NCBI Conserved Domain Search

second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; This subfamily includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricin. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is fruit specific SNAI. It functions as fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). 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. The model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467368 [Multi-domain] Cd Length: 125 Bit Score: 237.74 E-value: 2.06e-80

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      131 PIVASIVGYKEMCLQSNGENNGVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWF 210
Cdd:cd23490   1 PIVTFIVGYKEMCLQANGENNGVWMEDCVVTSVQQQWALYGDGTIRVNSDRSLCVTSNGYNSKDLIIILKCQGLPNQRWV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
3CA6_A      211 FNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPNQQWVTQV 255
Cdd:cd23490  81 FNTDGTIVNPNSKLVMDVKQSDVSLREIILFPPTGNPNQQWITQT 125

first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; The family includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricins. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is a Neu5Ac(alpha2-6)Gal/GalNAc-specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is a fruit-specific SNAI. It functions as a fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). 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: 467361 [Multi-domain] Cd Length: 127 Bit Score: 235.48 E-value: 1.47e-79

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        2 SFTRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAIK 81
Cdd:cd23483   1 EFTRRISGRDGLCVDVRNGYDTDGTPVQLWPCGTQRNQQWTFDTDGTIRSMGKCMTANGLNSGSYVMIYNCSTAAPEATK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
3CA6_A       82 WEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNN 128
Cdd:cd23483  81 WVVSIDGTITNPSSGLVLTAPRAASGTTLLLENNIHAASQGWTVGND 127

first 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 first ricin B-type lectin domain. Members of this subfamily 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: 467321 [Multi-domain] Cd Length: 123 Bit Score: 203.68 E-value: 4.69e-67

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        3 FTRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQ-RNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAIK 81
Cdd:cd23443   1 PTVRIVGRDGLCVDVKDGYYSDGNPVILWPCKSQdANQLWTFKRDGTIRSNGKCLTTNGYSPGSYVVIYDCSTAVAEATK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3CA6_A       82 WEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWT 124
Cdd:cd23443  81 WEVSDDGTIINPASGLVLTADSGTSGTTLTVETNIYASSQGWR 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: 185.17 E-value: 8.37e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      131 PIVASIVGYKEMCLQSNGENNgVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWF 210
Cdd:cd23444   1 PIVTSIVGLNDLCLQANGGNN-VWLEECVSNKKEQKWALYPDGTIRPNQNRNLCLTSSSDVQGSIIVVLSCSGSSGQRWV 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
3CA6_A      211 FNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPNQQW 251
Cdd:cd23444  80 FRNDGTILNLYTGLVMDVKESDPSLKQIILWPATGGPNQQW 120

first ricin B-type lectin domain, beta-trefoil fold, found in Ricinus communis ricin, agglutinin and similar proteins; This subfamily includes ricin and agglutinin (RCA), which are toxic lectins from Ricinus communis. Ricin is highly toxic to animal cells, and to a lesser extent to plant cells. As a prototype AB toxin, ricin is composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. Ricin A chain acts as an RNA N-glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. Ricin B functions as a lectin that mediates cell binding via different oligosaccharide residues on the cell surface, including N-acetylglucosamine and galactose residues found in glycolipids and glycoproteins. It is also responsible for cell agglutination. Agglutinin shows high sequence similarity with ricin. It is only a weak toxin but a strong hemagglutinin. By contrast, ricin is a potent toxin but a weak hemagglutinin. Like ricin, agglutinin consists of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The B chain of ricin and agglutinin 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: 467358 [Multi-domain] Cd Length: 137 Bit Score: 132.88 E-value: 3.54e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        7 IVGRDGLCVDVRNGYDTDGTPLQLWPC--GTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAIKWEV 84
Cdd:cd23480  13 IVGRNGLCVDVRDEEFFDGNAIQLWPCksNTDANQLWTLKKDNTIRSNGKCLTISGSSPGQQVMIYDCNTAATDATRWQI 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3CA6_A       85 PIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNN 128
Cdd:cd23480  93 WDNGTIINPRSGLVLAATSGNSGTKLTVQTNIYAVSQGWLPTNN 136

first ricin B-type lectin domain, beta-trefoil fold, found in bitter gourd (Momordica charantia) seed lectin (BGSL) and similar proteins; 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. BGSL is a non-toxic four-chain type II RIP resulting from covalent association through a disulfide bridge between two identical copies of a two-chain unit. The two-chain unit consists of a catalytic A-chain and a lectin B-chain. The catalytic A-chain cannot firmly bind adenine due to the substitution of an aromatic residue involved in ensuring the proper orientation of the base in toxic RIPs, by a glycyl residue. BGSL is a galactose-specific lectin containing two ricin B-type lectin domains in its B-chain. 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. This model corresponds to the first ricin B-type lectin domain. In BGSL, sugar does not bind at the 2gamma site. Its 1alpha site binds sugar, which is similar to that in snake gourd (Trichosanthes anguina) seed lectin (SGSL).

Pssm-ID: 467359 Cd Length: 132 Bit Score: 127.20 E-value: 6.61e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        4 TRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAiKWE 83
Cdd:cd23481   9 TTRISGRDGLCVDVYGALTADGSRVILYPCGQQQNQQWTFYPDNTIRSLGKCLATSALSSGSNVVITNCDYLRYDD-GWM 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3CA6_A       84 VPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTN 127
Cdd:cd23481  88 VSSSGTMMNKSSHLVLTANAATSRTNLTGENNVFAAKQAWRIGN 131

second ricin B-type lectin domain, beta-trefoil fold, found in Cinnamomum camphora type II ribosome-inactivating protein (RIP) cinnamomin and similar proteins; RIPs are a group of ribotoxins that inhibit mammalian protein biosynthesis by irreversible inactivation of their 60S ribosomal subunit. Type II RIPs in plant cells comprise part of the plant's defense system towards animals. Cinnamomin is a type II RIP isolated from Cinnamomum camphora seeds. It shows inhibitory effects on cultured carcinoma cells and on the larva of the bollworm and mosquito. There are three cinnamomin isoforms (I, II, III). They are composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. The A-chain displays specific activity as an RNA N-glycosidase that blocks protein synthesis, whereas the B-chain is responsible for the binding to galactose-terminated receptors on cell membranes. 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. The model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467371 Cd Length: 125 Bit Score: 125.56 E-value: 1.94e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      130 KPIVASIVGYKEMCLQSNGEnnGVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVT-TNGYNSKDLIIILKCQ-GLPSQ 207
Cdd:cd23493   1 EPFVTSIVGFNDLCMQANGD--AMWVVECESSKAEQKWALYPDGSIRPHQDRDRCLTsTDNHSQGSIIIISSCSpGSEGQ 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
3CA6_A      208 RWFFNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPNQQWV 252
Cdd:cd23493  79 RWVFMNDGTILNLKNGLVMDVKGSNPSLHQIIIWPATGKPNQKWL 123

second 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 composed of 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. The model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467369 Cd Length: 124 Bit Score: 120.14 E-value: 2.28e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      131 PIVASIVGYKEMCLQSNGENngVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKC-QGLPSQRW 209
Cdd:cd23491   1 PFVTSISGYSDLCMQAQGSN--VWLAVCDINKKEQQWALYTDGSIRSVQNTNNCLTSKDHKQGSTIVLMGCsNGWASQRW 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3CA6_A      210 FFNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPNQQWVT 253
Cdd:cd23491  79 VFKNDGSIYNLYDDMVMDVKSSDPSLKQIILWPYTGKPNQIWLT 122

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: 119.35 E-value: 6.66e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        4 TRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQ--RNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAIK 81
Cdd:cd23484  11 TVRIGGRDGMCVDVYDNGYHNGNRIIMWKCKDRleENQLWTLKSDKTIRSNGKCLTTYGYAPGNYVMIYDCTSAVAEATY 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
3CA6_A       82 WEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNN 128
Cdd:cd23484  91 WEIWDNGTIINPKSALVLSAESSSMGGTLTVQTNEYLMRQGWRTGNN 137

first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; 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. SGSL is a non-toxic three-chain type II RIP consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. 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. This model corresponds to the first ricin B-type lectin domain.

