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Conserved domains on  [gi|767958286|ref|XP_011517320|]
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polypeptide N-acetylgalactosaminyltransferase 12 isoform X1 [Homo sapiens]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 10118412)

polypeptide N-acetylgalactosaminyltransferase 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

CAZY:  GT2
EC:  2.4.1.41
Gene Ontology:  GO:0004653|GO:0030246|GO:0046872
PubMed:  12634319|12691742|9445404|8844840
SCOP:  3000077|3000678

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 65-359 2.54e-167

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


:

Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 474.39  E-value: 2.54e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  65 SVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANELSG-LPKVRLIRANKREGLVRARLLGAS 143
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 144 AARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFEYLGnSGEPQIGGFDWRLVFTWHTVPERERIR 223
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG-SSGDARGGFDWSLHFKWLPLPEEERRR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 224 mQSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFP-KQAPYSRNKA 302
Cdd:cd02510  160 -ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 303 LA----NSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVY 359
Cdd:cd02510  239 SGtvlrNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 369-505 3.04e-96

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.


The actual alignment was detected with superfamily member cd23471:

Pssm-ID: 483949  Cd Length: 140  Bit Score: 287.46  E-value: 3.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCE 448
Cdd:cd23471    1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 449 ET---APENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKER 505
Cdd:cd23471   81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 65-359 2.54e-167

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 474.39  E-value: 2.54e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  65 SVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANELSG-LPKVRLIRANKREGLVRARLLGAS 143
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 144 AARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFEYLGnSGEPQIGGFDWRLVFTWHTVPERERIR 223
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG-SSGDARGGFDWSLHFKWLPLPEEERRR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 224 mQSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFP-KQAPYSRNKA 302
Cdd:cd02510  160 -ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 303 LA----NSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVY 359
Cdd:cd02510  239 SGtvlrNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 369-505 3.04e-96

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.


Pssm-ID: 467349  Cd Length: 140  Bit Score: 287.46  E-value: 3.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCE 448
Cdd:cd23471    1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 449 ET---APENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKER 505
Cdd:cd23471   81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 65-246 5.50e-36

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.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 131.36  E-value: 5.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286   65 SVIIAFYNEaWSTLLRTVYSVLETSPDILleEVILVDDYSdREHLKERLANELSGLPKVRLIRANKREGLVRARLLGASA 144
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  145 ARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFEYLgnsgepqiggfdWRLVFTWHTVPERERIRM 224
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR------------RASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|..
gi 767958286  225 QSPVDVIRSPTMAGGLFAVSKK 246
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
371-500 1.77e-21

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 89.90  E-value: 1.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  371 FFGMLQNKGlTDYCFDYNPPDENqivGHQVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMD--TLIMHLCE 448
Cdd:pfam00652   1 ATGRIRNRA-SGKCLDVPGGSSA---GGPVGLYPCHGSNGNQLWTLTGDGTIR--SVASDLCLDVGSTADgaKVVLWPCH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767958286  449 ETAPeNQKFILQEDGS-LFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 500
Cdd:pfam00652  75 PGNG-NQRWRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 62-180 1.31e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 87.06  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  62 PRTSVIIAFYNEAwSTLLRTVYSVLE-TSPDIlleEVILVDDYSD---REHLKERLANElsglPKVRLIRANKREGLVRA 137
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAqTYPDF---EIIVVDDGSTdgtAEILRELAAKD----PRIRVIRLERNRGKGAA 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958286 138 RLLGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVC 180
Cdd:COG0463   74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 379-503 1.41e-16

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 75.63  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286   379 GLTDYCFDYNPPDENqivghqVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMDTLI-MHLCEETAPeNQKF 457
Cdd:smart00458   4 GNTGKCLDVNGNKNP------VGLFDCHGTGGNQLWKLTSDGAIR--IKDTDLCLTANGNTGSTVtLYSCDGTND-NQYW 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767958286   458 ILQEDGSLFHEQSKKCVQAarKESSDSFVPLLRDCTNSDHQKWFFK 503
Cdd:smart00458  75 EVNKDGTIRNPDSGKCLDV--KDGNTGTKVILWTCSGNPNQKWIFE 118
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 65-175 4.54e-05

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 44.81  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286   65 SVIIAFYNEA--WSTLLRTVYSVLETSpdilleEVILVDDYS-DRehlKERLANELsglpKVRLIRANKreGlvRARLL- 140
Cdd:TIGR04283   2 SIIIPVLNEAatLPELLADLQALRGDA------EVIVVDGGStDG---TVEIARSL----GAKVIHSPK--G--RARQMn 64

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767958286  141 -GASAARGDVLTFLdcHCEC--HEGWLEPLLQRIHEEE 175
Cdd:TIGR04283  65 aGAALAKGDILLFL--HADTrlPKDFLEAIRRALAKPG 100
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 62-154 8.36e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 41.57  E-value: 8.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  62 PRTSVIIAFYNeAWSTLLRTVYSVLETSPDILleEVILVDDYSDrEHLKERLANELSGLPKVRLIrANKREGLVRARLLG 141
Cdd:PRK10073   6 PKLSIIIPLYN-AGKDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTG 80

