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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 474 AEGEIRNVGTNFCIDTQFKEQNQRFGLRKCTSDDkdGGGEQDLRLTRWHDIRPKGRKICFDCSTSVDKAPVILFDCHSMK 553
Cdd:cd23439    1 ASGEIRNVGSGLCIDTKHGGENDEVRLSKCVKDG--GGGEQQFELTWHEDIRPKKRKVCFDVSSHTPGAPVILYACHGMK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 115533034 554 GNQLFKYRVAQKQIYHPISGQCLTADEnGKGFLHMKKCDSSSDLQKWAW 602
Cdd:cd23439   79 GNQLWKYRPNTKQLYHPVSGLCLDADP-GSGKVFMNHCDESSDTQKWTW 126

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 474 AEGEIRNVGTNFCIDTQFKEQNQRFGLRKCTSDDkdGGGEQDLRLTRWHDIRPKGRKICFDCSTSVDKAPVILFDCHSMK 553
Cdd:cd23439    1 ASGEIRNVGSGLCIDTKHGGENDEVRLSKCVKDG--GGGEQQFELTWHEDIRPKKRKVCFDVSSHTPGAPVILYACHGMK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 115533034 554 GNQLFKYRVAQKQIYHPISGQCLTADEnGKGFLHMKKCDSSSDLQKWAW 602
Cdd:cd23439   79 GNQLWKYRPNTKQLYHPVSGLCLDADP-GSGKVFMNHCDESSDTQKWTW 126

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 115533034  160 SVIFPFHEEhNSTLLRSVYSVINRSPPELlkEIILVDDFSeKPALRQPLEDFLKKnkiDHIVKVLRTKKREGLIRGRQLG 239
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKK---DPRVRVIRLPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034  240 AQDATGEILIFLDAHSEANYNWLPPLLDPIAEDYRTVVCPFVDVIDCETYEVRPQDEGargsfdwafnykRLPLTKKDRE 319
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRI------------TLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 115533034  320 SPTKPFNSPVMAGGYFAISAKWFWE 344
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 157 PTVSVIFPFH-EEHNstLLRSVYSVINRSPPELlkEIILVDDFSeKPALRQPLEDFLKKnkiDHIVKVLRTKKREGLIRG 235
Cdd:COG0463    2 PLVSVVIPTYnEEEY--LEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAK---DPRIRVIRLERNRGKGAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 236 RQLGAQDATGEILIFLDAHSEANYNWLPPLLDPIAEDYrtvvcpfVDVIDCETYeVRPQDEGARGSFDWAFNYKRLpltk 315
Cdd:COG0463   74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRL-IREGESDLRRLGSRLFNLVRL---- 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 115533034 316 kdresptkPFNSPVMAGGYFAISAKWFWELgGYDEGLdiwgGEQYEL 362
Cdd:COG0463  142 --------LTNLPDSTSGFRLFRREVLEEL-GFDEGF----LEDTEL 175

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 474 AEGEIRNVGTNFCIDTQFKEQNQRFGLRKCTSDDkdGGGEQDLRLTRWHDIRPKGRKICFDCSTSVDKAPVILFDCHSMK 553
Cdd:cd23439    1 ASGEIRNVGSGLCIDTKHGGENDEVRLSKCVKDG--GGGEQQFELTWHEDIRPKKRKVCFDVSSHTPGAPVILYACHGMK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 115533034 554 GNQLFKYRVAQKQIYHPISGQCLTADEnGKGFLHMKKCDSSSDLQKWAW 602
Cdd:cd23439   79 GNQLWKYRPNTKQLYHPVSGLCLDADP-GSGKVFMNHCDESSDTQKWTW 126

