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Conserved domains on  [gi|60498976|ref|NP_078848|]
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polypeptide N-acetylgalactosaminyltransferase 14 isoform 1 [Homo sapiens]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

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 ...
 114-408 0e+00

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: 512.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 114 SIIITFHNEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQL-----IKLPKVKCLRNNERQGLVRSRIRGAD 188
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 189 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESASELRGGFDWSLHFQWEQLSPEQKaRR 268
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 269 LDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFR-KKHPYVFPDGN 347
Cdd:cd02510 160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60498976 348 aNTYIKNTKRTAEVWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIY 408
Cdd:cd02510 240 -GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 413-552 3.65e-92

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


:

Pssm-ID: 467356  Cd Length: 140  Bit Score: 278.29  E-value: 3.65e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 413 IPKESSIQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVL 492
Cdd:cd23478   1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 493 CKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCESSLMSQHWDMVSS 552
Cdd:cd23478  81 CKEGDGKQRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 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 ...
 114-408 0e+00

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: 512.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 114 SIIITFHNEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQL-----IKLPKVKCLRNNERQGLVRSRIRGAD 188
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 189 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESASELRGGFDWSLHFQWEQLSPEQKaRR 268
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 269 LDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFR-KKHPYVFPDGN 347
Cdd:cd02510 160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60498976 348 aNTYIKNTKRTAEVWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIY 408
Cdd:cd02510 240 -GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 413-552 3.65e-92

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467356  Cd Length: 140  Bit Score: 278.29  E-value: 3.65e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 413 IPKESSIQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVL 492
Cdd:cd23478   1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 493 CKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCESSLMSQHWDMVSS 552
Cdd:cd23478  81 CKEGDGKQRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 140
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 114-289 3.74e-30

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: 115.96  E-value: 3.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   114 SIIITFHNEArSTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLIKL-PKVKCLRNNERQGLVRSRIRGADIA 190
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEEYAKKdPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   191 QGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIesaselrggfdWSLHFQWEQLSPEQKARRLD 270
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRLLG 146

                         170
                  ....*....|....*....
gi 60498976   271 PTEPIRTPIIAGGLFVIDK 289
Cdd:pfam00535 147 LNLPFLIGGFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
422-547 1.03e-22

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 93.75  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   422 GNIRQRQ--KCLESQRQNNQETPnLKLSPCAKVKGEdaksQVWAFTYTQQI--LQEELCLSVITLFPGAPVVLVLCKNGD 497
Cdd:pfam00652   3 GRIRNRAsgKCLDVPGGSSAGGP-VGLYPCHGSNGN----QLWTLTGDGTIrsVASDLCLDVGSTADGAKVVLWPCHPGN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 60498976   498 DRQQW--TKTGSHIEHIASHLCLDTDMFGDGTENgkeIVVNPCESSLMSQHW 547
Cdd:pfam00652  78 GNQRWryDEDGTQIRNPQSGKCLDVSGAGTSNGK---VILWTCDSGNPNQQW 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 111-225 2.12e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 78.21  E-value: 2.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 111 PPTSIIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSndPDDCKQLI-----KLPKVKCLRNNERQGLVRSRIR 185
Cdd:COG0463   2 PLVSVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGS--TDGTAEILrelaaKDPRIRVIRLERNRGKGAARNA 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 60498976 186 GADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVC 225
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 428-547 3.69e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 45.97  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976    428 QKCLESQRQNNqetpNLKLSPCakvkGEDAKSQVWAFTYTQQI--LQEELCLSVITLfPGAPVVLVLCKNGDDRQQWT-- 503
Cdd:smart00458   7 GKCLDVNGNKN----PVGLFDC----HGTGGNQLWKLTSDGAIriKDTDLCLTANGN-TGSTVTLYSCDGTNDNQYWEvn 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 60498976    504 KTGShIEHIASHLCLdtDMFGDGTenGKEIVVNPCESSLmSQHW 547
Cdd:smart00458  78 KDGT-IRNPDSGKCL--DVKDGNT--GTKVILWTCSGNP-NQKW 115
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 114-210 1.57e-03

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: 40.19  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   114 SIIITFHNEARsTLLRTIRSVLNRTPTHlirEIILVDDFSndPDDCKQLIKLPKVKCLRNNerQGlvRSR--IRGADIAQ 191
Cdd:TIGR04283   2 SIIIPVLNEAA-TLPELLADLQALRGDA---EVIVVDGGS--TDGTVEIARSLGAKVIHSP--KG--RARqmNAGAALAK 71

