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Conserved domains on  [gi|494884798|ref|WP_007610846|]
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MULTISPECIES: glycosyltransferase family 2 protein [Bacillus]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135621)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
9-190 9.44e-101

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: 293.61  E-value: 9.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYAE 88
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  89 GNAIAVIDADLQDPPELILDMIEQWKEGYDVVYAVRTKRKgETFFKKQTASMFYRLLRSVTDIDIPLDTGDFRLLDRKVC 168
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170       180
                 ....*....|....*....|..
gi 494884798 169 DEMKRLKEKNPFVRGLVSWVGF 190
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVGF 181
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
9-190 9.44e-101

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: 293.61  E-value: 9.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYAE 88
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  89 GNAIAVIDADLQDPPELILDMIEQWKEGYDVVYAVRTKRKgETFFKKQTASMFYRLLRSVTDIDIPLDTGDFRLLDRKVC 168
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170       180
                 ....*....|....*....|..
gi 494884798 169 DEMKRLKEKNPFVRGLVSWVGF 190
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVGF 181
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
8-321 1.99e-50

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 169.92  E-value: 1.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELVIQTTYQRLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLI-DPRVKIIDFSRNFGHQIAITAGMDY 86
Cdd:PRK10714   9 SVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIMAGFSH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  87 AEGNAIAVIDADLQDPPELILDMIEQWKEGYDVVYAVRTKRKgETFFKKQTASMFYRLLRSVTDIDIpldtGDF----RL 162
Cdd:PRK10714  89 VTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQ-DSWFRKTASKMINRLIQRTTGKAM----GDYgcmlRA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798 163 LDRKVCDEMKRLKEKNPFVRGLVSWVGFKQTAVEYERDERLAGETKYPLKKMLKLSMDGITTFSHKPLKAASYAGMIMSG 242
Cdd:PRK10714 164 YRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSIIAI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798 243 AGFLYMFIVLYMKLFTNSTitgWSS-----LIVIQLLFSGIVLLMLGMIGEYIGRIYDEAKDRPLYIVQKAYGMKNEKIY 317
Cdd:PRK10714 244 GGFSLAVLLVVLRLTFGPQ---WAAegvfmLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSNN 320

                 ....
gi 494884798 318 RDQH 321
Cdd:PRK10714 321 EKEN 324
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-217 5.26e-50

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 165.26  E-value: 5.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELVIQTTyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYA 87
Cdd:COG0463    5 SVVIPTYNEEEYLEEA---LESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  88 EGNAIAVIDADLQDPPELILDMIEQWKE-GYDVVYAVRTKRKGETFFKKQTASMFYrLLRSVTdiDIPLDTGDFRLLDRK 166
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRLFRRE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494884798 167 VCDEM---KRLKEKNPFVRglVSWVGFKQTAVEYERDErlaGETKYPLKKMLKL 217
Cdd:COG0463  159 VLEELgfdEGFLEDTELLR--ALRHGFRIAEVPVRYRA---GESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-170 9.68e-37

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: 129.44  E-value: 9.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798    8 SIVVPVYNEELVIQTTyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYA 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLET---LESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   88 EGNAIAVIDADLQDPPELILDMIEQW-KEGYDVVYAVRTKRKGETFFKKQT-----ASMFYRLLRSVTDIDIPLDTGDFR 161
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALeEDGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 494884798  162 LLDRKVCDE 170
Cdd:pfam00535 158 LYRREALEE 166
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
9-190 9.44e-101

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: 293.61  E-value: 9.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYAE 88
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  89 GNAIAVIDADLQDPPELILDMIEQWKEGYDVVYAVRTKRKgETFFKKQTASMFYRLLRSVTDIDIPLDTGDFRLLDRKVC 168
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170       180
                 ....*....|....*....|..
gi 494884798 169 DEMKRLKEKNPFVRGLVSWVGF 190
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVGF 181
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
9-190 4.37e-68

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: 210.89  E-value: 4.37e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEVMDQTKEhYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYAE 88
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYD-YEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  89 GNAIAVIDADLQDPPELILDMIE-QWKEGYDVVYAVRTKRKG---ETFFKKQTASMFYRLLRSVTDIDIPLDTGDFRLLD 164
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEkLLEGGADVVIGSRFVRGGgagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159
                        170       180
                 ....*....|....*....|....*.
gi 494884798 165 RKVCDEMKRLKEKNPFVRGLVSWVGF 190
Cdd:cd04179  160 REVLEALLSLLESNGFEFGLELLVGA 185
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
8-321 1.99e-50

