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Conserved domains on  [gi|827549293|ref|XP_012546773|]
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dolichyl-phosphate mannosyltransferase isoform X1 [Bombyx mori]

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
 9-246 1.11e-144

dolichyl-phosphate beta-D-mannosyltransferase


The actual alignment was detected with superfamily member PLN02726:

Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 404.08  E-value: 1.11e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   9 KRDKYSILLPTYNERENLPIIIWLIIKYLDESGvDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMKLGLGTAY 88
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  89 IHGIQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDFKRKLISRGANFLTQLMLRPGVSD 168
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827549293 169 LTGSFRLYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVDRVYGESKLGGSEIVQFAKALLYLFATT 246
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 9-246 1.11e-144

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 404.08  E-value: 1.11e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   9 KRDKYSILLPTYNERENLPIIIWLIIKYLDESGvDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMKLGLGTAY 88
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  89 IHGIQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDFKRKLISRGANFLTQLMLRPGVSD 168
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827549293 169 LTGSFRLYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVDRVYGESKLGGSEIVQFAKALLYLFATT 246
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 15-242 4.91e-125

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: 353.76  E-value: 4.91e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKYLdeSGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPRemKLGLGTAYIHGIQQ 94
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAAL--KGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPG--KRGLGSAYIEGFKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  95 ASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDFKRKLISRGANFLTQLMLRPGVSDLTGSFR 174
Cdd:cd06442   77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827549293 175 LYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVDRVYGESKLGGSEIVQFAKALLYL 242
Cdd:cd06442  157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 12-236 1.03e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 154.09  E-value: 1.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  12 KYSILLPTYNERENLPIIIWLIikyLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPRemKLGLGTAYIHG 91
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESL---LAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLER--NRGKGAARNAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  92 IQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVygwdFKRKLISRGANFLTQLMlrpGVSDLTG 171
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLLT---NLPDSTS 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827549293 172 SFRLYKKEVLEKLILscvSKGYVFQMEMiIRARQFDYSIGEVPISFVDrvyGESKLGGSEIVQFA 236
Cdd:COG0463  151 GFRLFRREVLEELGF---DEGFLEDTEL-LRALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 14-183 1.90e-39

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: 134.06  E-value: 1.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   14 SILLPTYNERENLPIIIWLIIKYLDEsgvDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPRemKLGLGTAYIHGIQ 93
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPE--NRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   94 QASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDF-KRKLISRGANFLTQLMLRPGVSDLTGS 172
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 827549293  173 FRLYKKEVLEK 183
Cdd:pfam00535 156 FALYRREALEE 166
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 14-106 6.45e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 51.74  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   14 SILLPTYNERENLPiiiwLIIKYLDESGVDYEVIIIDDGSPDGTSEVARQLqklygSSKIVLRPRemklglGTAY--IHG 91
Cdd:TIGR04283   2 SIIIPVLNEAATLP----ELLADLQALRGDAEVIVVDGGSTDGTVEIARSL-----GAKVIHSPK------GRARqmNAG 66

                          90
                  ....*....|....*
gi 827549293   92 IQQASGNFIIIMDAD 106
Cdd:TIGR04283  67 AALAKGDILLFLHAD 81
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 9-246 1.11e-144

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 404.08  E-value: 1.11e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   9 KRDKYSILLPTYNERENLPIIIWLIIKYLDESGvDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMKLGLGTAY 88
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  89 IHGIQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDFKRKLISRGANFLTQLMLRPGVSD 168
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827549293 169 LTGSFRLYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVDRVYGESKLGGSEIVQFAKALLYLFATT 246
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 15-242 4.91e-125

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: 353.76  E-value: 4.91e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKYLdeSGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPRemKLGLGTAYIHGIQQ 94
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAAL--KGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPG--KRGLGSAYIEGFKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  95 ASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDFKRKLISRGANFLTQLMLRPGVSDLTGSFR 174
Cdd:cd06442   77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827549293 175 LYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVDRVYGESKLGGSEIVQFAKALLYL 242
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 ...
 15-203 4.98e-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: 220.52  E-value: 4.98e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKYLDEsGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPRemKLGLGTAYIHGIQQ 94
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSR--NFGKGAAVRAGFKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  95 ASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGsGGVYGWDFKRKLISRGANFLTQLMLRPGVSDLTGSFR 174
Cdd:cd04179   78 ARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVR-GGGAGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFR 156

                        170       180
                 ....*....|....*....|....*....
gi 827549293 175 LYKKEVLEKLILSCVSKGYVFQMEMIIRA 203
Cdd:cd04179  157 LFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 12-236 1.03e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 154.09  E-value: 1.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  12 KYSILLPTYNERENLPIIIWLIikyLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPRemKLGLGTAYIHG 91
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESL---LAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLER--NRGKGAARNAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  92 IQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVygwdFKRKLISRGANFLTQLMlrpGVSDLTG 171
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLLT---NLPDSTS 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827549293 172 SFRLYKKEVLEKLILscvSKGYVFQMEMiIRARQFDYSIGEVPISFVDrvyGESKLGGSEIVQFA 236
Cdd:COG0463  151 GFRLFRREVLEELGF---DEGFLEDTEL-LRALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 14-183 1.90e-39

