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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 426 PVKEVLPGIIKQGTNCLESQGQDTAGNFQLGMGICRGSAKNPAAAQAWLFTDHLIQQQGKCLAATSTsvSPGSLVVLQAC 505
Cdd:cd23479     1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSF--SPGSKVILELC 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128207960 506 NPREGRQRWRRKASFIQHSVSGLCLEAKPAQLVTSKCQADVPAQQWQLLPH 556
Cdd:cd23479    79 NQKDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 426 PVKEVLPGIIKQGTNCLESQGQDTAGNFQLGMGICRGSAKNPAAAQAWLFTDHLIQQQGKCLAATSTsvSPGSLVVLQAC 505
Cdd:cd23479     1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSF--SPGSKVILELC 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128207960 506 NPREGRQRWRRKASFIQHSVSGLCLEAKPAQLVTSKCQADVPAQQWQLLPH 556
Cdd:cd23479    79 NQKDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 441 CLESQGQDTAGNfQLGMGICRGSAKNpaaaQAWLFT-DHLIQQ--QGKCLAATSTSvsPGSLVVLQACNPREGRQRWR-- 515
Cdd:pfam00652  13 CLDVPGGSSAGG-PVGLYPCHGSNGN----QLWTLTgDGTIRSvaSDLCLDVGSTA--DGAKVVLWPCHPGNGNQRWRyd 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2128207960 516 RKASFIQHSVSGLCLEAKPA-----QLVTSKCQADVPAQQW 551
Cdd:pfam00652  86 EDGTQIRNPQSGKCLDVSGAgtsngKVILWTCDSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960  434 IIKQGTN-CLESQGQDTagnfQLGMGICRGSAKNpaaaQAWLFT-DHLIQQQ--GKCLAATStsvSPGSLVVLQACNPRE 509
Cdd:smart00458   1 IISGNTGkCLDVNGNKN----PVGLFDCHGTGGN----QLWKLTsDGAIRIKdtDLCLTANG---NTGSTVTLYSCDGTN 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2128207960  510 GRQRWR-RKASFIQHSVSGLCLEAK----PAQLVTSKCQADvPAQQW 551
Cdd:smart00458  70 DNQYWEvNKDGTIRNPDSGKCLDVKdgntGTKVILWTCSGN-PNQKW 115

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 426 PVKEVLPGIIKQGTNCLESQGQDTAGNFQLGMGICRGSAKNPAAAQAWLFTDHLIQQQGKCLAATSTsvSPGSLVVLQAC 505
Cdd:cd23479     1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSF--SPGSKVILELC 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128207960 506 NPREGRQRWRRKASFIQHSVSGLCLEAKPAQLVTSKCQADVPAQQWQLLPH 556
Cdd:cd23479    79 NQKDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 126 SVIITFHNEArSTLLRTVKSVLNRTPasLIQEIILVDDFSSD--PEDCL-LLTRIPKVKCLRNDRREGLIRSRVRGADVA 202
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTY--PNFEIIVVDDGSTDgtVEIAEeYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 203 AAAVLTFLDSHCEVNTEWLQPMLQRVKEDHTRVVSPIIDVISLDNFAYlaasadlrggfdWSLHFKWEQIPLEQKIARTD 282
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRLL 145

                         170       180
                  ....*....|....*....|....
gi 2128207960 283 PTKpirTPVIAGGIFVIDKSWFNH 306
Cdd:pfam00535 146 GLN---LPFLIGGFALYRREALEE 166

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, 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. 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. GALNT14 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 433 GIIKQGTNCLESQ---GQDTAgnfQLGMGICRGSAKNPAAAQAWLFT-DHLIQQQGKCLAATSTSvsPGSLVVLQACNPR 508
Cdd:cd23478    10 GVIRQRQNCLESRrveGQELP---NLSLSPCIKSKGVPAKSQEWAYTyNQQIRQQQLCLSVHTLF--PGSPVVLVPCKEG 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2128207960 509 EGRQRWRRKASFIQHSVSGLCLEAKPA--------QLVTSKCQADVPAQQWQLLPH 556
Cdd:cd23478    85 DGKQRWTKVGSHIEHMASRFCLDTEMFgdgtesskEIVINPCESSAMSQRWDMVLS 140

