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Conserved domains on  [gi|4503363|ref|NP_003850|]
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dolichol-phosphate mannosyltransferase subunit 1 isoform 3 [Homo sapiens]

Protein Classification

polyprenol monophosphomannose synthase( domain architecture ID 11477088)

polyprenol monophosphomannose synthase transfers mannose from GDP-mannose to lipid acceptors, such as dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 23-260 6.02e-154

dolichyl-phosphate beta-D-mannosyltransferase


:

Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 428.35  E-value: 6.02e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    23 RQNKYSVLLPTYNERENLPLIVWLLVKSFSESGiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAY 102
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   103 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASD 182
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503363   183 LTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 260
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 23-260 6.02e-154

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 428.35  E-value: 6.02e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    23 RQNKYSVLLPTYNERENLPLIVWLLVKSFSESGiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAY 102
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   103 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASD 182
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503363   183 LTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 260
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 29-256 1.10e-133

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: 376.10  E-value: 1.10e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVKSFSesGINYEIIIIDDGSPDGTRDVAEQLEKIYGsdRILLRPREKKLGLGTAYIHGMKH 108
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYIEGFKA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  109 ATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFR 188
Cdd:cd06442  77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503363  189 LYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 256
Cdd:cd06442 157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 26-250 1.38e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 162.18  E-value: 1.38e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   26 KYSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIH 104
Cdd:COG0463   3 LVSVVIPTYNEEEYLEE----ALESLLAqTYPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAARNA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  105 GMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVygwdLKRKIISRGANFLTQILLRPgasDLT 184
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLLTNLP---DST 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503363  185 GSFRLYRKEVLEKLIekcVSKGYVFQMEMIvRARQLNYTIGEVPISFVDrvyGESKLGGNEIVSFL 250
Cdd:COG0463 150 SGFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 28-197 2.54e-43

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: 144.46  E-value: 2.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363     28 SVLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIHGMK 107
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    108 HATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDL-KRKIISRGANFLTQILLRPGASDLTGS 186
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 4503363    187 FRLYRKEVLEK 197
Cdd:pfam00535 156 FALYRREALEE 166
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 23-260 6.02e-154

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 428.35  E-value: 6.02e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    23 RQNKYSVLLPTYNERENLPLIVWLLVKSFSESGiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAY 102
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   103 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASD 182
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503363   183 LTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 260
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 29-256 1.10e-133

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: 376.10  E-value: 1.10e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVKSFSesGINYEIIIIDDGSPDGTRDVAEQLEKIYGsdRILLRPREKKLGLGTAYIHGMKH 108
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYIEGFKA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  109 ATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFR 188
Cdd:cd06442  77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503363  189 LYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 256
Cdd:cd06442 157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 29-217 4.96e-75

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: 226.30  E-value: 4.96e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLvKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPRekKLGLGTAYIHGMKH 108
Cdd:cd04179   1 VVIPAYNEEENIPELVERL-LAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSR--NFGKGAAVRAGFKA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  109 ATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVyGWDLKRKIISRGANFLTQILLRPGASDLTGSFR 188
Cdd:cd04179  78 ARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGA-GMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFR 156

                       170       180
                ....*....|....*....|....*....
gi 4503363  189 LYRKEVLEKLIEKCVSKGYVFQMEMIVRA 217
Cdd:cd04179 157 LFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 26-250 1.38e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 162.18  E-value: 1.38e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   26 KYSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIH 104
Cdd:COG0463   3 LVSVVIPTYNEEEYLEE----ALESLLAqTYPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAARNA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  105 GMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVygwdLKRKIISRGANFLTQILLRPgasDLT 184
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLLTNLP---DST 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503363  185 GSFRLYRKEVLEKLIekcVSKGYVFQMEMIvRARQLNYTIGEVPISFVDrvyGESKLGGNEIVSFL 250
Cdd:COG0463 150 SGFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 28-197 2.54e-43

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: 144.46  E-value: 2.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363     28 SVLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIHGMK 107
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    108 HATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDL-KRKIISRGANFLTQILLRPGASDLTGS 186
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 4503363    187 FRLYRKEVLEK 197
Cdd:pfam00535 156 FALYRREALEE 166
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 29-240 2.77e-40

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: 138.08  E-value: 2.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVKSFSES-GINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRpREKKLGLGTAYIHGMK 107
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEERpSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLT-LPKNRGKGGAVRAGML 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  108 HATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYK-GNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGS 186
Cdd:cd04188  80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHlASAAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4503363  187 FRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRvyGESK 240
Cdd:cd04188 160 FKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEI--PGSK 211
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 29-200 2.20e-36

