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Conserved domains on  [gi|302782365|ref|XP_002972956|]
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dolichol-phosphate mannosyltransferase subunit 1 [Selaginella moellendorffii]

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
 1-241 1.67e-175

dolichyl-phosphate beta-D-mannosyltransferase


:

Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 481.89  E-value: 1.67e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   1 MAIGDGAIRYSVLLPTYNERENVAIITYLLFKALQNV-SFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAKLGL 79
Cdd:PLN02726   2 EAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVkDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  80 GTAYIHGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVHGWDFKRKLTSRGANVLAQTLLWP 159
Cdd:PLN02726  82 GTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365 160 RVSDLTGSFRLYKKPVLEDLVKVCVSRGYVFQMELIVRASRSNYRIEEVPITFVDRVYGISKLGGSEIVQYLRGLIHLLL 239
Cdd:PLN02726 162 GVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLL 241


                 ..
gi 302782365 240 TT 241
Cdd:PLN02726 242 TT 243
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-241 1.67e-175

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 481.89  E-value: 1.67e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   1 MAIGDGAIRYSVLLPTYNERENVAIITYLLFKALQNV-SFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAKLGL 79
Cdd:PLN02726   2 EAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVkDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  80 GTAYIHGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVHGWDFKRKLTSRGANVLAQTLLWP 159
Cdd:PLN02726  82 GTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365 160 RVSDLTGSFRLYKKPVLEDLVKVCVSRGYVFQMELIVRASRSNYRIEEVPITFVDRVYGISKLGGSEIVQYLRGLIHLLL 239
Cdd:PLN02726 162 GVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLL 241


                 ..
gi 302782365 240 TT 241
Cdd:PLN02726 242 TT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 12-237 2.76e-127

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: 359.15  E-value: 2.76e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAIITYLLFKALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRhaKLGLGTAYIHGLKYAS 91
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPG--KRGLGSAYIEGFKAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  92 GEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVHGWDFKRKLTSRGANVLAQTLLWPRVSDLTGSFRLY 171
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFRAY 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302782365 172 KKPVLEDLVKVCVSRGYVFQMELIVRASRSNYRIEEVPITFVDRVYGISKLGGSEIVQYLRGLIHL 237
Cdd:cd06442  159 RREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 7-231 3.24e-43

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 145.23  E-value: 3.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   7 AIRYSVLLPTYNERENVAiityLLFKALQNVS---FEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHakLGLGTAY 83
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLE----EALESLLAQTypdFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERN--RGKGAAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  84 IHGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVhgwdFKRKLTSRGANVLAqtlLWPRVSD 163
Cdd:COG0463   75 NAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVR---LLTNLPD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302782365 164 LTGSFRLYKKPVLEDLVkvcVSRGYVFQMELIvRASRSNYRIEEVPITFVDrvyGISKLGGSEIVQYL 231
Cdd:COG0463  148 STSGFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 11-178 2.08e-33

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: 118.65  E-value: 2.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   11 SVLLPTYNERENVAIitylLFKALQNVS---FEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRhaKLGLGTAYIHGL 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLE----TLESLLNQTypnFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPE--NRGKAGARNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   88 KYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRY-IPGGGVHGWDFKRKLTSRGANVLAQTLLWPRVSDLTG 166
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYvIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG 154

                         170
                  ....*....|..
gi 302782365  167 SFRLYKKPVLED 178
Cdd:pfam00535 155 GFALYRREALEE 166
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
23-101 4.22e-08

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 52.87  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  23 VAIITY-------LLFKALQN------VSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAKLGLGTAYIHGLKY 89
Cdd:NF038302   5 VAIPTYnganrlpEVLERLRSqigtesLSWEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLRYCFEPQQGAAFARQRAIQE 84

                         90
                 ....*....|..
gi 302782365  90 ASGEFVIIMDAD 101
Cdd:NF038302  85 AKGELIGFLDDD 96
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-241 1.67e-175