                         90
                 ....*....|...
gi 767958286 142 ASAARGDVLTFLD 154
Cdd:PRK10073  81 LAVATGKYVAFPD 93
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 65-359 2.54e-167

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 474.39  E-value: 2.54e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  65 SVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANELSG-LPKVRLIRANKREGLVRARLLGAS 143
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 144 AARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFEYLGnSGEPQIGGFDWRLVFTWHTVPERERIR 223
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG-SSGDARGGFDWSLHFKWLPLPEEERRR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 224 mQSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFP-KQAPYSRNKA 302
Cdd:cd02510  160 -ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 303 LA----NSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVY 359
Cdd:cd02510  239 SGtvlrNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT12 cd23471
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 369-505 3.04e-96

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.


Pssm-ID: 467349  Cd Length: 140  Bit Score: 287.46  E-value: 3.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCE 448
Cdd:cd23471    1 PGFFGMLKNKGMTNYCFDYNPPDEHQIAGHQVILYQCHGMGQNQFFEYTSQNEIRYNTRQPEGCAAVDAGTDFLTMHLCR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 449 ET---APENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKER 505
Cdd:cd23471   81 ENrqaVPENQKFIFREDGSLFHVQTQKCVQAVRNESSGSPAPVLRPCTDSDHQKWFFKER 140
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 369-503 4.15e-49

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3)-like subfamily; The GALNT3-like subfamily includes GALNT3, GALNT4, GALNT6 and GALNT12. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467313 [Multi-domain]  Cd Length: 128  Bit Score: 164.81  E-value: 4.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGlTDYCFDYNPPDENqiVGHQVILYLCHGMGQNQFFEYTSQKEIRYNThQPEGCIAVEaGMDTLIMHLCE 448
Cdd:cd23435    1 PGYYGALRNKG-SELCLDVNNPNGQ--GGKPVIMYGCHGLGGNQYFEYTSKGEIRHNI-GKELCLHAS-GSDEVILQHCT 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958286 449 ET---APENQKFILQEDGSLFHEQSKKCVQAARKEssdsfvPLLRDCTNSD-HQKWFFK 503
Cdd:cd23435   76 SKgkdVPPEQKWLFTQDGTIRNPASGLCLHASGYK------VLLRTCNPSDdSQKWTFI 128
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 65-246 5.50e-36

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.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 131.36  E-value: 5.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286   65 SVIIAFYNEaWSTLLRTVYSVLETSPDILleEVILVDDYSdREHLKERLANELSGLPKVRLIRANKREGLVRARLLGASA 144
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  145 ARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFEYLgnsgepqiggfdWRLVFTWHTVPERERIRM 224
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR------------RASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|..
gi 767958286  225 QSPVDVIRSPTMAGGLFAVSKK 246
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_GALNT4 cd23469
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 369-503 3.90e-27

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.


Pssm-ID: 467347  Cd Length: 136  Bit Score: 106.14  E-value: 3.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGLTDYCFDYNPPDENQiVGHQVILYLCHGMGQNQFFEYTSQKEIRYNThQPEGCIAVEAGMDTLIMHLCE 448
Cdd:cd23469    1 PGWHGAVRSMGISSECLDYNSPEHNP-TGAHLSLFGCHGQGGNQFFEYTSNKEIRFNS-VTELCAEVPDQKNYIGMKHCP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958286 449 E---TAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPlLRDCTNSD-HQKWFFK 503
Cdd:cd23469   79 KdgsPVPANIIWHFKEDGTIYHPHSGMCISAYRTPEGRADVQ-MRTCDAGDkNQLWSFE 136
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
371-500 1.77e-21

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 89.90  E-value: 1.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  371 FFGMLQNKGlTDYCFDYNPPDENqivGHQVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMD--TLIMHLCE 448
Cdd:pfam00652   1 ATGRIRNRA-SGKCLDVPGGSSA---GGPVGLYPCHGSNGNQLWTLTGDGTIR--SVASDLCLDVGSTADgaKVVLWPCH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767958286  449 ETAPeNQKFILQEDGS-LFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 500
Cdd:pfam00652  75 PGNG-NQRWRYDEDGTqIRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 372-503 1.79e-20

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467311 [Multi-domain]  Cd Length: 127  Bit Score: 86.98  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 372 FGMLQNKGlTDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRynthQPEGCIAVEAGMDTLIMHLCEETa 451
Cdd:cd23433    6 LGEIRNVE-TNLCLDTMGRKAGEKVG----LSSCHGQGGNQVFSYTAKGEIR----SDDLCLDASRKGGPVKLEKCHGM- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767958286 452 PENQKFIL-QEDGSLFHEQSKKCVQAARKESSDsfVPLLRDCTNSDHQKWFFK 503
Cdd:cd23433   76 GGNQEWEYdKETKQIRHVNSGLCLTAPNEDDPN--EPVLRPCDGGPSQKWELE 126
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 369-502 7.48e-20

