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Conserved domains on  [gi|2258418|gb|AAC98797|]
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dolichol monophosphate mannose synthase, partial [Homo sapiens]

Protein Classification

dolichol-phosphate mannosyltransferase subunit 1( domain architecture ID 1002602)

dolichol-phosphate mannosyltransferase subunit 1 (DPM1) transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins

CAZY:  GT2
EC:  2.4.1.83
Gene Ontology:  GO:0004582|GO:0006488|GO:0019348|GO:0035269|GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02726 super family cl30529
dolichyl-phosphate beta-D-mannosyltransferase
 16-253 1.01e-150

dolichyl-phosphate beta-D-mannosyltransferase


The actual alignment was detected with superfamily member PLN02726:

Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 419.87  E-value: 1.01e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    16 RQNKYSVLLPTYNERENLPLIVWLLVKSFSESGiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAY 95
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    96 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIYGWDLKRKIISRGANFLTQILLTPGASD 175
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258418   176 LTGSFRLYPKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 253
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 16-253 1.01e-150

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 419.87  E-value: 1.01e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    16 RQNKYSVLLPTYNERENLPLIVWLLVKSFSESGiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAY 95
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    96 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIYGWDLKRKIISRGANFLTQILLTPGASD 175
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258418   176 LTGSFRLYPKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 253
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 22-249 1.34e-130

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: 368.01  E-value: 1.34e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVKSFSesGINYEIIIIDDGSPDGTRDVAEQLEKIYGsdRILLRPREKKLGLGTAYIHGMKH 101
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYIEGFKA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  102 ATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIYGWDLKRKIISRGANFLTQILLTPGASDLTGSFR 181
Cdd:cd06442  77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258418  182 LYPKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 249
Cdd:cd06442 157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 19-243 9.84e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 159.48  E-value: 9.84e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   19 KYSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIH 97
Cdd:COG0463   3 LVSVVIPTYNEEEYLEE----ALESLLAqTYPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAARNA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   98 GMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIygwdLKRKIISRGANFLTQILLTPgasDLT 177
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLLTNLP---DST 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258418  178 GSFRLYPKEVLEKLIekcVSKGYVFQMEMIvRARQLNYTIGEVPISFVDrvyGESKLGGNEIVSFL 243
Cdd:COG0463 150 SGFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 21-190 1.58e-41

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: 139.84  E-value: 1.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418     21 SVLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIHGMK 100
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    101 HATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIYGWDL-KRKIISRGANFLTQILLTPGASDLTGS 179
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 2258418    180 FRLYPKEVLEK 190
Cdd:pfam00535 156 FALYRREALEE 166
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 16-253 1.01e-150

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 419.87  E-value: 1.01e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    16 RQNKYSVLLPTYNERENLPLIVWLLVKSFSESGiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAY 95
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    96 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIYGWDLKRKIISRGANFLTQILLTPGASD 175
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258418   176 LTGSFRLYPKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 253
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 22-249 1.34e-130

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: 368.01  E-value: 1.34e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVKSFSesGINYEIIIIDDGSPDGTRDVAEQLEKIYGsdRILLRPREKKLGLGTAYIHGMKH 101
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYIEGFKA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  102 ATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIYGWDLKRKIISRGANFLTQILLTPGASDLTGSFR 181
Cdd:cd06442  77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258418  182 LYPKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 249
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 ...
 22-210 2.82e-73

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: 221.29  E-value: 2.82e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLvKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPRekKLGLGTAYIHGMKH 101
Cdd:cd04179   1 VVIPAYNEEENIPELVERL-LAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSR--NFGKGAAVRAGFKA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  102 ATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGnGGIYGWDLKRKIISRGANFLTQILLTPGASDLTGSFR 181
Cdd:cd04179  78 ARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVR-GGGAGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFR 156

                       170       180
                ....*....|....*....|....*....
gi 2258418  182 LYPKEVLEKLIEKCVSKGYVFQMEMIVRA 210
Cdd:cd04179 157 LFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 19-243 9.84e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 159.48  E-value: 9.84e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   19 KYSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIH 97
Cdd:COG0463   3 LVSVVIPTYNEEEYLEE----ALESLLAqTYPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAARNA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   98 GMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIygwdLKRKIISRGANFLTQILLTPgasDLT 177
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLLTNLP---DST 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258418  178 GSFRLYPKEVLEKLIekcVSKGYVFQMEMIvRARQLNYTIGEVPISFVDrvyGESKLGGNEIVSFL 243
Cdd:COG0463 150 SGFRLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 21-190 1.58e-41