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 471 KASAEGEIRNVGTNFCIDTQF--KEQNQRFGLRKCtsddKDGGGEQDLRLTRWHDIRPkgRKICFDcsTSVDKAPVILFD 548
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGrkKELNKPVGLYPC----HGQGGNQYWMLTKDGEIRR--DDLCLD--YAGGSGDVTLYP 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 115533034 549 CHSMKGNQLFKYRVAQKQIYHPISGQCLTADENGKGfLHMKKCDSSSDLQKWAWQ 603
Cdd:cd23462   73 CHGMKGNQFWIYDEETKQIVHGTSKKCLELSDDSSK-LVMEPCNGSSPRQQWEFE 126

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 469 EPKASAEGEIRNVGTNFCIDTQFKEQNQRFGLRKCTSDDKDG--GGEQDLRLTRWHDIRP----KGRKICFDCSTsvDKA 542
Cdd:cd23477    1 EPPPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSERtwSHEQLFTFGWREDIRPgeplHTRKFCFDAIS--HNS 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533034 543 PVILFDCHSMKGNQLFKYRvAQKQIYHPISGQCLTADENGKGfLHMKKCDSSSDLQKWAWQTVDNELLE 611
Cdd:cd23477   79 PVTLYDCHGMKGNQLWSYR-KDKTLFHPVSNSCMDCNPADKK-IFMNRCDPLSETQQWIFEHTNMTVLE 145

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034   478 IRNVGTNFCIDTQFkeQNQRFGLRKCTSddkdGGGEQDLRLTRWHDIRPKGRKICFDCSTSVDkAPVILFDCHSMKGNQL 557
Cdd:smart00458   1 IISGNTGKCLDVNG--NKNPVGLFDCHG----TGGNQLWKLTSDGAIRIKDTDLCLTANGNTG-STVTLYSCDGTNDNQY 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 115533034   558 FKYRVAqKQIYHPISGQCLTADENGKG-FLHMKKCDSSSDlQKW 600
Cdd:smart00458  74 WEVNKD-GTIRNPDSGKCLDVKDGNTGtKVILWTCSGNPN-QKW 115

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 474 AEGEIRNVG-TNFCIDTQFKEQNQRFGLRKCTSDDKDGGGEQDLRLTRWHDIRPKGRKICFDcstsVDKAPVILFDCHSM 552
Cdd:cd23461    2 ASGVIQSVAfPNLCLDILGRSHGGPPVLAKCSSNKSMPGTFQNFSLTFHRQIKHGTSDDCLE----VRGNNVRLSRCHYQ 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 115533034 553 KGNQLFKYRVAQKQIYHP-ISGQCLTADENGKGfLHMKKCDSSSDLQKWAW 602
Cdd:cd23461   78 GGNQYWKYDYETHQLINGgQNNKCLEADVESLK-ITLSICDSDNVEQKWKW 127

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 476 GEIRNVGTNFCIDTQFKEQNQRFGLRKCTSddkdGGGEQDLRLTRWHDIRPKgrKICFDCSTSvdKAPVILFDCHSMKGN 555
Cdd:cd23467    7 GEIRNVETNQCLDNMGRKENEKVGIFNCHG----MGGNQVFSYTADKEIRTD--DLCLDVSRL--NGPVVMLKCHHMRGN 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115533034 556 QLFKYRVAQKQIYHPISGQCLTA-DENGKGFLHMKKCdSSSDLQKW 600
Cdd:cd23467   79 QLWEYDAERLTLRHVNSNQCLDEpSEEDKMVPTMKDC-SGSRSQQW 123

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 471 KASAEGEIRNVGTNFCIDTQfKEQNQRFG---LRKCTSDDKdgggEQDLRLTRWHDIRPkGRKICFDcSTSVDKAPVILF 547
Cdd:cd23440    1 KVIRKGQLKHAGSGLCLVAE-DEVSQKGSllvLRPCSRNDK----KQLWYYTEDGELRL-ANLLCLD-SSETSSDFPRLM 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 115533034 548 DCHSMKGNQLFKYRVAqKQIYHPISGQCLTADENG-KGFLHMKKCDSSSdLQKW 600
Cdd:cd23440   74 KCHGSGGSQQWRFKKD-NRLYNPASGQCLAASKNGtSGYVTMDICSDSP-SQKW 125