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467337 [Multi-domain]  Cd Length: 132  Bit Score: 85.45  E-value: 7.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGlTDYCFD-YN-PPDENQIVGhqviLYLCHGMGQ-NQFFEYTSQKEIRynthQPEGCIAVE-AGMDTLIM 444
Cdd:cd23459    4 VLAYGQVRNPG-TNLCLDtLQrDEDKGYNLG----LYPCQGGLSsNQLFSLSKKGELR----REESCADVQgTEESKVIL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958286 445 HLCEETAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSfvPLLRDCTNSDHQKWFF 502
Cdd:cd23459   75 ITCHGLEKFNQKWKHTKGGQIVHLASGKCLDAEGLKSGDD--VTLAKCDGSLSQKWTF 130
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 62-180 1.31e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 87.06  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  62 PRTSVIIAFYNEAwSTLLRTVYSVLE-TSPDIlleEVILVDDYSD---REHLKERLANElsglPKVRLIRANKREGLVRA 137
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAqTYPDF---EIIVVDDGSTdgtAEILRELAAKD----PRIRVIRLERNRGKGAA 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958286 138 RLLGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVC 180
Cdd:COG0463   74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 54-226 2.77e-19

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 88.26  E-value: 2.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  54 KKYDYDNLPRTSVIIAFYNEAwSTLLRTVYSVLETSPDILLEEVILVDDYSDREhLKERLANELSGLPKVRLIRANKREG 133
Cdd:COG1215   21 RRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE-TAEIARELAAEYPRVRVIERPENGG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 134 LVRARLLGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIdVIDWNTFEylgnsgepQIGGFD------- 206
Cdd:COG1215   99 KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL-AFRREALE--------EVGGFDedtlged 169

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767958286 207 -----------WRLVF-----TWHTVPE--RERIRMQS 226
Cdd:COG1215  170 ldlslrllragYRIVYvpdavVYEEAPEtlRALFRQRR 207
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 369-502 7.92e-19

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT3 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467346  Cd Length: 129  Bit Score: 82.55  E-value: 7.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGlTDYCFDYNppdENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNThQPEGCIAVEAGMdtLIMHLC- 447
Cdd:cd23468    2 PLIFGAIKNVG-KELCLDVG---ENNHGGKPLIMYNCHGLGGNQYFEYSTHHEIRHNI-QKELCLHGSQGS--VQLKECt 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 448 ----EETAPENQKFILQEDGSLFHEQSKKCVqaarkeSSDSFVPLLRDCTNSD-HQKWFF 502
Cdd:cd23468   75 ykgrNTAVLPEEKWELQKDQLLYNPALNMCL------SANGENPSLVPCNPSDpFQQWIF 128
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 66-180 1.32e-18

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.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 82.94  E-value: 1.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNEAwSTLLRTVYSVLETSPDILleEVILVDDYSDREHLkERLANELSGLPKVRLIRANKREGLVRARLLGASAA 145
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTL-EILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767958286 146 RGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVC 180
Cdd:cd00761   77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 368-501 1.39e-18

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467320 [Multi-domain]  Cd Length: 124  Bit Score: 81.72  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 368 RPGFFGMLQNKGlTDYCFDYNPpdENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPegCIAVEAgmDTLIMHLC 447
Cdd:cd23442    1 APYFSGQLYNTG-TGYCADYIH--GWRLAGGPVELSPCSGQNGNQLFEYTSDKEIRFGSLQL--CLDVRQ--EQVVLQNC 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767958286 448 EETApENQKFILQEDGSLFHEQSKKCVQAArkESSDSFVPLLRDCTNSDHQKWF 501
Cdd:cd23442   74 TKEK-TSQKWDFQETGRIVHILSGKCIEAV--ESENSKLLFLSPCNGQRNQMWK 124
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 373-503 6.38e-17

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 77.02  E-value: 6.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 373 GMLQNKGlTDYCFDynPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEETaP 452
Cdd:cd23462    6 GEIRNLA-GKLCLD--APGRKKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRD----DLCLDYAGGSGDVTLYPCHGM-K 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767958286 453 ENQKFIL-QEDGSLFHEQSKKCVQAarkeSSDSFVPLLRDCT-NSDHQKWFFK 503
Cdd:cd23462   78 GNQFWIYdEETKQIVHGTSKKCLEL----SDDSSKLVMEPCNgSSPRQQWEFE 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 379-503 1.41e-16

