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Conserved domains on  [gi|359465583|ref|NP_001240755|]
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polypeptide N-acetylgalactosaminyltransferase 14 isoform 2 [Homo sapiens]

Protein Classification

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 ...
 119-413 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: 516.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 119 SIIITFHNEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQL-----IKLPKVKCLRNNERQGLVRSRIRGAD 193
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 194 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESASELRGGFDWSLHFQWEQLSPEQKaRR 273
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 274 LDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFR-KKHPYVFPDGN 352
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359465583 353 aNTYIKNTKRTAEVWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIY 413
Cdd:cd02510  240 -GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 418-557 2.48e-91

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


The actual alignment was detected with superfamily member cd23478:

Pssm-ID: 483949  Cd Length: 140  Bit Score: 276.37  E-value: 2.48e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 418 IPKESSIQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVL 497
Cdd:cd23478    1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 498 CKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCESSLMSQHWDMVSS 557
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 ...
 119-413 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: 516.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 119 SIIITFHNEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQL-----IKLPKVKCLRNNERQGLVRSRIRGAD 193
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 194 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESASELRGGFDWSLHFQWEQLSPEQKaRR 273
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 274 LDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFR-KKHPYVFPDGN 352
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359465583 353 aNTYIKNTKRTAEVWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIY 413
Cdd:cd02510  240 -GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 418-557 2.48e-91

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: 276.37  E-value: 2.48e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 418 IPKESSIQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVL 497
Cdd:cd23478    1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 498 CKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCESSLMSQHWDMVSS 557
Cdd:cd23478   81 CKEGDGKQRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 140
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 119-294 2.35e-31

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: 119.42  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  119 SIIITFHNEArSTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLIKL-PKVKCLRNNERQGLVRSRIRGADIA 195
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEEYAKKdPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  196 QGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIesaselrggfdWSLHFQWEQLSPEQKARRLD 275
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRLLG 146

                         170
                  ....*....|....*....
gi 359465583  276 PTEPIRTPIIAGGLFVIDK 294
Cdd:pfam00535 147 LNLPFLIGGFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
427-552 9.15e-23

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 93.75  E-value: 9.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  427 GNIRQRQ--KCLESQRQNNQETPnLKLSPCAKVKGEdaksQVWAFTYTQQI--LQEELCLSVITLFPGAPVVLVLCKNGD 502
Cdd:pfam00652   3 GRIRNRAsgKCLDVPGGSSAGGP-VGLYPCHGSNGN----QLWTLTGDGTIrsVASDLCLDVGSTADGAKVVLWPCHPGN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 359465583  503 DRQQW--TKTGSHIEHIASHLCLDTDMFGDGTENgkeIVVNPCESSLMSQHW 552
Cdd:pfam00652  78 GNQRWryDEDGTQIRNPQSGKCLDVSGAGTSNGK---VILWTCDSGNPNQQW 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 116-230 4.32e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 80.13  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 116 PPTSIIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSndPDDCKQLI-----KLPKVKCLRNNERQGLVRSRIR 190
Cdd:COG0463    2 PLVSVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGS--TDGTAEILrelaaKDPRIRVIRLERNRGKGAARNA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 359465583 191 GADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVC 230
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 433-552 1.78e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.12  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583   433 QKCLESQRQNNqetpNLKLSPCakvkGEDAKSQVWAFTYTQQI--LQEELCLSVITLfPGAPVVLVLCKNGDDRQQWT-- 508
Cdd:smart00458   7 GKCLDVNGNKN----PVGLFDC----HGTGGNQLWKLTSDGAIriKDTDLCLTANGN-TGSTVTLYSCDGTNDNQYWEvn 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 359465583   509 KTGShIEHIASHLCLdtDMFGDGTenGKEIVVNPCESSLmSQHW 552
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 ...
 119-215 1.14e-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: 40.57  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  119 SIIITFHNEARsTLLRTIRSVLNRTPTHlirEIILVDDFSndPDDCKQLIKLPKVKCLRNNerQGlvRSR--IRGADIAQ 196
Cdd:TIGR04283   2 SIIIPVLNEAA-TLPELLADLQALRGDA---EVIVVDGGS--TDGTVEIARSLGAKVIHSP--KG--RARqmNAGAALAK 71

