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Conserved domains on  [gi|2119483074|ref|XP_044517042|]
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dolichol-phosphate mannosyltransferase subunit 1 isoform X1 [Gracilinanus agilis]

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
 21-263 1.05e-151

dolichyl-phosphate beta-D-mannosyltransferase


:

Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 422.57  E-value: 1.05e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  21 AAAEGTGVDKYSVLLPTYNERENLPLIVWLLVKSFgESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKKL 100
Cdd:PLN02726    1 MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 101 GLGTAYIHGMQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKII-RGANFLTQILL 179
Cdd:PLN02726   80 GLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTsRGANVLAQTLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 180 RPGVSDLTGSFRLYRKEVLQKLMEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 259
Cdd:PLN02726  160 WPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYL 239


                  ....
gi 2119483074 260 FATT 263
Cdd:PLN02726  240 LLTT 243
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 21-263 1.05e-151

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 422.57  E-value: 1.05e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  21 AAAEGTGVDKYSVLLPTYNERENLPLIVWLLVKSFgESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKKL 100
Cdd:PLN02726    1 MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 101 GLGTAYIHGMQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKII-RGANFLTQILL 179
Cdd:PLN02726   80 GLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTsRGANVLAQTLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 180 RPGVSDLTGSFRLYRKEVLQKLMEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 259
Cdd:PLN02726  160 WPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYL 239


                  ....
gi 2119483074 260 FATT 263
Cdd:PLN02726  240 LLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 33-259 3.90e-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: 374.95  E-value: 3.90e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSFgeSGNNYEIIIIDDGSPDGTQEVAEQLKKIYGsdKILLRPRAKKLGLGTAYIHGMQH 112
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAAL--KGIDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYIEGFKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 113 ATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKII-RGANFLTQILLRPGVSDLTGSFR 191
Cdd:cd06442    77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLIsRGANLLARLLLGRKVSDPTSGFR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119483074 192 LYRKEVLQKLMEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 259
Cdd:cd06442   157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 30-253 6.07e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 160.64  E-value: 6.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  30 KYSVLLPTYNERENLPLivwlLVKSF-GESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRakKLGLGTAYIH 108
Cdd:COG0463     3 LVSVVIPTYNEEEYLEE----ALESLlAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLER--NRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 109 GMQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIIRGANFLTQIllrpgvSDLTG 188
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNL------PDSTS 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119483074 189 SFRLYRKEVLQKLMekcVSKGYVFQMEMIvRARQLNYTIGEVPISFVDrvyGESKLGGNEIVSFL 253
Cdd:COG0463   151 GFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 32-200 1.36e-42

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: 142.92  E-value: 1.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENLPLIVWLLVKSFGEsgnNYEIIIIDDGSPDGTQEVAEQLKKIYgsDKILLRPRAKKLGLGTAYIHGMQ 111
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 112 HATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGV--YGWDLKRKIIRGANFLTQILLRPGVSDLTGS 189
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETgeYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 2119483074 190 FRLYRKEVLQK 200
Cdd:pfam00535 156 FALYRREALEE 166
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 21-263 1.05e-151

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 422.57  E-value: 1.05e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  21 AAAEGTGVDKYSVLLPTYNERENLPLIVWLLVKSFgESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKKL 100
Cdd:PLN02726    1 MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 101 GLGTAYIHGMQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKII-RGANFLTQILL 179
Cdd:PLN02726   80 GLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTsRGANVLAQTLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 180 RPGVSDLTGSFRLYRKEVLQKLMEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 259
Cdd:PLN02726  160 WPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYL 239


                  ....
gi 2119483074 260 FATT 263
Cdd:PLN02726  240 LLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 33-259 3.90e-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: 374.95  E-value: 3.90e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSFgeSGNNYEIIIIDDGSPDGTQEVAEQLKKIYGsdKILLRPRAKKLGLGTAYIHGMQH 112
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAAL--KGIDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYIEGFKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 113 ATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKII-RGANFLTQILLRPGVSDLTGSFR 191
Cdd:cd06442    77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLIsRGANLLARLLLGRKVSDPTSGFR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119483074 192 LYRKEVLQKLMEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 259
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 ...
 33-220 6.49e-74