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 75.63  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286   379 GLTDYCFDYNPPDENqivghqVILYLCHGMGQNQFFEYTSQKEIRynTHQPEGCIAVEAGMDTLI-MHLCEETAPeNQKF 457
Cdd:smart00458   4 GNTGKCLDVNGNKNP------VGLFDCHGTGGNQLWKLTSDGAIR--IKDTDLCLTANGNTGSTVtLYSCDGTND-NQYW 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767958286   458 ILQEDGSLFHEQSKKCVQAarKESSDSFVPLLRDCTNSDHQKWFFK 503
Cdd:smart00458  75 EVNKDGTIRNPDSGKCLDV--KDGNTGTKVILWTCSGNPNQKWIFE 118
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
62-209 5.13e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 76.57  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  62 PRTSVIIAFYNEaWSTLLRTVYSVLETSPDILleEVILVDDYSD---REHLKERlanelsGLPKVRLIRANKREGLVRAR 138
Cdd:COG1216    3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGSTdgtAELLAAL------AFPRVRVIRNPENLGFAAAR 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 139 LLGASAARGDVLTFLDCHCECHEGWLEPLLqriheEESAVVCPViDVIDwntfeylgnsgepQIGGFDWRL 209
Cdd:COG1216   74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLL-----AAACLLIRR-EVFE-------------EVGGFDERF 125
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 373-504 1.45e-15

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 73.10  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 373 GMLQNKGlTDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEetAP 452
Cdd:cd23437    6 GEIRNLG-TGLCLDTMGHQNGGPVG----LYPCHGMGGNQLFRLNEAGQLAVG----EQCLTASGSGGKVKLRKCN--LG 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767958286 453 ENQKFILQE-DGSLFHEQSKKCVQaarKESSDSFVpLLRDCTN-SDHQKWFFKE 504
Cdd:cd23437   75 ETGKWEYDEaTGQIRHKGTGKCLD---LNEGTNKL-ILQPCDSsSPSQKWEFNE 124
beta-trefoil_Ricin_GALNT6 cd23470
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 369-502 1.49e-15

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.


Pssm-ID: 467348  Cd Length: 128  Bit Score: 72.98  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 369 PGFFGMLQNKGlTDYCFDYNppdENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQpEGCIAVEAG---MDTLIMH 445
Cdd:cd23470    1 PTFYGAIKNEG-TNQCLDVG---ENNRGGKPLIMYSCHGMGGNQYFEYTTHKELRHNIAK-QLCLRVSKGpvqLGECHYK 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958286 446 LCEETAPENQKFILQEDGSLFHEQSKKCVQAARKEssdsfvPLLRDCTNSD-HQKWFF 502
Cdd:cd23470   76 GKNSQVPPDEEWELTQDHLIRNSGSNMCLTARGKH------PAMAPCNPADpHQLWSF 127
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 381-503 2.76e-14

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


Pssm-ID: 467344  Cd Length: 127  Bit Score: 69.69  E-value: 2.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 381 TDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEETApENQkfILQ 460
Cdd:cd23466   14 TNQCLDNMARKENEKVG----IFNCHGMGGNQVFSYTANKEIRTD----DLCLDVSKLNGPVMMLKCHHLK-GNQ--LWE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767958286 461 EDG---SLFHEQSKKCVQAARKEssDSFVPLLRDCTNSDHQKWFFK 503
Cdd:cd23466   83 YDPvklTLLHVNSNQCLDKATEE--DSQVPSIRDCNGSRSQQWLLR 126
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 373-502 4.61e-13

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


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 66.22  E-value: 4.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 373 GMLQNKgltdyCFDYnpPDENQIVGHQVILYLCHGmGQNQFFEYTSQKEIRyntHQPEGCIAVEAGM----DTLIMHLCE 448
Cdd:cd23418   10 GYGSGR-----CLDV--PGGSTTNGTRLILWDCHG-GANQQFTFTSAGELR---VGGDKCLDAAGGGttngTPVVIWPCN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767958286 449 ETApeNQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFF 502
Cdd:cd23418   79 GGA--NQKWRFNSDGTIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWRR 130
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 381-503 9.99e-13

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


Pssm-ID: 467345  Cd Length: 127  Bit Score: 65.05  E-value: 9.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 381 TDYCFDYNPPDENQIVGhqviLYLCHGMGQNQFFEYTSQKEIRYNthqpEGCIAVEAGMDTLIMHLCEETApENQKFILQ 460
Cdd:cd23467   14 TNQCLDNMGRKENEKVG----IFNCHGMGGNQVFSYTADKEIRTD----DLCLDVSRLNGPVVMLKCHHMR-GNQLWEYD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767958286 461 -EDGSLFHEQSKKCVQAARKEssDSFVPLLRDCTNSDHQKWFFK 503
Cdd:cd23467   85 aERLTLRHVNSNQCLDEPSEE--DKMVPTMKDCSGSRSQQWLLR 126
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 371-503 1.16e-10

