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Conserved domains on  [gi|2525868524|ref|WP_287629201|]
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MULTISPECIES: glycosyltransferase family 2 protein [unclassified Microcystis]

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
PubMed:  12691742|9445404|16037492|10521532
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 ...
 6-187 3.47e-99

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: 289.38  E-value: 3.47e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELYRRVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFCR 85
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  86 GQVIIVLDADLQDPPELIPQMIEKWQEGYQVVYAQRTKRKqESWFKKLTAYLFYRLLKRLADVDIPADTGDFCLMDRQVV 165
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                         170       180
                  ....*....|....*....|..
gi 2525868524 166 DLLNSLPERNRYIRGLRAWIGF 187
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 ...
 6-187 3.47e-99

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: 289.38  E-value: 3.47e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELYRRVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFCR 85
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  86 GQVIIVLDADLQDPPELIPQMIEKWQEGYQVVYAQRTKRKqESWFKKLTAYLFYRLLKRLADVDIPADTGDFCLMDRQVV 165
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                         170       180
                  ....*....|....*....|..
gi 2525868524 166 DLLNSLPERNRYIRGLRAWIGF 187
Cdd:cd04187   160 DALLLLPERHRFLRGLIAWVGF 181
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 3-308 1.43e-54

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 180.32  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   3 KYSLIVPIYNEEETIAELYRRVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKA-DSRVCYISFARNFGHQAAVTAGL 81
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIMAGF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  82 NFCRGQVIIVLDADLQDPPELIPQMIEKWQEGYQVVYAQRTKRkQESWFKKLTAYLFYRLLKRLADVDIpadtGDFCLM- 160
Cdd:PRK10714   87 SHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNR-QDSWFRKTASKMINRLIQRTTGKAM----GDYGCMl 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524 161 ---DRQVVDLLNSLPERNRYIrglrawigfPQTAVKFERDA---------RFAGEVKYTFSKSLSLAINSLVSFSRVPLR 228
Cdd:PRK10714  162 rayRRHIVDAMLHCHERSTFI---------PILANTFARRAieipvhhaeREFGDSKYSFMRLINLMYDLVTCLTTTPLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524 229 FATYLGLFSALISLIMALLVLYWRLQ-QPNSPITGFATIMIAIFFLGSVQLISIGILGEYIGRIYDEVKGRPTYTIAELA 307
Cdd:PRK10714  233 LLSLLGSIIAIGGFSLAVLLVVLRLTfGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVV 312


                  .
gi 2525868524 308 G 308
Cdd:PRK10714  313 R 313
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-215 5.57e-45

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 152.16  E-value: 5.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   1 MLKYSLIVPIYNEEETIAELYRRVSAImnnLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAG 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQ---TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  81 LNFCRGQVIIVLDADLQDPPELIPQMIEKWQE-GYQVVYAQRTKRKQESWFKKLTAYLFYrLLKRLAdvDIPADTGDFCL 159
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2525868524 160 MDRQVVDLLNsLPERNRYIRGL--RAWIGFPQTAVKFERDarfAGEVKYTFSKSLSLA 215
Cdd:COG0463   155 FRREVLEELG-FDEGFLEDTELlrALRHGFRIAEVPVRYR---AGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-166 2.27e-36

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 128.28  E-value: 2.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFC 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLET---LESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  85 RGQVIIVLDADLQDPPELIPQMIEKWQE-GYQVVYAQRTKRKQESWFKKLT-----AYLFYRLLKRLADVDIPADTGDFC 158
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 2525868524 159 LMDRQVVD 166
Cdd:pfam00535 158 LYRREALE 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-107 1.42e-07

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: 51.36  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIAELYRRVSAimnnLDGAVELILVNDGSKDSSLKLLRELHkadsrVCYISFARNFGHQ---AAVTAgl 81
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADLQA----LRGDAEVIVVDGGSTDGTVEIARSLG-----AKVIHSPKGRARQmnaGAALA-- 70

                          90       100
                  ....*....|....*....|....*.
gi 2525868524  82 nfcRGQVIIVLDADLQDPPELIPQMI 107
Cdd:TIGR04283  71 ---KGDILLFLHADTRLPKDFLEAIR 93
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 6-187 3.47e-99