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 126 SVIITFHNEARsTLLRTVKSVLNRTPASLiqEIILVDDFSSDP-EDCL--LLTRIPKVKCLRNDRREGLIRSRVRGADVA 202
Cdd:COG0463     5 SVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTDGtAEILreLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2128207960 203 AAAVLTFLDSHCEVNTEWLQPMLQRVKEDHTRVV 236
Cdd:COG0463    82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 127 VIITFHNEARsTLLRTVKSVLNRTPASLiqEIILVDDFSSD--PEDCL-LLTRIPKVKCLRNDRREGLIRSRVRGADVAA 203
Cdd:cd00761     1 VIIPAYNEEP-YLERCLESLLAQTYPNF--EVIVVDDGSTDgtLEILEeYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2128207960 204 AAVLTFLDSHCEVNTEWLQPMLQRVKEDHTRVVspiidVISLDNFAYLAASADLRGGFDWSLHFKWE 270
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELLADPEADA-----VGGPGNLLFRRELLEEIGGFDEALLSGEE 139

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 119 SSDLPATSVIITFHNEARsTLLRTVKSVLNRT-PASLIqEIILVDDFSSDPEDCLLLT---RIPKVKCLRNDRREGLIRS 194
Cdd:COG1215    25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDyPKEKL-EVIVVDDGSTDETAEIARElaaEYPRVRVIERPENGGKAAA 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2128207960 195 RVRGADVAAAAVLTFLDSHCEVNTEWLQPMLQRVKEDHTRVV 236
Cdd:COG1215   103 LNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960  434 IIKQGTN-CLESQGQDTagnfQLGMGICRGSAKNpaaaQAWLFT-DHLIQQQ--GKCLAATStsvSPGSLVVLQACNPRE 509
Cdd:smart00458   1 IISGNTGkCLDVNGNKN----PVGLFDCHGTGGN----QLWKLTsDGAIRIKdtDLCLTANG---NTGSTVTLYSCDGTN 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2128207960  510 GRQRWR-RKASFIQHSVSGLCLEAK----PAQLVTSKCQADvPAQQW 551
Cdd:smart00458  70 DNQYWEvNKDGTIRNPDSGKCLDVKdgntGTKVILWTCSGN-PNQKW 115

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 434 IIKQGTN-CLESQGQDTAGNfQLGMGICRGSAKNpaaaQAWLFT-DHLIQQQGKCLAATSTSVspgslVVLQACNPREGR 511
Cdd:cd23460     5 IKHTESGlCLDWAGESNGDK-TVALKPCHGGGGN----QFWMYTgDGQIRQDHLCLTADEGNK-----VTLRECADQLPS 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2128207960 512 QRW--RRKASFIQHSVSGLCLEAKPA--QLVTSKCQADVPAQQW 551
Cdd:cd23460    75 QEWsyDEKTGTIRHRSTGLCLTLDANndVVILKECDSNSLWQKW 118

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 441 CLESQGQDTAGNFQLGMGICRGSAKnpaaaQAWLFTDH--LIQQQGKCLAATSTSVSPGSLVVLQACNPREGrQRWRRKA 518
Cdd:cd23418    16 CLDVPGGSTTNGTRLILWDCHGGAN-----QQFTFTSAgeLRVGGDKCLDAAGGGTTNGTPVVIWPCNGGAN-QKWRFNS 89

                          90
                  ....*....|....*
gi 2128207960 519 -SFIQHSVSGLCLEA 532
Cdd:cd23418    90 dGTIRNVNSGLCLDV 104

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 424 TVPVKEVLPGiikqgtNCLESQGQDTAGNFQLGMGICRGSAknpaaAQAWLF-TDHLIQQQGKCLAATSTSVSPGSLVVL 502
Cdd:cd23451     2 TGPVRLANAG------KCLDVPGSSTADGNPVQIYTCNGTA-----AQKWTLgTDGTLRVLGKCLDVSGGGTANGTLVQL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2128207960 503 QACNPrEGRQRWRRKAS-FIQHSVSGLCLEAKPA------QLVTSKCQAdVPAQQWQ 552
Cdd:cd23451    71 WDCNG-TGAQKWVPRADgTLYNPQSGKCLDAPGGsttdgtQLQLYTCNG-TAAQQWT 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 479 LIQ--QQGKCLAATStsvsPGSLVVLQACNPREGRQRWRR-KASFIQHSVSGLCL----EAKPAQLVTSKCQADVPAQQW 551
Cdd:cd23385     4 LIYneDLGKCLAARS----SSSKVSLSTCNPNSPNQQWKWtSGHRLFNVGTGKCLgvssSSPSSPLRLFECDSEDELQKW 79