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


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 58.99  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 371 FFGMLQNKGlTDYCFDYNPPDENQIVghqVILYLCHGMGQNQFFEYTSQKEIRYNTHqpegCI-AVEAGMDTLImhLCEE 449
Cdd:cd23460    1 GLGQIKHTE-SGLCLDWAGESNGDKT---VALKPCHGGGGNQFWMYTGDGQIRQDHL----CLtADEGNKVTLR--ECAD 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958286 450 TAPeNQKFILQEDGS-LFHEQSKKCVQAARKEssdsFVPLLRDCTNSDH-QKWFFK 503
Cdd:cd23460   71 QLP-SQEWSYDEKTGtIRHRSTGLCLTLDANN----DVVILKECDSNSLwQKWIFQ 121
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 65-283 2.08e-09

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.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 58.01  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  65 SVIIAFYNEAwSTLLRTVYSVLETSPDILLEEVILVDDYSD---REHLKERLANElsglPKVRLIRaNKREGLVRARLLG 141
Cdd:cd02525    3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTdgtREIVQEYAAKD----PRIRLID-NPKRIQSAGLNIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 142 ASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFE---------YLGNSGEPqiggfdwrlvft 212
Cdd:cd02525   77 IRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQkaiavaqssPLGSGGSA------------ 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 213 whtvpereriRMQSPVDVIRSPTMAGGLFavSKKYFEYLGSYDTGMEVwgGENLEFSFRIWQCGGVLETHP 283
Cdd:cd02525  145 ----------YRGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSP 201
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 66-196 4.97e-09

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.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 56.04  E-value: 4.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNEAwSTLLRTVYSVLETSPDILLEEVILVDDYS-DR--EHLKERLANelsgLPKVRLIRANKREGLVRARLLGA 142
Cdd:cd04179    1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGStDGtaEIARELAAR----VPRVRVIRLSRNFGKGAAVRAGF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958286 143 SAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPV----IDVIDWNTFEYLGN 196
Cdd:cd04179   76 KAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSrfvrGGGAGMPLLRRLGS 133
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 66-289 1.58e-08

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.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 54.10  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNeAWSTLLRTVYSVLETSPDILleEVILVDDYS---DREHLKERLanelsglPKVRLIRANKREGLVRARLLGA 142
Cdd:cd04186    1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNAStdgSVELLRELF-------PEVRLIRNGENLGFGAGNNQGI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 143 SAARGDVLTFLDCHCECHEGWLEPLLQRIHEE-ESAVVCPVID----VIDWNTFEylgnsgepQIGGFDwrlvftwhtvp 217
Cdd:cd04186   71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDpDVGIVGPKVSgaflLVRREVFE--------EVGGFD----------- 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958286 218 erERIRMqspvdvirsptmagglfavskkYFEylgsyDTgmevwggenlEFSFRIWQCGGVLETHPCSHVGH 289
Cdd:cd04186  132 --EDFFL----------------------YYE-----DV----------DLCLRARLAGYRVLYVPQAVIYH 164
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 395-502 8.30e-08

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 50.78  E-value: 8.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 395 IVGHQVILYLCHGMGQNQFFEYTSQKEIRynthQPEGCIAVE--AGMDTLIMHLCEETApENQKFILQEDGSLF-HEQSK 471
Cdd:cd23434   18 KAGGTVGLYPCHGTGGNQEWSFTKDGQIK----HDDLCLTVVdrAPGSLVTLQPCREDD-SNQKWEQIENNSKLrHVGSN 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 767958286 472 KCVqAARKESSDSFVplLRDCTNSDH-QKWFF 502
Cdd:cd23434   93 LCL-DSRNAKSGGLT--VETCDPSSGsQQWKF 121
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 62-155 2.56e-07

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 51.05  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  62 PRTSVIIAFYNEAWSTLLRTVYSVLE-TSPDIlleEVILVDDYSDREHLKERLANELSGLPKVRLIRANKREGLVRARLL 140
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAqTYPNW---ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNS 77

                         90
                 ....*....|....*
gi 767958286 141 GASAARGDVLTFLDC 155
Cdd:cd04184   78 ALELATGEFVALLDH 92
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 66-207 3.62e-07

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.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 51.14  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNEAwSTLLRTVYSVLETS-PDILLEeVILVDDYS-DREH-LKERLANElsGLPKVRLIRaNKREGLVR---ARL 139
Cdd:cd04192    1 VVIAARNEA-ENLPRLLQSLSALDyPKEKFE-VILVDDHStDGTVqILEFAAAK--PNFQLKILN-NSRVSISGkknALT 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767958286 140 LGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVC-PVIDVIDWNTFEYLGNsgepqiggFDW 207
Cdd:cd04192   76 TAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAgPVIYFKGKSLLAKFQR--------LDW 136
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 397-500 6.05e-07

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


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 48.48  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 397 GHQVILYLCHGMGqNQFFEYTSQKEIRYNTHqpegCIAVEAGMDT----LIMHLCEETApeNQKFILQEDGSLFHEQSKK 472
Cdd:cd23451   24 GNPVQIYTCNGTA-AQKWTLGTDGTLRVLGK----CLDVSGGGTAngtlVQLWDCNGTG--AQKWVPRADGTLYNPQSGK 96