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: 223.22  E-value: 6.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLvKSFGESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRakKLGLGTAYIHGMQH 112
Cdd:cd04179     1 VVIPAYNEEENIPELVERL-LAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSR--NFGKGAAVRAGFKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 113 ATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVyGWDLKRKII-RGANFLTQILLRPGVSDLTGSFR 191
Cdd:cd04179    78 ARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGA-GMPLLRRLGsRLFNFLIRLLLGVRISDTQSGFR 156

                         170       180
                  ....*....|....*....|....*....
gi 2119483074 192 LYRKEVLQKLMEKCVSKGYVFQMEMIVRA 220
Cdd:cd04179   157 LFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 30-253 6.07e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 160.64  E-value: 6.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  30 KYSVLLPTYNERENLPLivwlLVKSF-GESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRakKLGLGTAYIH 108
Cdd:COG0463     3 LVSVVIPTYNEEEYLEE----ALESLlAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLER--NRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 109 GMQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIIRGANFLTQIllrpgvSDLTG 188
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNL------PDSTS 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119483074 189 SFRLYRKEVLQKLMekcVSKGYVFQMEMIvRARQLNYTIGEVPISFVDrvyGESKLGGNEIVSFL 253
Cdd:COG0463   151 GFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 32-200 1.36e-42

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: 142.92  E-value: 1.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENLPLIVWLLVKSFGEsgnNYEIIIIDDGSPDGTQEVAEQLKKIYgsDKILLRPRAKKLGLGTAYIHGMQ 111
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 112 HATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGV--YGWDLKRKIIRGANFLTQILLRPGVSDLTGS 189
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETgeYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 2119483074 190 FRLYRKEVLQK 200
Cdd:pfam00535 156 FALYRREALEE 166
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 33-243 8.01e-38

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: 131.92  E-value: 8.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSFGESGN-NYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRpRAKKLGLGTAYIHGMQ 111
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSfSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLT-LPKNRGKGGAVRAGML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 112 HATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYK-GNGGVYGWDLKRKII-RGANFLTQILLRPGVSDLTGS 189
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHlASAAVVKRSWLRNLLgRGFNFLVRLLLGLGIKDTQCG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2119483074 190 FRLYRKEVLQKLMEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRvyGESK 243
Cdd:cd04188   160 FKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEI--PGSK 211
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 33-201 7.47e-35

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: 123.36  E-value: 7.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSFGESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDK-ILLrprAKKLGLGTAYIHGMQ 111
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKvIRL---SRNFGQQAALLAGLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 112 HATGNFIIIMDADLSHHPKFIPEFIRKQKEGnFDIVSGTRYKGNGGVygwdLKRKIIRGANFLTQILLRPGVSDLTGSFR 191
Cdd:cd04187    78 HARGDAVITMDADLQDPPELIPEMLAKWEEG-YDVVYGVRKNRKESW----LKRLTSKLFYRLINKLSGVDIPDNGGDFR 152

                         170
                  ....*....|
gi 2119483074 192 LYRKEVLQKL 201
Cdd:cd04187   153 LMDRKVVDAL 162
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 33-150 3.17e-21

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: 87.18  E-value: 3.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSFGEsgnNYEIIIIDDGSPDGTQEVAEQLKKIYgsDKILLRPRAKKLGLGTAYIHGMQH 112
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARNAGLKA 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2119483074 113 ATGNFIIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSGT 150
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLERLVAElLADPEADAVGGP 114
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 30-235 1.47e-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: 88.65  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  30 KYSVLLPTYNERENLPLivwlLVKSFGES---GNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKklGLGTAY 106
Cdd:COG1215    30 RVSVIIPAYNEEAVIEE----TLRSLLAQdypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENG--GKAAAL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 107 IHGMQHATGNFIIIMDADLSHHPKFIPEFIRKqkegnfdivsgtrykgnggvygwdlkrkiirganfltqiLLRPGVsDL 186
Cdd:COG1215   104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVAA---------------------------------------FADPGV-GA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2119483074 187 TGSFRLYRKEVLQKLmekcvsKGYVFQ-----MEMIVRARQLNYTIGEVPISFV 235
Cdd:COG1215   144 SGANLAFRREALEEV------GGFDEDtlgedLDLSLRLLRAGYRIVYVPDAVV 191
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 28-263 2.79e-20