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: 289.38  E-value: 3.47e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELYRRVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFCR 85
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  86 GQVIIVLDADLQDPPELIPQMIEKWQEGYQVVYAQRTKRKqESWFKKLTAYLFYRLLKRLADVDIPADTGDFCLMDRQVV 165
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                         170       180
                  ....*....|....*....|..
gi 2525868524 166 DLLNSLPERNRYIRGLRAWIGF 187
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 ...
 6-187 2.01e-67

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: 208.58  E-value: 2.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELYRRVSAIMNNlDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFCR 85
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  86 GQVIIVLDADLQDPPELIPQMIEK-WQEGYQVVYAQRTKRK---QESWFKKLTAYLFYRLLKRLADVDIPADTGDFCLMD 161
Cdd:cd04179    80 GDIVVTMDADLQHPPEDIPKLLEKlLEGGADVVIGSRFVRGggaGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159

                         170       180
                  ....*....|....*....|....*.
gi 2525868524 162 RQVVDLLNSLPERNRYIRGLRAWIGF 187
Cdd:cd04179   160 REVLEALLSLLESNGFEFGLELLVGA 185
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 3-308 1.43e-54

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 180.32  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   3 KYSLIVPIYNEEETIAELYRRVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKA-DSRVCYISFARNFGHQAAVTAGL 81
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIMAGF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  82 NFCRGQVIIVLDADLQDPPELIPQMIEKWQEGYQVVYAQRTKRkQESWFKKLTAYLFYRLLKRLADVDIpadtGDFCLM- 160
Cdd:PRK10714   87 SHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNR-QDSWFRKTASKMINRLIQRTTGKAM----GDYGCMl 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524 161 ---DRQVVDLLNSLPERNRYIrglrawigfPQTAVKFERDA---------RFAGEVKYTFSKSLSLAINSLVSFSRVPLR 228
Cdd:PRK10714  162 rayRRHIVDAMLHCHERSTFI---------PILANTFARRAieipvhhaeREFGDSKYSFMRLINLMYDLVTCLTTTPLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524 229 FATYLGLFSALISLIMALLVLYWRLQ-QPNSPITGFATIMIAIFFLGSVQLISIGILGEYIGRIYDEVKGRPTYTIAELA 307
Cdd:PRK10714  233 LLSLLGSIIAIGGFSLAVLLVVLRLTfGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVV 312


                  .
gi 2525868524 308 G 308
Cdd:PRK10714  313 R 313
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-215 5.57e-45

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 152.16  E-value: 5.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   1 MLKYSLIVPIYNEEETIAELYRRVSAImnnLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAG 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQ---TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  81 LNFCRGQVIIVLDADLQDPPELIPQMIEKWQE-GYQVVYAQRTKRKQESWFKKLTAYLFYrLLKRLAdvDIPADTGDFCL 159
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2525868524 160 MDRQVVDLLNsLPERNRYIRGL--RAWIGFPQTAVKFERDarfAGEVKYTFSKSLSLA 215
Cdd:COG0463   155 FRREVLEELG-FDEGFLEDTELlrALRHGFRIAEVPVRYR---AGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-166 2.27e-36

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 128.28  E-value: 2.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFC 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLET---LESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  85 RGQVIIVLDADLQDPPELIPQMIEKWQE-GYQVVYAQRTKRKQESWFKKLT-----AYLFYRLLKRLADVDIPADTGDFC 158
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 2525868524 159 LMDRQVVD 166
Cdd:pfam00535 158 LYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 6-170 1.41e-24

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: 98.76  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELYRRVSAIMNNLDgaVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFCR 85
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGID--YEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  86 GQVIIVLDADLQDPPELIPQMIEK-WQEGYQVVYAQR-----------TKRKQESWFKKLTAYLFYRLlkRLADVdipad 153
Cdd:cd06442    79 GDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRyvegggvegwgLKRKLISRGANLLARLLLGR--KVSDP----- 151

                         170
                  ....*....|....*..
gi 2525868524 154 TGDFCLMDRQVVDLLNS 170
Cdd:cd06442   152 TSGFRAYRREVLEKLID 168
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-121 1.59e-17