                         90       100
                 ....*....|....*....|....*...
gi 767958286 473 CVQAARKESSDSFVPLLRDCTNSDHQKW 500
Cdd:cd23451   97 CLDAPGGSTTDGTQLQLYTCNGTAAQQW 124
beta-trefoil_Ricin_GALNT8-like cd23438
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 371-503 6.23e-07

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)-like subfamily; The GALNT8-like subfamily includes GALNT8, GALNT9, GALNT17 and GALNT18. 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. GALNT9 does not glycosylate apomucin or SDC3. 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 is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467316  Cd Length: 134  Bit Score: 48.58  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 371 FFGMLQNKGLTDYCFDYNPpdenqIVGHQVILYLCHGMGQnQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHL---- 446
Cdd:cd23438    4 AYGEMRNSLVTDLCLDQGP-----KENHTAILYPCHGWSP-QLVRYTKDGQLYLGQLGSTASPDTRCLVDDGKSDKpqll 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958286 447 -CEETAPENQK-FILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNsdhQKWFFK 503
Cdd:cd23438   78 dCSKVKNRLQKyWDFSQGGAIQNRATGRCLEVEEDKLNFGHRLVLQTCSG---QKWNIK 133
beta-trefoil_Ricin_GALNT18 cd23475
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 372-500 1.63e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) and similar proteins; GALNT18 (EC 2.4.1.41), also called polypeptide GalNAc transferase 18, GalNAc-T18, polypeptide GalNAc transferase-like protein 4, GalNAc-T-like protein 4, pp-GaNTase-like protein 4, polypeptide N-acetylgalactosaminyltransferase-like protein 4, protein-UDP acetylgalactosaminyltransferase-like protein 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT18 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467353  Cd Length: 142  Bit Score: 47.61  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 372 FGMLQNKGLTDYCFDYNPPDENqivghQVILYLCHGMG-QNQFfeYTSQKEIRYNTHQP------EGCIAVEAGMDTLIM 444
Cdd:cd23475   10 YGVLQNSLKTDLCLDQGPDTDN-----IPIMYICHGMTpQNVY--YTSNQQLHVGILSPtiddddNRCLVDVNSRPRLIE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 445 hlCEETAPENQKFILQ--EDGSLFHEQSKKCVQAarKESSDS---FVPLLRDCTNsdhQKW 500
Cdd:cd23475   83 --CSYAKAKRMKLYWLftQGGSIQNKKSKRCLEL--QENADNefgYQLVLQKCSG---QRW 136
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 66-180 5.66e-06

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 46.84  E-value: 5.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNEAwSTLLRTVYSVLE-TSPDIlleEVILVDDYSDREHLkeRLANELSGLPKVRLIRANKREGLVRARLL--GA 142
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLAlDYPKL---EVIVVDDGSTDDTL--EILEELAALYIRRVLVVRDKENGGKAGALnaGL 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767958286 143 SAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVC 180
Cdd:cd06423   75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAV 112
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 372-500 9.11e-06

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 45.44  E-value: 9.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 372 FGMLQNKGlTDYCFDynPPDENQIVGHQVILYLCHGmGQNQFFEYTSQKEIRY-----NTHQpegCIAVEAGMDT----L 442
Cdd:cd00161    2 TYRIVNAA-SGKCLD--VAGGSTANGAPVQQWTCNG-GANQQWTLTPVGDGYYtirnvASGK---CLDVAGGSTAnganV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958286 443 IMHLCEETApeNQKFILQEDGS----LFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 500
Cdd:cd00161   75 QQWTCNGGD--NQQWRLEPVGDgyyrIVNKHSGKCLDVSGGSTANGANVQQWTCNGGANQQW 134
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 66-180 1.03e-05

DPG_synthase is involved in protein N-linked glycosylation; 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.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 46.41  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNEAwSTLLRTVYSVLETSPDILLE--EVILVDDYSDREHLK--ERLANELSGLpkVRLIRANKREGLVRARLLG 141
Cdd:cd04188    1 VVIPAYNEE-KRLPPTLEEAVEYLEERPSFsyEIIVVDDGSKDGTAEvaRKLARKNPAL--IRVLTLPKNRGKGGAVRAG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767958286 142 ASAARGDVLTFLD-------CHcechegwLEPLLQRIHEEESAVVC 180
Cdd:cd04188   78 MLAARGDYILFADadlatpfEE-------LEKLEEALKTSGYDIAI 116
beta-trefoil_Ricin_GALNT8 cd23472
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 359-500 2.24e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8) and similar proteins; GALNT8 (EC 2.4.1.41), also called polypeptide GalNAc transferase 8, GalNAc-T8, pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, may 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. GALNT8 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467350  Cd Length: 146  Bit Score: 44.42  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 359 YPELhVPEDRPGFFGMLQNKGLTDYCFDYNPpdenqIVGHQVILYLCHGMGQnQFFEYTSQKEI--------RYNTHQpe 430
Cdd:cd23472    1 YPVL-MPIQTIVGYGTMKNSLNENICIDQGP-----VPGNTPIMYGCHGYSP-QFVYYHLTGELyvgglkadIYASDR-- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958286 431 gCIAVEAGMDTLIMHLCEETAPE--NQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNsdhQKW 500
Cdd:cd23472   72 -CLTDPGEGWKPELVSCQDATLKglNMYWDFKQGTAIINRKTKRCLEISLDKTPSYYTLILQTCTG---QKW 139
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 65-277 3.04e-05