Pssm-ID: 467360 Cd Length: 135 Bit Score: 119.47 E-value: 6.81e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        4 TRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAIKWE 83
Cdd:cd23482   9 TTRISGRDALCVDVAGALTSDGSRLILYPCGQQVNQKWTFHSDGTVRSLGKCLATNNSKFGNLVVIYDCSKLAAEDISWD 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
3CA6_A       84 VPIDGSIINPS-SGLVMTAPRAASRTILLLEDNIYAASQGWTVTNNV 129
Cdd:cd23482  89 VSVGGTIMNPNyEDLALTSNKATRSTNLTMEVNTYSASQGWRVGNYV 135

first ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of beta-galactoside-specific lectins and similar proteins; This subfamily includes Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs), which inhibit growth of the human tumor cell line Molt4. They contain A and B chains. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). 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: 467363 Cd Length: 134 Bit Score: 118.55 E-value: 1.16e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        4 TRNIVGRDGLCVDVRNGYDTDGTPLQLWPC--GTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAIK 81
Cdd:cd23485   7 TVRIVGRNGMTVDVRDDDFHDGNQIQLWPSksNNDPNQLWTIKRDGTIRSNGSCLTTYGYTAGVYVMIFDCNTAVREATI 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
3CA6_A       82 WEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNN 128
Cdd:cd23485  87 WQIWGNGTIINPRSNLVLAASSGIKGTTLTVQTLDYTLGQGWLAGND 133

second ricin B-type lectin domain, beta-trefoil fold, found in Viscum album B chain of beta-galactoside-specific lectins and similar proteins; This subfamily includes Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs), which inhibit growth of the human tumor cell line Molt4. They contain A and B chains. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). 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. The model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467370 Cd Length: 124 Bit Score: 117.35 E-value: 2.98e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      131 PIVASIVGYKEMCLQSNGenNGVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQ-GLPSQRW 209
Cdd:cd23492   1 PREVTIYGFRDLCMESNG--GSVWVETCVSSQENQRWALYGDGSIRPKQNQSQCLTNGRDSVSTVINIVSCSaGSSGQRW 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3CA6_A      210 FFNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPNQQWV 252
Cdd:cd23492  79 VFTNEGAILNLKNGLAMDVAQANPSLRRIIIYPATGNPNQMWL 121

second ricin B-type lectin domain, beta-trefoil fold, found in bitter gourd (Momordica charantia) seed lectin (BGSL) and similar proteins; 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. BGSL is a non-toxic four-chain type II RIPs resulting from covalent association through a disulfide bridge between two identical copies of a two-chain unit. The two-chain unit consists of a catalytic A-chain and a lectin B-chain. The catalytic A-chain cannot firmly bind adenine due to the substitution of an aromatic residue involved in ensuring the proper orientation of the base in toxic RIPs, by a glycyl residue. BGSL is a galactose-specific lectin containing two ricin B-type lectin domains in B-chain. The ricin B-type lectin domain shows 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 model corresponds to the second ricin B-type lectin domain. In BGSL, sugar does not bind at the 2gamma site. Its 1alpha site binds sugar, which is similar to that in snake gourd (Trichosanthes anguina) seed lectin (SGSL).

Pssm-ID: 467366 Cd Length: 126 Bit Score: 117.16 E-value: 3.77e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      131 PIVASIVGYKEMCLQSNGENNGVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWF 210
Cdd:cd23488   1 PIVTTIIGLRHMCLEATDNDTNVWLESCVKNKTKQYWALYSDDTIRVNNNRNLCVSSSTDSSSKLIVIRRCDGSINQRWV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
3CA6_A      211 FNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPN-QQW 251
Cdd:cd23488  81 FTPQGTISNPGYEAVMDVAQNDVYLKKIVLSSATDKGNgQQW 122

first ricin B-type lectin domain, beta-trefoil fold, found in Cinnamomum camphora type II ribosome-inactivating protein (RIP) cinnamomin and similar proteins; RIPs are a group of ribotoxins that inhibit mammalian protein biosynthesis by irreversible inactivation of their 60S ribosomal subunit. Type II RIPs in plant cells comprise part of the plant's defense system towards animals. Cinnamomin is a type II RIP isolated from Cinnamomum camphora seeds. It shows inhibitory effects on cultured carcinoma cells and on the larvae of bollworm and mosquito. There are three cinnamomin isoforms (I, II, III). They are composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. The A-chain displays specific activity as an RNA N-glycosidase that blocks protein synthesis, whereas the B-chain is responsible for the binding to galactose-terminated receptors on cell membranes. 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: 467364 Cd Length: 129 Bit Score: 115.62 E-value: 1.49e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        4 TRNIVGRDGLCVDVRNGYDTDGTPLQLWPC--GTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAIK 81
Cdd:cd23486   3 TVRISGRNGLCVDVRDGKYNNGNPIQLWPCkqNSDVNQLWTLRRDGTIRSNGKCLTTNGYSAGDYVMIYDCRTPVTAASI 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
3CA6_A       82 WEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNN 128
Cdd:cd23486  83 WQFWANGTIINPQSALVLSAESGNPRTTLTVQADIYASRQGWLAGNN 129

second ricin B-type lectin domain, beta-trefoil fold, found in Ricinus communis ricin, agglutinin and similar proteins; This subfamily includes ricin and agglutinin (RCA), toxic lectins from Ricinus communis. Ricin is highly toxic to animal cells, and to a lesser extent to plant cells. As a prototype AB toxin, ricin is composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. Ricin A chain acts as an RNA N-glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. Ricin B chain functions as a lectin that mediates cell binding via different oligosaccharide residues on the cell surface, including N-acetylglucosamine and galactose residues found on glycolipids and glycoproteins. It is also responsible for cell agglutination. Agglutinin shows high sequence similarity with ricin. It is only a weak toxin but a strong hemagglutinin. By contrast, ricin is a potent toxin but a weak hemagglutinin. Like ricin, agglutinin consists of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The B-chain of ricin and agglutinin 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 second ricin B-type lectin domain.

Pssm-ID: 467365 Cd Length: 124 Bit Score: 110.50 E-value: 1.13e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      131 PIVASIVGYKEMCLQSNgeNNGVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPS-QRW 209
Cdd:cd23487   1 PFVTTIVGLYGLCLQAN--SGKVWIEDCSSEKAEQQWALYADGSIRPQQNRDNCLTSDANIKETVVKILSCGPASSgQRW 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3CA6_A      210 FFNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPNQQWV 252
Cdd:cd23487  79 MFKNDGTILNLYNGLVLDVRASDPSLKQIILHPFHGDLNQIWL 121

second ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; 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. SGSL is a non-toxic three-chain type II RIPs consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. The ricin B-type lectin domain shows 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 model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467367 Cd Length: 128 Bit Score: 110.18 E-value: 2.12e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      131 PIVASIVGYKEMCLQSNGENNGVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVT--TNGYNSKDLIIILKCQGLPSQR 208
Cdd:cd23489   1 PIIGSIVGLDDMCLEATDGNTNMWLEECVPNQREQSWALYSDGTIRVDDNRELCVTasSSTYDNWKVITILNCDGSNNQR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
3CA6_A      209 WFFNSDGAIVNP-KSRLVMDVRASNVSLREIIIFPATGNPNQQWV 252
Cdd:cd23489  81 WVFLADGSISTPgNQRLAMDVARSDVDLKKIILHRPHGDLNQQWV 125