                          90
                  ....*....|....*....
gi 60498976   192 GTTLTFLDSHCEVNRDWLQ 210
Cdd:TIGR04283  72 GDILLFLHADTRLPKDFLE 90
 
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 ...
 114-408 0e+00

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: 512.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 114 SIIITFHNEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQL-----IKLPKVKCLRNNERQGLVRSRIRGAD 188
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 189 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESASELRGGFDWSLHFQWEQLSPEQKaRR 268
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 269 LDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFR-KKHPYVFPDGN 347
Cdd:cd02510 160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60498976 348 aNTYIKNTKRTAEVWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIY 408
Cdd:cd02510 240 -GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 413-552 3.65e-92

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. GALNT14 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467356  Cd Length: 140  Bit Score: 278.29  E-value: 3.65e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 413 IPKESSIQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVL 492
Cdd:cd23478   1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 493 CKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCESSLMSQHWDMVSS 552
Cdd:cd23478  81 CKEGDGKQRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 140
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 419-549 8.67e-44

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 151.40  E-value: 8.67e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 419 IQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKgedaKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVLCKNgDD 498
Cdd:cd23441   3 LAYGQIKQGNLCLDSDEQLFQGPALLILAPCSNSS----DSQEWSFTKDGQLQTQGLCLTVDSSSKDLPVVLETCSD-DP 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 60498976 499 RQQWTKTGSHIEHIASHLCLDTDMFgdgtengKEIVVNPCESSLMSQHWDM 549
Cdd:cd23441  78 KQKWTRTGRQLVHSESGLCLDSRKK-------KGLVVSPCRSGAPSQKWDF 121
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 114-289 3.74e-30

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: 115.96  E-value: 3.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   114 SIIITFHNEArSTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLIKL-PKVKCLRNNERQGLVRSRIRGADIA 190
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEEYAKKdPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   191 QGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIesaselrggfdWSLHFQWEQLSPEQKARRLD 270
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRLLG 146

                         170
                  ....*....|....*....
gi 60498976   271 PTEPIRTPIIAGGLFVIDK 289
Cdd:pfam00535 147 LNLPFLIGGFALYRREALE 165
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 414-549 4.07e-23

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT16 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467357  Cd Length: 129  Bit Score: 94.87  E-value: 4.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 414 PKESSIqKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTyTQQILQEELCLSVITLFPGAPVVLVLC 493
Cdd:cd23479   1 PEKEAI-PGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLS-DPLIRQQDKCLAITSFSPGSKVILELC 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 60498976 494 KNGDDRQQWTKTGSHIEHIASHLCLDtdmfgdgTENGKeIVVNPCESSLMSQHWDM 549
Cdd:cd23479  79 NQKDGRQKWKLKGSFIQHQVSGLCLD-------SQSGR-VVINQCQADLASQQWEL 126
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
422-547 1.03e-22

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 93.75  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   422 GNIRQRQ--KCLESQRQNNQETPnLKLSPCAKVKGEdaksQVWAFTYTQQI--LQEELCLSVITLFPGAPVVLVLCKNGD 497
Cdd:pfam00652   3 GRIRNRAsgKCLDVPGGSSAGGP-VGLYPCHGSNGN----QLWTLTGDGTIrsVASDLCLDVGSTADGAKVVLWPCHPGN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 60498976   498 DRQQW--TKTGSHIEHIASHLCLDTDMFGDGTENgkeIVVNPCESSLMSQHW 547
Cdd:pfam00652  78 GNQRWryDEDGTQIRNPQSGKCLDVSGAGTSNGK---VILWTCDSGNPNQQW 126
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 422-548 5.26e-19

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: 82.75  E-value: 5.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 422 GNIRQRQKCLESQRQNNQETPNLklSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVLCKNGDDRQQ 501
Cdd:cd23434   3 GSLKQGNLCLDTLGHKAGGTVGL--YPCHGTGG----NQEWSFTKDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQK 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 60498976 502 W--TKTGSHIEHIASHLCLDTDmfgdgTENGKEIVVNPCESSLMSQHWD 548
Cdd:cd23434  77 WeqIENNSKLRHVGSNLCLDSR-----NAKSGGLTVETCDPSSGSQQWK 120
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 111-225 2.12e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 78.21  E-value: 2.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 111 PPTSIIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSndPDDCKQLI-----KLPKVKCLRNNERQGLVRSRIR 185
Cdd:COG0463   2 PLVSVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGS--TDGTAEILrelaaKDPRIRVIRLERNRGKGAARNA 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 60498976 186 GADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVC 225
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 422-549 2.50e-15