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 481.89  E-value: 1.67e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   1 MAIGDGAIRYSVLLPTYNERENVAIITYLLFKALQNV-SFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAKLGL 79
Cdd:PLN02726   2 EAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVkDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  80 GTAYIHGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVHGWDFKRKLTSRGANVLAQTLLWP 159
Cdd:PLN02726  82 GTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365 160 RVSDLTGSFRLYKKPVLEDLVKVCVSRGYVFQMELIVRASRSNYRIEEVPITFVDRVYGISKLGGSEIVQYLRGLIHLLL 239
Cdd:PLN02726 162 GVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLL 241


                 ..
gi 302782365 240 TT 241
Cdd:PLN02726 242 TT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 12-237 2.76e-127

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: 359.15  E-value: 2.76e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAIITYLLFKALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRhaKLGLGTAYIHGLKYAS 91
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPG--KRGLGSAYIEGFKAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  92 GEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVHGWDFKRKLTSRGANVLAQTLLWPRVSDLTGSFRLY 171
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFRAY 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302782365 172 KKPVLEDLVKVCVSRGYVFQMELIVRASRSNYRIEEVPITFVDRVYGISKLGGSEIVQYLRGLIHL 237
Cdd:cd06442  159 RREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 12-198 2.92e-66

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: 203.19  E-value: 2.92e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAIITYLLFKAL-QNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRhaKLGLGTAYIHGLKYA 90
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLeEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSR--NFGKGAAVRAGFKAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  91 SGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVhGWDFKRKLTSRGANVLAQTLLWPRVSDLTGSFRL 170
Cdd:cd04179   79 RGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGA-GMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                        170       180
                 ....*....|....*....|....*...
gi 302782365 171 YKKPVLEDLVKVCVSRGYVFQMELIVRA 198
Cdd:cd04179  158 FRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 7-231 3.24e-43

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 145.23  E-value: 3.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   7 AIRYSVLLPTYNERENVAiityLLFKALQNVS---FEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHakLGLGTAY 83
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLE----EALESLLAQTypdFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERN--RGKGAAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  84 IHGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVhgwdFKRKLTSRGANVLAqtlLWPRVSD 163
Cdd:COG0463   75 NAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVR---LLTNLPD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302782365 164 LTGSFRLYKKPVLEDLVkvcVSRGYVFQMELIvRASRSNYRIEEVPITFVDrvyGISKLGGSEIVQYL 231
Cdd:COG0463  148 STSGFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 12-214 1.54e-34

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: 122.68  E-value: 1.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNE--RENVAIITYL-LFKALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDD-RILLRPRHakLGLGTAYIHGL 87
Cdd:cd04188    1 VVIPAYNEekRLPPTLEEAVeYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALiRVLTLPKN--RGKGGAVRAGM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  88 KYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGG--GVHGwDFKRKLTSRGANVLAQTLLWPRVSDLT 165
Cdd:cd04188   79 LAARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASaaVVKR-SWLRNLLGRGFNFLVRLLLGLGIKDTQ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 302782365 166 GSFRLYKKPVLEDLVKVCVSRGYVFQMELIVRASRSNYRIEEVPITFVD 214
Cdd:cd04188  158 CGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVE 206
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 11-178 2.08e-33

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: 118.65  E-value: 2.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   11 SVLLPTYNERENVAIitylLFKALQNVS---FEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRhaKLGLGTAYIHGL 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLE----TLESLLNQTypnFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPE--NRGKAGARNAGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   88 KYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRY-IPGGGVHGWDFKRKLTSRGANVLAQTLLWPRVSDLTG 166
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYvIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG 154

                         170
                  ....*....|..
gi 302782365  167 SFRLYKKPVLED 178
Cdd:pfam00535 155 GFALYRREALEE 166
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 12-181 1.75e-28