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 476 GEIRNVGTNFCIDTqFKEQNQRFGLR--KCTsddkDGGGEQDLRLTrwhdirPKGRKIC-FDCSTSVDKAPVILFDCHSM 552
Cdd:cd23460    3 GQIKHTESGLCLDW-AGESNGDKTVAlkPCH----GGGGNQFWMYT------GDGQIRQdHLCLTADEGNKVTLRECADQ 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 115533034 553 KGNQLFKYRVAQKQIYHPISGQCLTADENGKGFLhMKKCDSSSDLQKW 600
Cdd:cd23460   72 LPSQEWSYDEKTGTIRHRSTGLCLTLDANNDVVI-LKECDSNSLWQKW 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 157 PTVSVIFPFH-EEHNstLLRSVYSVINRSPPELlkEIILVDDFSeKPALRQPLEDFLKKnkiDHIVKVLRTKKREGLIRG 235
Cdd:COG0463    2 PLVSVVIPTYnEEEY--LEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAK---DPRIRVIRLERNRGKGAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 236 RQLGAQDATGEILIFLDAHSEANYNWLPPLLDPIAEDYrtvvcpfVDVIDCETYeVRPQDEGARGSFDWAFNYKRLpltk 315
Cdd:COG0463   74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRL-IREGESDLRRLGSRLFNLVRL---- 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 115533034 316 kdresptkPFNSPVMAGGYFAISAKWFWELgGYDEGLdiwgGEQYEL 362
Cdd:COG0463  142 --------LTNLPDSTSGFRLFRREVLEEL-GFDEGF----LEDTEL 175

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 157 PTVSVIFPFHEEHnSTLLRSVYSVINRSPPELlkEIILVDDFSEKPALrqpleDFLKKNKIDHiVKVLRTKKREGLIRGR 236
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFPR-VRVIRNPENLGFAAAR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 237 QLGAQDATGEILIFLDAHSEANYNWLPPLLdpiaedyrtvvcpfvdvidcetyevrpqdegargsfDWAFnykrlpltkk 316
Cdd:COG1216   74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLL------------------------------------AAAC---------- 107

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533034 317 dresptkpfnspvmaggyFAISAKWFWELGGYDEGLDIWGGEqYELSFKVWQCHGRMVDAPCSRVAH 383
Cdd:COG1216  108 ------------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYH 155

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034  524 IRPKGRKICFDC-STSVDKAPVILFDCHSMKGNQLFKYRvAQKQIYHPISGQCLTADENGKG-FLHMKKCDSSSDLQKWA 601
Cdd:pfam00652   5 IRNRASGKCLDVpGGSSAGGPVGLYPCHGSNGNQLWTLT-GDGTIRSVASDLCLDVGSTADGaKVVLWPCHPGNGNQRWR 83

                  ....*...
gi 115533034  602 WQTVDNEL 609
Cdd:pfam00652  84 YDEDGTQI 91

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 476 GEIRNvGTNfCIDTQFKEQNQRFGLRKCtsddKDGGGEQDLRLTRWHDIrpKGRKICFDCSTSVDKAPVILFDCHSMKGN 555
Cdd:cd23434    3 GSLKQ-GNL-CLDTLGHKAGGTVGLYPC----HGTGGNQEWSFTKDGQI--KHDDLCLTVVDRAPGSLVTLQPCREDDSN 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 115533034 556 QLFKYRVAQKQIYHPISGQCLTADENGKGFLHMKKCDSSSDLQKW 600
Cdd:cd23434   75 QKWEQIENNSKLRHVGSNLCLDSRNAKSGGLTVETCDPSSGSQQW 119