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: 72.48  E-value: 2.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 422 GNIR--QRQKCLESQRQNNQEtPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVitlFPGAPVVLVLCKNGDDR 499
Cdd:cd23460   3 GQIKhtESGLCLDWAGESNGD-KTVALKPCHGGGG----NQFWMYTGDGQIRQDHLCLTA---DEGNKVTLRECADQLPS 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 60498976 500 QQW--TKTGSHIEHIASHLCLDTDMfgdgteNGKEIVVNPCESSLMSQHWDM 549
Cdd:cd23460  75 QEWsyDEKTGTIRHRSTGLCLTLDA------NNDVVILKECDSNSLWQKWIF 120
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 115-219 3.92e-15

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: 72.92  E-value: 3.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 115 IIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLIKL-PKVKCLRNNERQGLVRSRIRGADIAQ 191
Cdd:cd00761   1 VIIPAYNEEP-YLERCLESLLAQTYPNF--EVIVVDDGSTDgtLEILEEYAKKdPRVIRVINEENQGLAAARNAGLKAAR 77

                        90       100
                ....*....|....*....|....*...
gi 60498976 192 GTTLTFLDSHCEVNRDWLQPLLHRVKED 219
Cdd:cd00761  78 GEYILFLDADDLLLPDWLERLVAELLAD 105
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 109-213 8.82e-15

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: 75.16  E-value: 8.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 109 DLPPTSIIITFHNEARsTLLRTIRSVLNRTPTHLIREIILVDDFSNDP--DDCKQLI-KLPKVKCLRNNERQGLVRSRIR 185
Cdd:COG1215  27 DLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDEtaEIARELAaEYPRVRVIERPENGGKAAALNA 105

                        90       100
                ....*....|....*....|....*...
gi 60498976 186 GADIAQGTTLTFLDSHCEVNRDWLQPLL 213
Cdd:COG1215 106 GLKAARGDIVVFLDADTVLDPDWLRRLV 133
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
111-214 1.59e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 72.33  E-value: 1.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 111 PPTSIIITFHNEArSTLLRTIRSVLNRTPTHLirEIILVDDFSNDP--DDCKQLiKLPKVKCLRNNERQGLVRSRIRGAD 188
Cdd:COG1216   3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGtaELLAAL-AFPRVRVIRNPENLGFAAARNLGLR 78

                        90       100
                ....*....|....*....|....*.
gi 60498976 189 IAQGTTLTFLDSHCEVNRDWLQPLLH 214
Cdd:COG1216  79 AAGGDYLLFLDDDTVVEPDWLERLLA 104
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 429-547 7.93e-14

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: 68.14  E-value: 7.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 429 KCLESQrQNNQETPnLKLSPCakVKGEDAKSQVWAFTYTQQILQE--ELCLSVITLFPGAPVVLVLCKNGDDRQQWT--K 504
Cdd:cd23439  12 LCIDTK-HGGENDE-VRLSKC--VKDGGGGEQQFELTWHEDIRPKkrKVCFDVSSHTPGAPVILYACHGMKGNQLWKyrP 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 60498976 505 TGSHIEHIASHLCLDTDmfgdgtENGKEIVVNPCESSLMSQHW 547
Cdd:cd23439  88 NTKQLYHPVSGLCLDAD------PGSGKVFMNHCDESSDTQKW 124
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 428-549 2.22e-12

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: 64.26  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 428 QKCLESQ-RQNNQetpNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITlfPGAPVVLVLCKNGDDRQQWT--K 504
Cdd:cd23433  15 NLCLDTMgRKAGE---KVGLSSCHGQGG----NQVFSYTAKGEIRSDDLCLDASR--KGGPVKLEKCHGMGGNQEWEydK 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 60498976 505 TGSHIEHIASHLCLDTdmfgDGTENGKEIVVNPCESSlMSQHWDM 549
Cdd:cd23433  86 ETKQIRHVNSGLCLTA----PNEDDPNEPVLRPCDGG-PSQKWEL 125
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 430-547 5.35e-12