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: 106.02  E-value: 1.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAIITYLLFKALQNV--SFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAklGLGTAYIHGLKY 89
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLgyDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNF--GQQAALLAGLDH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  90 ASGEFVIIMDADLSHHPKYLRSFMKKQEEtGADIVTGSRyipGGGVHGWdFKRkLTSRGANVLAQTLLWPRVSDLTGSFR 169
Cdd:cd04187   79 ARGDAVITMDADLQDPPELIPEMLAKWEE-GYDVVYGVR---KNRKESW-LKR-LTSKLFYRLINKLSGVDIPDNGGDFR 152

                        170
                 ....*....|..
gi 302782365 170 LYKKPVLEDLVK 181
Cdd:cd04187  153 LMDRKVVDALLL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 12-126 2.50e-19

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 81.40  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAIitylLFKALQNVS---FEIIVIDNASPDGTQDVVRQLQKvyGDDRILLRPRHAKLGLGTAYIHGLK 88
Cdd:cd00761    1 VIIPAYNEEPYLER----CLESLLAQTypnFEVIVVDDGSTDGTLEILEEYAK--KDPRVIRVINEENQGLAAARNAGLK 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 302782365  89 YASGEFVIIMDADLSHHPKYLRSFMKK-QEETGADIVTG 126
Cdd:cd00761   75 AARGEYILFLDADDLLLPDWLERLVAElLADPEADAVGG 113
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 9-127 1.71e-18

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 82.48  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   9 RYSVLLPTYNERENV-AIITYLLFKALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAklGLGTAYIHGL 87
Cdd:COG1215   30 RVSVIIPAYNEEAVIeETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENG--GKAAALNAGL 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 302782365  88 KYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGS 127
Cdd:COG1215  108 KAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGAN 147
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 11-138 6.28e-14

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: 6.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENV-AIITYLLFKALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPrhaKLGLGTAYIHGLKY 89
Cdd:cd02525    3 SIIIPVRNEEKYIeELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNP---KRIQSAGLNIGIRN 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 302782365  90 ASGEFVIIMDADlSHHPK-YLRSFMKKQEETGADIVTGSRYIPGGGVHGW 138
Cdd:cd02525   80 SRGDIIIRVDAH-AVYPKdYILELVEALKRTGADNVGGPMETIGESKFQK 128
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 12-179 9.48e-14

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: 67.25  E-value: 9.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAI-ITYLLfkALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLR--PRHAKLGlgtAYIHGLK 88
Cdd:cd06423    1 IIVPAYNEEAVIERtIESLL--ALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRdkENGGKAG---ALNAGLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  89 YASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGVHGWDFKRK----LTSRGANVLAQTLLWpRVSDL 164
Cdd:cd06423   76 HAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQaieyLSIFRLGRRAQSALG-GVLVL 154

                        170
                 ....*....|....*
gi 302782365 165 TGSFRLYKKPVLEDL 179
Cdd:cd06423  155 SGAFGAFRREALREV 169
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-109 1.44e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 66.94  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   9 RYSVLLPTYNEREnvaiitYLL-----FKALQNVSFEIIVIDNASPDGTQDVVRQLQkvygDDRILLRPRHAKLGLGTAY 83
Cdd:COG1216    4 KVSVVIPTYNRPE------LLRrclesLLAQTYPPFEVIVVDNGSTDGTAELLAALA----FPRVRVIRNPENLGFAAAR 73

                         90       100
                 ....*....|....*....|....*.
gi 302782365  84 IHGLKYASGEFVIIMDADLSHHPKYL 109
Cdd:COG1216   74 NLGLRAAGGDYLLFLDDDTVVEPDWL 99
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 11-232 5.34e-13