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.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 45.25  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  65 SVIIAFYNEAwSTLLRTVYSVLETSPDILleEVILVDDYSDREHLkerlanELSGLPKVRLIRANKreGlvRARLL--GA 142
Cdd:cd02522    2 SIIIPTLNEA-ENLPRLLASLRRLNPLPL--EIIVVDGGSTDGTV------AIARSAGVVVISSPK--G--RARQMnaGA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 143 SAARGDVLTFLdcHCEChegWLEP--LLQRIHEEESavvcpviDVIDWNTFEYLGNSGEPqiggFDWRLVFTWHTvpeRE 220
Cdd:cd02522   69 AAARGDWLLFL--HADT---RLPPdwDAAIIETLRA-------DGAVAGAFRLRFDDPGP----RLRLLELGANL---RS 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 221 RIRmqspvdviRSPTmaG--GLFaVSKKYFEYLGSYDTG--MevwggENLEFSFRIWQCGG 277
Cdd:cd02522  130 RLF--------GLPY--GdqGLF-IRRELFEELGGFPELplM-----EDVELVRRLRRRGR 174
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 66-155 4.17e-05

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 44.39  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNEAWS--TLLRTVYSVLETSPDILleEVILVDDYS-DR--EHLKERLANElsglPKVRLIRANKREGLVRARLL 140
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAVLESLGYDY--EIIFVDDGStDRtlEILRELAARD----PRVKVIRLSRNFGQQAALLA 74

                         90
                 ....*....|....*
gi 767958286 141 GASAARGDVLTFLDC 155
Cdd:cd04187   75 GLDHARGDAVITMDA 89
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 66-179 4.31e-05

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 44.83  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  66 VIIAFYNEAwSTLLRTVYSVLETSPDILLEeVILVDDYS-DRE-HLKERLANELsglPKVRLIRANKREGLVRARLLGAS 143
Cdd:cd06442    1 IIIPTYNER-ENIPELIERLDAALKGIDYE-IIVVDDNSpDGTaEIVRELAKEY---PRVRLIVRPGKRGLGSAYIEGFK 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767958286 144 AARGDVLTFLDC---HcecHEGWLEPLLQRIHEEESAVV 179
Cdd:cd06442   76 AARGDVIVVMDAdlsH---PPEYIPELLEAQLEGGADLV 111
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 65-175 4.54e-05

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 44.81  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286   65 SVIIAFYNEA--WSTLLRTVYSVLETSpdilleEVILVDDYS-DRehlKERLANELsglpKVRLIRANKreGlvRARLL- 140
Cdd:TIGR04283   2 SIIIPVLNEAatLPELLADLQALRGDA------EVIVVDGGStDG---TVEIARSL----GAKVIHSPK--G--RARQMn 64

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767958286  141 -GASAARGDVLTFLdcHCEC--HEGWLEPLLQRIHEEE 175
Cdd:TIGR04283  65 aGAALAKGDILLFL--HADTrlPKDFLEAIRRALAKPG 100
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 49-154 7.02e-05

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 44.50  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  49 FRCKEKKYDYDNLPRTSVIIAFYNEAwSTLLRTVYSVLETS-PDILLeEVILVDDYSD-------REHLKERlanelsgl 120
Cdd:cd06439   16 RPKPPSLPDPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDyPRDRL-EIIVVSDGSTdgtaeiaREYADKG-------- 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767958286 121 pkVRLIRANKREGLVRARLLGASAARGDVLTFLD 154
Cdd:cd06439   86 --VKLLRFPERRGKAAALNRALALATGEIVVFTD 117
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 65-272 7.33e-05