                  .
gi 2128207960 552 Q 552
Cdd:cd23385    80 K 80

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 126 SVIITFHNEARsTLLRTVKSVLNRTPASLIQEIILVDDFSSD-PEDCL--LLTRIPKVKCLRNDRReglIRS--RVRGAD 200
Cdd:cd02525     3 SIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVDGGSTDgTREIVqeYAAKDPRIRLIDNPKR---IQSagLNIGIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 201 VAAAAVLTFLDSHCEVNTEWLQPMLQRVKEDHTRVVSPIIDVISLDNF----AYLAASADLRGGfdwSLHfkweqipleq 276
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFqkaiAVAQSSPLGSGG---SAY---------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2128207960 277 kiaRTDPTKPIRTPVIAGGIFviDKSWFNHLGKYDAQMDIwgGENFELSFRVWMCGGSLEIVPCSRVGHVFR 348
Cdd:cd02525   146 ---RGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 484 GKCLAATSTSVSPGSLVVLQACNPREGrQRWRRKAS-----FIQHSVSGLCLEAKP------AQLVTSKCQADvPAQQWQ 552
Cdd:cd00161    11 GKCLDVAGGSTANGAPVQQWTCNGGAN-QQWTLTPVgdgyyTIRNVASGKCLDVAGgstangANVQQWTCNGG-DNQQWR 88

                  ...
gi 2128207960 553 LLP 555
Cdd:cd00161    89 LEP 91

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 460 CRGSAKNPAAAQAWLftdHLIQQQGKCLAATSTSVSPGslvvLQACNPREGRQRWRRK--ASF--------IQHSVSGLC 529
Cdd:cd23436    30 CDLNNKSQHFNYTWL---RLIRQGELCLAPVEAEGALT----LHPCDNTNNGLRWLHKslIAFpelmdhimLEHQSQPTC 102

                          90       100
                  ....*....|....*....|....*
gi 2128207960 530 LEAKPAQ--LVTSKCQADVPAQQWQ 552
Cdd:cd23436   103 LEADPSQkiLRLNACDSFKRYQKWR 127

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 481 QQQGKCLAAtSTSVSPGSLVVLQACNPREGrQRW-RRKASFIQHSV-SGLCLEAKP-----AQLVTSKCQaDVPAQQWQL 553
Cdd:cd23456     8 QASGLCLDV-SGGATNGANVVVYDCNNSNS-QKWyYDATGRLHSKAnPGKCLDAGGensngANVVLWACN-DSANQRWDF 84

ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and similar proteins; AglA (EC 3.2.1.22), also called melibiase A, hydrolyzes a variety of simple alpha-D-galactosides as well as more complex molecules such as oligosaccharides and polysaccharides. It belongs to the glycosyl hydrolase 27 (GH27) family. AglA contains an N-terminal GH27 catalytic domain, an alpha galactosidase C-terminal beta sandwich domain in the middle region, and a carbohydrate-binding domain at the C-terminus. The carbohydrate-binding domain is also known as a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128207960 424 TVPVKEVLPgiiKQGTNCLesqgqdTAGNFQLGMGICRGSAKnpaaaQAW-LFTDHLIQ---QQGKCLAATstsvspGSL 499
Cdd:cd23425     1 VVATGIIFN---TASGNCL------TADAAEVKFQTCDGSDS-----QIWqVRKSGILRnlsNTGQCLTAD------GAN 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2128207960 500 VVLQACNPREGrQRWRRKASF-IQHSVSGLCLEAKPAQLVTSK-CQADVPAQQWQL 553
Cdd:cd23425    61 VSLSPCDTSTS-QNWSYEISGnLVNKKTGLCLTEGNDAQVTVTdCGNELDSQVFGL 115

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2128207960 292 IAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCsRVGHVFRKRHP 352
Cdd:pfam02709  19 YFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLYHK 78

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2128207960 484 GKCLAATSTSVSPGSLVVLQACNPREGRQRWR--RKASFIQHSVsgLCLEA---KPAQLVTSKCQADVPAQQWQL 553
Cdd:cd23440    14 GLCLVAEDEVSQKGSLLVLRPCSRNDKKQLWYytEDGELRLANL--LCLDSsetSSDFPRLMKCHGSGGSQQWRF 86