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: 127.21  E-value: 2.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDR-ILLRpreKKLGLGTAYIHGMK 107
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKvIRLS---RNFGQQAALLAGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  108 HATGNYIIIMDADLSHHPKFIPEFIRKQKEGnFDIVSGTRYKGNGGVYgwdlkRKIISRGANFLTQILLRPGASDLTGSF 187
Cdd:cd04187  78 HARGDAVITMDADLQDPPELIPEMLAKWEEG-YDVVYGVRKNRKESWL-----KRLTSKLFYRLINKLSGVDIPDNGGDF 151

                       170
                ....*....|...
gi 4503363  188 RLYRKEVLEKLIE 200
Cdd:cd04187 152 RLMDRKVVDALLL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 29-146 1.61e-22

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: 90.26  E-value: 1.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIHGMKH 108
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARNAGLKA 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 4503363  109 ATGNYIIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSGT 146
Cdd:cd00761  76 ARGEYILFLDADDLLLPDWLERLVAElLADPEADAVGGP 114
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 25-260 1.70e-20

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 88.64  E-value: 1.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    25 NKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSD--RILLrprEKKLGLGTAY 102
Cdd:PRK10714   6 KKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHivAILL---NRNYGQHSAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   103 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGnFDIVSGTRYKGNGGVYgwdlkRKIISRGANFLTQILLRPGASD 182
Cdd:PRK10714  83 MAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEG-YDVVGTVRQNRQDSWF-----RKTASKMINRLIQRTTGKAMGD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503363   183 LTGSFRLYRKEVLEKLIEkCVSKGYVFQMEMIVRARQlnyTIgEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 260
Cdd:PRK10714 157 YGCMLRAYRRHIVDAMLH-CHERSTFIPILANTFARR---AI-EIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTT 229
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 26-232 7.78e-20

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: 86.72  E-value: 7.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   26 KYSVLLPTYNERENLPLivwlLVKSFSES---GINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKklGLGTAY 102
Cdd:COG1215  30 RVSVIIPAYNEEAVIEE----TLRSLLAQdypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENG--GKAAAL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  103 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKqkegnfdivsgtrykgnggvygwdlkrkiisrganfltqiLLRPGAsD 182
Cdd:COG1215 104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVAA----------------------------------------FADPGV-G 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4503363  183 LTGSFRLYRKEVLEKLiekcvsKGYVFQ-----MEMIVRARQLNYTIGEVPISFV 232
Cdd:COG1215 143 ASGANLAFRREALEEV------GGFDEDtlgedLDLSLRLLRAGYRIVYVPDAVV 191
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 29-198 3.14e-16

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: 74.19  E-value: 3.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKlGLGTAYIHGMKH 108
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENG-GKAGALNAGLRH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  109 ATGNYIIIMDADLSHHPKFIPE-FIRKQKEGNFDIVSGtrykgnggvygwdlKRKIISRGANFLT----------QILLR 177
Cdd:cd06423  77 AKGDIVVVLDADTILEPDALKRlVVPFFADPKVGAVQG--------------RVRVRNGSENLLTrlqaieylsiFRLGR 142

                       170       180
                ....*....|....*....|....*..
gi 4503363  178 PGASDL------TGSFRLYRKEVLEKL 198
Cdd:cd06423 143 RAQSALggvlvlSGAFGAFRREALREV 169
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
26-141 4.32e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.26  E-value: 4.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   26 KYSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEkiygSDRILLRPREKKLGLGTAYIH 104
Cdd:COG1216   4 KVSVVIPTYNRPELLRR----CLESLLAqTYPPFEVIVVDNGSTDGTAELLAALA----FPRVRVIRNPENLGFAAARNL 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 4503363  105 GMKHATGNYIIIMDADLSHHPKFIPE-------FIRK---QKEGNFD 141
Cdd:COG1216  76 GLRAAGGDYLLFLDDDTVVEPDWLERllaaaclLIRRevfEEVGGFD 122
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 28-233 8.63e-16

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 75.57  E-value: 8.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    28 SVLLPTYNERENLPL-----IVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQL--EKIYGSDRILLRPREKKLGLGT 100
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKmlketIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLLSLLRNKGKGG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   101 AYIHGMKHATGNYIIIMDADLSHHpkfIPEFIR------KQKEGNFDIVSGTR--YKGNGGVYGWDLKRKIISRGANFLT 172
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADGATD---IDDFDKledimlKIEQNGLGIVFGSRnhLVDSDVVAKRKWYRNILMYGFHFIV 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503363   173 QILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVD 233
Cdd:PTZ00260 230 NTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTE 290
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 28-198 1.01e-13