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 169.92  E-value: 1.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELVIQTTYQRLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLI-DPRVKIIDFSRNFGHQIAITAGMDY 86
Cdd:PRK10714   9 SVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIMAGFSH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  87 AEGNAIAVIDADLQDPPELILDMIEQWKEGYDVVYAVRTKRKgETFFKKQTASMFYRLLRSVTDIDIpldtGDF----RL 162
Cdd:PRK10714  89 VTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQ-DSWFRKTASKMINRLIQRTTGKAM----GDYgcmlRA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798 163 LDRKVCDEMKRLKEKNPFVRGLVSWVGFKQTAVEYERDERLAGETKYPLKKMLKLSMDGITTFSHKPLKAASYAGMIMSG 242
Cdd:PRK10714 164 YRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSIIAI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798 243 AGFLYMFIVLYMKLFTNSTitgWSS-----LIVIQLLFSGIVLLMLGMIGEYIGRIYDEAKDRPLYIVQKAYGMKNEKIY 317
Cdd:PRK10714 244 GGFSLAVLLVVLRLTFGPQ---WAAegvfmLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSNN 320

                 ....
gi 494884798 318 RDQH 321
Cdd:PRK10714 321 EKEN 324
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-217 5.26e-50

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 165.26  E-value: 5.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELVIQTTyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYA 87
Cdd:COG0463    5 SVVIPTYNEEEYLEEA---LESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  88 EGNAIAVIDADLQDPPELILDMIEQWKE-GYDVVYAVRTKRKGETFFKKQTASMFYrLLRSVTdiDIPLDTGDFRLLDRK 166
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRLFRRE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494884798 167 VCDEM---KRLKEKNPFVRglVSWVGFKQTAVEYERDErlaGETKYPLKKMLKL 217
Cdd:COG0463  159 VLEELgfdEGFLEDTELLR--ALRHGFRIAEVPVRYRA---GESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-170 9.68e-37

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: 129.44  E-value: 9.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798    8 SIVVPVYNEELVIQTTyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYA 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLET---LESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   88 EGNAIAVIDADLQDPPELILDMIEQW-KEGYDVVYAVRTKRKGETFFKKQT-----ASMFYRLLRSVTDIDIPLDTGDFR 161
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALeEDGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 494884798  162 LLDRKVCDE 170
Cdd:pfam00535 158 LYRREALEE 166
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
9-216 1.33e-25

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


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 101.84  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEVMDqtKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYAE 88
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  89 GNAIAVIDADLQDPPELILDMIE-QWKEGYDVVYAVRTKRKGET----FFKK---QTASMFYRLL--RSVTDIdipldTG 158
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEaQLEGGADLVIGSRYVEGGGVegwgLKRKlisRGANLLARLLlgRKVSDP-----TS 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494884798 159 DFRLLDRKVCDE-MKRLKEKNP------FVRGLVSwvGFKQTAVEYERDERLAGETKYPLKKMLK 216
Cdd:cd06442  154 GFRAYRREVLEKlIDSLVSKGYkfqlelLVRARRL--GYRIVEVPITFVDREHGESKLGGKEIVE 216
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
9-130 4.27e-20

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 86.85  E-value: 4.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEVMDQTKE-HYELIFVNDGSKDRSIEILREQSLIDP-RVKIIDFSRNFGHQIAITAGMDY 86
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEERPSfSYEIIVVDDGSKDGTAEVARKLARKNPaLIRVLTLPKNRGKGGAVRAGMLA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494884798  87 AEGNAIAVIDADLQDPPELILDMIEQ-WKEGYDVVYAVRTKRKGE 130
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEAlKTSGYDIAIGSRAHLASA 125
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
9-123 1.01e-19

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: 84.09  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEvmdQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGMDYAE 88
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLA---QTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494884798  89 GNAIAVIDADLQDPPELILDMIE--QWKEGYDVVYAV 123
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAelLADPEADAVGGP 114
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
7-111 4.75e-18

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: 82.87  E-value: 4.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   7 YSIVVPVYNEELVIQTTyqrLKEVMDQT--KEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDFSRNFGHQIAITAGM 84
Cdd:COG1215   31 VSVIIPAYNEEAVIEET---LRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGL 107
                         90       100
                 ....*....|....*....|....*..
gi 494884798  85 DYAEGNAIAVIDADLQDPPELILDMIE 111
Cdd:COG1215  108 KAARGDIVVFLDADTVLDPDWLRRLVA 134
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
9-143 1.35e-17