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: 63.11  E-value: 5.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 430 CLESQRQNNQETPNLKLSPCAKVKgedAKSQVWAFTYTQQILQEELCLSViTLFPGAPVVLVLC-KNGDDRQQWTKT-GS 507
Cdd:cd23459  18 CLDTLQRDEDKGYNLGLYPCQGGL---SSNQLFSLSKKGELRREESCADV-QGTEESKVILITChGLEKFNQKWKHTkGG 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 60498976 508 HIEHIASHLCLDTdmfgDGTENGKEIVVNPCESSLmSQHW 547
Cdd:cd23459  94 QIVHLASGKCLDA----EGLKSGDDVTLAKCDGSL-SQKW 128
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 422-549 1.13e-11

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: 61.93  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 422 GNIRQRQ--KCLESQrqNNQETPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITlfPGAPVVLVLCkNGDDR 499
Cdd:cd23437   6 GEIRNLGtgLCLDTM--GHQNGGPVGLYPCHGMGG----NQLFRLNEAGQLAVGEQCLTASG--SGGKVKLRKC-NLGET 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 60498976 500 QQW--TKTGSHIEHIASHLCLDTdmfgdgTENGKEIVVNPCESSLMSQHWDM 549
Cdd:cd23437  77 GKWeyDEATGQIRHKGTGKCLDL------NEGTNKLILQPCDSSSPSQKWEF 122
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 418-549 1.53e-11

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467318 [Multi-domain]  Cd Length: 127  Bit Score: 61.62  E-value: 1.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 418 SIQKGNIRQRQ--KCLESQRQNNQETPNLKLSPCAKvkgeDAKSQVWAFTYTQQI-LQEELCLSVITlFPGAPVVLVLCK 494
Cdd:cd23440   2 VIRKGQLKHAGsgLCLVAEDEVSQKGSLLVLRPCSR----NDKKQLWYYTEDGELrLANLLCLDSSE-TSSDFPRLMKCH 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 60498976 495 NGDDRQQWT-KTGSHIEHIASHLCLdtdmFGDGTENGKEIVVNPCESSLmSQHWDM 549
Cdd:cd23440  77 GSGGSQQWRfKKDNRLYNPASGQCL----AASKNGTSGYVTMDICSDSP-SQKWVF 127
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 425-547 1.23e-09

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


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 56.61  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 425 RQRQKCLESQRQNNQETPNLKLSPCAkvkgeDAKSQVWAFT------YTQQILQEELCLSV--ITLFPGAPVVLVLCkNG 496
Cdd:cd00161   8 AASGKCLDVAGGSTANGAPVQQWTCN-----GGANQQWTLTpvgdgyYTIRNVASGKCLDVagGSTANGANVQQWTC-NG 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 60498976 497 DDRQQWTKT-----GSHIEHIASHLCLDTDmfGDGTENGKEIVVNPCESSLmSQHW 547
Cdd:cd00161  82 GDNQQWRLEpvgdgYYRIVNKHSGKCLDVS--GGSTANGANVQQWTCNGGA-NQQW 134
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 418-547 2.90e-09

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: 55.06  E-value: 2.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 418 SIQKGNIRQR--QKCLESQRQNNQETPNLKLSPCAKVKGEdaksQVWAFTYTQQILQEELCLSV------ITLFPgapvv 489
Cdd:cd23462   2 ALAYGEIRNLagKLCLDAPGRKKELNKPVGLYPCHGQGGN----QYWMLTKDGEIRRDDLCLDYaggsgdVTLYP----- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60498976 490 lvlCKNGDDRQQWT---KTGsHIEHIASHLCLDTDmfgdgtENGKEIVVNPCESSLMSQHW 547
Cdd:cd23462  73 ---CHGMKGNQFWIydeETK-QIVHGTSKKCLELS------DDSSKLVMEPCNGSSPRQQW 123
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 114-336 7.44e-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: 56.47  E-value: 7.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 114 SIIITFHNEARsTLLRTIRSVLNRTPTHLIREIILVDDFSND--PDDCKQLIKL-PKVKcLRNNERQGLVRSRIRGADIA 190
Cdd:cd02525   3 SIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVDGGSTDgtREIVQEYAAKdPRIR-LIDNPKRIQSAGLNIGIRNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 191 QGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIES-ASELRGGFDWSLHfqweqlspEQKARRL 269
Cdd:cd02525  81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAvAQSSPLGSGGSAY--------RGGAVKI 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60498976 270 DPTEPirtpiIAGGLFviDKAWFDYLGKYDMDMDIwgGENFEISFRVWMCGGSLEIVPCSRVGHVFR 336
Cdd:cd02525 153 GYVDT-----VHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 115-255 3.08e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 54.60  E-value: 3.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 115 IIITFHNEARsTLLRTIRSVLNRT-PTHLIrEIILVDDFSNDpdDCKQLIKL------PKVKCLRNNERQGlvrSRIR-- 185
Cdd:cd04192   1 VVIAARNEAE-NLPRLLQSLSALDyPKEKF-EVILVDDHSTD--GTVQILEFaaakpnFQLKILNNSRVSI---SGKKna 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 186 ---GADIAQGTTLTFLDSHCEVNRDWLQPLL-HRVKEDYTRVVCPVIDIIN---LDTFTYIESASEL---RGGFDWSLHF 255
Cdd:cd04192  74 lttAIKAAKGDWIVTTDADCVVPSNWLLTFVaFIQKEQIGLVAGPVIYFKGkslLAKFQRLDWLSLLgliAGSFGLGKPF 153
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 419-547 4.40e-08