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: 68.80  E-value: 1.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   28 SVLLPTYNERENLP-LIVWLLVKSFSESgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLgLGTAYIHGM 106
Cdd:cd02525   3 SIIIPVRNEEKYIEeLLESLLNQSYPKD--LIEIIVVDGGSTDGTREIVQEYAAKD--PRIRLIDNPKRI-QSAGLNIGI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  107 KHATGNYIIIMDADlSHHPK-FIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISR----GANFltqillRPGAS 181
Cdd:cd02525  78 RNSRGDIIIRVDAH-AVYPKdYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSPlgsgGSAY------RGGAV 150

                       170       180
                ....*....|....*....|.
gi 4503363  182 DL----TGSFRLYRKEVLEKL 198
Cdd:cd02525 151 KIgyvdTVHHGAYRREVFEKV 171
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 29-153 2.13e-11

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: 61.92  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLivwlLVKSFSEsgINY-----EIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKL-GLGTAY 102
Cdd:cd04192   1 VVIAARNEAENLPR----LLQSLSA--LDYpkekfEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVSIsGKKNAL 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4503363  103 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSGTRYKGNGG 153
Cdd:cd04192  75 TTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFiQKEQIGLVAGPVIYFKGKS 126
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 29-149 1.65e-10

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 58.36  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVksfSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRprEKKLGLGTAYI--HGM 106
Cdd:cd06420   1 LIITTYNRPEALELVLKSVL---NQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVW--QEDEGFRKAKIrnKAI 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4503363  107 KHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFdiVSGTRYK 149
Cdd:cd06420  76 AAAKGDYLIFIDGDCIPHPDFIADHIELAEPGVF--LSGSRVL 116
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 28-120 5.84e-10

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: 57.64  E-value: 5.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   28 SVLLPTYN-ERenlplivWLL--VKS-FSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPrEKKLGLGTAYI 103
Cdd:cd04196   1 AVLMATYNgEK-------YLReqLDSiLAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRN-GKNLGVARNFE 72

                        90
                ....*....|....*..
gi 4503363  104 HGMKHATGNYIIIMDAD 120
Cdd:cd04196  73 SLLQAADGDYVFFCDQD 89
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 24-239 2.02e-09

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: 56.23  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363     24 QNKYSVLLPTYNERENL-PLIVWLLVKSFsesgINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLG--- 99
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLgRVLEAILAQPY----PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgks 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    100 TAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYgWDL--KRKIISRGANFLtQILLR 177
Cdd:pfam13641  77 RGLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTM-LSAlgALEFALRHLRMM-SLRLA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503363    178 PGASDLTGSFRLYRKEVLeKLIEKCVSKGYVFQ-MEMIVRARQLNYTIGEVPISFVDRVYGES 239
Cdd:pfam13641 155 LGVLPLSGAGSAIRREVL-KELGLFDPFFLLGDdKSLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 25-142 1.21e-08

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 54.67  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    25 NKYSVLLPTYNERENLPlivwllvkSFSESGI-----NYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILlrpREKKLGLG 99
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFR--------AFMESLIaqtwtALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL---HQANAGVS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 4503363   100 TAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDI 142
Cdd:PRK10073  75 VARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDV 117
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 28-120 1.22e-07

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: 51.14  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   28 SVLLPTYNERENLP--LIVwllVKSFSEsginyEIIIIDDGSPDGTRDVAEQlekiYGsDRILLRPrekKLGLGTAYIHG 105
Cdd:cd02511   3 SVVIITKNEERNIErcLES---VKWAVD-----EIIVVDSGSTDRTVEIAKE----YG-AKVYQRW---WDGFGAQRNFA 66

                        90
                ....*....|....*
gi 4503363  106 MKHATGNYIIIMDAD 120
Cdd:cd02511  67 LELATNDWVLSLDAD 81
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 29-133 1.82e-07

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 49.48  E-value: 1.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLivwlLVKSF-SESGINYEIIIIDDGSPDGTRDVAEQLEKiygsDRILLRPrEKKLGLGTAYIHGMK 107
Cdd:cd04186   1 IIIVNYNSLEYLKA----CLDSLlAQTYPDFEVIVVDNASTDGSVELLRELFP----EVRLIRN-GENLGFGAGNNQGIR 71