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: 79.19  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILRE-QSLIDPRVKIIDFSRNFGHQIAITAGMDYA 87
Cdd:cd06423    1 IIVPAYNEEAVIERT---IESLLALDYPKLEVIVVDDGSTDDTLEILEElAALYIRRVLVVRDKENGGKAGALNAGLRHA 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494884798  88 EGNAIAVIDADLQDPPELILDMIEQWKEGYDVVYA---VRTKRKGETFFKKQTASMFYR 143
Cdd:cd06423   78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVqgrVRVRNGSENLLTRLQAIEYLS 136
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-171 2.66e-16

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 77.05  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   1 MSRHIQYSIVVPVYNEELVIQTTYQRLKEVMDQTKEhYELIFVNDGSKDRSIEILRE--QSLIDPRVKIIDFSRNFGHQI 78
Cdd:PLN02726   5 GEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVKD-FEIIVVDDGSPDGTQDVVKQlqKVYGEDRILLRPRPGKLGLGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  79 AITAGMDYAEGNAIAVIDADLQDPPELILDMIEQWKE-GYDVVYAVRTKRKGET----FFKKQTaSMFYRLLRS------ 147
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVTGTRYVKGGGVhgwdLRRKLT-SRGANVLAQtllwpg 162
                        170       180
                 ....*....|....*....|....
gi 494884798 148 VTDIdipldTGDFRLLDRKVCDEM 171
Cdd:PLN02726 163 VSDL-----TGSFRLYKRSALEDL 181
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-113 8.58e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 71.95  E-value: 8.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYN-EELVIQTtyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSliDPRVKIIDFSRNFGHQIAITAGMDY 86
Cdd:COG1216    6 SVVIPTYNrPELLRRC----LESLLAQTYPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLGLRA 79
                         90       100
                 ....*....|....*....|....*..
gi 494884798  87 AEGNAIAVIDADLQDPPELILDMIEQW 113
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLERLLAAA 106
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-112 3.16e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.30  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   1 MSRHIQYSIVVPVYNEELVIQTTYQRLKevmDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIIDfSRNFGHQIAI 80
Cdd:PRK10073   2 MNSTPKLSIIIPLYNAGKDFRAFMESLI---AQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVAR 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494884798  81 TAGMDYAEGNAIAVIDADLQDPPEL---ILDMIEQ 112
Cdd:PRK10073  78 NTGLAVATGKYVAFPDADDVVYPTMyetLMTMALE 112
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-135 1.35e-12

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: 66.16  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLkEVMDQTKEHYELIFVNDGSKDRSIEILREQSLI-DPRVKIIDFSR--NFGHQIAITAGMD 85
Cdd:cd04192    1 VVIAARNEAENLPRLLQSL-SALDYPKEKFEVILVDDHSTDGTVQILEFAAAKpNFQLKILNNSRvsISGKKNALTTAIK 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494884798  86 YAEGNAIAVIDADLQDPPELILDMIE--QWKEGYDVVYAVrTKRKGETFFKK 135
Cdd:cd04192   80 AAKGDWIVTTDADCVVPSNWLLTFVAfiQKEQIGLVAGPV-IYFKGKSLLAK 130
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
8-98 2.41e-11

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: 62.99  E-value: 2.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELVIQTTYQRLKEvMDQTKEHYELIFVNDGSKDRSIEILREQslIDPRVKIIDFSRNFGHQIAITAGMDYA 87
Cdd:cd06439   32 TIIIPAYNEEAVIEAKLENLLA-LDYPRDRLEIIVVSDGSTDGTAEIAREY--ADKGVKLLRFPERRGKAAALNRALALA 108
                         90
                 ....*....|.
gi 494884798  88 EGNAIAVIDAD 98
Cdd:cd06439  109 TGEIVVFTDAN 119
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
5-166 2.78e-11

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 63.63  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   5 IQYSIVVPVYNEE----LVIQTTYQRLKEVMD-QTKEHYELIFVNDGSKDRSIEI----LREQSLIDPRVKIIDFSRNFG 75
Cdd:PTZ00260  70 VDLSIVIPAYNEEdrlpKMLKETIKYLESRSRkDPKFKYEIIIVNDGSKDKTLKVakdfWRQNINPNIDIRLLSLLRNKG 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  76 HQIAITAGMDYAEGNAIAVIDAD----LQDPPELILDMIEQWKEGYDVVYAVRT---------KRKgetFFKKQTASMFY 142
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDADgatdIDDFDKLEDIMLKIEQNGLGIVFGSRNhlvdsdvvaKRK---WYRNILMYGFH 226
                        170       180
                 ....*....|....*....|....
gi 494884798 143 RLLRSVTDIDIPLDTGDFRLLDRK 166
Cdd:PTZ00260 227 FIVNTICGTNLKDTQCGFKLFTRE 250
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
8-98 2.93e-10