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 88.25  E-value: 2.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  28 VDKYSVLLPTYNERENLPLIVWLLVKSFGESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSD--KILLRpraKKLGLGTA 105
Cdd:PRK10714    5 IKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHivAILLN---RNYGQHSA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 106 YIHGMQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGnFDIVsGTRYKGNGGVYGWDLKRKIIrgaNFLTQILLRPGVSD 185
Cdd:PRK10714   82 IMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEG-YDVV-GTVRQNRQDSWFRKTASKMI---NRLIQRTTGKAMGD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119483074 186 LTGSFRLYRKEVLQKlMEKCVSKGYVFQMEMIVRARQlnyTIgEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 263
Cdd:PRK10714  157 YGCMLRAYRRHIVDA-MLHCHERSTFIPILANTFARR---AI-EIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTT 229
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 32-236 1.24e-16

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 77.89  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENLPL-----IVWLLVKSFGESGNNYEIIIIDDGSPDGTQEVAEQL--KKIYGSDKILLRPRAKKLGLGT 104
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKmlketIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLLSLLRNKGKGG 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 105 AYIHGMQHATGNFIIIMDADLSHHpkfIPEFIR------KQKEGNFDIVSGTR---YKGNGGVygwdlKRKIIR-----G 170
Cdd:PTZ00260  153 AVRIGMLASRGKYILMVDADGATD---IDDFDKledimlKIEQNGLGIVFGSRnhlVDSDVVA-----KRKWYRnilmyG 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119483074 171 ANFLTQILLRPGVSDLTGSFRLYRKEVLQKLMEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVD 236
Cdd:PTZ00260  225 FHFIVNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTE 290
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 33-202 1.08e-15

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: 73.03  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSFGEsgnNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKKlGLGTAYIHGMQH 112
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENG-GKAGALNAGLRH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 113 ATGNFIIIMDADLSHHPKFIPE-FIRKQKEGNFDIVSGTRYKGNGGVYGW----DLKRKIIRGANFLTQILLRpGVSDLT 187
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRlVVPFFADPKVGAVQGRVRVRNGSENLLtrlqAIEYLSIFRLGRRAQSALG-GVLVLS 155

                         170
                  ....*....|....*
gi 2119483074 188 GSFRLYRKEVLQKLM 202
Cdd:cd06423   156 GAFGAFRREALREVG 170
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
30-145 8.93e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 70.79  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  30 KYSVLLPTYNERENLPLivwlLVKSFGE-SGNNYEIIIIDDGSPDGTQEVAEQLKkiygSDKILLRPRAKKLGLGTAYIH 108
Cdd:COG1216     4 KVSVVIPTYNRPELLRR----CLESLLAqTYPPFEVIVVDNGSTDGTAELLAALA----FPRVRVIRNPENLGFAAARNL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119483074 109 GMQHATGNFIIIMDADLSHHPKFIPE-------FIRK---QKEGNFD 145
Cdd:COG1216    76 GLRAAGGDYLLFLDDDTVVEPDWLERllaaaclLIRRevfEEVGGFD 122
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 32-201 3.93e-11

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: 61.48  E-value: 3.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENLP-LIVWLLVKSFGesGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPraKKLgLGTAYIHGM 110
Cdd:cd02525     3 SIIIPVRNEEKYIEeLLESLLNQSYP--KDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNP--KRI-QSAGLNIGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 111 QHATGNFIIIMDADlSHHPK-FIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDL------KRKIIrGANFltqillRPGV 183
Cdd:cd02525    78 RNSRGDIIIRVDAH-AVYPKdYILELVEALKRTGADNVGGPMETIGESKFQKAIavaqssPLGSG-GSAY------RGGA 149