                          90
                  ....*....|....*....
gi 359465583  197 GTTLTFLDSHCEVNRDWLQ 215
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 ...
 119-413 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: 516.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 119 SIIITFHNEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQL-----IKLPKVKCLRNNERQGLVRSRIRGAD 193
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 194 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESASELRGGFDWSLHFQWEQLSPEQKaRR 273
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 274 LDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFR-KKHPYVFPDGN 352
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359465583 353 aNTYIKNTKRTAEVWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIY 413
Cdd:cd02510  240 -GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 418-557 2.48e-91

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: 276.37  E-value: 2.48e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 418 IPKESSIQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVL 497
Cdd:cd23478    1 IPDESDIQSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYTYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 498 CKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCESSLMSQHWDMVSS 557
Cdd:cd23478   81 CKEGDGKQRWTKVGSHIEHMASRFCLDTEMFGDGTESSKEIVINPCESSAMSQRWDMVLS 140
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 424-554 3.70e-43

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: 149.86  E-value: 3.70e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 424 IQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKgedaKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVLCKNgDD 503
Cdd:cd23441    3 LAYGQIKQGNLCLDSDEQLFQGPALLILAPCSNSS----DSQEWSFTKDGQLQTQGLCLTVDSSSKDLPVVLETCSD-DP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 359465583 504 RQQWTKTGSHIEHIASHLCLDTDMFgdgtengKEIVVNPCESSLMSQHWDM 554
Cdd:cd23441   78 KQKWTRTGRQLVHSESGLCLDSRKK-------KGLVVSPCRSGAPSQKWDF 121
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 119-294 2.35e-31

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: 119.42  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  119 SIIITFHNEArSTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLIKL-PKVKCLRNNERQGLVRSRIRGADIA 195
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEEYAKKdPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  196 QGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIesaselrggfdWSLHFQWEQLSPEQKARRLD 275
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRLLG 146

                         170
                  ....*....|....*....
gi 359465583  276 PTEPIRTPIIAGGLFVIDK 294
Cdd:pfam00535 147 LNLPFLIGGFALYRREALE 165
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
427-552 9.15e-23

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 93.75  E-value: 9.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  427 GNIRQRQ--KCLESQRQNNQETPnLKLSPCAKVKGEdaksQVWAFTYTQQI--LQEELCLSVITLFPGAPVVLVLCKNGD 502
Cdd:pfam00652   3 GRIRNRAsgKCLDVPGGSSAGGP-VGLYPCHGSNGN----QLWTLTGDGTIrsVASDLCLDVGSTADGAKVVLWPCHPGN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 359465583  503 DRQQW--TKTGSHIEHIASHLCLDTDMFGDGTENgkeIVVNPCESSLMSQHW 552
Cdd:pfam00652  78 GNQRWryDEDGTQIRNPQSGKCLDVSGAGTSNGK---VILWTCDSGNPNQQW 126
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 419-554 1.38e-22