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: 139.84  E-value: 1.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418     21 SVLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIHGMK 100
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    101 HATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGIYGWDL-KRKIISRGANFLTQILLTPGASDLTGS 179
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 2258418    180 FRLYPKEVLEK 190
Cdd:pfam00535 156 FALYRREALEE 166
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 22-233 6.13e-40

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 136.93  E-value: 6.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVKSFSES-GINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRpREKKLGLGTAYIHGMK 100
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEERpSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLT-LPKNRGKGGAVRAGML 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  101 HATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYK-GNGGIYGWDLKRKIISRGANFLTQILLTPGASDLTGS 179
Cdd:cd04188  80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHlASAAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 2258418  180 FRLYPKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRvyGESK 233
Cdd:cd04188 160 FKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEI--PGSK 211
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 22-193 2.19e-33

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: 119.12  E-value: 2.19e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDR-ILLRpreKKLGLGTAYIHGMK 100
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKvIRLS---RNFGQQAALLAGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  101 HATGNYIIIMDADLSHHPKFIPEFIRKKKEGnFDIASGTRYKGNGGiygwdLKRKIISRGANFLTQILLTPGASDLTGSF 180
Cdd:cd04187  78 HARGDAVITMDADLQDPPELIPEMLAKWEEG-YDVVYGVRKNRKES-----WLKRLTSKLFYRLINKLSGVDIPDNGGDF 151

                       170
                ....*....|...
gi 2258418  181 RLYPKEVLEKLIE 193
Cdd:cd04187 152 RLMDRKVVDALLL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 22-139 3.42e-22

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 89.49  E-value: 3.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLGLGTAYIHGMKH 101
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARNAGLKA 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2258418  102 ATGNYIIIMDADLSHHPKFIPEFIRK-KKEGNFDIASGT 139
Cdd:cd00761  76 ARGEYILFLDADDLLLPDWLERLVAElLADPEADAVGGP 114
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 19-126 2.02e-19

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: 85.18  E-value: 2.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   19 KYSVLLPTYNERENLPLivwlLVKSFSES---GINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKklGLGTAY 95
Cdd:COG1215  30 RVSVIIPAYNEEAVIEE----TLRSLLAQdypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENG--GKAAAL 103

                        90       100       110
                ....*....|....*....|....*....|.
gi 2258418   96 IHGMKHATGNYIIIMDADLSHHPKFIPEFIR 126
Cdd:COG1215 104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVA 134
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 18-253 7.43e-19

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 84.02  E-value: 7.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    18 NKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSD--RILLrprEKKLGLGTAY 95
Cdd:PRK10714   6 KKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHivAILL---NRNYGQHSAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    96 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGnFDIASGTRYKGNGGIYgwdlkRKIISRGANFLTQILLTPGASD 175
Cdd:PRK10714  83 MAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEG-YDVVGTVRQNRQDSWF-----RKTASKMINRLIQRTTGKAMGD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258418   176 LTGSFRLYPKEVLEKLIEkCVSKGYVFQMEMIVRARQlnyTIgEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 253
Cdd:PRK10714 157 YGCMLRAYRRHIVDAMLH-CHERSTFIPILANTFARR---AI-EIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTT 229
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
19-173 4.51e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.26  E-value: 4.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   19 KYSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEkiygSDRILLRPREKKLGLGTAYIH 97
Cdd:COG1216   4 KVSVVIPTYNRPELLRR----CLESLLAqTYPPFEVIVVDNGSTDGTAELLAALA----FPRVRVIRNPENLGFAAARNL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   98 GMKHATGNYIIIMDADLSHHPKFIPE-------FIRK---KKEGNFDiasgTRYkgngGIYG--WDLKRKIISRGAnflt 165
Cdd:COG1216  76 GLRAAGGDYLLFLDDDTVVEPDWLERllaaaclLIRRevfEEVGGFD----ERF----FLYGedVDLCLRLRKAGY---- 143


                ....*...
gi 2258418  166 QILLTPGA 173
Cdd:COG1216 144 RIVYVPDA 151
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 21-226 4.66e-16

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 76.34  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    21 SVLLPTYNERENLPL-----IVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQL--EKIYGSDRILLRPREKKLGLGT 93
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKmlketIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLLSLLRNKGKGG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    94 AYIHGMKHATGNYIIIMDADLSHHpkfIPEFIR------KKKEGNFDIASGTRYKGNGGIYGWDLK--RKIISRGANFLT 165
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADGATD---IDDFDKledimlKIEQNGLGIVFGSRNHLVDSDVVAKRKwyRNILMYGFHFIV 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258418   166 QILLTPGASDLTGSFRLYPKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVD 226
Cdd:PTZ00260 230 NTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTE 290
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 22-113 7.52e-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: 70.33  E-value: 7.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVKSFSEsgiNYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKlGLGTAYIHGMKH 101
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENG-GKAGALNAGLRH 76