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 67.10  E-value: 5.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVAI-----ITYLLFKALQNVSF--EIIVIDNASPDGTQDVVRQL--QKVYGDDRILLRPRHAKLGLGT 81
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKmlketIKYLESRSRKDPKFkyEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLLSLLRNKGKGG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  82 AYIHGLKYASGEFVIIMDADLSHHPK---YLRSFMKKQEETGADIVTGSRYI--PGGGVHGWDFKRKLTSRGANVLAQTL 156
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADGATDIDdfdKLEDIMLKIEQNGLGIVFGSRNHlvDSDVVAKRKWYRNILMYGFHFIVNTI 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302782365 157 LWPRVSDLTGSFRLYKKPVLEDLVKVCVSRGYVFQMELIVRASRSNYRIEEVPITFVDrVYGiSKLGG-SEIVQYLR 232
Cdd:PTZ00260 233 CGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTE-VEG-SKLNViSASIQMAR 307
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-175 2.99e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 58.45  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAiityLLFKALQNVS-----FEIIVIDNASPDGTQDVvrqLQKVYGDDR---ILLRPRHAKL-GLGTA 82
Cdd:cd04192    1 VVIAARNEAENLP----RLLQSLSALDypkekFEVILVDDHSTDGTVQI---LEFAAAKPNfqlKILNNSRVSIsGKKNA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  83 YIHGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGsryiPGGGVHGWDFKRKLtsrganvlaQTLLWPRVS 162
Cdd:cd04192   74 LTTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAG----PVIYFKGKSLLAKF---------QRLDWLSLL 140

                        170
                 ....*....|...
gi 302782365 163 DLTGSFRLYKKPV 175
Cdd:cd04192  141 GLIAGSFGLGKPF 153
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 9-135 7.13e-09

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: 54.51  E-value: 7.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   9 RYSVLLPTYNERENVAiityllfKALQNVS--------FEIIVIDNASPDGTQDVVRQlqkvYGDDRILLRPRHAKLGLG 80
Cdd:cd06439   30 TVTIIIPAYNEEAVIE-------AKLENLLaldyprdrLEIIVVSDGSTDGTAEIARE----YADKGVKLLRFPERRGKA 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302782365  81 TAYIHGLKYASGEFVIIMDADLSHHPKYLRSFMK--KQEETGAdiVTGS-RYIPGGGV 135
Cdd:cd06439   99 AALNRALALATGEIVVFTDANALLDPDALRLLVRhfADPSVGA--VSGElVIVDGGGS 154
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 11-221 1.02e-08

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: 53.70  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVAiityllfKALQNV------SFEIIVIDNASPDGTQDVVRQlqkvYGDdrillrpRHAKL------G 78
Cdd:cd06433    1 SIITPTYNQAETLE-------ETIDSVlsqtypNIEYIVIDGGSTDGTVDIIKK----YED-------KITYWisepdkG 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  79 LGTAYIHGLKYASGEFVIIMDADLSHHPKYLRSFMKK-QEETGADIVTG--------SRYIPGGGVHGWDFKRKLtsRGA 149
Cdd:cd06433   63 IYDAMNKGIALATGDIIGFLNSDDTLLPGALLAVVAAfAEHPEVDVVYGdvllvdenGRVIGRRRPPPFLDKFLL--YGM 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302782365 150 NVLAQTLLWPR-VSDLTGSFRLyKKPVLEDLvkvcvsrgyvfqmELIVRASRSNYRIEEVPITFVD-RVYGISK 221
Cdd:cd06433  141 PICHQATFFRRsLFEKYGGFDE-SYRIAADY-------------DLLLRLLLAGKIFKYLPEVLAAfRLGGVSS 200
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 12-120 3.79e-08

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: 52.19  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAIITYLLFKAL--QNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRIL-LRPRHAKLGlgtAYIHGLK 88
Cdd:cd06421    5 VFIPTYNEPLEIVRKTLRAALAIdyPHDKLRVYVLDDGRRPELRALAAELGVEYGYRYLTrPDNRHAKAG---NLNNALA 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 302782365  89 YASGEFVIIMDADLSHHPKYLR---SFMKKQEETG 120
Cdd:cd06421   82 HTTGDFVAILDADHVPTPDFLRrtlGYFLDDPKVA 116
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
23-101 4.22e-08

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 52.87  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  23 VAIITY-------LLFKALQN------VSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAKLGLGTAYIHGLKY 89
Cdd:NF038302   5 VAIPTYnganrlpEVLERLRSqigtesLSWEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLRYCFEPQQGAAFARQRAIQE 84

