ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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 2024399599 494 PTSYGAIKNEGTNSCLDVGENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNVGKQLCLRAGAGPVQLGECRFRGQPTR 573
Cdd:cd23470     1 PTFYGAIKNEGTNQCLDVGENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNSQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024399599 574 VPPDEEWELTQDHLIKNHASRMCLTARGKHPAMAPCDPSDPHQLWSFT 621
Cdd:cd23470    81 VPPDEEWELTQDHLIRNSGSNMCLTARGKHPAMAPCNPADPHQLWSFS 128

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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 2024399599 494 PTSYGAIKNEGTNSCLDVGENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNVGKQLCLRAGAGPVQLGECRFRGQPTR 573
Cdd:cd23470     1 PTFYGAIKNEGTNQCLDVGENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNSQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024399599 574 VPPDEEWELTQDHLIKNHASRMCLTARGKHPAMAPCDPSDPHQLWSFT 621
Cdd:cd23470    81 VPPDEEWELTQDHLIRNSGSNMCLTARGKHPAMAPCNPADPHQLWSFS 128

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 496 SYGAIKNEGTNSCLDVGENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNvGKQLCL----RAGAGPVQLGECRFRGqp 571
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSV-ASDLCLdvgsTADGAKVVLWPCHPGN-- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024399599 572 trvpPDEEWELTQDH-LIKNHASRMCLTARGKHPA-----MAPCDPSDPHQLW 618
Cdd:pfam00652  78 ----GNQRWRYDEDGtQIRNPQSGKCLDVSGAGTSngkviLWTCDSGNPNQQW 126

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599  500 IKNEGTNSCLDVgenNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNvGKQLCLRAGA---GPVQLGECrfrgqpTRVPP 576
Cdd:smart00458   1 IISGNTGKCLDV---NGNKNPVGLFDCHGTGGNQLWKLTSDGAIRIK-DTDLCLTANGntgSTVTLYSC------DGTND 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024399599  577 DEEWELTQDHLIKNHASRMCLTAR----GKHPAMAPCDPSdPHQLWSFT 621
Cdd:smart00458  71 NQYWEVNKDGTIRNPDSGKCLDVKdgntGTKVILWTCSGN-PNQKWIFE 118

putative glycosyl transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 176 PTTSVVIVFHNEAwsTLLRTVYSVLHASPAALLrEIILVDDASTDEYLkDELDRYVKQLQIVRVVRQaERKGLITARLLG 255
Cdd:PRK10073    6 PKLSIIIPLYNAG--KDFRAFMESLIAQTWTAL-EIIIVNDGSTDNSV-EIAKHYAENYPHVRLLHQ-ANAGVSVARNTG 80

                          90
                  ....*....|....
gi 2024399599 256 ASVASGEVLTFLDA 269
Cdd:PRK10073   81 LAVATGKYVAFPDA 94

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) and similar proteins; GALNT6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, 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. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT6 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 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 2024399599 494 PTSYGAIKNEGTNSCLDVGENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNVGKQLCLRAGAGPVQLGECRFRGQPTR 573
Cdd:cd23470     1 PTFYGAIKNEGTNQCLDVGENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAKQLCLRVSKGPVQLGECHYKGKNSQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024399599 574 VPPDEEWELTQDHLIKNHASRMCLTARGKHPAMAPCDPSDPHQLWSFT 621
Cdd:cd23470    81 VPPDEEWELTQDHLIRNSGSNMCLTARGKHPAMAPCNPADPHQLWSFS 128

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 494 PTSYGAIKNEGTNSCLDVGENNH-GGKPLIMYPCHGMGGNQYFEYTTQRDLRHNVGKQLCLRA-GAGPVQLGECRFRGQp 571
Cdd:cd23435     1 PGYYGALRNKGSELCLDVNNPNGqGGKPVIMYGCHGLGGNQYFEYTSKGEIRHNIGKELCLHAsGSDEVILQHCTSKGK- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024399599 572 tRVPPDEEWELTQDHLIKNHASRMCLTARGKHPAMAPCDPSDPHQLWSFT 621
Cdd:cd23435    80 -DVPPEQKWLFTQDGTIRNPASGLCLHASGYKVLLRTCNPSDDSQKWTFI 128

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 496 SYGAIKNEGTNSCLDVGENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNvGKQLCL----RAGAGPVQLGECRFRGqp 571
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSV-ASDLCLdvgsTADGAKVVLWPCHPGN-- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024399599 572 trvpPDEEWELTQDH-LIKNHASRMCLTARGKHPA-----MAPCDPSDPHQLW 618
Cdd:pfam00652  78 ----GNQRWRYDEDGtQIRNPQSGKCLDVSGAGTSngkviLWTCDSGNPNQQW 126