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: 93.33  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 419 PKESSIqKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTyTQQILQEELCLSVITLFPGAPVVLVLC 498
Cdd:cd23479    1 PEKEAI-PGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLS-DPLIRQQDKCLAITSFSPGSKVILELC 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 359465583 499 KNGDDRQQWTKTGSHIEHIASHLCLDtdmfgdgTENGKeIVVNPCESSLMSQHWDM 554
Cdd:cd23479   79 NQKDGRQKWKLKGSFIQHQVSGLCLD-------SQSGR-VVINQCQADLASQQWEL 126
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 427-553 6.16e-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: 6.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 427 GNIRQRQKCLESQRQNNQETPNLklSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVLCKNGDDRQQ 506
Cdd:cd23434    3 GSLKQGNLCLDTLGHKAGGTVGL--YPCHGTGG----NQEWSFTKDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDSNQK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 359465583 507 W--TKTGSHIEHIASHLCLDTDmfgdgTENGKEIVVNPCESSLMSQHWD 553
Cdd:cd23434   77 WeqIENNSKLRHVGSNLCLDSR-----NAKSGGLTVETCDPSSGSQQWK 120
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 116-230 4.32e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 80.13  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 116 PPTSIIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSndPDDCKQLI-----KLPKVKCLRNNERQGLVRSRIR 190
Cdd:COG0463    2 PLVSVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGS--TDGTAEILrelaaKDPRIRVIRLERNRGKGAARNA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 359465583 191 GADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVC 230
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 120-263 1.14e-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: 74.46  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 120 IIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLIKL-PKVKCLRNNERQGLVRSRIRGADIAQ 196
Cdd:cd00761    1 VIIPAYNEEP-YLERCLESLLAQTYPNF--EVIVVDDGSTDgtLEILEEYAKKdPRVIRVINEENQGLAAARNAGLKAAR 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359465583 197 GTTLTFLDSHCEVNRDWL--QPLLHRVKEDYTRVVCPVIDIINLDTFTYIesaselrGGFDWSLHFQWE 263
Cdd:cd00761   78 GEYILFLDADDLLLPDWLerLVAELLADPEADAVGGPGNLLFRRELLEEI-------GGFDEALLSGEE 139
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 427-554 1.66e-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: 72.86  E-value: 1.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 427 GNIR--QRQKCLESQRQNNQEtPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVitlFPGAPVVLVLCKNGDDR 504
Cdd:cd23460    3 GQIKhtESGLCLDWAGESNGD-KTVALKPCHGGGG----NQFWMYTGDGQIRQDHLCLTA---DEGNKVTLRECADQLPS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 359465583 505 QQW--TKTGSHIEHIASHLCLDTDMfgdgteNGKEIVVNPCESSLMSQHWDM 554
Cdd:cd23460   75 QEWsyDEKTGTIRHRSTGLCLTLDA------NNDVVILKECDSNSLWQKWIF 120
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
116-219 5.47e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 73.87  E-value: 5.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 116 PPTSIIITFHNEArSTLLRTIRSVLNRTPTHLirEIILVDDFSNDP--DDCKQLiKLPKVKCLRNNERQGLVRSRIRGAD 193
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGtaELLAAL-AFPRVRVIRNPENLGFAAARNLGLR 78

                         90       100
                 ....*....|....*....|....*.
gi 359465583 194 IAQGTTLTFLDSHCEVNRDWLQPLLH 219
Cdd:COG1216   79 AAGGDYLLFLDDDTVVEPDWLERLLA 104
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 114-218 6.66e-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: 75.55  E-value: 6.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 114 DLPPTSIIITFHNEARsTLLRTIRSVLNRTPTHLIREIILVDDFSNDP--DDCKQLI-KLPKVKCLRNNERQGLVRSRIR 190
Cdd:COG1215   27 DLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDEtaEIARELAaEYPRVRVIERPENGGKAAALNA 105