                         90
                 ....*....|..
gi 302782365  90 ASGEFVIIMDAD 101
Cdd:NF038302  85 AKGELIGFLDDD 96
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 25-133 4.90e-08

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 51.48  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  25 IITY----LL---FKALQNVSF---EIIVIDNASPDGTQDVVRQLQkvyGDDRILLRPRHAKLGlGTAYIH-GLKYASGE 93
Cdd:cd04185    3 VVTYnrldLLkecLDALLAQTRppdHIIVIDNASTDGTAEWLTSLG---DLDNIVYLRLPENLG-GAGGFYeGVRRAYEL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 302782365  94 ---FVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGG 133
Cdd:cd04185   79 gydWIWLMDDDAIPDPDALEKLLAYADKDNPQFLAPLVLDPDG 121
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 11-241 6.89e-08

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 52.05  E-value: 6.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVAIITYLLFKALQNVS--FEIIVIDNASPDGTQDVVRQLQKVYGDD--RILLRPRHaklGLGTAYIHG 86
Cdd:PRK10714   9 SVVIPVYNEQESLPELIRRTTAACESLGkeYEILLIDDGSSDNSAEMLVEAAQAPDSHivAILLNRNY---GQHSAIMAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  87 LKYASGEFVIIMDADLSHHPKYLRSFMKKQEEtGADIVTGSRyipgggVHGWD-FKRKLTSRGANVLAQTLLWPRVSDLT 165
Cdd:PRK10714  86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVR------QNRQDsWFRKTASKMINRLIQRTTGKAMGDYG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302782365 166 GSFRLYKKPVLEDLVKvCVSRGYVfqmeLIVRASRSNYRIEEVPITFVDRVYGISKLGGSEIVQYLRGLIHLLLTT 241
Cdd:PRK10714 159 CMLRAYRRHIVDAMLH-CHERSTF----IPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTT 229
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 11-101 8.82e-08

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: 8.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVAiityllfKALQNVSF---EIIVIDNASPDGTQDVVRQL-QKVYgddrillrpRHAKLGLGTAYIHG 86
Cdd:cd02511    3 SVVIITKNEERNIE-------RCLESVKWavdEIIVVDSGSTDRTVEIAKEYgAKVY---------QRWWDGFGAQRNFA 66

                         90
                 ....*....|....*
gi 302782365  87 LKYASGEFVIIMDAD 101
Cdd:cd02511   67 LELATNDWVLSLDAD 81
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-121 1.62e-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: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNEREnvaiITYLLFKALQN---VSFEIIVIDNASPDGTQDVVRQLQKvygdDRILLRPrHAKLGLGTAYIHGLK 88
Cdd:cd04186    1 IIIVNYNSLE----YLKACLDSLLAqtyPDFEVIVVDNASTDGSVELLRELFP----EVRLIRN-GENLGFGAGNNQGIR 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 302782365  89 YASGEFVIIMDADLSHHP---KYLRSFMKKQEETGA 121
Cdd:cd04186   72 EAKGDYVLLLNPDTVVEPgalLELLDAAEQDPDVGI 107
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 9-179 9.83e-07

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: 9.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365    9 RYSVLLPTYNERENV-AIITYLLfkALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHAKLGLG---TAYI 84
Cdd:pfam13641   3 DVSVVVPAFNEDSVLgRVLEAIL--AQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgksRGLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   85 HGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTGSRYIPGGGvHGWDF--KRKLTSRGANVLAQTLLwPRVS 162
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRS-TMLSAlgALEFALRHLRMMSLRLA-LGVL 158

                         170
                  ....*....|....*..
gi 302782365  163 DLTGSFRLYKKPVLEDL 179
Cdd:pfam13641 159 PLSGAGSAIRREVLKEL 175
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-101 1.24e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 47.63  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYN-ERenvaiitYLL-----FKALQNVSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILLRPRHaKLGLGTAYI 84
Cdd:cd04196    1 AVLMATYNgEK-------YLReqldsILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGK-NLGVARNFE 72

