-type lectin domain, beta-trefoil fold, found in cytolethal distending toxin subunit A (CdtA) and similar proteins; Cytolethal distending toxins (CDTs) are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CDT is a heterotrimer consisting of the three subunits, CdtA, CdtB, and CdtC. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of nuclease CdtB. CdtA 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 sugar-binding pocket.

Pssm-ID: 469576 Cd Length: 147 Bit Score: 39.58 E-value: 8.13e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  45 QIIICGDGT--IRNEARNYCFTPDGSGnanVMSSPCTlypEIPSSQRWrqgrRKTFTDNGgieqvATEIINLASGKCLDI 122
Cdd:cd23414  47 QIIYNPDGTvsFRNVYTGTCLTAYGNG---VIHNPCD---SNNPAQKF----ELIPTDNG-----AVQIKNVSTGKCLQT 111

                        90       100
                ....*....|....*....|....*....
gi 55670424 123 EGSDGTGDIGVY--DC-----QNLDDQYF 144
Cdd:cd23414 112 PFGSRTYAYSIYltKCptpgeVNLDQQWY 140

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467339 Cd Length: 128 Bit Score: 38.92 E-value: 1.07e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 102 GGIEQVAteiinlASGKCLDIEGSDGTGDIGVYDCQNLDD-----QYFYVRsrgpelFYGRLRNEKSDLCLDVEGSdgkg 176
Cdd:cd23461   4 GVIQSVA------FPNLCLDILGRSHGGPPVLAKCSSNKSmpgtfQNFSLT------FHRQIKHGTSDDCLEVRGN---- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55670424 177 NVLMYSCEDNL-DQWFRY-YENGEIVNAKSG-MCLdvEGSDGSGNVGIYRCD-DLRDQMWS 233
Cdd:cd23461  68 NVRLSRCHYQGgNQYWKYdYETHQLINGGQNnKCL--EADVESLKITLSICDsDNVEQKWK 126

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 38.67 E-value: 1.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424    11 GELRSFKSKQCVDIVGNQGSGNIATYDCDGLSDQQ--IIICGDGTIRNEARNYCFTPDGSGNAN---VMSSPCTLYPeip 85
Cdd:pfam00652  46 GTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQrwRYDEDGTQIRNPQSGKCLDVSGAGTSNgkvILWTCDSGNP--- 122


                  ....*
gi 55670424    86 sSQRW 90
Cdd:pfam00652 123 -NQQW 126

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-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. One member of this family, MRC1, is missing the gamma subdomain.

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 38.73 E-value: 1.26e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 199 IVNAKSGMCLDVegSDGSGNVGIYRCDDL-RDQMWSRpnaycNGDYcSFLNKESNKCLDVSGDQGTGDVGTWQCDGLpDQ 277
Cdd:cd23385   5 IYNEDLGKCLAA--RSSSSKVSLSTCNPNsPNQQWKW-----TSGH-RLFNVGTGKCLGVSSSSPSSPLRLFECDSE-DE 75


                ....*
gi 55670424 278 RFKWV 282
Cdd:cd23385  76 LQKWK 80

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: 40.15 E-value: 1.33e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424   11 GELRSfKSKQCVDIVGNQGSGN-IATYDCDGLSDQQIIICGDGTIRneARNYCF-TPDGSGN--ANVMSSPCTLYPeips 86
Cdd:NF035930 120 REIRG-KGGLCLDVSGGLRPGNgLIVYNCNGGENQRFTWGRGGELR--VGDLCLdVADGNTRdgARVIAWSCSGGP---- 192

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55670424   87 SQRWRQgrrktftdNGGieqvatEIINLASGKCLDIEG 124
Cdd:NF035930 193 NQRWRW--------RGG------QIRSRLSGKCLDIEG 216

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: 37.70 E-value: 2.77e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55670424  21 CVDIVGNqGSGN---IATYDCDGLSDQQIIICGDGTIRNEARNYCFTPDGSGNANvmSSPCTLYPEIPS-SQRWR 91
Cdd:cd23451  54 CLDVSGG-GTANgtlVQLWDCNGTGAQKWVPRADGTLYNPQSGKCLDAPGGSTTD--GTQLQLYTCNGTaAQQWT 125

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: 36.98 E-value: 5.13e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424  86 SSQRWRqgrrktFTDNGGIEQvatEIINLASGKCLDIEGS---DGtGDIGVYDCQNLDDQYFYVRSRGPElfYGRLRNEK 162
Cdd:cd23446  36 TSQQWY------FTDVGGGYY---KIVNRNSGKALDVNGAstaDG-AAIIQWTSNGGDNQQWQIVDTGDG--YYKIVNRN 103

                        90       100
                ....*....|....*....|...
gi 55670424 163 SDLCLDVEG---SDGkGNVLMYS 182
Cdd:cd23446 104 SGKLLDVNGwstADG-ADIIQWS 125

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the 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 bears a potential sugar binding site.

Pssm-ID: 467339 Cd Length: 128 Bit Score: 37.00 E-value: 5.42e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55670424 163 SDLCLDVEGSDGKGNVLMYSCEDNLD-----QWFRYYENGEIVNAKSGMCLDVEGSdgsgNVGIYRCDDLR-DQMWSrpn 236
Cdd:cd23461  12 PNLCLDILGRSHGGPPVLAKCSSNKSmpgtfQNFSLTFHRQIKHGTSDDCLEVRGN----NVRLSRCHYQGgNQYWK--- 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 55670424 237 aYcngDYCSFL---NKESNKCL--DVSGDQGTGDVgtwqCDglPDQRF-KWVFD 284
Cdd:cd23461  85 -Y---DYETHQlinGGQNNKCLeaDVESLKITLSI----CD--SDNVEqKWKWG 128

first ricin B-type lectin domain, beta-trefoil fold, found in Abrus precatorius abrin, agglutinin-I and similar proteins; This subfamily includes Abrus precatorius abrin (ABR) and agglutinin-I (AAG), which share a high degree of sequence similarity and belong to the type II ribosome-inactivating protein (RIP) family. Type II RIPs inhibit protein synthesis in eukaryotic cells and can also induce apoptosis. They are two-polypeptide proteins with a toxic A chain and a lectin-like B chain linked by a disulfide bond. The A chain of abrin and agglutinin-I is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. Agglutinin-I is less toxic than abrin. The B chain is a galactose-specific lectin that facilitates the binding to the cell membrane that precedes endocytosis. The B-chain 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. This model corresponds to the first ricin B-type lectin domain.

Pssm-ID: 467362 Cd Length: 137 Bit Score: 36.92 E-value: 7.32e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55670424 166 CLDVEGSDGKGNVLMYSCEDNLDQ--WFRYYENGEIVNAKSGMCLDVEGSDGSGNVGIYRCDDLRDQMWSRPN 236
Cdd:cd23484  64 CLTTYGYAPGNYVMIYDCTSAVAEatYWEIWDNGTIINPKSALVLSAESSSMGGTLTVQTNEYLMRQGWRTGN 136

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 35.43 E-value: 8.72e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 55670424   230 QMWSRPNAYCNGDYcSFLNKESNKCLDVSGDQGTG--DVGTWQCDGLPDQRFK 280
Cdd:pfam14200   3 QQWRFGGTVGDGYY-TIVNVASGKYLDVAGGSTANgaNVQQWTDNGNDNQQWR 54