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 4 (GALNT4) and similar proteins; GALNT4 (EC 2.4.1.41), also called polypeptide GalNAc transferase 4, GalNAc-T4, pp-GaNTase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, 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. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT4 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 2024399599 494 PTSYGAIKNEGTNS-CLDVG--ENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNVGKQLCLRAGAGPVQLG--ECRFR 568
Cdd:cd23469     1 PGWHGAVRSMGISSeCLDYNspEHNPTGAHLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPDQKNYIGmkHCPKD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024399599 569 GQPtrVPPDEEWELTQDHLIKNHASRMCLTA----RGKHPA-MAPCDPSDPHQLWSF 620
Cdd:cd23469    81 GSP--VPANIIWHFKEDGTIYHPHSGMCISAyrtpEGRADVqMRTCDAGDKNQLWSF 135

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 492 LNPTSYGAIKNEGTNSCLDVGENNHGGKPLiMYPCHGMGGNQYFEYTTQRDLRHNVgkqLCLRAGA--GPVQLGECrfrg 569
Cdd:cd23433     1 LDYYSLGEIRNVETNLCLDTMGRKAGEKVG-LSSCHGQGGNQVFSYTAKGEIRSDD---LCLDASRkgGPVKLEKC---- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024399599 570 qpTRVPPDEEWEL-TQDHLIKNHASRMCLTARGK----HPAMAPCDPsDPHQLWSF 620
Cdd:cd23433    73 --HGMGGNQEWEYdKETKQIRHVNSGLCLTAPNEddpnEPVLRPCDG-GPSQKWEL 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 491 DLNPTSYGAIKNEGTNSCLD-VGENNHGGKPLIMYPCHGMG-GNQYFEYTTQRDLRHNVGkqlCLRA---GAGPVQLGEC 565
Cdd:cd23459     1 DEDVLAYGQVRNPGTNLCLDtLQRDEDKGYNLGLYPCQGGLsSNQLFSLSKKGELRREES---CADVqgtEESKVILITC 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024399599 566 RfrgqpTRVPPDEEWELTQDHLIKNHASRMCLTAR----GKHPAMAPCDPsDPHQLWSF 620
Cdd:cd23459    78 H-----GLEKFNQKWKHTKGGQIVHLASGKCLDAEglksGDDVTLAKCDG-SLSQKWTF 130

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 2024399599 496 SYGAIKNEGTNSCLDVGENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNvgkQLCLRAGAG-PVQLGECRFRGqptrv 574
Cdd:cd23460     1 GLGQIKHTESGLCLDWAGESNGDKTVALKPCHGGGGNQFWMYTGDGQIRQD---HLCLTADEGnKVTLRECADQL----- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024399599 575 pPDEEWE-LTQDHLIKNHASRMCLTAR--GKHPAMAPCDPSDPHQLWSFT 621
Cdd:cd23460    73 -PSQEWSyDEKTGTIRHRSTGLCLTLDanNDVVILKECDSNSLWQKWIFQ 121

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 176 PTTSVVIVFHNEaWSTLLRTVYSVLHASPAALlrEIILVDDASTDEYLkdeldRYVKQLQI--VRVVRQAERKGLITARL 253
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFprVRVIRNPENLGFAAARN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 254 LGASVASGEVLTFLDAHCECFHGWLEPLLSriaeeptavvspdittidlntfefskpvqygkqhsrgnfdwsltfgwevv 333
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA-------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 334 pprerqrrkdetvpiksptFAGglFAISRSYFEHIGSYDDQMEIWGGEnVEMSFRVWQCGGQLEIIPCSVVGHVfRSKSP 413
Cdd:COG1216   105 -------------------AAC--LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHL-GGASS 161

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2024399599 414 HTFPKgTQVISRNQVRLAEVWMDDYKEIFYRRNQQAAQMAR 454
Cdd:COG1216   162 GPLLR-AYYLGRNRLLFLRKHGPRPLLRLALLRGLRLRLRG 201

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 12 (GALNT12) and similar proteins; GALNT12 (EC 2.4.1.41), also called polypeptide GalNAc transferase 12, GalNAc-T12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12, 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. 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. GALNT12 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 2024399599 494 PTSYGAIKNEG-TNSCLDVG---ENNHGGKPLIMYPCHGMGGNQYFEYTTQRDLRHNVGK-QLCLRAGAGPVQLGE--CR 566
Cdd:cd23471     1 PGFFGMLKNKGmTNYCFDYNppdEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQpEGCAAVDAGTDFLTMhlCR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 567 FRGQPtrVPPDEEWELTQDHLIKNHASRMCLTARGKH------PAMAPCDPSDpHQLWSF 620
Cdd:cd23471    81 ENRQA--VPENQKFIFREDGSLFHVQTQKCVQAVRNEssgspaPVLRPCTDSD-HQKWFF 137