                         90
                 ....*....|....*..
gi 302782365  85 HGLKYASGEFVIIMDAD 101
Cdd:cd04196   73 SLLQAADGDYVFFCDQD 89
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 62-179 1.46e-06

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 46.89  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365   62 VYGDDRILLRPRHAKLglgtayIHGLKYASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVTG-SRYIPGGGVHGwDF 140
Cdd:pfam13506   7 VVGGPPVGVNPKVNNL------LQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTSpPVGSDPKGLAA-AL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 302782365  141 KRKLTSRGANVLAQTLLwpRVSDLTGSFRLYKKPVLEDL 179
Cdd:pfam13506  80 EAAFFNTLAGVLQAALS--GIGFAVGMSMAFRRADLERI 116
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 11-110 2.18e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 47.60  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVA----IITYLLFKALQNvsfEIIVIDNASPDGTQDVVRQL-QKVYGDDRIL--LRPRHAKlglGTAY 83
Cdd:PRK13915  34 SVVLPALNEEETVGkvvdSIRPLLMEPLVD---ELIVIDSGSTDATAERAAAAgARVVSREEILpeLPPRPGK---GEAL 107

                         90       100
                 ....*....|....*....|....*...
gi 302782365  84 IHGLKYASGEFVIIMDADL-SHHPKYLR 110
Cdd:PRK13915 108 WRSLAATTGDIVVFVDADLiNFDPMFVP 135
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 11-110 5.28e-05

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


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 43.07  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVAiityllfKALQNVS--------FEIIVIDnaspDGTQDVVRQLQKvygddRILlrpRHAKLGLGTA 82
Cdd:cd06437    4 TVQLPVFNEKYVVE-------RLIEAACaldypkdrLEIQVLD----DSTDETVRLARE-----IVE---EYAAQGVNIK 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 302782365  83 YI--------------HGLKYASGEFVIIMDADLSHHPKYLR 110
Cdd:cd06437   65 HVrradrtgykagalaEGMKVAKGEYVAIFDADFVPPPDFLQ 106
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 12-129 5.75e-05

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: 42.56  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAiityLLFKALQNVS---FEIIVIDNASPDGTQDVVRQLQKvygDDRILLRP-RHAKLGLGTAYI--H 85
Cdd:cd06420    1 LIITTYNRPEALE----LVLKSVLNQSilpFEVIIADDGSTEETKELIEEFKS---QFPIPIKHvWQEDEGFRKAKIrnK 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 302782365  86 GLKYASGEFVIIMDADLSHHPKYLRSFMkKQEETGAdIVTGSRY 129
Cdd:cd06420   74 AIAAAKGDYLIFIDGDCIPHPDFIADHI-ELAEPGV-FLSGSRV 115
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 11-134 9.31e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 42.73  E-value: 9.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYN-ERENVAIITYLLFKALQnvSFEIIVIDNASPDGTQDVVRQLQKVYGDDRILlrpRHAKLGLGTAYIHGLKY 89
Cdd:PRK10073   9 SIIIPLYNaGKDFRAFMESLIAQTWT--ALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL---HQANAGVSVARNTGLAV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 302782365  90 ASGEFVIIMDADLSHHPKYLRSFMKKQEETGADIVT--GSRYIPGGG 134
Cdd:PRK10073  84 ATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQcnADWCFRDTG 130
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 10-101 1.52e-04

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: 41.79  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  10 YSVLLPTYNERENVAIityLL--FKALQNVSFEIIVIDNASPDGTQDVVRQLQKVYgddrillrpRHAKLGLGTAYIHGL 87
Cdd:cd02522    1 LSIIIPTLNEAENLPR---LLasLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVV---------ISSPKGRARQMNAGA 68

                         90
                 ....*....|....
gi 302782365  88 KYASGEFVIIMDAD 101
Cdd:cd02522   69 AAARGDWLLFLHAD 82
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 11-101 1.54e-04