                         90       100
                 ....*....|....*....|....*...
gi 359465583 191 GADIAQGTTLTFLDSHCEVNRDWLQPLL 218
Cdd:COG1215  106 GLKAARGDIVVFLDADTVLDPDWLRRLV 133
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 434-552 7.94e-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: 7.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 434 KCLESQrQNNQETPnLKLSPCakVKGEDAKSQVWAFTYTQQILQE--ELCLSVITLFPGAPVVLVLCKNGDDRQQWT--K 509
Cdd:cd23439   12 LCIDTK-HGGENDE-VRLSKC--VKDGGGGEQQFELTWHEDIRPKkrKVCFDVSSHTPGAPVILYACHGMKGNQLWKyrP 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 359465583 510 TGSHIEHIASHLCLDTDmfgdgtENGKEIVVNPCESSLMSQHW 552
Cdd:cd23439   88 NTKQLYHPVSGLCLDAD------PGSGKVFMNHCDESSDTQKW 124
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 433-554 2.26e-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: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 433 QKCLESQ-RQNNQetpNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITlfPGAPVVLVLCKNGDDRQQWT--K 509
Cdd:cd23433   15 NLCLDTMgRKAGE---KVGLSSCHGQGG----NQVFSYTAKGEIRSDDLCLDASR--KGGPVKLEKCHGMGGNQEWEydK 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 359465583 510 TGSHIEHIASHLCLDTdmfgDGTENGKEIVVNPCESSlMSQHWDM 554
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 ...
 435-552 4.25e-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: 63.49  E-value: 4.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 435 CLESQRQNNQETPNLKLSPCAKVKgedAKSQVWAFTYTQQILQEELCLSViTLFPGAPVVLVLC-KNGDDRQQWTKT-GS 512
Cdd:cd23459   18 CLDTLQRDEDKGYNLGLYPCQGGL---SSNQLFSLSKKGELRREESCADV-QGTEESKVILITChGLEKFNQKWKHTkGG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 359465583 513 HIEHIASHLCLDTdmfgDGTENGKEIVVNPCESSLmSQHW 552
Cdd:cd23459   94 QIVHLASGKCLDA----EGLKSGDDVTLAKCDGSL-SQKW 128
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 427-554 1.33e-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: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 427 GNIRQRQ--KCLESQrqNNQETPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITlfPGAPVVLVLCkNGDDR 504
Cdd:cd23437    6 GEIRNLGtgLCLDTM--GHQNGGPVGLYPCHGMGG----NQLFRLNEAGQLAVGEQCLTASG--SGGKVKLRKC-NLGET 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 359465583 505 QQW--TKTGSHIEHIASHLCLDTdmfgdgTENGKEIVVNPCESSLMSQHWDM 554
Cdd:cd23437   77 GKWeyDEATGQIRHKGTGKCLDL------NEGTNKLILQPCDSSSPSQKWEF 122
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 423-554 1.82e-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: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 423 SIQKGNIRQRQ--KCLESQRQNNQETPNLKLSPCAKvkgeDAKSQVWAFTYTQQI-LQEELCLSVITlFPGAPVVLVLCK 499
Cdd:cd23440    2 VIRKGQLKHAGsgLCLVAEDEVSQKGSLLVLRPCSR----NDKKQLWYYTEDGELrLANLLCLDSSE-TSSDFPRLMKCH 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 359465583 500 NGDDRQQWT-KTGSHIEHIASHLCLdtdmFGDGTENGKEIVVNPCESSLmSQHWDM 554
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 ...
 434-552 1.08e-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: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 434 KCLESQRQNNQETPNLKLSPCAkvkgeDAKSQVWAFT------YTQQILQEELCLSV--ITLFPGAPVVLVLCkNGDDRQ 505
Cdd:cd00161   12 KCLDVAGGSTANGAPVQQWTCN-----GGANQQWTLTpvgdgyYTIRNVASGKCLDVagGSTANGANVQQWTC-NGGDNQ 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 359465583 506 QW--TKTGS---HIEHIASHLCLDTDmfGDGTENGKEIVVNPCESSLmSQHW 552
Cdd:cd00161   86 QWrlEPVGDgyyRIVNKHSGKCLDVS--GGSTANGANVQQWTCNGGA-NQQW 134
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 423-552 1.93e-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: 55.83  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 423 SIQKGNIRQR--QKCLESQRQNNQETPNLKLSPCAKVKGEdaksQVWAFTYTQQILQEELCLSV------ITLFPgapvv 494
Cdd:cd23462    2 ALAYGEIRNLagKLCLDAPGRKKELNKPVGLYPCHGQGGN----QYWMLTKDGEIRRDDLCLDYaggsgdVTLYP----- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359465583 495 lvlCKNGDDRQQWT---KTGsHIEHIASHLCLDTDmfgdgtENGKEIVVNPCESSLMSQHW 552
Cdd:cd23462   73 ---CHGMKGNQFWIydeETK-QIVHGTSKKCLELS------DDSSKLVMEPCNGSSPRQQW 123
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 119-341 4.37e-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: 57.24  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 119 SIIITFHNEARsTLLRTIRSVLNRTPTHLIREIILVDDFSND--PDDCKQLIKL-PKVKcLRNNERQGLVRSRIRGADIA 195
Cdd:cd02525    3 SIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVDGGSTDgtREIVQEYAAKdPRIR-LIDNPKRIQSAGLNIGIRNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 196 QGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIES-ASELRGGFDWSLHfqweqlspEQKARRL 274
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAvAQSSPLGSGGSAY--------RGGAVKI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359465583 275 DPTEPirtpiIAGGLFviDKAWFDYLGKYDMDMDIwgGENFEISFRVWMCGGSLEIVPCSRVGHVFR 341
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 ...
 120-260 3.12e-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: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 120 IIITFHNEARsTLLRTIRSVLNRT-PTHLIrEIILVDDFSNDpdDCKQLIKL------PKVKCLRNNERQGlvrSRIR-- 190
Cdd:cd04192    1 VVIAARNEAE-NLPRLLQSLSALDyPKEKF-EVILVDDHSTD--GTVQILEFaaakpnFQLKILNNSRVSI---SGKKna 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 191 ---GADIAQGTTLTFLDSHCEVNRDWLQPLL-HRVKEDYTRVVCPVIDIIN---LDTFTYIESASEL---RGGFDWSLHF 260
Cdd:cd04192   74 lttAIKAAKGDWIVTTDADCVVPSNWLLTFVaFIQKEQIGLVAGPVIYFKGkslLAKFQRLDWLSLLgliAGSFGLGKPF 153
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 424-552 1.04e-07