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

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 95.27 E-value: 7.83e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A         135 SIVGYKEMCLQSNGENNGVWMEDCEATSLQQQWALYGDRTIRVNSTrGLCVTTNGYNSkDLIIILKCQG-LPSQRWFFNS 213
Cdd:smart00458   1 IISGNTGKCLDVNGNKNPVGLFDCHGTGGNQLWKLTSDGAIRIKDT-DLCLTANGNTG-STVTLYSCDGtNDNQYWEVNK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
3CA6_A         214 DGAIVNPKSRLVMDVRASNVSlREIIIFPATGNPNQQWVTQ 254
Cdd:smart00458  79 DGTIRNPDSGKCLDVKDGNTG-TKVILWTCSGNPNQKWIFE 118

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

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 91.80 E-value: 1.95e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A           7 IVGRDGLCVDVRNGydtdGTPLQLWPC-GTQRNQRWTFDSDDTIRSM--GKCMTANGlNNGSNIVIFNCSTAAENaIKWE 83
Cdd:smart00458   2 ISGNTGKCLDVNGN----KNPVGLFDChGTGGNQLWKLTSDGAIRIKdtDLCLTANG-NTGSTVTLYSCDGTNDN-QYWE 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
3CA6_A          84 VPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVT 126
Cdd:smart00458  76 VNKDGTIRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 118

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 89.90 E-value: 1.30e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        142 MCLQSNGE---NNGVWMEDCEATSLQQQWALYGDRTIRVNSTrGLCVTTNGYNSKDLIIILKC-QGLPSQRWFFNSDGA- 216
Cdd:pfam00652  12 KCLDVPGGssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSVAS-DLCLDVGSTADGAKVVLWPChPGNGNQRWRYDEDGTq 90

                          90       100       110
                  ....*....|....*....|....*....|....*.
3CA6_A        217 IVNPKSRLVMDVRASNVSLREIII-FPATGNPNQQW 251
Cdd:pfam00652  91 IRNPQSGKCLDVSGAGTSNGKVILwTCDSGNPNQQW 126

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 87.59 E-value: 8.68e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A          3 FTRNIVGR-DGLCVDVRNGyDTDGTPLQLWPC-GTQRNQRWTFDSDDTIRSM--GKCMTANGLNNGSNIVIFNCSTAAEN 78
Cdd:pfam00652   1 ATGRIRNRaSGKCLDVPGG-SSAGGPVGLYPChGSNGNQLWTLTGDGTIRSVasDLCLDVGSTADGAKVVLWPCHPGNGN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
3CA6_A         79 aIKWEVPIDGS-IINPSSGLVMTAPRA--ASRTILLLEDNIYAASQGW 123
Cdd:pfam00652  80 -QRWRYDEDGTqIRNPQSGKCLDVSGAgtSNGKVILWTCDSGNPNQQW 126

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

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 87.00 E-value: 1.36e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCM--TANGLNNGSNIVIFNCSTAAenAIKWEVPIDGS 89
Cdd:cd23451  11 GKCLDVPGSSTADGNPVQIYTCNGTAAQKWTLGTDGTLRVLGKCLdvSGGGTANGTLVQLWDCNGTG--AQKWVPRADGT 88

                        90       100       110
                ....*....|....*....|....*....|....*..
3CA6_A       90 IINPSSGLVMTAPRAASR--TILLLEDNIYAASQGWT 124
Cdd:cd23451  89 LYNPQSGKCLDAPGGSTTdgTQLQLYTCNGTAAQQWT 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: 84.32 E-value: 1.43e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        9 GRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRS-MGKCMTA--NGLNNGSNIVIFNCSTAAENaiKWEVP 85
Cdd:cd23418  11 YGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELRVgGDKCLDAagGGTTNGTPVVIWPCNGGANQ--KWRFN 88

                        90       100
                ....*....|....*....|..
3CA6_A       86 IDGSIINPSSGLVMTAPRAASR 107
Cdd:cd23418  89 SDGTIRNVNSGLCLDVAGGGTA 110

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: 77.56 E-value: 4.55e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        7 IVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCMTA--NGLNNGSNIVIFNCSTaaENAIKWEV 84
Cdd:cd23452   6 IIGLANKCIDVPNSSTTDGAPLQLWDCNGTNAQKWTFASDGTLRALGKCLDVawGGTDNGTAVQLWTCSG--NPAQQFVL 83


                ....*....
3CA6_A       85 PIDGSIINP 93
Cdd:cd23452  84 SGAGDLVNP 92

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: 74.71 E-value: 7.58e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDD----TIRSM--GKCMTANG--LNNGSNIVIFNCSTAAENaiKWE 83
Cdd:cd00161  11 GKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVGdgyyTIRNVasGKCLDVAGgsTANGANVQQWTCNGGDNQ--QWR 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
3CA6_A       84 V----PIDGSIINPSSGLVMTAPRA--ASRTILLLEDNIYAASQGW 123
Cdd:cd00161  89 LepvgDGYYRIVNKHSGKCLDVSGGstANGANVQQWTCNGGANQQW 134

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: 62.29 E-value: 2.52e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        6 NIVGRDGLCVDVrngydTDGTPLQLWPC-GTQRNQRWTFDSDDTIR---SMGKCMTANGLNNGSNIVIFNCSTAAenAIK 81
Cdd:cd23444   5 SIVGLNDLCLQA-----NGGNNVWLEECvSNKKEQKWALYPDGTIRpnqNRNLCLTSSSDVQGSIIVVLSCSGSS--GQR 77

                        90
                ....*....|....*...
3CA6_A       82 WEVPIDGSIINPSSGLVM 99
Cdd:cd23444  78 WVFRNDGTILNLYTGLVM 95

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: 61.60 E-value: 4.52e-12

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3CA6_A        4 TRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRS--MGKCMTA--NGLNNGSNIVIFNCSTAA 76
Cdd:cd23418  48 AGELRVGGDKCLDAAGGGTTNGTPVVIWPCNGGANQKWRFNSDGTIRNvnSGLCLDVagGGTANGTRLILWSCNGGS 124

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: 60.83 E-value: 9.37e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      155 MEDCEATSlQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWFFNSDGAIVNPKSRLVMDV-RASNV 233
Cdd:cd23418  32 LWDCHGGA-NQQFTFTSAGELRVGGDKCLDAAGGGTTNGTPVVIWPCNGGANQKWRFNSDGTIRNVNSGLCLDVaGGGTA 110

                        90
                ....*....|....*...
3CA6_A      234 SLREIIIFPATGNPNQQW 251
Cdd:cd23418 111 NGTRLILWSCNGGSNQRW 128

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: 58.14 E-value: 8.56e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        9 GRDGLCVDVRNGyDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSM---GKCMTANGLN-NGSNIVIFNCSTAAENAikWEv 84
Cdd:cd23456   8 QASGLCLDVSGG-ATNGANVVVYDCNNSNSQKWYYDATGRLHSKanpGKCLDAGGENsNGANVVLWACNDSANQR--WD- 83

                        90
                ....*....|....*....
3CA6_A       85 pIDGSIINP--SSGLVMTA 101
Cdd:cd23456  84 -FDGNFIRSrnNTNLALDA 101

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: 56.61 E-value: 3.66e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      142 MCLQ----SNGENNGVWMEDCEATSlQQQWALY----GDRTIRVNSTrGLCVTTNGYNSKD--LIIILKCQGLPSQRWFF 211
Cdd:cd00161  12 KCLDvaggSTANGAPVQQWTCNGGA-NQQWTLTpvgdGYYTIRNVAS-GKCLDVAGGSTANgaNVQQWTCNGGDNQQWRL 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
3CA6_A      212 ----NSDGAIVNPKSRLVMDVR-ASNVSLREIIIFPATGNPNQQW 251
Cdd:cd00161  90 epvgDGYYRIVNKHSGKCLDVSgGSTANGANVQQWTCNGGANQQW 134