                        90       100
                ....*....|....*....|....*.
gi 4503363  108 HATGNYIIIMDADLSHHPKFIPEFIR 133
Cdd:cd04186  72 EAKGDYVLLLNPDTVVEPGALLELLD 97
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 26-120 5.39e-07

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: 49.50  E-value: 5.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   26 KYSVLLPTYNEREnlplivWLLVKSFSESGINY-----EIIIIDDGSPDGTRDVAEQlekiYGSDRILLRPREKKLGLGT 100
Cdd:cd06439  30 TVTIIIPAYNEEA------VIEAKLENLLALDYprdrlEIIVVSDGSTDGTAEIARE----YADKGVKLLRFPERRGKAA 99

                        90       100
                ....*....|....*....|
gi 4503363  101 AYIHGMKHATGNYIIIMDAD 120
Cdd:cd06439 100 ALNRALALATGEIVVFTDAN 119
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 28-134 6.75e-07

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: 48.85  E-value: 6.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   28 SVLLPTYNEREnlplIVWLLVKSFSEsgINY-----EIIIIDDGSPDGTRDVAEQLEKIYGSD-RILLRPREKKLGL-GT 100
Cdd:cd06437   4 TVQLPVFNEKY----VVERLIEAACA--LDYpkdrlEIQVLDDSTDETVRLAREIVEEYAAQGvNIKHVRRADRTGYkAG 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 4503363  101 AYIHGMKHATGNYIIIMDADLShhPKfiPEFIRK 134
Cdd:cd06437  78 ALAEGMKVAKGEYVAIFDADFV--PP--PDFLQK 107
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 27-120 8.38e-07

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: 48.34  E-value: 8.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   27 YSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEKiygsdrillRPREKKLGLGTAYIHG 105
Cdd:cd02522   1 LSIIIPTLNEAENLPR----LLASLRRlNPLPLEIIVVDGGSTDGTVAIARSAGV---------VVISSPKGRARQMNAG 67

                        90
                ....*....|....*
gi 4503363  106 MKHATGNYIIIMDAD 120
Cdd:cd02522  68 AAAARGDWLLFLHAD 82
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 28-240 1.55e-06

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: 47.54  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   28 SVLLPTYNERENLPLivwlLVKS-FSESGINYEIIIIDDGSPDGTRDVAeqleKIYGSDRILLRpREKKLGLGTAYIHGM 106
Cdd:cd06433   1 SIITPTYNQAETLEE----TIDSvLSQTYPNIEYIVIDGGSTDGTVDII----KKYEDKITYWI-SEPDKGIYDAMNKGI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  107 KHATGNYIIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSgtrykGNGGVYGWDLKRKIISRGANFLTQILLR------PG 179
Cdd:cd06433  72 ALATGDIIGFLNSDDTLLPGALLAVVAAfAEHPEVDVVY-----GDVLLVDENGRVIGRRRPPPFLDKFLLYgmpichQA 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503363  180 AsdltgsfrLYRKEVLEKLieKCVSKGYVFQM--EMIVRARQLNYTIGEVPISFVD-RVYGESK 240
Cdd:cd06433 147 T--------FFRRSLFEKY--GGFDESYRIAAdyDLLLRLLLAGKIFKYLPEVLAAfRLGGVSS 200
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 28-120 1.88e-06

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: 47.20  E-value: 1.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   28 SVLLPTYNerenlPLIVWL--LVKSF-SESGINYEIIIIDDGSPDgtRDVAEQLEKIYGSD-RILLRPREKKLGLGTAYI 103
Cdd:cd04184   4 SIVMPVYN-----TPEKYLreAIESVrAQTYPNWELCIADDASTD--PEVKRVLKKYAAQDpRIKVVFREENGGISAATN 76

                        90
                ....*....|....*..
gi 4503363  104 HGMKHATGNYIIIMDAD 120
Cdd:cd04184  77 SALELATGEFVALLDHD 93
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 29-198 2.88e-06

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 47.18  E-value: 2.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   29 VLLPTYNERENLPLIVWLLVKsfsesGINY-----EIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREK-KLGlgtAY 102
Cdd:cd06421   5 VFIPTYNEPLEIVRKTLRAAL-----AIDYphdklRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHaKAG---NL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  103 IHGMKHATGNYIIIMDADLSHHPKF----IPEFIRKQKEG---------NFDIVSGTrykGNGGVYGWDLKRKIISRGAN 169
Cdd:cd06421  77 NNALAHTTGDFVAILDADHVPTPDFlrrtLGYFLDDPKVAlvqtpqffyNPDPFDWL---ADGAPNEQELFYGVIQPGRD 153