                        90
                ....*....|..
gi 2258418  102 ATGNYIIIMDAD 113
Cdd:cd06423  77 AKGDIVVVLDAD 88
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 22-146 1.02e-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: 59.99  E-value: 1.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLivwlLVKSFSEsgINY-----EIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKL-GLGTAY 95
Cdd:cd04192   1 VVIAARNEAENLPR----LLQSLSA--LDYpkekfEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVSIsGKKNAL 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 2258418   96 IHGMKHATGNYIIIMDADLSHHPKFIPEFIRK-KKEGNFDIASGTRYKGNGG 146
Cdd:cd04192  75 TTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFiQKEQIGLVAGPVIYFKGKS 126
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 21-191 1.99e-10

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: 59.17  E-value: 1.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   21 SVLLPTYNERENLP-LIVWLLVKSFSESgiNYEIIIIDDGSPDGTRDVAEQLEKIYgsDRILLRPREKKLgLGTAYIHGM 99
Cdd:cd02525   3 SIIIPVRNEEKYIEeLLESLLNQSYPKD--LIEIIVVDGGSTDGTREIVQEYAAKD--PRIRLIDNPKRI-QSAGLNIGI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  100 KHATGNYIIIMDADlSHHPK-FIPEFIRKKKEGNFDIASG---TRYKG-NGGIYGWDLKRKIISRGANFLTQIlLTPGAS 174
Cdd:cd02525  78 RNSRGDIIIRVDAH-AVYPKdYILELVEALKRTGADNVGGpmeTIGESkFQKAIAVAQSSPLGSGGSAYRGGA-VKIGYV 155

                       170
                ....*....|....*..
gi 2258418  175 DlTGSFRLYPKEVLEKL 191
Cdd:cd02525 156 D-TVHHGAYRREVFEKV 171
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 21-113 5.18e-10

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 57.64  E-value: 5.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   21 SVLLPTYN-ERenlplivWLL--VKS-FSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPrEKKLGLGTAYI 96
Cdd:cd04196   1 AVLMATYNgEK-------YLReqLDSiLAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRN-GKNLGVARNFE 72

                        90
                ....*....|....*..
gi 2258418   97 HGMKHATGNYIIIMDAD 113
Cdd:cd04196  73 SLLQAADGDYVFFCDQD 89
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 22-142 8.65e-10

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


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 56.43  E-value: 8.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVksfSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRprEKKLGLGTAYI--HGM 99
Cdd:cd06420   1 LIITTYNRPEALELVLKSVL---NQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVW--QEDEGFRKAKIrnKAI 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 2258418  100 KHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFdiASGTRYK 142
Cdd:cd06420  76 AAAKGDYLIFIDGDCIPHPDFIADHIELAEPGVF--LSGSRVL 116
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 18-136 2.52e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 56.59  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418    18 NKYSVLLPTYNERENLPlivwllvkSFSESGI-----NYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILlrpREKKLGLG 92
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFR--------AFMESLIaqtwtALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL---HQANAGVS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 2258418    93 TAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIA 136
Cdd:PRK10073  75 VARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVA 118
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 17-232 1.85e-08

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: 53.53  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418     17 QNKYSVLLPTYNERENL-PLIVWLLVKSFsesgINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLG--- 92
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLgRVLEAILAQPY----PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgks 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418     93 TAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKKKEGNFDIASGTRYKGNGGiYGWDL--KRKIISRGANFLtQILLT 170
Cdd:pfam13641  77 RGLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRS-TMLSAlgALEFALRHLRMM-SLRLA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258418    171 PGASDLTGSFRLYPKEVLeKLIEKCVSKGYVFQ-MEMIVRARQLNYTIGEVPISFVDRVYGES 232
Cdd:pfam13641 155 LGVLPLSGAGSAIRREVL-KELGLFDPFFLLGDdKSLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 21-140 4.50e-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: 52.29  E-value: 4.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   21 SVLLPTYNERENLP--LIVwllVKSFSEsginyEIIIIDDGSPDGTRDVAEQLekiygSDRILLRPrekKLGLGTAYIHG 98
Cdd:cd02511   3 SVVIITKNEERNIErcLES---VKWAVD-----EIIVVDSGSTDRTVEIAKEY-----GAKVYQRW---WDGFGAQRNFA 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 2258418   99 MKHATGNYIIIMDAD--LShhPKFIPEFIRKKKEGNFDIASGTR 140
Cdd:cd02511  67 LELATNDWVLSLDADerLT--PELADEILALLATDDYDGYYVPR 108
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 22-126 1.15e-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: 50.25  E-value: 1.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLivwlLVKSF-SESGINYEIIIIDDGSPDGTRDVAEQLEKiygsDRILLRPrEKKLGLGTAYIHGMK 100
Cdd:cd04186   1 IIIVNYNSLEYLKA----CLDSLlAQTYPDFEVIVVDNASTDGSVELLRELFP----EVRLIRN-GENLGFGAGNNQGIR 71