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: 56.18 E-value: 6.19e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      136 IVGYKEMCLQ--SNGENNG--VWMEDC-EATSLQQQWALYGDRTIRvnsTRGLCVTTNGYNSKDLIIILKCQGLPSQR-- 208
Cdd:cd23484  14 IGGRDGMCVDvyDNGYHNGnrIIMWKCkDRLEENQLWTLKSDKTIR---SNGKCLTTYGYAPGNYVMIYDCTSAVAEAty 90

                        90       100
                ....*....|....*....|....*
3CA6_A      209 WFFNSDGAIVNPKSRLVMDVRASNV 233
Cdd:cd23484  91 WEIWDNGTIINPKSALVLSAESSSM 115

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: 55.42 E-value: 6.94e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      150 NNGVWMEDCEATSlQQQWALYGDRTIRVnstRGLC--VTTNGYNSKDLIIILKCQGLPSQRWFFNSDGAIVNPKSRLVMD 227
Cdd:cd23451  24 GNPVQIYTCNGTA-AQKWTLGTDGTLRV---LGKCldVSGGGTANGTLVQLWDCNGTGAQKWVPRADGTLYNPQSGKCLD 99

                        90       100
                ....*....|....*....|....*
3CA6_A      228 V-RASNVSLREIIIFPATGNPNQQW 251
Cdd:cd23451 100 ApGGSTTDGTQLQLYTCNGTAAQQW 124

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. 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. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. 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: 467319 [Multi-domain] Cd Length: 122 Bit Score: 54.72 E-value: 1.15e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      140 KEMCLQSNGENN----GVWMEDCEATSLQQQWALYGDRTIRvnsTRGLCVTTNGYnSKDLIIILK-CQGLPSQRWFFnSD 214
Cdd:cd23441  11 GNLCLDSDEQLFqgpaLLILAPCSNSSDSQEWSFTKDGQLQ---TQGLCLTVDSS-SKDLPVVLEtCSDDPKQKWTR-TG 85

                        90       100       110
                ....*....|....*....|....*....|....*...
3CA6_A      215 GAIVNPKSRLVMDvrasNVSLREIIIFPA-TGNPNQQW 251
Cdd:cd23441  86 RQLVHSESGLCLD----SRKKKGLVVSPCrSGAPSQKW 119

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: 53.48 E-value: 4.53e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        6 NIVGRD-GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDT----IRSM--GKCMTANGLN--NGSNIVIFNCSTAA 76
Cdd:cd23458   4 RIRNRNsGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEIDNgyyrIKAShsGKCLDVAGGStaNGANIQQWDCVGGA 83

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

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 51.58 E-value: 2.22e-08

                        10        20        30
                ....*....|....*....|....*....|....*....
3CA6_A        6 NIVGR-DGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTF 43
Cdd:cd23418  92 TIRNVnSGLCLDVAGGGTANGTRLILWSCNGGSNQRWRR 130

first ricin B-type lectin domain, beta-trefoil fold, found in Cinnamomum camphora type II ribosome-inactivating protein (RIP) cinnamomin and similar proteins; RIPs are a group of ribotoxins that inhibit mammalian protein biosynthesis by irreversible inactivation of their 60S ribosomal subunit. Type II RIPs in plant cells comprise part of the plant's defense system towards animals. Cinnamomin is a type II RIP isolated from Cinnamomum camphora seeds. It shows inhibitory effects on cultured carcinoma cells and on the larvae of bollworm and mosquito. There are three cinnamomin isoforms (I, II, III). They are composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. The A-chain displays specific activity as an RNA N-glycosidase that blocks protein synthesis, whereas the B-chain is responsible for the binding to galactose-terminated receptors on cell membranes. 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: 467364 Cd Length: 129 Bit Score: 50.52 E-value: 4.69e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      150 NNG--VWMEDCEATS-LQQQWALYGDRTIRVNstrGLCVTTNGYNSKDLIIILKCQG--LPSQRWFFNSDGAIVNPKSRL 224
Cdd:cd23486  22 NNGnpIQLWPCKQNSdVNQLWTLRRDGTIRSN---GKCLTTNGYSAGDYVMIYDCRTpvTAASIWQFWANGTIINPQSAL 98


                ....*...
3CA6_A      225 VMDVRASN 232
Cdd:cd23486  99 VLSAESGN 106

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: 48.13 E-value: 2.95e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPC-GTQRNQRWTFDSDDTIRSMGKCMTANGLNNgsNIVIFNCSTAAENAiKWE-VPIDGS 89
Cdd:cd23462  14 KLCLDAPGRKKELNKPVGLYPChGQGGNQYWMLTKDGEIRRDDLCLDYAGGSG--DVTLYPCHGMKGNQ-FWIyDEETKQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       90 IINPSSGLvmtapraasrtillledniyaasqgwtvtnnvkpivasivgykemCLQSNGENNGVWMEDCEATSLQQQWAL 169
Cdd:cd23462  91 IVHGTSKK---------------------------------------------CLELSDDSSKLVMEPCNGSSPRQQWEF 125

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: 48.52 E-value: 3.01e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      177 VNSTRGLCVTTNGYNSKD--LIIILKCQGLPSQRWFFNSDGA----IVNPKSRLVMDVR-ASNVSLREIIIFPATGNPNQ 249
Cdd:cd00161   6 VNAASGKCLDVAGGSTANgaPVQQWTCNGGANQQWTLTPVGDgyytIRNVASGKCLDVAgGSTANGANVQQWTCNGGDNQ 85


                ..
3CA6_A      250 QW 251
Cdd:cd00161  86 QW 87

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: 47.75 E-value: 4.78e-07

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3CA6_A      139 YKEMCLQSNGENNGVWMEDCEATSLQQQWaLYGDRTIR-VNSTRGLCVTTNgyNSKDLIIILKCQG-LPSQRWFFN 212
Cdd:cd23462  54 RDDLCLDYAGGSGDVTLYPCHGMKGNQFW-IYDEETKQiVHGTSKKCLELS--DDSSKLVMEPCNGsSPRQQWEFE 126

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: 47.46 E-value: 5.58e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       10 RDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFD-SDDTIRSM---GKCMTANG--LNNGSNIVIFNCStAAENAIKWE 83
Cdd:cd23500   9 RSGKCLSAANGSQLNGSLVQLDACHASAGQLWYFDpKKGTIRSAldgNKCLAIPGgnTGNHTQLQLADCD-ASNPAQQFN 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
3CA6_A       84 VpiDGSIINP--SSGLVMTAPRAASRTILLLEDNIYAASQGW 123
Cdd:cd23500  88 Y--DGGVFRSrlNSNQVIDASGGSDGSELILYDYHGGSNQRW 127

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: 47.12 E-value: 6.84e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      134 ASIVGYKEMCLQSNGENN----GVWMEDCEATSlQQQWALYGDRTIRVNstrGLC--VTTNGYNSKDLIIILKCQGLPSQ 207
Cdd:cd23452   4 TPIIGLANKCIDVPNSSTtdgaPLQLWDCNGTN-AQKWTFASDGTLRAL---GKCldVAWGGTDNGTAVQLWTCSGNPAQ 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
3CA6_A      208 RWFFNSDGAIVNPKSRLVMDVRASNV-SLREIIIFPATGNPNQQW 251
Cdd:cd23452  80 QFVLSGAGDLVNPQANKCVDVSGGNSgNGTRLQLWECSGNANQKW 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: 46.97 E-value: 8.35e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      142 MCLQ-SNGENNG--VWMEDCEATSlQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIIL-KCQGLPSQRWFFNSDGAI 217
Cdd:cd23456  12 LCLDvSGGATNGanVVVYDCNNSN-SQKWYYDATGRLHSKANPGKCLDAGGENSNGANVVLwACNDSANQRWDFDGNFIR 90

