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Conserved domains on  [gi|1926444691|gb|QOV09104|]
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putative glycosyltransferase [uncultured Actinomycetes bacterium]

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 ...
11-192 1.35e-77

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: 234.68  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  11 IVVPVFNEVDNVAIFHQRVSEVAASLTaYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTKA 90
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLG-YDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  91 RGVAAIQLDVDLQDPPELIADFIAHWESGYKVVYGIRRSRKEGRAITTARKIFYRLVNVLSEDPIPVDAGDFRLVDRVVL 170
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|..
gi 1926444691 171 DELIAMPDSQPYLRGAIASLGF 192
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 ...
11-192 1.35e-77

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: 234.68  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  11 IVVPVFNEVDNVAIFHQRVSEVAASLTaYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTKA 90
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLG-YDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  91 RGVAAIQLDVDLQDPPELIADFIAHWESGYKVVYGIRRSRKEGRAITTARKIFYRLVNVLSEDPIPVDAGDFRLVDRVVL 170
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|..
gi 1926444691 171 DELIAMPDSQPYLRGAIASLGF 192
Cdd:cd04187   160 DALLLLPERHRFLRGLIAWVGF 181
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-219 8.95e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.88  E-value: 8.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691   6 KPLISIVVPVFNEVDNVAIFHQRVSEVaaslTAYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWT 85
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQ----TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  86 GYTKARGVAAIQLDVDLQDPPELIADFIAHWES-GYKVVYGIRRSRKEGRAITTARKIFYRLVNVLSedPIPVDAGDFRL 164
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLVRLLT--NLPDSTSGFRL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1926444691 165 VDRVVLDELI---AMPDSQPYLRgaIASLGFDQIGIPYDREArerGESKFSFKDLIGL 219
Cdd:COG0463   155 FRREVLEELGfdeGFLEDTELLR--ALRHGFRIAEVPVRYRA---GESKLNLRDLLRL 207
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
9-312 1.84e-30

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 117.14  E-value: 1.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691   9 ISIVVPVFNEVDNVAIFHQRVSEVAASLTAyEFEFVFTDNHSSDGTfAALAEIAAADPRVRVFS--FSRNFGFQRSIWTG 86
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAACESLGK-EYEILLIDDGSSDNS-AEMLVEAAQAPDSHIVAilLNRNYGQHSAIMAG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  87 YTKARGVAAIQLDVDLQDPPELIADFIAHWESGYKVVYGIRRSRKEgraiTTARKIFYRLVNVLSEDPIPVDAGDF---- 162
Cdd:PRK10714   86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD----SWFRKTASKMINRLIQRTTGKAMGDYgcml 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691 163 RLVDRVVLDELIAMPDSQPYLRGAIASLGFDQIGIPYDREARERGESKFSFKDLIGLSLDAILNHSIIPLRIASYVGLTV 242
Cdd:PRK10714  162 RAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSII 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926444691 243 AGVTLIGTIGMFIARWLFGADWPAGFATTTVLILFsISLNALF--LGIIGEYLGRIYKQVKPSSITVIEKAI 312
Cdd:PRK10714  242 AIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLF-TFIGAQFigMGLLGEYIGRIYNDVRARPRYFVQQVV 312
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-172 2.38e-15

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: 72.43  E-value: 2.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  10 SIVVPVFNEVDNVAIFHQRVsevaASLTAYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTK 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL----LNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  90 ARGVAAIQLDVDLQDPPELIADFIAHWES-GYKVVYGIRRSRKEGRA------ITTARKIFYRLVNVLSEDPIPVDAGDF 162
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGeyrrasRITLSRLPFFLGLRLLGLNLPFLIGGF 156
                         170
                  ....*....|
gi 1926444691 163 RLVDRVVLDE 172
Cdd:pfam00535 157 ALYRREALEE 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 ...
11-192 1.35e-77