                        90       100
                ....*....|....*....|....*.
gi 2258418  101 HATGNYIIIMDADLSHHPKFIPEFIR 126
Cdd:cd04186  72 EAKGDYVLLLNPDTVVEPGALLELLD 97
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 19-113 4.86e-07

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


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 49.50  E-value: 4.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   19 KYSVLLPTYNEREnlplivWLLVKSFSESGINY-----EIIIIDDGSPDGTRDVAEQlekiYGSDRILLRPREKKLGLGT 93
Cdd:cd06439  30 TVTIIIPAYNEEA------VIEAKLENLLALDYprdrlEIIVVSDGSTDGTAEIARE----YADKGVKLLRFPERRGKAA 99

                        90       100
                ....*....|....*....|
gi 2258418   94 AYIHGMKHATGNYIIIMDAD 113
Cdd:cd06439 100 ALNRALALATGEIVVFTDAN 119
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 21-127 6.33e-07

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


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 48.85  E-value: 6.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   21 SVLLPTYNEREnlplIVWLLVKSFSEsgINY-----EIIIIDDGSPDGTRDVAEQLEKIYGSD-RILLRPREKKLGL-GT 93
Cdd:cd06437   4 TVQLPVFNEKY----VVERLIEAACA--LDYpkdrlEIQVLDDSTDETVRLAREIVEEYAAQGvNIKHVRRADRTGYkAG 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 2258418   94 AYIHGMKHATGNYIIIMDADLShhPKfiPEFIRK 127
Cdd:cd06437  78 ALAEGMKVAKGEYVAIFDADFV--PP--PDFLQK 107
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 20-113 1.03e-06

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 48.34  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   20 YSVLLPTYNERENLPLivwlLVKSFSE-SGINYEIIIIDDGSPDGTRDVAEQLEKiygsdrillRPREKKLGLGTAYIHG 98
Cdd:cd02522   1 LSIIIPTLNEAENLPR----LLASLRRlNPLPLEIIVVDGGSTDGTVAIARSAGV---------VVISSPKGRARQMNAG 67

                        90
                ....*....|....*
gi 2258418   99 MKHATGNYIIIMDAD 113
Cdd:cd02522  68 AAAARGDWLLFLHAD 82
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 21-113 1.90e-06

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


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 47.20  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   21 SVLLPTYNerenlPLIVWL--LVKSF-SESGINYEIIIIDDGSPDgtRDVAEQLEKIYGSD-RILLRPREKKLGLGTAYI 96
Cdd:cd04184   4 SIVMPVYN-----TPEKYLreAIESVrAQTYPNWELCIADDASTD--PEVKRVLKKYAAQDpRIKVVFREENGGISAATN 76

                        90
                ....*....|....*..
gi 2258418   97 HGMKHATGNYIIIMDAD 113
Cdd:cd04184  77 SALELATGEFVALLDHD 93
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-122 3.00e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 47.22  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418     1 RSPRRSRWELE--VRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINyEIIIIDDGSPDGTRDVAEQL-EKIYGS 77
Cdd:PRK13915  12 RTWHAPDWTIEelVAAKAGRTVSVVLPALNEEETVGKVVDSIRPLLMEPLVD-ELIVIDSGSTDATAERAAAAgARVVSR 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 2258418    78 DRIL--LRPREKKlglGTAYIHGMKHATGNYIIIMDADL-SHHPKFIP 122
Cdd:PRK13915  91 EEILpeLPPRPGK---GEALWRSLAATTGDIVVFVDADLiNFDPMFVP 135
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 21-119 1.05e-05

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 45.00  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   21 SVLLPTYNeRENLPLIVWLLVKSFSESGINYEIIIIDDGS-PDGTRDVAEQLEKIYGSDRILLrprEKKLGLGTAYIHGM 99
Cdd:cd04195   1 SVLMSVYI-KEKPEFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPL---EKNRGLGKALNEGL 76