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: 51.95  E-value: 4.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 419 IQKGNIRQR--QKCLESQRQNNQETPNLKLSPCakvKGEDaKSQVWAFTYTQQIL---QEELCLSVItlfPGAPVVLVLC 493
Cdd:cd23435   2 GYYGALRNKgsELCLDVNNPNGQGGKPVIMYGC---HGLG-GNQYFEYTSKGEIRhniGKELCLHAS---GSDEVILQHC 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 60498976 494 ----KNGDDRQQWTKT-GSHIEHIASHLCLDTdmfgdgteNGKEIVVNPCESSLMSQHW 547
Cdd:cd23435  75 tskgKDVPPEQKWLFTqDGTIRNPASGLCLHA--------SGYKVLLRTCNPSDDSQKW 125
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
475-548 1.84e-07

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 50.22  E-value: 1.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60498976   475 LCLSVITLFP-GAPVVLVLCKNGDDRQQWTKTGS-HIEHIASHLCLDTDmfgdGTENGKEIVVNPCESSLMSQHWD 548
Cdd:pfam00652  12 KCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDgTIRSVASDLCLDVG----STADGAKVVLWPCHPGNGNQRWR 83
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 115-333 5.01e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 49.87  E-value: 5.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 115 IIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLikLPKVKCLRNNERQGLVRSRIRGADIAQG 192
Cdd:cd04186   1 IIIVNYNSLE-YLKACLDSLLAQTYPDF--EVIVVDNASTDgsVELLREL--FPEVRLIRNGENLGFGAGNNQGIREAKG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 193 TTLTFLDSHCEVNRDWLQPLLhrvkedytrvvcpvidiinldtftyiesaselrggfdwslhfqweqlspeqKARRLDPT 272
Cdd:cd04186  76 DYVLLLNPDTVVEPGALLELL---------------------------------------------------DAAEQDPD 104

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60498976 273 EPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWgGENFEISFRVWMCGGSLEIVPCSRVGH 333
Cdd:cd04186 105 VGIVGPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 115-200 1.30e-06

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: 48.72  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 115 IIITFHNEARstllrTIRSVLNRTPTHLIR----EIILVDDFSndPDDCKQLIK-----LPKVKCLRNNERQGLVRSRIR 185
Cdd:cd04179   1 VVIPAYNEEE-----NIPELVERLLAVLEEgydyEIIVVDDGS--TDGTAEIARelaarVPRVRVIRLSRNFGKGAAVRA 73

                        90
                ....*....|....*
gi 60498976 186 GADIAQGTTLTFLDS 200
Cdd:cd04179  74 GFKAARGDIVVTMDA 88
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 428-547 3.69e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 45.97  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976    428 QKCLESQRQNNqetpNLKLSPCakvkGEDAKSQVWAFTYTQQI--LQEELCLSVITLfPGAPVVLVLCKNGDDRQQWT-- 503
Cdd:smart00458   7 GKCLDVNGNKN----PVGLFDC----HGTGGNQLWKLTSDGAIriKDTDLCLTANGN-TGSTVTLYSCDGTNDNQYWEvn 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 60498976    504 KTGShIEHIASHLCLdtDMFGDGTenGKEIVVNPCESSLmSQHW 547
Cdd:smart00458  78 KDGT-IRNPDSGKCL--DVKDGNT--GTKVILWTCSGNP-NQKW 115
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 114-210 1.31e-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: 46.41  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 114 SIIITFHNEARsTLLRTIRSVLNRTPthLIREIILVDDFSNDpdDCKQLIKLPKVKCLRnnERQGlvRSR--IRGADIAQ 191
Cdd:cd02522   2 SIIIPTLNEAE-NLPRLLASLRRLNP--LPLEIIVVDGGSTD--GTVAIARSAGVVVIS--SPKG--RARqmNAGAAAAR 72