                        90       100       110
                ....*....|....*....|....*....|....
3CA6_A      218 VNPKSRLVMDVRASNVSlrEIIIFPATGNPNQQW 251
Cdd:cd23456  91 SRNNTNLALDAYGSQGS--NVGLWQFHGGANQQW 122

Ricin-type beta-trefoil lectin domain-like;

Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 45.06 E-value: 1.87e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3CA6_A         12 GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDD----TIRSM--GKCMT-ANGLNNGSNIVIF 70
Cdd:pfam14200  24 GKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGdgyyRIVNKasGKVLDvAGSTANGTNVQQW 89

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. 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. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. 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: 467319 [Multi-domain] Cd Length: 122 Bit Score: 45.47 E-value: 2.20e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       13 LCVDVRNGYDTDGTPLQLWPCGTQRN-QRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENaiKWEVpIDGSII 91
Cdd:cd23441  13 LCLDSDEQLFQGPALLILAPCSNSSDsQEWSFTKDGQLQTQGLCLTVDSSSKDLPVVLETCSDDPKQ--KWTR-TGRQLV 89

                        90       100       110
                ....*....|....*....|....*....|...
3CA6_A       92 NPSSGLVMTAPRaaSRTILLLEDNIYAASQGWT 124
Cdd:cd23441  90 HSESGLCLDSRK--KKGLVVSPCRSGAPSQKWD 120

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: 45.39 E-value: 3.37e-06

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3CA6_A      141 EMCLQSNG-ENNGVWMEDCEATSLQ-QQWALYGDRTIrVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWFFN 212
Cdd:cd23459  59 ESCADVQGtEESKVILITCHGLEKFnQKWKHTKGGQI-VHLASGKCLDAEGLKSGDDVTLAKCDGSLSQKWTFE 131

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: 44.74 E-value: 4.46e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPCGTQR-NQRWTFDSDDTIR--SMGKCMTanglNNGSNIVIFNCSTAAEnAIKWEVPIDG 88
Cdd:cd23442  14 GYCADYIHGWRLAGGPVELSPCSGQNgNQLFEYTSDKEIRfgSLQLCLD----VRQEQVVLQNCTKEKT-SQKWDFQETG 88


                ....*...
3CA6_A       89 SIINPSSG 96
Cdd:cd23442  89 RIVHILSG 96

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: 44.29 E-value: 7.33e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      142 MCLQSNGEN----NGVWMEDCEATSLQQQWALYGDRTIRVNSTrgLCVTTNGYNsKDLIIILKCQG-LPSQRWFFNSDGA 216
Cdd:cd23440  15 LCLVAEDEVsqkgSLLVLRPCSRNDKKQLWYYTEDGELRLANL--LCLDSSETS-SDFPRLMKCHGsGGSQQWRFKKDNR 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
3CA6_A      217 IVNPKS----RLVMDVRASNVSLrEIiifpATGNPNQQWV 252
Cdd:cd23440  92 LYNPASgqclAASKNGTSGYVTM-DI----CSDSPSQKWV 126

ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin (MytiLec) and similar proteins; MytiLec is a D-galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types. It has hemagglutinating activity towards rabbit erythrocytes. It induces glycan-mediated cytotoxicity of human globotriaosylceramide-expressing lymphoma cells. The family also includes lectin from the mussel Mytilus californianus (MCL) and lectin from the sea mussel Crenomytilus grayanus (CGL). MCL is specific for binding D-galactose and N-Acetyl-d-galactosamine that contained carbohydrate moieties that were also inhibited by melibiose and raffinose. It can agglutinate all types of human erythrocytes, as well as rabbit red blood cells. CGL is specific for binding GalNAc/Gal-containing carbohydrate moieties. It displays antibacterial, antifungal, and antiviral activities. It also possesses anti-cancer activity through recognizing globotriose Gb3. Members of this family contain 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 harbor a sugar-binding pocket.

Pssm-ID: 467296 Cd Length: 132 Bit Score: 43.87 E-value: 1.07e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       10 RDGLCVDVRNGYD--TDGTPLQLWPCGTQRNQRWTFDSDDTIR--SMGKCMTANG--LNNGSNIVIF-NCStaaENAIKW 82
Cdd:cd23417   9 ASGKCIHPKGGSCnpPDGTKLVLYSDCSEDRMEFQLDSDGYLKhvCSGKCVCPKGgsADNGTKLVLHsNCG---DDRAKF 85

                        90
                ....*....|....*
3CA6_A       83 EVPIDGSIINPSSGL 97
Cdd:cd23417  86 RRTSKGSLQHKSSGK 100

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: 43.85 E-value: 1.09e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3CA6_A       10 RDGLCVDVRngyDTDGTPLQLWPCGT--QRNQRWTFDSDDTIRSM--GKCMTANGLNNGSNIVIFNCS 73
Cdd:cd23459  57 REESCADVQ---GTEESKVILITCHGleKFNQKWKHTKGGQIVHLasGKCLDAEGLKSGDDVTLAKCD 121

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: 43.84 E-value: 1.18e-05

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3CA6_A      141 EMCLQSNGENNGVWMEDCEATSLQQQWaLYGD--RTIR-VNStrGLCVTTNGYNSKDLIIILKCQGLPSQRWFFNS 213
Cdd:cd23433  55 DLCLDASRKGGPVKLEKCHGMGGNQEW-EYDKetKQIRhVNS--GLCLTAPNEDDPNEPVLRPCDGGPSQKWELEG 127

second ricin B-type lectin domain, beta-trefoil fold, found in Cinnamomum camphora type II ribosome-inactivating protein (RIP) cinnamomin and similar proteins; RIPs are a group of ribotoxins that inhibit mammalian protein biosynthesis by irreversible inactivation of their 60S ribosomal subunit. Type II RIPs in plant cells comprise part of the plant's defense system towards animals. Cinnamomin is a type II RIP isolated from Cinnamomum camphora seeds. It shows inhibitory effects on cultured carcinoma cells and on the larva of the bollworm and mosquito. There are three cinnamomin isoforms (I, II, III). They are composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. The A-chain displays specific activity as an RNA N-glycosidase that blocks protein synthesis, whereas the B-chain is responsible for the binding to galactose-terminated receptors on cell membranes. 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. The model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467371 Cd Length: 125 Bit Score: 42.36 E-value: 3.34e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        3 FTRNIVGRDGLCVDvrngydTDGTPLQLWPCGTQR-NQRWTFDSDDTIR---SMGKCMTA-NGLNNGSNIVIFNCSTAAE 77
Cdd:cd23493   3 FVTSIVGFNDLCMQ------ANGDAMWVVECESSKaEQKWALYPDGSIRphqDRDRCLTStDNHSQGSIIIISSCSPGSE 76

                        90       100
                ....*....|....*....|..
3CA6_A       78 NAiKWEVPIDGSIINPSSGLVM 99
Cdd:cd23493  77 GQ-RWVFMNDGTILNLKNGLVM 97

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: 42.05 E-value: 3.48e-05

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3CA6_A       32 PCGTQRNQRWTFDSDDTIRSM---GKCMTANGlnngSNIVIFNCSTAAENaiKWEVPIDGSIINPSSGLVMTA 101
Cdd:cd23425  27 TCDGSDSQIWQVRKSGILRNLsntGQCLTADG----ANVSLSPCDTSTSQ--NWSYEISGNLVNKKTGLCLTE 93