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: 41.42  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVaiitylLFKALQNVS------FEIIVIDNASPD-GTQDVVRQLQKvyGDDRILLRPRHAKLGLGTAY 83
Cdd:cd04184    4 SIVMPVYNTPEKY------LREAIESVRaqtypnWELCIADDASTDpEVKRVLKKYAA--QDPRIKVVFREENGGISAAT 75

                         90
                 ....*....|....*...
gi 302782365  84 IHGLKYASGEFVIIMDAD 101
Cdd:cd04184   76 NSALELATGEFVALLDHD 93
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 11-126 1.91e-04

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: 41.15  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNeRENVAiityLLFKALQNVSFE-------IIVIDNASPDGTQDVVRQLQKVYGDDRILLrPRHakLGLGTAY 83
Cdd:cd04195    1 SVLMSVYI-KEKPE----FLREALESILKQtlppdevVLVKDGPVTQSLNEVLEEFKRKLPLKVVPL-EKN--RGLGKAL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 302782365  84 IHGLKYASGEFVIIMDADLSHHP----KYLRSFMKkqeETGADIVTG 126
Cdd:cd04195   73 NEGLKHCTYDWVARMDTDDISLPdrfeKQLDFIEK---NPEIDIVGG 116
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 12-114 1.37e-03

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 39.62  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  12 VLLPTYNERENVAIITylLFKAL----QNVSFEIIVIDnaspDGTQDVVRQLQKVYGDDRILlRP--RHAKLGlgtaYI- 84
Cdd:PRK11498 264 IFVPTYNEDLNVVKNT--IYASLgidwPKDKLNIWILD----DGGREEFRQFAQEVGVKYIA-RPthEHAKAG----NIn 332

                         90       100       110
                 ....*....|....*....|....*....|
gi 302782365  85 HGLKYASGEFVIIMDADlsHHPkyLRSFMK 114
Cdd:PRK11498 333 NALKYAKGEFVAIFDCD--HVP--TRSFLQ 358
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 25-109 5.05e-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: 37.26  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  25 IITY--------LLFKALQNVSFEIIVIDNaSPDGTQdvvrQLQKVYGDDRILLRPRHAKLGLGTAYIHGLKYASG---E 93
Cdd:cd02526    3 VVTYnpdlsklkELLAALAEQVDKVVVVDN-SSGNDI----ELRLRLNSEKIELIHLGENLGIAKALNIGIKAALEngaD 77

                         90
                 ....*....|....*.
gi 302782365  94 FVIIMDADLSHHPKYL 109
Cdd:cd02526   78 YVLLFDQDSVPPPDMV 93
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 11-114 6.88e-03

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


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 36.61  E-value: 6.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  11 SVLLPTYNERENVAIITYLLFKALQNVSFEIIVIDNASPDGT-----QDVVRQLQKvygddrillRPRHAKLGLGTAYIH 85
Cdd:cd06435    1 SIHVPCYEEPPEMVKETLDSLAALDYPNFEVIVIDNNTKDEAlwkpvEAHCAQLGE---------RFRFFHVEPLPGAKA 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 302782365  86 G-LKYA------SGEFVIIMDADLSHHPKYLRSFMK 114
Cdd:cd06435   72 GaLNYAlertapDAEIIAVIDADYQVEPDWLKRLVP 107
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 39-126 7.78e-03

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 36.42  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302782365  39 FEII-VIDNASpDGTQDVVRQLQKVYGDDRILL----RPR--HAKLG-LGTAYIHglkyASGEFVIIMDADLSHHPKYLR 110
Cdd:cd02520   31 YEILfCVQDED-DPAIPVVRKLIAKYPNVDARLliggEKVgiNPKVNnLIKGYEE----ARYDILVISDSDISVPPDYLR 105

                         90
                 ....*....|....*.
gi 302782365 111 SFMKKQEETGADIVTG 126
Cdd:cd02520  106 RMVAPLMDPGVGLVTC 121
 
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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