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: 234.68  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  11 IVVPVFNEVDNVAIFHQRVSEVAASLTaYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTKA 90
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLG-YDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  91 RGVAAIQLDVDLQDPPELIADFIAHWESGYKVVYGIRRSRKEGRAITTARKIFYRLVNVLSEDPIPVDAGDFRLVDRVVL 170
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|..
gi 1926444691 171 DELIAMPDSQPYLRGAIASLGF 192
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 ...
11-192 6.89e-47

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: 156.19  E-value: 6.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  11 IVVPVFNEVDNVAIFHQRVSEVAASltAYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTKA 90
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE--GYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  91 RGVAAIQLDVDLQDPPELIADFIA-HWESGYKVVYGIRRSRKEGRAITTAR----KIFYRLVNVLSEDPIPVDAGDFRLV 165
Cdd:cd04179    79 RGDIVVTMDADLQHPPEDIPKLLEkLLEGGADVVIGSRFVRGGGAGMPLLRrlgsRLFNFLIRLLLGVRISDTQSGFRLF 158
                         170       180
                  ....*....|....*....|....*..
gi 1926444691 166 DRVVLDELIAMPDSQPYLRGAIASLGF 192
Cdd:cd04179   159 RREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-219 8.95e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.88  E-value: 8.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691   6 KPLISIVVPVFNEVDNVAIFHQRVSEVaaslTAYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWT 85
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQ----TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  86 GYTKARGVAAIQLDVDLQDPPELIADFIAHWES-GYKVVYGIRRSRKEGRAITTARKIFYRLVNVLSedPIPVDAGDFRL 164
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLVRLLT--NLPDSTSGFRL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1926444691 165 VDRVVLDELI---AMPDSQPYLRgaIASLGFDQIGIPYDREArerGESKFSFKDLIGL 219
Cdd:COG0463   155 FRREVLEELGfdeGFLEDTELLR--ALRHGFRIAEVPVRYRA---GESKLNLRDLLRL 207
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
9-312 1.84e-30

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 117.14  E-value: 1.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691   9 ISIVVPVFNEVDNVAIFHQRVSEVAASLTAyEFEFVFTDNHSSDGTfAALAEIAAADPRVRVFS--FSRNFGFQRSIWTG 86
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAACESLGK-EYEILLIDDGSSDNS-AEMLVEAAQAPDSHIVAilLNRNYGQHSAIMAG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  87 YTKARGVAAIQLDVDLQDPPELIADFIAHWESGYKVVYGIRRSRKEgraiTTARKIFYRLVNVLSEDPIPVDAGDF---- 162
Cdd:PRK10714   86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD----SWFRKTASKMINRLIQRTTGKAMGDYgcml 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691 163 RLVDRVVLDELIAMPDSQPYLRGAIASLGFDQIGIPYDREARERGESKFSFKDLIGLSLDAILNHSIIPLRIASYVGLTV 242
Cdd:PRK10714  162 RAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSII 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926444691 243 AGVTLIGTIGMFIARWLFGADWPAGFATTTVLILFsISLNALF--LGIIGEYLGRIYKQVKPSSITVIEKAI 312
Cdd:PRK10714  242 AIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLF-TFIGAQFigMGLLGEYIGRIYNDVRARPRYFVQQVV 312
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-172 2.38e-15

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: 72.43  E-value: 2.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  10 SIVVPVFNEVDNVAIFHQRVsevaASLTAYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTK 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL----LNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  90 ARGVAAIQLDVDLQDPPELIADFIAHWES-GYKVVYGIRRSRKEGRA------ITTARKIFYRLVNVLSEDPIPVDAGDF 162
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGeyrrasRITLSRLPFFLGLRLLGLNLPFLIGGF 156
                         170
                  ....*....|
gi 1926444691 163 RLVDRVVLDE 172
Cdd:pfam00535 157 ALYRREALEE 166
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
11-217 1.64e-14