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: 43.62 E-value: 4.27e-05

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
3CA6_A        12 GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFdSDDTIRSM--GKCM 56
Cdd:NF035930 167 DLCLDVADGNTRDGARVIAWSCSGGPNQRWRW-RGGQIRSRlsGKCL 212

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

Pssm-ID: 467333 [Multi-domain] Cd Length: 131 Bit Score: 41.93 E-value: 4.78e-05

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
3CA6_A        1 TSFTRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTF 43
Cdd:cd23455  89 GGYQIQPVDDPDLVLDLAGSNDEDGTPVILYNNDGGDNQKWYF 131

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: 41.90 E-value: 5.06e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGydTDGTPLQLWPC-GTQRNQRWTFDSDDTIRSMGKCMTANGlnNGSNIVIFNCStaAENAIKWE-VPIDGS 89
Cdd:cd23437  14 GLCLDTMGH--QNGGPVGLYPChGMGGNQLFRLNEAGQLAVGEQCLTASG--SGGKVKLRKCN--LGETGKWEyDEATGQ 87

                        90       100       110
                ....*....|....*....|....*....|....*...
3CA6_A       90 IINPSSGLVMTAPRAASRTILLLEDNIyAASQGWTVTN 127
Cdd:cd23437  88 IRHKGTGKCLDLNEGTNKLILQPCDSS-SPSQKWEFNE 124

first ricin B-type lectin domain, beta-trefoil fold, found in bitter gourd (Momordica charantia) seed lectin (BGSL) and similar proteins; 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. BGSL is a non-toxic four-chain type II RIP resulting from covalent association through a disulfide bridge between two identical copies of a two-chain unit. The two-chain unit consists of a catalytic A-chain and a lectin B-chain. The catalytic A-chain cannot firmly bind adenine due to the substitution of an aromatic residue involved in ensuring the proper orientation of the base in toxic RIPs, by a glycyl residue. BGSL is a galactose-specific lectin containing two ricin B-type lectin domains in its B-chain. 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. This model corresponds to the first ricin B-type lectin domain. In BGSL, sugar does not bind at the 2gamma site. Its 1alpha site binds sugar, which is similar to that in snake gourd (Trichosanthes anguina) seed lectin (SGSL).

Pssm-ID: 467359 Cd Length: 132 Bit Score: 42.07 E-value: 5.07e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3CA6_A      165 QQWALYGDRTIRvnsTRGLCVTTNGYNSKDLIIILKCQGLP-SQRWFFNSDGAIVNPKSRLVMDVRAS 231
Cdd:cd23481  44 QQWTFYPDNTIR---SLGKCLATSALSSGSNVVITNCDYLRyDDGWMVSSSGTMMNKSSHLVLTANAA 108

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: 41.27 E-value: 7.70e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGYDTDGTPlQLWPC-GTQRNQRWTFDSDDTIRSMGKCMTAnglNNGSNIVIFNCSTAAENAIkWEV-PIDGS 89
Cdd:cd23460  11 GLCLDWAGESNGDKTV-ALKPChGGGGNQFWMYTGDGQIRQDHLCLTA---DEGNKVTLRECADQLPSQE-WSYdEKTGT 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       90 IINPSSGLvmtapraasrtillledniyaasqgwtvtnnvkpivasivgykemCLQSNGENNGVWMEDCEATSLQQQWAL 169
Cdd:cd23460  86 IRHRSTGL---------------------------------------------CLTLDANNDVVILKECDSNSLWQKWIF 120

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: 41.16 E-value: 8.58e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      140 KEMCLQSNGENN----GVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSkdlIIILKCQG-----LPSQRWF 210
Cdd:cd23435  12 SELCLDVNNPNGqggkPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHASGSDE---VILQHCTSkgkdvPPEQKWL 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
3CA6_A      211 FNSDGAIVNPKSRLVMDVRASNVSLREIIifpaTGNPNQQWV 252
Cdd:cd23435  89 FTQDGTIRNPASGLCLHASGYKVLLRTCN----PSDDSQKWT 126

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: 41.16 E-value: 1.03e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPC-GTQRNQRWTFDSDDTIR-SMGK--CMTANGLNNgsnIVIFNCSTAAENA---IKWEV 84
Cdd:cd23435  13 ELCLDVNNPNGQGGKPVIMYGChGLGGNQYFEYTSKGEIRhNIGKelCLHASGSDE---VILQHCTSKGKDVppeQKWLF 89

                        90
                ....*....|....*..
3CA6_A       85 PIDGSIINPSSGLVMTA 101
Cdd:cd23435  90 TQDGTIRNPASGLCLHA 106

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: 41.15 E-value: 1.09e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       13 LCVDVRNGYDTDGTPLQLWPC--GTQRNQRWTFDSDDTIRSMGKCMTANGlNNGSNIVIFNCSTAAENAIKWEVPIDGSI 90
Cdd:cd23459  17 LCLDTLQRDEDKGYNLGLYPCqgGLSSNQLFSLSKKGELRREESCADVQG-TEESKVILITCHGLEKFNQKWKHTKGGQI 95

                        90       100       110
                ....*....|....*....|....*....|....
3CA6_A       91 INPSSGLVMTAPRAASRTILLLEDNIYAASQGWT 124
Cdd:cd23459  96 VHLASGKCLDAEGLKSGDDVTLAKCDGSLSQKWT 129

second ricin B-type lectin domain, beta-trefoil fold, found in Ricinus communis ricin, agglutinin and similar proteins; This subfamily includes ricin and agglutinin (RCA), toxic lectins from Ricinus communis. Ricin is highly toxic to animal cells, and to a lesser extent to plant cells. As a prototype AB toxin, ricin is composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. Ricin A chain acts as an RNA N-glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. Ricin B chain functions as a lectin that mediates cell binding via different oligosaccharide residues on the cell surface, including N-acetylglucosamine and galactose residues found on glycolipids and glycoproteins. It is also responsible for cell agglutination. Agglutinin shows high sequence similarity with ricin. It is only a weak toxin but a strong hemagglutinin. By contrast, ricin is a potent toxin but a weak hemagglutinin. Like ricin, agglutinin consists of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The B-chain of ricin and agglutinin 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 second ricin B-type lectin domain.

Pssm-ID: 467365 Cd Length: 124 Bit Score: 40.78 E-value: 1.12e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        3 FTRNIVGRDGLCVDVRNGydtdgtplQLW--PCGTQR-NQRWTFDSDDTIR---SMGKCMTANGLNNGSNIVIFNCSTAA 76
Cdd:cd23487   2 FVTTIVGLYGLCLQANSG--------KVWieDCSSEKaEQQWALYADGSIRpqqNRDNCLTSDANIKETVVKILSCGPAS 73

                        90       100
                ....*....|....*....|....*...
3CA6_A       77 ENAiKWEVPIDGSIINPSSGLVMTAPRA 104
Cdd:cd23487  74 SGQ-RWMFKNDGTILNLYNGLVLDVRAS 100

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: 40.66 E-value: 1.23e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      140 KEMCLQSNGENNGVWMEDCEATSLQQQWALYGDRTIRvNSTRGLCVTTNGYNSKDLIIILKC-QGLPSQRWFFNSDG--A 216
Cdd:cd23385  10 LGKCLAARSSSSKVSLSTCNPNSPNQQWKWTSGHRLF-NVGTGKCLGVSSSSPSSPLRLFECdSEDELQKWKCSKDGllL 88

                        90       100       110
                ....*....|....*....|....*....|....*..
3CA6_A      217 IVNPKSRLVMDVRASNVSLREIIifpatgNPNQQWVT 253
Cdd:cd23385  89 LKGLGLLLLYDKSGKNVVVSKGS------GLSSRWKI 119