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 2024399599 494 PTSYGAIKNEGTNSCLDVGENN-HGGKPLIMYPCHGmGGNQYFEYTTQRDLRHNVGKqlCLRAGAG------PVQLGECR 566
Cdd:cd23418     2 GAGGGQIRGYGSGRCLDVPGGStTNGTRLILWDCHG-GANQQFTFTSAGELRVGGDK--CLDAAGGgttngtPVVIWPCN 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2024399599 567 frGQPtrvppDEEWELTQDHLIKNHASRMCL 597
Cdd:cd23418    79 --GGA-----NQKWRFNSDGTIRNVNSGLCL 102

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 2024399599 180 VVIVFHNEAwSTLLRTVYSVLHAS-PAALLrEIILVDDASTD---EYLKDELDRYVKQLQIVRVVRqAERKGLITARLLG 255
Cdd:cd04192     1 VVIAARNEA-ENLPRLLQSLSALDyPKEKF-EVILVDDHSTDgtvQILEFAAAKPNFQLKILNNSR-VSISGKKNALTTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 256 ASVASGEVLTFLDAHCECFHGWLEPLLSRIAEEPTAVVSPDITTIDLNTFeFSKpvqygkqhsRGNFDWSLT-------F 328
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSL-LAK---------FQRLDWLSLlgliagsF 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024399599 329 GWEVvpprerqrrkdetvpiksPTFAGGL-FAISRSYFEHIGSYDDQMEIWGGENV 383
Cdd:cd04192   148 GLGK------------------PFMCNGAnMAYRKEAFFEVGGFEGNDHIASGDDE 185

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 2024399599 497 YGAIKNEGTNSCLDV-GENNHGGKPLIMYPCHGmGGNQYFEYTTQRD----LRhNVGKQLCLRAGAG------PVQLGEC 565
Cdd:cd00161     2 TYRIVNAASGKCLDVaGGSTANGAPVQQWTCNG-GANQQWTLTPVGDgyytIR-NVASGKCLDVAGGstangaNVQQWTC 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024399599 566 rfRGQptrvpPDEEWELTQ----DHLIKNHASRMCLTARGKHPA------MAPCDpSDPHQLW 618
Cdd:cd00161    80 --NGG-----DNQQWRLEPvgdgYYRIVNKHSGKCLDVSGGSTAnganvqQWTCN-GGANQQW 134

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 496 SYGAIKNEGTNSCLD---VGENNHGGkpliMYPCHGMGGNQYFEYTTQRDLRHNvgkQLCLRAGA--GPVQLGEC-RFRG 569
Cdd:cd23466     5 SLGEIRNVETNQCLDnmaRKENEKVG----IFNCHGMGGNQVFSYTANKEIRTD---DLCLDVSKlnGPVMMLKChHLKG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024399599 570 qptrvppDEEWE-----LTQDHLIKNHASRMCLTARGKHPAMAPCDPSDPHQlW 618
Cdd:cd23466    78 -------NQLWEydpvkLTLLHVNSNQCLDKATEEDSQVPSIRDCNGSRSQQ-W 123

Ricin-type beta-trefoil lectin domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024399599 495 TSYGAIKNEGTNSCLDVGENNHGGKpLIMYPCHGMGGNQYFEYTTQRDLRHNVGKQLCLRA-----GAGPVQLGECR 566
Cdd:pfam00652  43 TGDGTIRSVASDLCLDVGSTADGAK-VVLWPCHPGNGNQRWRYDEDGTQIRNPQSGKCLDVsgagtSNGKVILWTCD 118

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 180 VVIVFHNEAwSTLLRTVYSVLHASPAALLREIILVDDASTDEYLkDELDRYVKQLQIVRVVRQAERKGLITARLLGASVA 259
Cdd:cd04179     1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTA-EIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAA 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024399599 260 SGEVLTFLDA---HCECFhgwLEPLLSRIAEEPTAVV 293
Cdd:cd04179    79 RGDIVVTMDAdlqHPPED---IPKLLEKLLEGGADVV 112

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 2024399599 179 SVVIVFHNEAwSTLLRTVYSVLHASPAALLREIILVDDASTDEyLKDELDRYVKQLQIVRVVRQaERKGLITARLLGASV 258
Cdd:cd02525     3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDG-TREIVQEYAAKDPRIRLIDN-PKRIQSAGLNIGIRN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024399599 259 ASGEVLTFLDAHCECFHGWLEPLLSRIAEEPTAVVSPDITTIDLNTFEFSkpVQYGKQHSRGNFDwsltfgwevvpprER 338
Cdd:cd02525    80 SRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKA--IAVAQSSPLGSGG-------------SA 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024399599 339 QRRKDETvPIKSPTFAGGLFaiSRSYFEHIGSYDDQMEIwgGENVEMSFRVWQCGGQLEIIPCSVVGHVFRSK 411
Cdd:cd02525   145 YRGGAVK-IGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPRST 212