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: 50.79  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 424 IQKGNIRQR--QKCLESQRQNNQETPNLKLSPCakvKGEDaKSQVWAFTYTQQIL---QEELCLSVItlfPGAPVVLVLC 498
Cdd:cd23435    2 GYYGALRNKgsELCLDVNNPNGQGGKPVIMYGC---HGLG-GNQYFEYTSKGEIRhniGKELCLHAS---GSDEVILQHC 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 359465583 499 ----KNGDDRQQWTKT-GSHIEHIASHLCLDTdmfgdgteNGKEIVVNPCESSLMSQHW 552
Cdd:cd23435   75 tskgKDVPPEQKWLFTqDGTIRNPASGLCLHA--------SGYKVLLRTCNPSDDSQKW 125
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
480-553 1.71e-07

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 50.22  E-value: 1.71e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359465583  480 LCLSVITLFP-GAPVVLVLCKNGDDRQQWTKTGS-HIEHIASHLCLDTDmfgdGTENGKEIVVNPCESSLMSQHWD 553
Cdd:pfam00652  12 KCLDVPGGSSaGGPVGLYPCHGSNGNQLWTLTGDgTIRSVASDLCLDVG----STADGAKVVLWPCHPGNGNQRWR 83
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 120-338 2.41e-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: 50.64  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 120 IIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDFSND--PDDCKQLikLPKVKCLRNNERQGLVRSRIRGADIAQG 197
Cdd:cd04186    1 IIIVNYNSLE-YLKACLDSLLAQTYPDF--EVIVVDNASTDgsVELLREL--FPEVRLIRNGENLGFGAGNNQGIREAKG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 198 TTLTFLDSHCEVNRDWLQPLLhrvkedytrvvcpvidiinldtftyiesaselrggfdwslhfqweqlspeqKARRLDPT 277
Cdd:cd04186   76 DYVLLLNPDTVVEPGALLELL---------------------------------------------------DAAEQDPD 104

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359465583 278 EPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWgGENFEISFRVWMCGGSLEIVPCSRVGH 338
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 ...
 120-205 1.04e-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: 49.11  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 120 IIITFHNEARstllrTIRSVLNRTPTHLIR----EIILVDDFSndPDDCKQLIK-----LPKVKCLRNNERQGLVRSRIR 190
Cdd:cd04179    1 VVIPAYNEEE-----NIPELVERLLAVLEEgydyEIIVVDDGS--TDGTAEIARelaarVPRVRVIRLSRNFGKGAAVRA 73

                         90
                 ....*....|....*
gi 359465583 191 GADIAQGTTLTFLDS 205
Cdd:cd04179   74 GFKAARGDIVVTMDA 88
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 433-552 1.78e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.12  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583   433 QKCLESQRQNNqetpNLKLSPCakvkGEDAKSQVWAFTYTQQI--LQEELCLSVITLfPGAPVVLVLCKNGDDRQQWT-- 508
Cdd:smart00458   7 GKCLDVNGNKN----PVGLFDC----HGTGGNQLWKLTSDGAIriKDTDLCLTANGN-TGSTVTLYSCDGTNDNQYWEvn 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 359465583   509 KTGShIEHIASHLCLdtDMFGDGTenGKEIVVNPCESSLmSQHW 552
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; ...
 119-215 8.88e-06