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: 58.75  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYN--EELVIQTtyqrLKEVMDQTKEHYELIFVNDGSKDRSI-EILREQSLIDPRVKIIDFSRNFGHQIAITAGM 84
Cdd:cd04184    4 SIVMPVYNtpEKYLREA----IESVRAQTYPNWELCIADDASTDPEVkRVLKKYAAQDPRIKVVFREENGGISAATNSAL 79
                         90
                 ....*....|....
gi 494884798  85 DYAEGNAIAVIDAD 98
Cdd:cd04184   80 ELATGEFVALLDHD 93
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
8-111 4.17e-10

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: 59.17  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELVIQTTyqrLKEVMDQT--KEHYELIFVNDGSKDRSIEILREQSLIDPRVKIID-FSRNFGhqIAITAGM 84
Cdd:cd02525    3 SIIIPVRNEEKYIEEL---LESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDnPKRIQS--AGLNIGI 77
                         90       100
                 ....*....|....*....|....*..
gi 494884798  85 DYAEGNAIAVIDADLQDPPELILDMIE 111
Cdd:cd02525   78 RNSRGDIIIRVDAHAVYPKDYILELVE 104
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
7-112 2.76e-08

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: 53.34  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   7 YSIVVPVYNEELVIQTTYQRLKEVMDQTKehyELIFVNDGSKDRSIEILReqsliDPRVKIIDFSRNFGHQIAitAGMDY 86
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPL---EIIVVDGGSTDGTVAIAR-----SAGVVVISSPKGRARQMN--AGAAA 70
                         90       100
                 ....*....|....*....|....*.
gi 494884798  87 AEGNAIAVIDADLQDPPELILDMIEQ 112
Cdd:cd02522   71 ARGDWLLFLHADTRLPPDWDAAIIET 96
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-111 1.09e-06

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: 47.94  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYN-EELVIQTtyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSlidPRVKIIDFSRNFGHQIAITAGMDYA 87
Cdd:cd04186    1 IIIVNYNsLEYLKAC----LDSLLAQTYPDFEVIVVDNASTDGSVELLRELF---PEVRLIRNGENLGFGAGNNQGIREA 73
                         90       100
                 ....*....|....*....|....
gi 494884798  88 EGNAIAVIDADLQDPPELILDMIE 111
Cdd:cd04186   74 KGDYVLLLNPDTVVEPGALLELLD 97
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
8-124 1.27e-06

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: 48.44  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELVIQTTYQRLKEVMDqtkehyELIFVNDGSKDRSIEILREqslidPRVKIIDFS-RNFGHQiaITAGMDY 86
Cdd:cd02511    3 SVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTVEIAKE-----YGAKVYQRWwDGFGAQ--RNFALEL 69
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494884798  87 AEGNAIAVIDADLQDPPELILDMIEQWKEGYDVVYAVR 124
Cdd:cd02511   70 ATNDWVLSLDADERLTPELADEILALLATDDYDGYYVP 107
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
9-112 1.39e-05

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 45.07  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKEVMDQTKehyeLIFVNDGSKDRSIEILREQsLIDPRVKIIDFSR-----------NFGH- 76
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNKPNFL----VLVIDDASDDDTAGIVRLA-ITDSRVHLLRRHLpnartgkgdalNAAYd 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494884798  77 ---QIAITAGMDyAEGNAIAVIDADLQDPPELiLDMIEQ 112
Cdd:cd06436   76 qirQILIEEGAD-PERVIIAVIDADGRLDPNA-LEAVAP 112
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
8-104 7.55e-05

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 43.45  E-value: 7.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELViqttYQRLKEV---MDQTKEHYElIFVNDGSKDRSIEILREqslidprvkIIDFSRNFGHQI------ 78
Cdd:cd06437    4 TVQLPVFNEKYV----VERLIEAacaLDYPKDRLE-IQVLDDSTDETVRLARE---------IVEEYAAQGVNIkhvrra 69
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494884798  79 --------AITAGMDYAEGNAIAVIDADLQDPPE 104
Cdd:cd06437   70 drtgykagALAEGMKVAKGEYVAIFDADFVPPPD 103
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
8-98 4.30e-04