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: 71.41  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  11 IVVPVFNEVDNVAIFHQRVSevaASLTAYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTKA 90
Cdd:cd06442     1 IIIPTYNERENIPELIERLD---AALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  91 RGVAAIQLDVDLQDPPELIADFI-AHWESGYKVVYGIRRSRK---EGRAITtaRKIFYRLVNVLSE--------DPIpvd 158
Cdd:cd06442    78 RGDVIVVMDADLSHPPEYIPELLeAQLEGGADLVIGSRYVEGggvEGWGLK--RKLISRGANLLARlllgrkvsDPT--- 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926444691 159 aGDFRLVDRVVLDELIAMPDSQPY-----LRGAIASLGFDQIGIPYDREARERGESKFSFKDLI 217
Cdd:cd06442   153 -SGFRAYRREVLEKLIDSLVSKGYkfqleLLVRARRLGYRIVEVPITFVDREHGESKLGGKEIV 215
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
2-182 2.47e-11

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 62.79  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691   2 AKPQKPLISIVVPVFNEVDNVAIFHQRVSEVAASltAYEFEFVFTDNHSSDGT--FAALAEIAAADPRVRVFSFSRNFGF 79
Cdd:PLN02726    4 PGEGAMKYSIIVPTYNERLNIALIVYLIFKALQD--VKDFEIIVVDDGSPDGTqdVVKQLQKVYGEDRILLRPRPGKLGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  80 QRSIWTGYTKARGVAAIQLDVDLQDPPELIADFIA-HWESGYKVVYGIRRSRKEGRA-ITTARKIFYRLVNVLSE---DP 154
Cdd:PLN02726   82 GTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKkQRETGADIVTGTRYVKGGGVHgWDLRRKLTSRGANVLAQtllWP 161
                         170       180
                  ....*....|....*....|....*....
gi 1926444691 155 IPVD-AGDFRLVDRVVLDELIAMPDSQPY 182
Cdd:PLN02726  162 GVSDlTGSFRLYKRSALEDLVSSVVSKGY 190
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
11-150 6.83e-07

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: 49.10  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  11 IVVPVFNEVDNVAIFHQRVSEVAASLTAYEFEFVFTDNHSSDGTFAALAEIAAADP-RVRVFSFSRNFGFQRSIWTGYTK 89
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPaLIRVLTLPKNRGKGGAVRAGMLA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926444691  90 ARGVAAIQLDVDLQDPPELIADFI-AHWESGYKVVYGIRRSRKEGRAIT--TARKI----FYRLVNVL 150
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEeALKTSGYDIAIGSRAHLASAAVVKrsWLRNLlgrgFNFLVRLL 148
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-129 1.38e-05

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: 45.89  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691   2 AKPQKPLISIVVPVFNEVDNVAifhqrvsEVAASLTA-----YEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRN 76
Cdd:COG1215    24 APADLPRVSVIIPAYNEEAVIE-------ETLRSLLAqdypkEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPEN 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1926444691  77 FGFQRSIWTGYTKARGVAAIQLDVDLQDPPELIADFIAHWESGYKVVYG----IRRS 129
Cdd:COG1215    97 GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGanlaFRRE 153
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
11-125 1.68e-05

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: 44.42  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691  11 IVVPVFNEVDNVAifhqRVSEVAASLTAYEFEFVFTDNHSSDGTFAALAEIAAADPRVRVFSFSRNFGFQRSIWTGYTKA 90
Cdd:cd00761     1 VIIPAYNEEPYLE----RCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1926444691  91 RGVAAIQLDVDLQDPPELIADFIA--HWESGYKVVYG 125
Cdd:cd00761    77 RGEYILFLDADDLLLPDWLERLVAelLADPEADAVGG 113
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
6-116 5.02e-05

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 43.44  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926444691   6 KPLISIVVPVFNEVDNVAIFHQRVsevaASLTAYEFEFVFTDNHSSDGTfaALAEIAAADPRVRVFSFSRNFGFqrsiwt 85
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESL----LAQTYPPFEVIVVDNGSTDGT--AELLAALAFPRVRVIRNPENLGF------ 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1926444691  86 GYTKARGVAAIQ------LDVDLQDPPELIADFIAHW 116
Cdd:COG1216    70 AAARNLGLRAAGgdyllfLDDDTVVEPDWLERLLAAA 106
 
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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