                         170       180
                  ....*....|....*....|..
gi 2119483074 184 SDL----TGSFRLYRKEVLQKL 201
Cdd:cd02525   150 VKIgyvdTVHHGAYRREVFEKV 171
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 33-157 5.68e-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: 57.68  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSfgesgnNY-----EIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKKL-GLGTAY 106
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSAL------DYpkekfEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVSIsGKKNAL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2119483074 107 IHGMQHATGNFIIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSGTRYKGNGG 157
Cdd:cd04192    75 TTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFiQKEQIGLVAGPVIYFKGKS 126
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 29-202 1.77e-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: 56.61  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  29 DKYSVLLPTYNERENL-PLIVWLLVKSFGesgnNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKKLGLG---T 104
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLgRVLEAILAQPYP----PVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgksR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 105 AYIHGMQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYG--WDLKRKIIRGANFLtQILLRPG 182
Cdd:pfam13641  78 GLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMLsaLGALEFALRHLRMM-SLRLALG 156

                         170       180
                  ....*....|....*....|
gi 2119483074 183 VSDLTGSFRLYRKEVLQKLM 202
Cdd:pfam13641 157 VLPLSGAGSAIRREVLKELG 176
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 33-153 2.42e-09

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: 55.28  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVksfGESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRprAKKLGLGTAYI--HGM 110
Cdd:cd06420     1 LIITTYNRPEALELVLKSVL---NQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVW--QEDEGFRKAKIrnKAI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2119483074 111 QHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFdiVSGTRYK 153
Cdd:cd06420    76 AAAKGDYLIFIDGDCIPHPDFIADHIELAEPGVF--LSGSRVL 116
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 32-124 6.04e-09

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: 54.56  E-value: 6.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYN-ERenlplivWLL--VKS-FGESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPrAKKLGLGTAYI 107
Cdd:cd04196     1 AVLMATYNgEK-------YLReqLDSiLAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRN-GKNLGVARNFE 72

                          90
                  ....*....|....*..
gi 2119483074 108 HGMQHATGNFIIIMDAD 124
Cdd:cd04196    73 SLLQAADGDYVFFCDQD 89
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 32-124 1.41e-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: 50.75  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENLP--LIVwllVKSFGEsgnnyEIIIIDDGSPDGTQEVAEQlkkiYGsDKILLRPrakKLGLGTAYIHG 109
Cdd:cd02511     3 SVVIITKNEERNIErcLES---VKWAVD-----EIIVVDSGSTDRTVEIAKE----YG-AKVYQRW---WDGFGAQRNFA 66

                          90
                  ....*....|....*
gi 2119483074 110 MQHATGNFIIIMDAD 124
Cdd:cd02511    67 LELATNDWVLSLDAD 81
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 30-146 3.07e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.43  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  30 KYSVLLPTYNERENLPLIVWLLVKsfgESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAkklGLGTAYIHG 109
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIA---QTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANA---GVSVARNTG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2119483074 110 MQHATGNFIIIMDADLSHHPKFIPEFIRKQKEGNFDI 146
Cdd:PRK10073   81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDV 117
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 20-133 2.26e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 47.99  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  20 EAAAEGTGVdkySVLLPTYNERENLPLIV----WLLVksfgeSGNNYEIIIIDDGSPDGTQEVAEQL-KKIYGSDKIL-- 92
Cdd:PRK13915   25 VAAKAGRTV---SVVLPALNEEETVGKVVdsirPLLM-----EPLVDELIVIDSGSTDATAERAAAAgARVVSREEILpe 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2119483074  93 LRPRAKKlglGTAYIHGMQHATGNFIIIMDADL-SHHPKFIP 133
Cdd:PRK13915   97 LPPRPGK---GEALWRSLAATTGDIVVFVDADLiNFDPMFVP 135
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 30-124 8.06e-06