                        90
                ....*....|....*....
gi 60498976 192 GTTLTFLDSHCEVNRDWLQ 210
Cdd:cd02522  73 GDWLLFLHADTRLPPDWDA 91
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 115-302 1.91e-05

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: 45.30  E-value: 1.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 115 IIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDfsNDPDDCKQLIK------LPKVKCLRNNERQGLVRSRIRGAD 188
Cdd:cd06423   1 IIVPAYNEEA-VIERTIESLLALDYPKL--EVIVVDD--GSTDDTLEILEelaalyIRRVLVVRDKENGGKAGALNAGLR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 189 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDyTRV--VCPVIDIIN-----LDTFTYIESASelrgGFDWSLHFQWeqls 261
Cdd:cd06423  76 HAKGDIVVVLDADTILEPDALKRLVVPFFAD-PKVgaVQGRVRVRNgsenlLTRLQAIEYLS----IFRLGRRAQS---- 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 60498976 262 peqkarRLDptepiRTPIIAGGLFVIDKAWFDYLGKYDMDM 302
Cdd:cd06423 147 ------ALG-----GVLVLSGAFGAFRREALREVGGWDEDT 176
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 428-521 6.53e-05

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 42.58  E-value: 6.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 428 QKCLesqrQNNQETPNLKLSPCakvkGEDAKSQVWAFTYTQQILQEE--LCLSVITLFPGAPVVLVLCKNGDDRQQWT-- 503
Cdd:cd23385  11 GKCL----AARSSSSKVSLSTC----NPNSPNQQWKWTSGHRLFNVGtgKCLGVSSSSPSSPLRLFECDSEDELQKWKcs 82

                        90
                ....*....|....*....
gi 60498976 504 -KTGSHIEHIASHLCLDTD 521
Cdd:cd23385  83 kDGLLLLKGLGLLLLYDKS 101
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 472-548 1.09e-04

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 41.81  E-value: 1.09e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60498976 472 QEELCLSVITlfPGAPVVLVLCKNGDDRQQWTKTGSH-IEHIASHLCLDTDmfgdGTENGKEIVVNPCESSLMSQHWD 548
Cdd:cd23385   9 DLGKCLAARS--SSSKVSLSTCNPNSPNQQWKWTSGHrLFNVGTGKCLGVS----SSSPSSPLRLFECDSEDELQKWK 80
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 115-174 3.41e-04

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: 41.69  E-value: 3.41e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60498976 115 IIITFHNEARS--TLLRTIRSVLNRTptHLIREIILVDDFSndPDDCKQLIK-----LPKVKCLRNN 174
Cdd:cd04187   1 IVVPVYNEEENlpELYERLKAVLESL--GYDYEIIFVDDGS--TDRTLEILRelaarDPRVKVIRLS 63
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 421-503 3.78e-04

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: 40.39  E-value: 3.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 421 KGNIR---QRQKCLEsqrqnNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEE--LCLSVITLFpgapVVLVLCKN 495
Cdd:cd23435  48 KGEIRhniGKELCLH-----ASGSDEVILQHCTSKGKDVPPEQKWLFTQDGTIRNPAsgLCLHASGYK----VLLRTCNP 118


                ....*...
gi 60498976 496 GDDRQQWT 503
Cdd:cd23435 119 SDDSQKWT 126
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
 476-549 4.01e-04

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467341  Cd Length: 136  Bit Score: 40.88  E-value: 4.01e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60498976 476 CLSVI--TLFPGAPVVLvLCKNGDDRQQW--TKTGSHIEHIASHLCLDtdMFGDGTENGKEIVVNPCESSLMSQHWDM 549
Cdd:cd23463  59 CLDVIggKDNPGSKVAL-WTEHGKTHQKWriNEDGTISSHLSDDLVLD--LKGGNYYDKDHLIVNNPEEDQQTQKWDI 133
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 469-549 4.96e-04