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: 47.18  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 119 SIIITFHNEARsTLLRTIRSVLNRTPthLIREIILVDDFSNDpdDCKQLIKLPKVKCLRnnERQGlvRSR--IRGADIAQ 196
Cdd:cd02522    2 SIIIPTLNEAE-NLPRLLASLRRLNP--LPLEIIVVDGGSTD--GTVAIARSAGVVVIS--SPKG--RARqmNAGAAAAR 72

                         90
                 ....*....|....*....
gi 359465583 197 GTTLTFLDSHCEVNRDWLQ 215
Cdd:cd02522   73 GDWLLFLHADTRLPPDWDA 91
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 120-307 1.93e-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: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 120 IIITFHNEARsTLLRTIRSVLNRTPTHLirEIILVDDfsNDPDDCKQLIK------LPKVKCLRNNERQGLVRSRIRGAD 193
Cdd:cd06423    1 IIVPAYNEEA-VIERTIESLLALDYPKL--EVIVVDD--GSTDDTLEILEelaalyIRRVLVVRDKENGGKAGALNAGLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 194 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDyTRV--VCPVIDIIN-----LDTFTYIESASelrgGFDWSLHFQWeqls 266
Cdd:cd06423   76 HAKGDIVVVLDADTILEPDALKRLVVPFFAD-PKVgaVQGRVRVRNgsenlLTRLQAIEYLS----IFRLGRRAQS---- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 359465583 267 peqkarRLDptepiRTPIIAGGLFVIDKAWFDYLGKYDMDM 307
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) ...
 433-526 6.34e-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: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 433 QKCLesqrQNNQETPNLKLSPCakvkGEDAKSQVWAFTYTQQILQEE--LCLSVITLFPGAPVVLVLCKNGDDRQQWT-- 508
Cdd:cd23385   11 GKCL----AARSSSSKVSLSTC----NPNSPNQQWKWTSGHRLFNVGtgKCLGVSSSSPSSPLRLFECDSEDELQKWKcs 82

                         90
                 ....*....|....*....
gi 359465583 509 -KTGSHIEHIASHLCLDTD 526
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) ...
 477-553 1.07e-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: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359465583 477 QEELCLSVITlfPGAPVVLVLCKNGDDRQQWTKTGSH-IEHIASHLCLDTDmfgdGTENGKEIVVNPCESSLMSQHWD 553
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 ...
 120-179 1.65e-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: 42.46  E-value: 1.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359465583 120 IIITFHNEARS--TLLRTIRSVLNRTptHLIREIILVDDFSndPDDCKQLIK-----LPKVKCLRNN 179
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAVLESL--GYDYEIIFVDDGS--TDRTLEILRelaarDPRVKVIRLS 63
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
 481-554 2.71e-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: 41.27  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 481 CLSVI--TLFPGAPVVLvLCKNGDDRQQW--TKTGshieHIASHLC--LDTDMFGDGTENGKEIVVNPCESSLMSQHWDM 554
Cdd:cd23463   59 CLDVIggKDNPGSKVAL-WTEHGKTHQKWriNEDG----TISSHLSddLVLDLKGGNYYDKDHLIVNNPEEDQQTQKWDI 133
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 427-552 4.54e-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: 40.40  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 427 GNIR--QRQKCLESQrqNNQETPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITLfpGAPVVLVLCKNGDDR 504
Cdd:cd23467    7 GEIRnvETNQCLDNM--GRKENEKVGIFNCHGMGG----NQVFSYTADKEIRTDDLCLDVSRL--NGPVVMLKCHHMRGN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 359465583 505 QQWTKTGSH--IEHIASHLCLDtdmfGDGTENGKEIVVNPCESSlMSQHW 552
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 ...
 285-345 4.90e-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: 38.75  E-value: 4.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359465583  285 IAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCsRVGHVFRKKHP 345
Cdd:pfam02709  19 YFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLYHK 78
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 474-554 5.79e-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: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 474 QILQEELCLSVITLFPGAPVVLVLCKNGDDRQQW--TKTGsHIEHiaSHLCLDTDmfgDGTEnGKEIVVNPCESSLMSQH 551
Cdd:cd23434    4 SLKQGNLCLDTLGHKAGGTVGLYPCHGTGGNQEWsfTKDG-QIKH--DDLCLTVV---DRAP-GSLVTLQPCREDDSNQK 76