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 46.04  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  30 KYSVLLPTYNERENLplivwllvksfGESGNN----------YEIIIIDDGSPDGTQEVAEQlkkiYGSDKILLRPRAKK 99
Cdd:cd06439    30 TVTIIIPAYNEEAVI-----------EAKLENllaldyprdrLEIIVVSDGSTDGTAEIARE----YADKGVKLLRFPER 94

                          90       100
                  ....*....|....*....|....*
gi 2119483074 100 LGLGTAYIHGMQHATGNFIIIMDAD 124
Cdd:cd06439    95 RGKAAALNRALALATGEIVVFTDAN 119
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 32-124 8.35e-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: 45.27  E-value: 8.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNerenlPLIVWL--LVKSF-GESGNNYEIIIIDDGSPDGtqEVAEQLKKIYGSD-KILLRPRAKKLGLGTAYI 107
Cdd:cd04184     4 SIVMPVYN-----TPEKYLreAIESVrAQTYPNWELCIADDASTDP--EVKRVLKKYAAQDpRIKVVFREENGGISAATN 76

                          90
                  ....*....|....*..
gi 2119483074 108 HGMQHATGNFIIIMDAD 124
Cdd:cd04184    77 SALELATGEFVALLDHD 93
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 32-243 9.81e-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: 45.23  E-value: 9.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENLPLivwlLVKS-FGESGNNYEIIIIDDGSPDGTQEVAE--QLKKIY---GSDKillrprakklGLGTA 105
Cdd:cd06433     1 SIITPTYNQAETLEE----TIDSvLSQTYPNIEYIVIDGGSTDGTVDIIKkyEDKITYwisEPDK----------GIYDA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 106 YIHGMQHATGNFIIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSG--TRYKGNGGVygwdlkRKIIRGANFLTQILLRPG 182
Cdd:cd06433    67 MNKGIALATGDIIGFLNSDDTLLPGALLAVVAAfAEHPEVDVVYGdvLLVDENGRV------IGRRRPPPFLDKFLLYGM 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119483074 183 VSDLTGSFrlYRKEVLQKLmeKCVSKGYVFQM--EMIVRARQLNYTIGEVPISFVD-RVYGESK 243
Cdd:cd06433   141 PICHQATF--FRRSLFEKY--GGFDESYRIAAdyDLLLRLLLAGKIFKYLPEVLAAfRLGGVSS 200
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 32-124 1.09e-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: 45.73  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENLPLIVWLLVKSFgESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRaKKLGLGTAYIHGMQ 111
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTF-QYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPD-TTYSLAASRNRGTS 78

                          90
                  ....*....|...
gi 2119483074 112 HATGNFIIIMDAD 124
Cdd:pfam10111  79 HAIGEYISFIDGD 91
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 63-169 1.12e-05

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 44.93  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  63 EIIIIDDGSPDGTQEVaeqLKKIYGSDKILLRPRAKKLGlGTAYIH-GMQHA--TG-NFIIIMDADLSHHPKFIPEFIRK 138
Cdd:cd04185    28 HIIVIDNASTDGTAEW---LTSLGDLDNIVYLRLPENLG-GAGGFYeGVRRAyeLGyDWIWLMDDDAIPDPDALEKLLAY 103

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2119483074 139 QKEGNFDIVSGTRYKGNGGVYGWDLKRKIIR 169
Cdd:cd04185   104 ADKDNPQFLAPLVLDPDGSFVGVLISRRVVE 134
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 31-124 1.21e-05

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: 45.25  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  31 YSVLLPTYNERENLPLivwlLVKSFgESGNNY--EIIIIDDGSPDGTQEVAEQLkkiygsDKILLRP---RAKKLglgta 105
Cdd:cd02522     1 LSIIIPTLNEAENLPR----LLASL-RRLNPLplEIIVVDGGSTDGTVAIARSA------GVVVISSpkgRARQM----- 64