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: 40.00  E-value: 4.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 469 QILQEELCLSVITLFPGAPVVLVLCKNGDDRQQW--TKTGsHIEHiaSHLCLDTDmfgDGTEnGKEIVVNPCESSLMSQH 546
Cdd:cd23434   4 SLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWsfTKDG-QIKH--DDLCLTVV---DRAP-GSLVTLQPCREDDSNQK 76


                ...
gi 60498976 547 WDM 549
Cdd:cd23434  77 WEQ 79
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 422-547 7.07e-04

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: 40.01  E-value: 7.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 422 GNIR--QRQKCLESQrqNNQETPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITLfpGAPVVLVLCKNGDDR 499
Cdd:cd23467   7 GEIRnvETNQCLDNM--GRKENEKVGIFNCHGMGG----NQVFSYTADKEIRTDDLCLDVSRL--NGPVVMLKCHHMRGN 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 60498976 500 QQWTKTGSH--IEHIASHLCLDtdmfGDGTENGKEIVVNPCESSlMSQHW 547
Cdd:cd23467  79 QLWEYDAERltLRHVNSNQCLD----EPSEEDKMVPTMKDCSGS-RSQQW 123
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 280-340 7.39e-04

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: 38.36  E-value: 7.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60498976   280 IAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCsRVGHVFRKKHP 340
Cdd:pfam02709  19 YFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLYHK 78
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 422-547 1.03e-03

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: 39.26  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 422 GNIR--QRQKCLESQRQnnQETPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITLfpGAPVVLVLCKNGDDR 499
Cdd:cd23466   7 GEIRnvETNQCLDNMAR--KENEKVGIFNCHGMGG----NQVFSYTANKEIRTDDLCLDVSKL--NGPVMMLKCHHLKGN 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 60498976 500 QQWT--KTGSHIEHIASHLCLDTDMfgdgTENGKEIVVNPCESSlMSQHW 547
Cdd:cd23466  79 QLWEydPVKLTLLHVNSNQCLDKAT----EEDSQVPSIRDCNGS-RSQQW 123
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 114-210 1.57e-03

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: 40.19  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   114 SIIITFHNEARsTLLRTIRSVLNRTPTHlirEIILVDDFSndPDDCKQLIKLPKVKCLRNNerQGlvRSR--IRGADIAQ 191
Cdd:TIGR04283   2 SIIIPVLNEAA-TLPELLADLQALRGDA---EVIVVDGGS--TDGTVEIARSLGAKVIHSP--KG--RARqmNAGAALAK 71

                          90
                  ....*....|....*....
gi 60498976   192 GTTLTFLDSHCEVNRDWLQ 210
Cdd:TIGR04283  72 GDILLFLHADTRLPKDFLE 90
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 420-503 1.60e-03

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 38.65  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976    420 QKGNIR--QRQKCLESQRQNNQetpNLKLSPCAKvkgeDAKSQVWAFTYTQQI--LQEELCLSVITLFPGAPVVLVLCkN 495
Cdd:smart00458  37 SDGAIRikDTDLCLTANGNTGS---TVTLYSCDG----TNDNQYWEVNKDGTIrnPDSGKCLDVKDGNTGTKVILWTC-S 108


                   ....*...
gi 60498976    496 GDDRQQWT 503
Cdd:smart00458 109 GNPNQKWI 116
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 444-547 2.09e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 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: 467354  Cd Length: 150  Bit Score: 38.79  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 444 LKLSPCAKVKGEDA--KSQVWAFTYTQQIL------QEELCLSVITlfPGAPVVLVLCKNGDDRQQWT-KTGSHIEHIAS 514
Cdd:cd23476  30 LRLEGCVKGRGEAAwnNGQVFTFGWREDIRpgdpqhTKKFCFDAIS--HNSPVTLYDCHGMKGNQLWRyRKDKTLYHPVS 107

                        90       100       110
                ....*....|....*....|....*....|...
gi 60498976 515 HLCLDTdmfgdgTENGKEIVVNPCESSLMSQHW 547
Cdd:cd23476 108 NSCMDC------SESDHRIFMNTCNPSSPTQQW 134
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 484-547 2.33e-03