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 80.13  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   1 MLKYSLIVPIYNEEETIAELYRRVSAIMNNLDGaVELILVNDGSKDSSLKLLRELHKA--DSRVCYISFARNFGHQAAVT 78
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIALIVYLIFKALQDVKD-FEIIVVDDGSPDGTQDVVKQLQKVygEDRILLRPRPGKLGLGTAYI 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2525868524  79 AGLNFCRGQVIIVLDADLQDPPELIPQMIEKWQE-GYQVVYAQR 121
Cdd:PLN02726   87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVTGTR 130
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 6-140 2.66e-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: 78.04  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLREL-HKADSRVCYISFARNFGHQAAVTAGLNFC 84
Cdd:cd06423     1 IIVPAYNEEAVIERT---IESLLALDYPKLEVIVVDDGSTDDTLEILEELaALYIRRVLVVRDKENGGKAGALNAGLRHA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2525868524  85 RGQVIIVLDADLQDPPELIPQMIEKWQEGYQVVYAQ---RTKRKQESWFKKLTAYLFYR 140
Cdd:cd06423    78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQgrvRVRNGSENLLTRLQAIEYLS 136
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 6-146 3.52e-17

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: 78.38  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETI-AELYRRVSAIMNNLDGAVELILVNDGSKDSSLKLLREL-HKADSRVCYISFARNFGHQAAVTAGLNF 83
Cdd:cd04188     1 VVIPAYNEEKRLpPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLaRKNPALIRVLTLPKNRGKGGAVRAGMLA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525868524  84 CRGQVIIVLDADLQDPPELIPQMIE-KWQEGYQVVYAQRTKR-----KQESWFKKLTAYLFYRLLKRLA 146
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEEaLKTSGYDIAIGSRAHLasaavVKRSWLRNLLGRGFNFLVRLLL 149
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-120 3.59e-17

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: 77.16  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   7 IVPIYNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAGLNFCRG 86
Cdd:cd00761     2 IIPAYNEEPYLERC---LESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2525868524  87 QVIIVLDADLQDPPELIPQMIE--KWQEGYQVVYAQ 120
Cdd:cd00761    79 EYILFLDADDLLLPDWLERLVAelLADPEADAVGGP 114
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 2-165 6.12e-15

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 74.03  E-value: 6.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   2 LKYSLIVPIYNEEETIAELYRRVSAIMNNLDG-----AVELILVNDGSKDSSLKL----LRELHKADSRVCYISFARNFG 72
Cdd:PTZ00260   70 VDLSIVIPAYNEEDRLPKMLKETIKYLESRSRkdpkfKYEIIIVNDGSKDKTLKVakdfWRQNINPNIDIRLLSLLRNKG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  73 HQAAVTAGLNFCRGQVIIVLDAD----LQDPPELIPQMIEKWQEGYQVVYAQRTK------RKQESWFKKLTAYLFYRLL 142
Cdd:PTZ00260  150 KGGAVRIGMLASRGKYILMVDADgatdIDDFDKLEDIMLKIEQNGLGIVFGSRNHlvdsdvVAKRKWYRNILMYGFHFIV 229

                         170       180
                  ....*....|....*....|....
gi 2525868524 143 KRLADVDIpADTG-DFCLMDRQVV 165
Cdd:PTZ00260  230 NTICGTNL-KDTQcGFKLFTRETA 252
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-112 1.22e-14

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: 72.85  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   1 MLKYSLIVPIYNEEETIAELYRRVSAiMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYISFARNFGHQAAVTAG 80
Cdd:COG1215    28 LPRVSVIIPAYNEEAVIEETLRSLLA-QDYPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAG 106

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2525868524  81 LNFCRGQVIIVLDADLQDPPELIPQMIEKWQE 112
Cdd:COG1215   107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFAD 138
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-108 5.26e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 66.55  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   1 MLKYSLIVPIYNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHkaDSRVCYISFARNFGHQAAVTAG 80
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRC---LESLLAQTYPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLG 76

                          90       100
                  ....*....|....*....|....*...
gi 2525868524  81 LNFCRGQVIIVLDADLQDPPELIPQMIE 108
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEPDWLERLLA 104
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 5-109 1.06e-07

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: 51.85  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIAELYRrvsAIMNNLD--GAVELILVNDGSKDSSLKLLRELHKADSRV-------CYISFARNFGHQA 75
Cdd:cd02525     3 SIIIPVRNEEKYIEELLE---SLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIrlidnpkRIQSAGLNIGIRN 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2525868524  76 AvtaglnfcRGQVIIVLDADLQDPPELIPQMIEK 109
Cdd:cd02525    80 S--------RGDIIIRVDAHAVYPKDYILELVEA 105
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-107 1.42e-07