                 ...
gi 359465583 552 WDM 554
Cdd:cd23434   77 WEQ 79
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 426-508 6.54e-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: 40.01  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 426 KGNIR---QRQKCLEsqrqnNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEE--LCLSVITLFpgapVVLVLCKN 500
Cdd:cd23435   48 KGEIRhniGKELCLH-----ASGSDEVILQHCTSKGKDVPPEQKWLFTQDGTIRNPAsgLCLHASGYK----VLLRTCNP 118


                 ....*...
gi 359465583 501 GDDRQQWT 508
Cdd:cd23435  119 SDDSQKWT 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 425-508 1.02e-03

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 39.03  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583   425 QKGNIR--QRQKCLESQRQNNQetpNLKLSPCAKvkgeDAKSQVWAFTYTQQI--LQEELCLSVITLFPGAPVVLVLCkN 500
Cdd:smart00458  37 SDGAIRikDTDLCLTANGNTGS---TVTLYSCDG----TNDNQYWEVNKDGTIrnPDSGKCLDVKDGNTGTKVILWTC-S 108


                   ....*...
gi 359465583   501 GDDRQQWT 508
Cdd:smart00458 109 GNPNQKWI 116
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 427-552 1.04e-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: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 427 GNIR--QRQKCLESQRQnnQETPNLKLSPCAKVKGedakSQVWAFTYTQQILQEELCLSVITLfpGAPVVLVLCKNGDDR 504
Cdd:cd23466    7 GEIRnvETNQCLDNMAR--KENEKVGIFNCHGMGG----NQVFSYTANKEIRTDDLCLDVSKL--NGPVMMLKCHHLKGN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 359465583 505 QQWT--KTGSHIEHIASHLCLDTDMfgdgTENGKEIVVNPCESSlMSQHW 552
Cdd:cd23466   79 QLWEydPVKLTLLHVNSNQCLDKAT----EEDSQVPSIRDCNGS-RSQQW 123
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 119-332 1.05e-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: 41.11  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  119 SIIITFHN-EARSTLLRTIRsvLNRTPTHLIREIILVDDFSNDP--DDCKQLIKLPKVKCLRNNERQ--GLVRSRIRGAD 193
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERIL--NQTFQYDPEFELIIINDGSTDKtlEEVSSIKDHNLQVYYPNAPDTtySLAASRNRGTS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  194 IAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTR------VVCPVIDIINldtftyiESASELRGGFD--WSLHFQWEQL 265
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFEKQLKIATSLALQeniqaaVVLPVTDLND-------ESSNFLRRGGDltASGDVLRDLL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359465583  266 SPEqkarrlDPTEPIRTPiiAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVP 332
Cdd:pfam10111 152 VFY------SPLAIFFAP--NSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRLAARYPFVAVMP 210
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 119-215 1.14e-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: 40.57  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  119 SIIITFHNEARsTLLRTIRSVLNRTPTHlirEIILVDDFSndPDDCKQLIKLPKVKCLRNNerQGlvRSR--IRGADIAQ 196
Cdd:TIGR04283   2 SIIIPVLNEAA-TLPELLADLQALRGDA---EVIVVDGGS--TDGTVEIARSLGAKVIHSP--KG--RARqmNAGAALAK 71