                        90       100
                ....*....|....*....|
gi 2258418  100 KHATGNYIIIMDADLSHHPK 119
Cdd:cd04195  77 KHCTYDWVARMDTDDISLPD 96
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 22-129 1.55e-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: 44.87  E-value: 1.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   22 VLLPTYNERENLPLIVWLLVKsfsesGINY-----EIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREK-KLGlgtAY 95
Cdd:cd06421   5 VFIPTYNEPLEIVRKTLRAAL-----AIDYphdklRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHaKAG---NL 76

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2258418   96 IHGMKHATGNYIIIMDADLSHHPKF----IPEFIRKKK 129
Cdd:cd06421  77 NNALAHTTGDFVAILDADHVPTPDFlrrtLGYFLDDPK 114
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 21-233 2.54e-05

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: 43.69  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   21 SVLLPTYNERENLPLivwlLVKS-FSESGINYEIIIIDDGSPDGTRDVAeqleKIYGSDRILLRpREKKLGLGTAYIHGM 99
Cdd:cd06433   1 SIITPTYNQAETLEE----TIDSvLSQTYPNIEYIVIDGGSTDGTVDII----KKYEDKITYWI-SEPDKGIYDAMNKGI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  100 KHATGNYIIIMDAD---LSHHPKFIPEFIRKKKEGNFdIASGTRYKGNGGIYGWDLKRKIISRGANFLTQILLTPGAsdl 176
Cdd:cd06433  72 ALATGDIIGFLNSDdtlLPGALLAVVAAFAEHPEVDV-VYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPICHQAT--- 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  177 tgsfrLYPKEVLEKLieKCVSKGYVFQM--EMIVRARQLNYTIGEVPISFVD-RVYGESK 233
Cdd:cd06433 148 -----FFRRSLFEKY--GGFDESYRIAAdyDLLLRLLLAGKIFKYLPEVLAAfRLGGVSS 200
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 52-159 3.51e-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: 43.39  E-value: 3.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   52 EIIIIDDGSPDGTRDVaeqLEKIYGSDRILLRPREKKLGlGTAYIH-GMKHA--TG-NYIIIMDADLSHHPKFIPEFIRK 127
Cdd:cd04185  28 HIIVIDNASTDGTAEW---LTSLGDLDNIVYLRLPENLG-GAGGFYeGVRRAyeLGyDWIWLMDDDAIPDPDALEKLLAY 103

                        90       100       110
                ....*....|....*....|....*....|..
gi 2258418  128 KKEGNFDIASGTRYKGNGGIYGWDLKRKIISR 159
Cdd:cd04185 104 ADKDNPQFLAPLVLDPDGSFVGVLISRRVVEK 135
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 21-113 5.20e-05

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 43.42  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418     21 SVLLPTYNERENLPLIVWLLVKSFsESGINYEIIIIDDGSPDgtrDVAEQLEKIYGSDRILLRPRE--KKLGLGTAYIHG 98
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTF-QYDPEFELIIINDGSTD---KTLEEVSSIKDHNLQVYYPNApdTTYSLAASRNRG 76

                          90
                  ....*....|....*
gi 2258418     99 MKHATGNYIIIMDAD 113
Cdd:pfam10111  77 TSHAIGEYISFIDGD 91
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 52-221 1.10e-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: 39.19  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418   52 EIIIIDDGSpdgtRDVAEQLEKIYGSDRILLRPREKkLGLGTAYIHGMKHATGN---YIIIMDADLSHHPKFIPEFI--R 126
Cdd:cd02526  26 KVVVVDNSS----GNDIELRLRLNSEKIELIHLGEN-LGIAKALNIGIKAALENgadYVLLFDQDSVPPPDMVEKLLayK 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258418  127 KKKEGN----------FDIASGTRYKGNGGIYGWDLKRKIISRGANFLTQILltpgASdltGSfrLYPKEVLEKLIEKCV 196
Cdd:cd02526 101 ILSDKNsnigavgpriIDRRTGENSPGVRKSGYKLRIQKEGEEGLKEVDFLI----TS---GS--LISLEALEKVGGFDE 171

                       170       180
                ....*....|....*....|....*....
gi 2258418  197 SkgyVF----QMEMIVRARQLNYTIGEVP 221
Cdd:cd02526 172 D---LFidyvDTEWCLRARSKGYKIYVVP 197
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 52-112 3.89e-03

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 37.95  E-value: 3.89e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258418   52 EIIIIDDGSPDG--TRDVAEQLEKIYGSDRILlrpR-EKKLGLGTAYIHGMKHATGNYIIIMDA 112
Cdd:cd02510  32 EIILVDDFSDKPelKLLLEEYYKKYLPKVKVL---RlKKREGLIRARIAGARAATGDVLVFLDS 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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