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: 51.36  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIAELYRRVSAimnnLDGAVELILVNDGSKDSSLKLLRELHkadsrVCYISFARNFGHQ---AAVTAgl 81
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADLQA----LRGDAEVIVVDGGSTDGTVEIARSLG-----AKVIHSPKGRARQmnaGAALA-- 70

                          90       100
                  ....*....|....*....|....*.
gi 2525868524  82 nfcRGQVIIVLDADLQDPPELIPQMI 107
Cdd:TIGR04283  71 ---KGDILLFLHADTRLPKDFLEAIR 93
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-108 4.29e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.81  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   2 LKYSLIVPIYNEEETIAELYrrVSAIMNNLDgAVELILVNDGSKDSSLKLLRE----------LHKADSRVcyiSFARNF 71
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFM--ESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHyaenyphvrlLHQANAGV---SVARNT 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2525868524  72 GHQAAvtaglnfcRGQVIIVLDADLQDPPELIPQMIE 108
Cdd:PRK10073   80 GLAVA--------TGKYVAFPDADDVVYPTMYETLMT 108
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 5-95 9.76e-07

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 48.35  E-value: 9.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIaeLYRRVSAIMNNLDGAVELILVNDGSKDSSLK-LLRELHKADSRVCYIsFARNFGHQAAVT-AGLN 82
Cdd:cd04184     4 SIVMPVYNTPEKY--LREAIESVRAQTYPNWELCIADDASTDPEVKrVLKKYAAQDPRIKVV-FREENGGISAATnSALE 80

                          90
                  ....*....|...
gi 2525868524  83 FCRGQVIIVLDAD 95
Cdd:cd04184    81 LATGEFVALLDHD 93
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-188 1.75e-06

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: 48.14  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   4 YSLIVPIYNEEETIAELYRRVSAIMNnldGAVELILVNDGSKDSSLKLLRELHKA--DSRVCYISFARNFGHQAAVTA-- 79
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPY---PPVEVVVVVNPSDAETLDVAEEIAARfpDVRLRVIRNARLLGPTGKSRGln 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  80 -GLNFCRGQVIIVLDADLQDPPELIPQMI-----EKWQEGYQVVYAQRTKRKQESWFKKLTAYLFYRLLKRLADVDIPAD 153
Cdd:pfam13641  81 hGFRAVKSDLVVLHDDDSVLHPGTLKKYVqyfdsPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRLALGVLPL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2525868524 154 TGDFCLMDRQVV------DLLNSLPErnRYIRGLRAWI-GFP 188
Cdd:pfam13641 161 SGAGSAIRREVLkelglfDPFFLLGD--DKSLGRRLRRhGWR 200
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 4-109 2.19e-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: 47.57  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   4 YSLIVPIYNEEETIAELYRRVSAImnnLDGAVELILVNDGSKDSSLKLLRELHkadsrVCYISFAR------NFGHQAAv 77
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRL---NPLPLEIIVVDGGSTDGTVAIARSAG-----VVVISSPKgrarqmNAGAAAA- 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2525868524  78 taglnfcRGQVIIVLDADLQDPPELIPQMIEK 109
Cdd:cd02522    72 -------RGDWLLFLHADTRLPPDWDAAIIET 96
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-95 3.52e-06

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: 47.58  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   3 KYSLIVPIYNEEETIAELYRRVSAimnnLD---GAVELILVNDGSKDSSLKLLRELhkADSRVCYISFARNFGHQAAVTA 79
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLA----LDyprDRLEIIVVSDGSTDGTAEIAREY--ADKGVKLLRFPERRGKAAALNR 103

                          90
                  ....*....|....*.
gi 2525868524  80 GLNFCRGQVIIVLDAD 95
Cdd:cd06439   104 ALALATGEIVVFTDAN 119
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-133 2.20e-05

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: 44.97  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELYRRVSAImNNLDGAVELILVNDGSKDSSLKLLRELH-KADSRVCYISFAR--NFGHQAAVTAGLN 82
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSAL-DYPKEKFEVILVDDHSTDGTVQILEFAAaKPNFQLKILNNSRvsISGKKNALTTAIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2525868524  83 FCRGQVIIVLDADLQDPPELIPQMIEKWQ-EGYQVVYAQRTKRKQESWFKKL 133
Cdd:cd04192    80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQkEQIGLVAGPVIYFKGKSLLAKF 131
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 6-95 2.88e-04