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: 40.77 E-value: 1.25e-04

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTF-DSDDTI-----RSMGKCMTANGLN--NGSNIVIFNCST 74
Cdd:cd23458  58 GKCLDVAGGSTANGANIQQWDCVGGANQQWKLqDLGNGYfelkaRHSGKCLDVAGGStaNGASIQQWTCNG 128

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: 40.18 E-value: 2.22e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      140 KEMCLQSNGENNG---VWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVttngYNSKDLIIILKCQ-------GLPSQRW 209
Cdd:cd23468  13 KELCLDVGENNHGgkpLIMYNCHGLGGNQYFEYSTHHEIRHNIQKELCL----HGSQGSVQLKECTykgrntaVLPEEKW 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
3CA6_A      210 FFNSDGAIVNPKSRLVMDVRASNVSLreiiifpATGNPN---QQWV 252
Cdd:cd23468  89 ELQKDQLLYNPALNMCLSANGENPSL-------VPCNPSdpfQQWI 127

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: 39.37 E-value: 4.42e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      145 QSNGENNGVWMEDCEATSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKD--LIIILKCQGL-PSQRWffNSDGAIVNPK 221
Cdd:cd23500  19 GSQLNGSLVQLDACHASAGQLWYFDPKKGTIRSALDGNKCLAIPGGNTGNhtQLQLADCDASnPAQQF--NYDGGVFRSR 96

                        90       100       110
                ....*....|....*....|....*....|..
3CA6_A      222 --SRLVMDVRASNVSlREIIIFPATGNPNQQW 251
Cdd:cd23500  97 lnSNQVIDASGGSDG-SELILYDYHGGSNQRW 127

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: 39.22 E-value: 4.93e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      178 NSTRGLCVT----TNGYNSKDLIIILKCQGLPSQRWFFNsDGAIVNPKSRLVMDVRA-SNVSLREIIIFPATGNP---NQ 249
Cdd:cd23454   7 SSSNGLVLDvehgSLKSGAKVVLAPLKTKDYESQLWRYD-DGYLVNKASGLVLDIQGgVVKSGTRLVQSPKKPSKdanNQ 85


                ..
3CA6_A      250 QW 251
Cdd:cd23454  86 RW 87

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: 39.25 E-value: 5.12e-04

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
3CA6_A        5 RNIvgRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRS 51
Cdd:cd23416  58 QNV--RSGTYLDLAGGSSANGTAIVGWQSTNNPNQQWVIKPANGGTY 102

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: 38.97 E-value: 5.68e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        4 TRNIVGR-DGLCVDVrNGYD---TDGTPLQLWPC-GTQRNQRWTFDSDD-TIRSMG---KCMTANG-LNNGSNIVIFNCS 73
Cdd:cd23499   2 FVRIVNRaSGKCLDI-PGNDndvVNGANVILWDCaDKSADQRWIYDAASgMLRNKAnpsYCLDNRGqAYNGGEVVLWQCE 80


                ....
3CA6_A       74 TAAE 77
Cdd:cd23499  81 DSDN 84

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: 39.07 E-value: 5.96e-04

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3CA6_A      175 IRVNSTRgLCVTTNGYNSKDLIIILKCQGLPSQRWFFNSDGAIVNPKSRLVMDVRASNVSlREIIIFPATGNPNQQW 251
Cdd:cd23420   8 LRNEKSD-LCLDVEGSDGKGNVLMYSCEDNLDQWFRYYENGEIVNAKSRMCLDVSGSDGS-GNVGIYRCEDLRDQMW 82

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: 38.43 E-value: 7.28e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      142 MCLQSNGENNG--VWMEDCEATSLQQQWALYGDRTIRVNStrgLCVTTNGYNSKdlIIILKCQGLPSQRWFFN-SDGAIV 218
Cdd:cd23437  15 LCLDTMGHQNGgpVGLYPCHGMGGNQLFRLNEAGQLAVGE---QCLTASGSGGK--VKLRKCNLGETGKWEYDeATGQIR 89

                        90       100       110
                ....*....|....*....|....*....|....*
3CA6_A      219 NPKSRLVMDVrasNVSLREIIIFPATGN-PNQQWV 252
Cdd:cd23437  90 HKGTGKCLDL---NEGTNKLILQPCDSSsPSQKWE 121

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: 38.68 E-value: 8.18e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      142 MCLQ---SNGENNgVWMEDCEaTSLQQQWALYGDRTIrVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRW-----FFNS 213
Cdd:cd23420  15 LCLDvegSDGKGN-VLMYSCE-DNLDQWFRYYENGEI-VNAKSRMCLDVSGSDGSGNVGIYRCEDLRDQMWsrpnqYCNG 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3CA6_A      214 DG-AIVNPKSRLVMDVrASNVSLREIIIFPATGNPNQ--QWVT 253
Cdd:cd23420  92 DYcSFLNKESNKCLDV-SGDQGTGDVGTYQCDGLPDQrfKWVF 133

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: 38.46 E-value: 8.52e-04

                        10        20        30
                ....*....|....*....|....*....|.
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWT 42
Cdd:cd23458 105 GKCLDVAGGSTANGASIQQWTCNGNDNQRFK 135

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: 38.13 E-value: 9.63e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPC-GTQRNQRWTFDSDDTIRSMGK-CMTANGLNNGSnIVIFNCSTAAeNAIKWEVPIDGS 89
Cdd:cd23440  14 GLCLVAEDEVSQKGSLLVLRPCsRNDKKQLWYYTEDGELRLANLlCLDSSETSSDF-PRLMKCHGSG-GSQQWRFKKDNR 91

                        90       100       110
                ....*....|....*....|....*....|....*..
3CA6_A       90 IINPSSGLVMTAPRAASRTILLLE--DNiyAASQGWT 124
Cdd:cd23440  92 LYNPASGQCLAASKNGTSGYVTMDicSD--SPSQKWV 126

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: 37.69 E-value: 1.22e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDvRNGYDTDGTPlQLWPC-GTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAiKWEV-PIDGS 89
Cdd:cd23434   9 NLCLD-TLGHKAGGTV-GLYPChGTGGNQEWSFTKDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQ-KWEQiENNSK 85

                        90
                ....*....|..
3CA6_A       90 IINPSSGLVMTA 101
Cdd:cd23434  86 LRHVGSNLCLDS 97

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: 37.72 E-value: 1.25e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3CA6_A      177 VNSTRGLCVTTNGYNSKD-LIIILKCQGLPSQRWFFNSDGAI---VNPKsrLVMDVRASNVSLREIIIFPATGNPNQQW 251
Cdd:cd23456   6 KSQASGLCLDVSGGATNGaNVVVYDCNNSNSQKWYYDATGRLhskANPG--KCLDAGGENSNGANVVLWACNDSANQRW 82

ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin (MytiLec) and similar proteins; MytiLec is a D-galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types. It has hemagglutinating activity towards rabbit erythrocytes. It induces glycan-mediated cytotoxicity of human globotriaosylceramide-expressing lymphoma cells. The family also includes lectin from the mussel Mytilus californianus (MCL) and lectin from the sea mussel Crenomytilus grayanus (CGL). MCL is specific for binding D-galactose and N-Acetyl-d-galactosamine that contained carbohydrate moieties that were also inhibited by melibiose and raffinose. It can agglutinate all types of human erythrocytes, as well as rabbit red blood cells. CGL is specific for binding GalNAc/Gal-containing carbohydrate moieties. It displays antibacterial, antifungal, and antiviral activities. It also possesses anti-cancer activity through recognizing globotriose Gb3. Members of this family contain 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 harbor a sugar-binding pocket.