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 44.58  E-value: 7.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286   65 SVIIAFYN-EAWSTLLRTVysVLETSPDILLEEVILVDDYSdrehlKERLANELSGLPKVRLIRANKRE-----GLVRAR 138
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERI--LNQTFQYDPEFELIIINDGS-----TDKTLEEVSSIKDHNLQVYYPNApdttySLAASR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  139 LLGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEE------ESAVVCPVIDVIDWNTfEYLGNSGEpqiggfdwrlvFT 212
Cdd:pfam10111  74 NRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLalqeniQAAVVLPVTDLNDESS-NFLRRGGD-----------LT 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  213 WHTVPERERIRMQSPVDVIRSPTmaGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRI 272
Cdd:pfam10111 142 ASGDVLRDLLVFYSPLAIFFAPN--SSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
beta-trefoil_Ricin_GALNT17 cd23474
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 372-503 9.30e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 17 (GALNT17) and similar proteins; GALNT17 (EC 2.4.1.41), also called polypeptide GalNAc transferase-like protein 3, GalNAc-T-like protein 3, pp-GaNTase-like protein 3, protein-UDP acetylgalactosaminyltransferase-like protein 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3, or Williams-Beuren syndrome chromosomal region 17 protein, may 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. GALNT17 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467352  Cd Length: 142  Bit Score: 42.58  E-value: 9.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 372 FGMLQNKGLTDYCFDYNPPdENqivgHQVILYLCHGMGQnQFFEYTSQKEIRY-----NTHQPEGCIAVEAGMDTLIMHL 446
Cdd:cd23474   10 YGELRNNKAKDVCLDQGPP-EN----HTAILYPCHGWGP-QLARYTKEGYLHLgalgtTTLLPDTRCLVDNKKSRFPQLL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958286 447 -CEETAPENQK---FIlqEDGSLFHEQSKKCVQAARKeSSDSFVPLLRDCTNsdhQKWFFK 503
Cdd:cd23474   84 dCDKVKSILHKrwnFI--QNGAIMNLGTGRCLEVENR-GNFGIDLILRSCTG---QRWTIK 138
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 381-456 3.41e-04

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 40.40  E-value: 3.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958286 381 TDYCFDynppDENQIVGHQVILYLCHGMGQNQFFEY-TSQKEIRYNTHQpeGCIAVEAGMDTLIMHLCEETAPeNQK 456
Cdd:cd23439   54 RKVCFD----VSSHTPGAPVILYACHGMKGNQLWKYrPNTKQLYHPVSG--LCLDADPGSGKVFMNHCDESSD-TQK 123
beta-trefoil_Ricin_GALNT9 cd23473
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 372-503 6.29e-04

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 9 (GALNT9) and similar proteins; GALNT9 (EC 2.4.1.41), also called polypeptide GalNAc transferase 9, GalNAc-T9, pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, 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. GALNT9 does not glycosylate apomucin or SDC3. GALNT9 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467351  Cd Length: 145  Bit Score: 40.33  E-value: 6.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 372 FGMLQNKGLTDYCFDYNPPDENQivghqVILYLCHGMgQNQFFEYTSQKEIRYN-----THQPEG-CIAVEAGMDTLIMH 445
Cdd:cd23473   10 YGEVRNSKASGYCLDQGSEEDDK-----AILYPCHGM-SSQLVRYSTEGLLQLGplgstAFLPDTkCLVDDGRGRTPTLK 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 446 LCEETAPENQKFI-LQEDGSLFHEQSKKCVQAA-RKESSDSFVPLLRDCTNsdhQKWFFK 503
Cdd:cd23473   84 KCEDVARPAQRLWdFTQNGPIISRDTGRCLEVEmSKDANFGLRLVVQRCSG---QKWMIR 140
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 62-154 8.36e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 41.57  E-value: 8.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  62 PRTSVIIAFYNeAWSTLLRTVYSVLETSPDILleEVILVDDYSDrEHLKERLANELSGLPKVRLIrANKREGLVRARLLG 141
Cdd:PRK10073   6 PKLSIIIPLYN-AGKDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTG 80

                         90
                 ....*....|...
gi 767958286 142 ASAARGDVLTFLD 154
Cdd:PRK10073  81 LAVATGKYVAFPD 93
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 232-284 1.18e-03

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.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 37.59  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767958286  232 RSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPC 284
Cdd:pfam02709  15 PYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG 67
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 64-156 1.39e-03

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 40.32  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286  64 TSVIIAFYNEAWSTLLRTVYSVLETSPDilleEVILVDDySDREHLKERLANELsGLPKVRLI---RANKREGLVRarll 140
Cdd:cd06434    2 VTVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTD-GDDEPYLSILSQTV-KYGGIFVItvpHPGKRRALAE---- 71

                         90
                 ....*....|....*.
gi 767958286 141 GASAARGDVLTFLDCH 156
Cdd:cd06434   72 GIRHVTTDIVVLLDSD 87
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 397-500 2.05e-03

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 38.46  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958286 397 GHQVILYLCHGmGQNQFFEYTSQK----EIRYNTHQPegCIAVEAG--MDTLIMHL--CEETApeNQKFILQEDGSLFHE 468
Cdd:cd23458   24 GANIQQWDCGS-GSNQQWTLVEIDngyyRIKASHSGK--CLDVAGGstANGANIQQwdCVGGA--NQQWKLQDLGNGYFE 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767958286 469 ----QSKKCVQAARKESSDSFVPLLRDCTNSDHQKW 500
Cdd:cd23458   99 lkarHSGKCLDVAGGSTANGASIQQWTCNGNDNQRF 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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