                          90
                  ....*....|....*....
gi 359465583  197 GTTLTFLDSHCEVNRDWLQ 215
Cdd:TIGR04283  72 GDILLFLHADTRLPKDFLE 90
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 119-223 1.42e-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: 40.26  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 119 SIIITFHNEARSTLLRTIRSVLNRTPTHLirEIILVDDFSNDPDDCKQLIKL----PKVKCLRNNERQGLVRSRIRGADI 194
Cdd:cd04184    4 SIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYaaqdPRIKVVFREENGGISAATNSALEL 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 359465583 195 AQGTTLTFLDshcevNRDWLQP--LLHRVKE 223
Cdd:cd04184   82 ATGEFVALLD-----HDDELAPhaLYEVVKA 107
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 449-552 2.02e-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: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 449 LKLSPCAKVKGEDA--KSQVWAFTYTQQIL------QEELCLSVITlfPGAPVVLVLCKNGDDRQQWT-KTGSHIEHIAS 519
Cdd:cd23476   30 LRLEGCVKGRGEAAwnNGQVFTFGWREDIRpgdpqhTKKFCFDAIS--HNSPVTLYDCHGMKGNQLWRyRKDKTLYHPVS 107

                         90       100       110
                 ....*....|....*....|....*....|...
gi 359465583 520 HLCLDTdmfgdgTENGKEIVVNPCESSLMSQHW 552
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, ...
 489-552 2.08e-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: 2.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359465583 489 PGAPVVLVLCKNGDDrQQWTKTGSHIEHIASHLCLDTDmfGDGTENGKEIVVNPCESSLmSQHW 552
Cdd:cd23418   26 NGTRLILWDCHGGAN-QQFTFTSAGELRVGGDKCLDAA--GGGTTNGTPVVIWPCNGGA-NQKW 85
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 458-553 3.16e-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: 38.04  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 458 KGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVLCKNGDDRQQWTKTGSHIEHIA-SHLCLdtDMFGDGTENGK 536
Cdd:cd23449   33 KGGAEDNQLWYEDEVTGTIRSKLNDFCLDASGDKGLILNPYDPSNPKQQWKISGNKIQNRSnPDNVL--DIKGGSKDDGA 110

                         90
                 ....*....|....*..
gi 359465583 537 EIVVNPCESSLmSQHWD 553
Cdd:cd23449  111 RLCAWEYNGGP-NQLWD 126
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 115-247 3.29e-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: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583 115 LPPTSIIITFHNEARsTLLRTIRSVLNRT-PTHLIrEIILVDDFSND--PDDCKQLIKlPKVKCLRNNERQGLVRSRIRG 191
Cdd:cd06439   28 LPTVTIIIPAYNEEA-VIEAKLENLLALDyPRDRL-EIIVVSDGSTDgtAEIAREYAD-KGVKLLRFPERRGKAAALNRA 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 359465583 192 ADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESA 247
Cdd:cd06439  105 LALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGSGSGEGL 160
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 116-343 3.60e-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: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  116 PPTSIIITFHNEArSTLLRTIRSVLNRTptHLIREIILVDDFSND--PDDCKQLIKLP---KVKCLRNNERQGL---VRS 187
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQP--YPPVEVVVVVNPSDAetLDVAEEIAARFpdvRLRVIRNARLLGPtgkSRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359465583  188 RIRGADIAQGTTLTFLDSHCEVNRDWLQPLLHRVK-EDYTRVVCPViDIINLDTFTyiesasELRGGFDWSLHFqweqls 266
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDsPKVGAVGTPV-FSLNRSTML------SALGALEFALRH------ 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359465583  267 peqkARRLDPTEPIRTPIIAGGLFVIDKAWFDYLGkydmDMDIWG--GENFEISFRVWMCGGSLEIVPCSRVGHVFRKK 343
Cdd:pfam13641 146 ----LRMMSLRLALGVLPLSGAGSAIRREVLKELG----LFDPFFllGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 500-557 4.39e-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: 37.41  E-value: 4.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359465583 500 NGDDRQQWTKTGS-----HIEHIASHLCLDTDMFGDgtengkeIVVNPCESSLmSQHWDMVSS 557
Cdd:cd23415   28 NGGPYQRWTWSGVgdgtvTLRNAATGRCLDSNGNGG-------VYTLPCNGGS-YQRWRVTST 82
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 120-160 4.58e-03

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 38.81  E-value: 4.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 359465583 120 IIITFhNEARsTLLRTIRSVLNrtpthLIREIILVDDFSND 160
Cdd:cd02511    5 VIITK-NEER-NIERCLESVKW-----AVDEIIVVDSGSTD 38
 
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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