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: 41.29  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   6 LIVPIYNEEETIAELYRRVSAimNNLDGAVELILVNDGSKDSSLKLLRELHK--ADSRVCYISFARNFGHQAAVTAGLNF 83
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQ--QDFEGTLELSVFNDASTDKSAEIIEKWRKklEDSGVIVLVGSHNSPSPKGVGYAKNQ 78

                          90
                  ....*....|....*.
gi 2525868524  84 C----RGQVIIVLDAD 95
Cdd:cd06913    79 AiaqsSGRYLCFLDSD 94
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 8-101 4.15e-04

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: 41.14  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   8 VPIYNEEETIAELyrrvsaimnnLDGAVEL--------ILVNDGSKDSSLKLLREL--HKADS--RVCYISFARNFGHQA 75
Cdd:cd06437     7 LPVFNEKYVVERL----------IEAACALdypkdrleIQVLDDSTDETVRLAREIveEYAAQgvNIKHVRRADRTGYKA 76

                          90       100
                  ....*....|....*....|....*..
gi 2525868524  76 -AVTAGLNFCRGQVIIVLDADLQDPPE 101
Cdd:cd06437    77 gALAEGMKVAKGEYVAIFDADFVPPPD 103
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-108 4.57e-04

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: 40.24  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   7 IVPIYNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLRELhkaDSRVCYISFARNFGHQAAVTAGLNFCRG 86
Cdd:cd04186     2 IIVNYNSLEYLKAC---LDSLLAQTYPDFEVIVVDNASTDGSVELLREL---FPEVRLIRNGENLGFGAGNNQGIREAKG 75

                          90       100
                  ....*....|....*....|..
gi 2525868524  87 QVIIVLDADLQDPPELIPQMIE 108
Cdd:cd04186    76 DYVLLLNPDTVVEPGALLELLD 97
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 5-94 1.27e-03

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: 39.88  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIaeLYRRVSAIMN--NLDGAVELILVNDGSKDSSLK-LLRELHKA----------DSRVCYISfARNF 71
Cdd:cd02510     1 SVIIIFHNEALST--LLRTVHSVINrtPPELLKEIILVDDFSDKPELKlLLEEYYKKylpkvkvlrlKKREGLIR-ARIA 77

                          90       100
                  ....*....|....*....|...
gi 2525868524  72 GHQAAVtaglnfcrGQVIIVLDA 94
Cdd:cd02510    78 GARAAT--------GDVLVFLDS 92
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-95 2.34e-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: 38.80  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETiAELYRRVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVcYISFA--RNFGHQAAVTAGLN 82
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQV-YYPNApdTTYSLAASRNRGTS 78

                          90
                  ....*....|...
gi 2525868524  83 FCRGQVIIVLDAD 95
Cdd:pfam10111  79 HAIGEYISFIDGD 91
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-98 2.65e-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: 38.38  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524  11 YNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLRELHKADSRVCYI-------SFARNFGHqaavtaGLNF 83
Cdd:cd04196     7 YNGEKYLREQ---LDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILirngknlGVARNFES------LLQA 77

                          90
                  ....*....|....*
gi 2525868524  84 CRGQVIIVLDadlQD 98
Cdd:cd04196    78 ADGDYVFFCD---QD 89
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 5-95 3.27e-03

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: 37.91  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIAELyrrVSAIMNNLDGAVELILVNDGSKDSSLKLLRELhkADSRVCYISfARNFGHQAAVTAGLNFC 84
Cdd:cd06433     1 SIITPTYNQAETLEET---IDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKY--EDKITYWIS-EPDKGIYDAMNKGIALA 74

                          90
                  ....*....|.
gi 2525868524  85 RGQVIIVLDAD 95
Cdd:cd06433    75 TGDIIGFLNSD 85
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 5-104 4.00e-03

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 38.36  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525868524   5 SLIVPIYNEEETIAELyrrVSAIMNNLDGAV--ELILVNDGSKDSSLKLLRElhkADSRVCYIS-----FARNFGHQAAV 77
Cdd:PRK13915   34 SVVLPALNEEETVGKV---VDSIRPLLMEPLvdELIVIDSGSTDATAERAAA---AGARVVSREeilpeLPPRPGKGEAL 107

                          90       100
                  ....*....|....*....|....*...
gi 2525868524  78 TAGLNFCRGQVIIVLDADLQDP-PELIP 104
Cdd:PRK13915  108 WRSLAATTGDIVVFVDADLINFdPMFVP 135
 
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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