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 41.52  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEElviQTTYQRLKEVMDQTKEHYELIFVNDGSKdrSIEILRE--QSLIDPRVKIIDFSRNFGHQIAITAGMD 85
Cdd:PRK10018   8 SIYMPTWNRQ---QLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQyvTALNDPRITYIHNDINSGACAVRNQAIM 82
                         90
                 ....*....|...
gi 494884798  86 YAEGNAIAVIDAD 98
Cdd:PRK10018  83 LAQGEYITGIDDD 95
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
8-56 7.92e-04

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 39.84  E-value: 7.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 494884798   8 SIVVPVYNEELVIQTTyqrLKEVMDQTKEHYELIFVNDGSKDRSIEILR 56
Cdd:cd06433    1 SIITPTYNQAETLEET---IDSVLSQTYPNIEYIVIDGGSTDGTVDIIK 46
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
8-98 1.08e-03

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 39.95  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798    8 SIVVPVYNEElviQTTY--QRLKEVMDQTKEHYELIFVNDGSKDRSIEILReqSLIDPRVKII---DFSRNFGHQIAITA 82
Cdd:pfam10111   1 SVVIPVYNGE---KTHWiqERILNQTFQYDPEFELIIINDGSTDKTLEEVS--SIKDHNLQVYypnAPDTTYSLAASRNR 75
                          90
                  ....*....|....*.
gi 494884798   83 GMDYAEGNAIAVIDAD 98
Cdd:pfam10111  76 GTSHAIGEYISFIDGD 91
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
9-124 2.52e-03

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 38.35  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEELVIQTTYQRLKeVMDQTKEHYELIFVNDGSKDRSIEILREQSLI-----DPRVKIIDFSRNFG-HQIAITA 82
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLK-AQDYPRELYRIFVVADNCTDDTAQVARAAGATvlerhDPERRGKGYALDFGfRHLLNLA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494884798  83 GmDYaegNAIAVIDADLQDPPELILDMIEQWKEGYDVVYAVR 124
Cdd:cd06438   80 D-DP---DAVVVFDADNLVDPNALEELNARFAAGARVVQAYY 117
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
8-170 3.62e-03

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 38.15  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNE--ELVIQTtyqrLKEVMDQTKEHYELIFVNDGSKD----RSIEILREQslIDPRVKIIDFSRNFGHQI-AI 80
Cdd:cd06435    1 SIHVPCYEEppEMVKET----LDSLAALDYPNFEVIVIDNNTKDealwKPVEAHCAQ--LGERFRFFHVEPLPGAKAgAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798  81 TAGMDYAEGNA--IAVIDADLQDPPELILDMIEQWKE-GYDVVYAVRTKRKGETFFKKQTASMFYRLLRSV-----TDID 152
Cdd:cd06435   75 NYALERTAPDAeiIAVIDADYQVEPDWLKRLVPIFDDpRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIgmvsrNERN 154
                        170
                 ....*....|....*...
gi 494884798 153 IPLDTGDFRLLDRKVCDE 170
Cdd:cd06435  155 AIIQHGTMCLIRRSALDD 172
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-74 4.50e-03

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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 37.61  E-value: 4.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494884798   8 SIVVPVYNEELVIQttyQRLKEVMDQTKEHYELIFVNDGSKDRSIEILREQSLIDPRVKIID-------FSRNF 74
Cdd:cd04196    1 AVLMATYNGEKYLR---EQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIrngknlgVARNF 71
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
9-93 8.30e-03

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 37.05  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   9 IVVPVYNEElviQTTYQRLKEVMDQT-KEHYELIFVNDGSKDRSIEILR--EQSLIDPRVKIIDFSRNFGHqiaiTAGMD 85
Cdd:cd06913    1 IILPVHNGE---QWLDECLESVLQQDfEGTLELSVFNDASTDKSAEIIEkwRKKLEDSGVIVLVGSHNSPS----PKGVG 73

                 ....*...
gi 494884798  86 YAEGNAIA 93
Cdd:cd06913   74 YAKNQAIA 81
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
8-110 9.19e-03

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 36.85  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494884798   8 SIVVPVYNEELviqttyQRLKEVMDQTKEH--YELIFVNDGSKDRSIEILrEQSLIDPRVKIIDFSRNfGHQIAITAGMD 85
Cdd:cd06434    3 TVIIPVYDEDP------DVFRECLRSILRQkpLEIIVVTDGDDEPYLSIL-SQTVKYGGIFVITVPHP-GKRRALAEGIR 74
                         90       100
                 ....*....|....*....|....*
gi 494884798  86 YAEGNAIAVIDADLQDPPELILDMI 110
Cdd:cd06434   75 HVTTDIVVLLDSDTVWPPNALPEML 99
 
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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