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 115533034 158 TVSVIFPFHEEHNsTLLRSVYSVINRSPPELLKEIILVDDFSEKpALRQPLEDFLKKNKIdhiVKVLRTKKReglIR--G 235
Cdd:cd02525    1 FVSIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVDGGSTD-GTREIVQEYAAKDPR---IRLIDNPKR---IQsaG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 236 RQLGAQDATGEILIFLDAHSEANYNWLPPLLDPIAEDYRTVVCPFVDVIDCETYEVRPQD--EGARGSFDWAFNYKRlpl 313
Cdd:cd02525   73 LNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVaqSSPLGSGGSAYRGGA--- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533034 314 tKKDRESPTKPFnspvmaGGYfaiSAKWFWELGGYDEGLDIwgGEQYELS-------FKVWQC 369
Cdd:cd02525  150 -VKIGYVDTVHH------GAY---RREVFEKVGGFDESLVR--NEDAELNyrlrkagYKIWLS 200

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
                 ....*....|....*....|....*....|....*..
gi 115533034 566 QIYHPISGQCLTADENGkGFLHMKKCDSSSDLQKWAW 602
Cdd:cd23385    4 LIYNEDLGKCLAARSSS-SKVSLSTCNPNSPNQQWKW 39

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 159 VSVIFP-FHEEHN-STLLRSVysvinRSPPELLKEIILVD----DFSEKPALRQPledflkknkidhiVKVLRTKKreGl 232
Cdd:cd02522    1 LSIIIPtLNEAENlPRLLASL-----RRLNPLPLEIIVVDggstDGTVAIARSAG-------------VVVISSPK--G- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 233 iRGRQL--GAQDATGEILIFLDAHSeanynWLPPlldpiaedyrtvvcPFVDVIdcetYEVRPQDEGARGSFDWAFNYKR 310
Cdd:cd02522   60 -RARQMnaGAAAARGDWLLFLHADT-----RLPP--------------DWDAAI----IETLRADGAVAGAFRLRFDDPG 115

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 311 LPLTKKDRESPTKpFNSPVMAGG---YFaISAKWFWELGGYDEgLDIwgGEQYELSFKVwQCHGRMVDAP 377
Cdd:cd02522  116 PRLRLLELGANLR-SRLFGLPYGdqgLF-IRRELFEELGGFPE-LPL--MEDVELVRRL-RRRGRPALLP 179

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 161 VIFPF-HEEHNstLLRSVYSVINRSPPELLKEIILVDDFSEKpALRQPLEDFLKKNkiDHIVKVLRTKKREglIRGR--- 236
Cdd:cd04192    1 VVIAArNEAEN--LPRLLQSLSALDYPKEKFEVILVDDHSTD-GTVQILEFAAAKP--NFQLKILNNSRVS--ISGKkna 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 237 -QLGAQDATGEILIFLDAHSEANYNWLPPLLDPIAEDYRTVVCPFVdvidceTYEVRPQDEGARGSFDWAFNYKRlpltk 315
Cdd:cd04192   74 lTTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPV------IYFKGKSLLAKFQRLDWLSLLGL----- 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 115533034 316 kdrespTKPF---NSPVMA-GGYFAISAKWFWELGGYDEGLDIWGGE 358
Cdd:cd04192  143 ------IAGSfglGKPFMCnGANMAYRKEAFFEVGGFEGNDHIASGD 183

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 115533034 476 GEIRNVGTNFCIDTQ--FKEQNQRFGLRKCtsddkDGGGEQDLRLTRWHD----IRPKGRKICFD---CSTSvDKAPVIL 546
Cdd:cd00161    3 YRIVNAASGKCLDVAggSTANGAPVQQWTC-----NGGANQQWTLTPVGDgyytIRNVASGKCLDvagGSTA-NGANVQQ 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533034 547 FDCHSmKGNQLFKYRVA---QKQIYHPISGQCLTADENGKGF---LHMKKCDSSSDlQKW 600
Cdd:cd00161   77 WTCNG-GDNQQWRLEPVgdgYYRIVNKHSGKCLDVSGGSTANganVQQWTCNGGAN-QQW 134