Pssm-ID: 467296 Cd Length: 132 Bit Score: 37.70 E-value: 1.42e-03

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3CA6_A       12 GLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIR--SMGKCMTANGLN----NGSNIVIFN 71
Cdd:cd23417  56 GKCVCPKGGSADNGTKLVLHSNCGDDRAKFRRTSKGSLQhkSSGKCVHPKGGSpnpsNGTKLVLWS 121

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: 37.49 E-value: 1.57e-03

                        10        20
                ....*....|....*....|....*...
3CA6_A       14 CVDVRNGYDTDGTPLQLWPCGTQRNQRW 41
Cdd:cd23452  97 CVDVSGGNSGNGTRLQLWECSGNANQKW 124

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. 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. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. 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: 467319 [Multi-domain] Cd Length: 122 Bit Score: 37.38 E-value: 1.62e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      120 SQGWTVTNnvkpivASIVGYKEMCL--QSNGENNGVWMEDCEATSlQQQWaLYGDRTIrVNSTRGLCVTtngyNSKDL-I 196
Cdd:cd23441  39 SQEWSFTK------DGQLQTQGLCLtvDSSSKDLPVVLETCSDDP-KQKW-TRTGRQL-VHSESGLCLD----SRKKKgL 105

                        90
                ....*....|....*.
3CA6_A      197 IILKCQ-GLPSQRWFF 211
Cdd:cd23441 106 VVSPCRsGAPSQKWDF 121

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains 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 may harbor a sugar-binding pocket.

Pssm-ID: 467341 Cd Length: 136 Bit Score: 37.80 E-value: 1.66e-03

                        10        20        30
                ....*....|....*....|....*....|....*...
3CA6_A       14 CVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRS 51
Cdd:cd23463  59 CLDVIGGKDNPGSKVALWTEHGKTHQKWRINEDGTISS 96

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: 37.29 E-value: 1.98e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       38 NQRWTFDSDDTIRSMGKCMTANglNNGSNIVIFNCSTAAENAiKWEV-PIDGSIINPSSGLVMTAPRAASRTILLLEDNI 116
Cdd:cd23433  40 NQVFSYTAKGEIRSDDLCLDAS--RKGGPVKLEKCHGMGGNQ-EWEYdKETKQIRHVNSGLCLTAPNEDDPNEPVLRPCD 116

                        90
                ....*....|.
3CA6_A      117 YAASQGWTVTN 127
Cdd:cd23433 117 GGPSQKWELEG 127

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: 36.64 E-value: 2.88e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3CA6_A      142 MCLQSNGeNNGVWMEDCEATSLQQ---QWALYGDRTIRVNSTrGLCVTTNGYNSkdlIIILKCQGLPSQRW 209
Cdd:cd23415  54 RCLDSNG-NGGVYTLPCNGGSYQRwrvTSTSGGGVTLRNVAT-GRCLDSNGSGG---VYTRPCNGGSYQRW 119

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: 36.65 E-value: 2.93e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A      143 CLQSNGENngVWMEDCEAtSLQQQWALYGDRTIRVNSTRGLCVTTNGynskDLIIILKCQGLPSQRWFFNSDGAIVNPKS 222
Cdd:cd23425  15 CLTADAAE--VKFQTCDG-SDSQIWQVRKSGILRNLSNTGQCLTADG----ANVSLSPCDTSTSQNWSYEISGNLVNKKT 87


                ....
3CA6_A      223 RLVM 226
Cdd:cd23425  88 GLCL 91

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

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 36.56 E-value: 3.29e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3CA6_A      182 GLCVTTNGYNSKD--LIIILKCQGLPSQRWFFNSDGAIVNPKSRLVMDVRASNVSLREIIIFPATGNPNQQWV 252
Cdd:cd23418  14 GRCLDVPGGSTTNgtRLILWDCHGGANQQFTFTSAGELRVGGDKCLDAAGGGTTNGTPVVIWPCNGGANQKWR 86

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357 Cd Length: 129 Bit Score: 36.32 E-value: 3.98e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        5 RNIVGRDGLCVDVRNGYDTDGTPLQLWPC-GTQRN----QRWTFdSDDTIRSMGKCMTANGLNNGSNIVIFNCSTaAENA 79
Cdd:cd23479   7 PGLIRQGGNCLESQGQDTTGDTLLGLGECrGTASNlpasQEWVL-SDPLIRQQDKCLAITSFSPGSKVILELCNQ-KDGR 84

                        90
                ....*....|....*....
3CA6_A       80 IKWEvpIDGSIINPS-SGL 97
Cdd:cd23479  85 QKWK--LKGSFIQHQvSGL 101

second ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; 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. SGSL is a non-toxic three-chain type II RIPs consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. The ricin B-type lectin domain shows 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 model corresponds to the second ricin B-type lectin domain.

Pssm-ID: 467367 Cd Length: 128 Bit Score: 36.22 E-value: 5.53e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A        6 NIVGRDGLCVDVRNGydtdGTPLQLWPC-GTQRNQRWTFDSDDTIR---SMGKCMTANG--LNNGSNIVIFNCStaAENA 79
Cdd:cd23489   5 SIVGLDDMCLEATDG----NTNMWLEECvPNQREQSWALYSDGTIRvddNRELCVTASSstYDNWKVITILNCD--GSNN 78

                        90
                ....*....|....*.
3CA6_A       80 IKWEVPIDGSIINPSS 95
Cdd:cd23489  79 QRWVFLADGSISTPGN 94

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: 35.65 E-value: 6.28e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3CA6_A       12 GLCVDVRNgydtDGTPLQLWPC-GTQRNQRWTFDSDDTIRSMG--KCMTANGLNNGSNIVIFNCSTAAENaIKWE 83
Cdd:cd23385  11 GKCLAARS----SSSKVSLSTCnPNSPNQQWKWTSGHRLFNVGtgKCLGVSSSSPSSPLRLFECDSEDEL-QKWK 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: 37.07 E-value: 6.96e-03

                         10        20        30
                 ....*....|....*....|....*....|....*.
3CA6_A         7 IVGRD-GLCVDVRNGYDTDGTPLQLWPCGTQRNQRW 41
Cdd:NF035930 203 IRSRLsGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, 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. GALNTL6 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: 467355 Cd Length: 148 Bit Score: 36.07 E-value: 7.00e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       88 GSIINPSSGLVMTAPRAASRTILLLE-------DNIYAASQ----GWTvtNNVKPivASIVGYKEMCLQSNGENNGVWME 156
Cdd:cd23477   8 GEIRNVAANLCVDSKHGATGTELRLDicvkdgsERTWSHEQlftfGWR--EDIRP--GEPLHTRKFCFDAISHNSPVTLY 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3CA6_A      157 DCEATSLQQQWALYGDRTIRVNSTRGlCVTTNGYNSKdlIIILKCQGLP-SQRWFFNSDGAIV 218
Cdd:cd23477  84 DCHGMKGNQLWSYRKDKTLFHPVSNS-CMDCNPADKK--IFMNRCDPLSeTQQWIFEHTNMTV 143

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: 35.40 E-value: 8.33e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CA6_A       12 GLCVDVRNGydTDGTPLQLWPC---GTQRNQRWTFDSDDTIRSMGK--CMTANGLNNGSNIVIFNCSTAAENAIkWE-VP 85
Cdd:cd23439  11 GLCIDTKHG--GENDEVRLSKCvkdGGGGEQQFELTWHEDIRPKKRkvCFDVSSHTPGAPVILYACHGMKGNQL-WKyRP 87

                        90       100       110
                ....*....|....*....|....*....|....*....
3CA6_A       86 IDGSIINPSSGLVMTApRAASRTILLLEDNIYAASQGWT 124
Cdd:cd23439  88 NTKQLYHPVSGLCLDA-DPGSGKVFMNHCDESSDTQKWT 125