                       170       180
                ....*....|....*....|....*....
gi 4503363  170 FLtqillrpGASDLTGSFRLYRKEVLEKL 198
Cdd:cd06421 154 RW-------GAAFCCGSGAVVRREALDEI 175
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 28-146 7.00e-06

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 45.77  E-value: 7.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   28 SVLLPTYNeRENLPLIVWLLVKSFSESGINYEIIIIDDGS-PDGTRDVAEQLEKIYGSDRILLrprEKKLGLGTAYIHGM 106
Cdd:cd04195   1 SVLMSVYI-KEKPEFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPL---EKNRGLGKALNEGL 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4503363  107 KHATGNYIIIMDADLSHHP----KFIPEFirkQKEGNFDIVSGT 146
Cdd:cd04195  77 KHCTYDWVARMDTDDISLPdrfeKQLDFI---EKNPEIDIVGGG 117
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 59-166 8.68e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 45.32  E-value: 8.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   59 EIIIIDDGSPDGTRDVaeqLEKIYGSDRILLRPREKKLGlGTAYIH-GMKHA--TG-NYIIIMDADLSHHPKFIPEFIRK 134
Cdd:cd04185  28 HIIVIDNASTDGTAEW---LTSLGDLDNIVYLRLPENLG-GAGGFYeGVRRAyeLGyDWIWLMDDDAIPDPDALEKLLAY 103

                        90       100       110
                ....*....|....*....|....*....|..
gi 4503363  135 QKEGNFDIVSGTRYKGNGGVYGWDLKRKIISR 166
Cdd:cd04185 104 ADKDNPQFLAPLVLDPDGSFVGVLISRRVVEK 135
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 28-120 5.12e-05

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: 43.42  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363     28 SVLLPTYNERENLPLIVWLLVKSFsESGINYEIIIIDDGSPDgtrDVAEQLEKIYGSDRILLRPRE--KKLGLGTAYIHG 105
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTF-QYDPEFELIIINDGSTD---KTLEEVSSIKDHNLQVYYPNApdTTYSLAASRNRG 76

                          90
                  ....*....|....*
gi 4503363    106 MKHATGNYIIIMDAD 120
Cdd:pfam10111  77 TSHAIGEYISFIDGD 91
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 19-129 8.77e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 42.98  E-value: 8.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363    19 VRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINyEIIIIDDGSPDGTRDVAEQL-EKIYGSDRIL--LRPREKK 95
Cdd:PRK13915  25 VAAKAGRTVSVVLPALNEEETVGKVVDSIRPLLMEPLVD-ELIVIDSGSTDATAERAAAAgARVVSREEILpeLPPRPGK 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 4503363    96 lglGTAYIHGMKHATGNYIIIMDADL-SHHPKFIP 129
Cdd:PRK13915 104 ---GEALWRSLAATTGDIVVFVDADLiNFDPMFVP 135
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 59-228 2.66e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 38.03  E-value: 2.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363   59 EIIIIDDGSpdgtRDVAEQLEKIYGSDRILLRPREKkLGLGTAYIHGMKHATGN---YIIIMDADLSHHPKFIPEFI--R 133
Cdd:cd02526  26 KVVVVDNSS----GNDIELRLRLNSEKIELIHLGEN-LGIAKALNIGIKAALENgadYVLLFDQDSVPPPDMVEKLLayK 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503363  134 KQKEGN----------FDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILlrpgASdltGSfrLYRKEVLEKLIEKCV 203
Cdd:cd02526 101 ILSDKNsnigavgpriIDRRTGENSPGVRKSGYKLRIQKEGEEGLKEVDFLI----TS---GS--LISLEALEKVGGFDE 171

                       170       180
                ....*....|....*....|....*....
gi 4503363  204 SkgyVF----QMEMIVRARQLNYTIGEVP 228
Cdd:cd02526 172 D---LFidyvDTEWCLRARSKGYKIYVVP 197
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 59-119 3.36e-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: 37.95  E-value: 3.36e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503363   59 EIIIIDDGSPDG--TRDVAEQLEKIYGSDRILlrpR-EKKLGLGTAYIHGMKHATGNYIIIMDA 119
Cdd:cd02510  32 EIILVDDFSDKPelKLLLEEYYKKYLPKVKVL---RlKKREGLIRARIAGARAATGDVLVFLDS 92
 
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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