                          90
                  ....*....|....*....
gi 2119483074 106 yIHGMQHATGNFIIIMDAD 124
Cdd:cd02522    65 -NAGAAAARGDWLLFLHAD 82
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 33-137 2.02e-05

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 43.70  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLivwlLVKSF-GESGNNYEIIIIDDGSPDGTQE-VAEQLKKIygsdkILLRPrAKKLGLGTAYIHGM 110
Cdd:cd04186     1 IIIVNYNSLEYLKA----CLDSLlAQTYPDFEVIVVDNASTDGSVElLRELFPEV-----RLIRN-GENLGFGAGNNQGI 70

                          90       100
                  ....*....|....*....|....*..
gi 2119483074 111 QHATGNFIIIMDADLSHHPKFIPEFIR 137
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLD 97
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 32-138 3.18e-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: 43.84  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNEREnlplIVWLLVKSFGE---SGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSD-KILLRPRAKKLGL-GTAY 106
Cdd:cd06437     4 TVQLPVFNEKY----VVERLIEAACAldyPKDRLEIQVLDDSTDETVRLAREIVEEYAAQGvNIKHVRRADRTGYkAGAL 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2119483074 107 IHGMQHATGNFIIIMDADLShhPKfiPEFIRK 138
Cdd:cd06437    80 AEGMKVAKGEYVAIFDADFV--PP--PDFLQK 107
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 33-138 6.34e-05

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: 42.94  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  33 VLLPTYNERENLPLIVWLLVKSFGESGNNYEIIIIDDGSPDGTQEVAEQLKKIYGSdKILLRP--RAKKLGlgtAYIHGM 110
Cdd:cd06421     5 VFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGY-RYLTRPdnRHAKAG---NLNNAL 80

                          90       100
                  ....*....|....*....|....*...
gi 2119483074 111 QHATGNFIIIMDADlsHHPKfiPEFIRK 138
Cdd:cd06421    81 AHTTGDFVAILDAD--HVPT--PDFLRR 104
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 32-150 1.99e-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: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNeRENLPLIVWLLVKSFGESGNNYEIIIIDDGS-PDGTQEVAEQLKKIYGSDKILLRpraKKLGLGTAYIHGM 110
Cdd:cd04195     1 SVLMSVYI-KEKPEFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPLE---KNRGLGKALNEGL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2119483074 111 QHATGNFIIIMDADLSHHP----KFIPEFirkQKEGNFDIVSGT 150
Cdd:cd04195    77 KHCTYDWVARMDTDDISLPdrfeKQLDFI---EKNPEIDIVGGG 117
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 32-203 1.47e-03

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 39.16  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074  32 SVLLPTYNERENL---PLIVWLlvksfgeSGNNYEIIIIDDGSpdgTQEVAEQLKKIYGSDK--ILLRPRAKKLGlgtAY 106
Cdd:cd06434     3 TVIIPVYDEDPDVfreCLRSIL-------RQKPLEIIVVTDGD---DEPYLSILSQTVKYGGifVITVPHPGKRR---AL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119483074 107 IHGMQHATGNFIIIMDADLSHHPKFIPEfirkqkegnfdIVSGTRYKGNGGVYG----WDLKRKIIR--GANFLTQI--L 178
Cdd:cd06434    70 AEGIRHVTTDIVVLLDSDTVWPPNALPE-----------MLKPFEDPKVGGVGTnqriLRPRDSKWSflAAEYLERRneE 138

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2119483074 179 LRP------GVSDLTGSFRLYRKEVLQKLME 203
Cdd:cd06434   139 IRAamsydgGVPCLSGRTAAYRTEILKDFLF 169
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 63-123 1.91e-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: 38.72  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119483074  63 EIIIIDDGSPDGTQEVAEQLKKIYGSDKILLRPRAKKLGLGTAYIHGMQHATGNFIIIMDA 123
Cdd:cd02510    32 EIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDS 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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