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: 38.48  E-value: 2.33e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60498976 484 PGAPVVLVLCKNGDDrQQWTKTGSHIEHIASHLCLDTDmfGDGTENGKEIVVNPCESSLmSQHW 547
Cdd:cd23418  26 NGTRLILWDCHGGAN-QQFTFTSAGELRVGGDKCLDAA--GGGTTNGTPVVIWPCNGGA-NQKW 85
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 114-327 2.36e-03

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: 39.95  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   114 SIIITFHN-EARSTLLRTIRsvLNRTPTHLIREIILVDDFSNDP--DDCKQLIKLPKVKCLRNNERQ--GLVRSRIRGAD 188
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERIL--NQTFQYDPEFELIIINDGSTDKtlEEVSSIKDHNLQVYYPNAPDTtySLAASRNRGTS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   189 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTR------VVCPVIDIINldtftyiESASELRGGFD--WSLHFQWEQL 260
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFEKQLKIATSLALQeniqaaVVLPVTDLND-------ESSNFLRRGGDltASGDVLRDLL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60498976   261 SPEqkarrlDPTEPIRTPiiAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVP 327
Cdd:pfam10111 152 VFY------SPLAIFFAP--NSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRLAARYPFVAVMP 210
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 114-218 2.39e-03

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: 39.49  E-value: 2.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 114 SIIITFHNEARSTLLRTIRSVLNRTPTHLirEIILVDDFSNDPDDCKQLIKL----PKVKCLRNNERQGLVRSRIRGADI 189
Cdd:cd04184   4 SIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYaaqdPRIKVVFREENGGISAATNSALEL 81

                        90       100       110
                ....*....|....*....|....*....|.
gi 60498976 190 AQGTTLTFLDshcevNRDWLQP--LLHRVKE 218
Cdd:cd04184  82 ATGEFVALLD-----HDDELAPhaLYEVVKA 107
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 111-338 2.97e-03

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 39.28  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   111 PPTSIIITFHNEArSTLLRTIRSVLNRTptHLIREIILVDDFSND--PDDCKQLIKLP---KVKCLRNNERQGL---VRS 182
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQP--YPPVEVVVVVNPSDAetLDVAEEIAARFpdvRLRVIRNARLLGPtgkSRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976   183 RIRGADIAQGTTLTFLDSHCEVNRDWLQPLLHRVK-EDYTRVVCPViDIINLDTFTyiesasELRGGFDWSLHFqweqls 261
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDsPKVGAVGTPV-FSLNRSTML------SALGALEFALRH------ 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60498976   262 peqkARRLDPTEPIRTPIIAGGLFVIDKAWFDYLGkydmDMDIWG--GENFEISFRVWMCGGSLEIVPCSRVGHVFRKK 338
Cdd:pfam13641 146 ----LRMMSLRLALGVLPLSGAGSAIRREVLKELG----LFDPFFllGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 110-242 3.25e-03

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: 39.49  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 110 LPPTSIIITFHNEARsTLLRTIRSVLNRT-PTHLIrEIILVDDFSND--PDDCKQLIKlPKVKCLRNNERQGLVRSRIRG 186
Cdd:cd06439  28 LPTVTIIIPAYNEEA-VIEAKLENLLALDyPRDRL-EIIVVSDGSTDgtAEIAREYAD-KGVKLLRFPERRGKAAALNRA 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 60498976 187 ADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESA 242
Cdd:cd06439 105 LALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGSGSGEGL 160
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 453-548 5.20e-03

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.


Pssm-ID: 467327 [Multi-domain]  Cd Length: 128  Bit Score: 37.27  E-value: 5.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498976 453 KGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVLCKNGDDRQQWTKTGSHIEHIA-SHLCLdtDMFGDGTENGK 531
Cdd:cd23449  33 KGGAEDNQLWYEDEVTGTIRSKLNDFCLDASGDKGLILNPYDPSNPKQQWKISGNKIQNRSnPDNVL--DIKGGSKDDGA 110

                        90
                ....*....|....*..
gi 60498976 532 EIVVNPCESSLmSQHWD 548
Cdd:cd23449 111 RLCAWEYNGGP-NQLWD 126
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 495-552 6.08e-03

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 37.03  E-value: 6.08e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60498976 495 NGDDRQQWTKTGS-----HIEHIASHLCLDTDMFGDgtengkeIVVNPCESSLmSQHWDMVSS 552
Cdd:cd23415  28 NGGPYQRWTWSGVgdgtvTLRNAATGRCLDSNGNGG-------VYTLPCNGGS-YQRWRVTST 82
 
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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