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: 134.06  E-value: 1.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   14 SILLPTYNERENLPIIIWLIIKYLDEsgvDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPRemKLGLGTAYIHGIQ 93
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPE--NRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   94 QASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDF-KRKLISRGANFLTQLMLRPGVSDLTGS 172
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 827549293  173 FRLYKKEVLEK 183
Cdd:pfam00535 156 FALYRREALEE 166
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 15-226 1.99e-39

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: 135.39  E-value: 1.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKYLDES-GVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRpREMKLGLGTAYIHGIQ 93
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEERpSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLT-LPKNRGKGGAVRAGML 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  94 QASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYK-GSGGVYGWDFKRKLISRGANFLTQLMLRPGVSDLTGS 172
Cdd:cd04188   80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHlASAAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 827549293 173 FRLYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVDRvyGESK 226
Cdd:cd04188  160 FKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEI--PGSK 211
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 15-186 3.87e-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: 3.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKYLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMklGLGTAYIHGIQQ 94
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNF--GQQAALLAGLDH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  95 ASGNFIIIMDADLSHHPKFIPEFIKLQLKyDYDIVSGTRYKGSGGvygwdFKRKLISRGANFLTQLMLRPGVSDLTGSFR 174
Cdd:cd04187   79 ARGDAVITMDADLQDPPELIPEMLAKWEE-GYDVVYGVRKNRKES-----WLKRLTSKLFYRLINKLSGVDIPDNGGDFR 152

                        170
                 ....*....|..
gi 827549293 175 LYKKEVLEKLIL 186
Cdd:cd04187  153 LMDRKVVDALLL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 15-132 2.39e-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: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKYLDEsgvDYEVIIIDDGSPDGTSEVARQLQKLYgsSKIVLRPREMKLGLGTAYIHGIQQ 94
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARNAGLKA 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 827549293  95 ASGNFIIIMDADLSHHPKFIPEFIKLQLKY-DYDIVSGT 132
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADpEADAVGGP 114
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 12-141 4.26e-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: 84.02  E-value: 4.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  12 KYSILLPTYNERENLPIIIWLIIKyLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMklGLGTAYIHG 91
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLA-QDYPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENG--GKAAALNAG 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 827549293  92 IQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVsgtrykGSGGVY 141
Cdd:COG1215  107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS------GANLAF 150
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 11-226 5.10e-18

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 81.32  E-value: 5.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  11 DKYSILLPTYNERENLPIIIWLIIKYLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKI-VLRPRemKLGLGTAYI 89
Cdd:PRK10714   6 KKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVaILLNR--NYGQHSAIM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  90 HGIQQASGNFIIIMDADLSHHPKFIPEFIKlQLKYDYDIVSGTRYKGSGGVYgwdfkRKLISRGANFLTQLMLRPGVSDL 169
Cdd:PRK10714  84 AGFSHVTGDLIITLDADLQNPPEEIPRLVA-KADEGYDVVGTVRQNRQDSWF-----RKTASKMINRLIQRTTGKAMGDY 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 827549293 170 TGSFRLYKKEVLEKLiLSCVSKGYVFQmemiIRARQFDYSIGEVPISFVDRVYGESK 226
Cdd:PRK10714 158 GCMLRAYRRHIVDAM-LHCHERSTFIP----ILANTFARRAIEIPVHHAEREFGDSK 209
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 14-240 1.33e-17

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 80.58  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNERENLPIIIWLIIKYLDE-SGVD----YEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMK--LGLGT 86
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETIKYLESrSRKDpkfkYEIIIVNDGSKDKTLKVAKDFWRQNINPNIDIRLLSLLrnKGKGG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  87 AYIHGIQQASGNFIIIMDADLSHHpkfIPEFIKLQ------LKYDYDIVSGTR--YKGSGGVYGWDFKRKLISRGANFLT 158
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADGATD---IDDFDKLEdimlkiEQNGLGIVFGSRnhLVDSDVVAKRKWYRNILMYGFHFIV 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293 159 QLMLRPGVSDLTGSFRLYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVDrVYGeSKLGG-SEIVQFAK 237
Cdd:PTZ00260 230 NTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTE-VEG-SKLNViSASIQMAR 307


                 ...
gi 827549293 238 ALL 240
Cdd:PTZ00260 308 DIL 310
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 15-184 9.97e-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: 69.95  E-value: 9.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKyLDESgvDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREmKLGLGTAYIHGIQQ 94
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLA-LDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKE-NGGKAGALNAGLRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  95 ASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYGWDFKRKLISRGANFLTQLMLRP---GVSDLTG 171
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSalgGVLVLSG 156

                        170
                 ....*....|...
gi 827549293 172 SFRLYKKEVLEKL 184
Cdd:cd06423  157 AFGAFRREALREV 169
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 14-184 4.69e-14

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 69.18  E-value: 4.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNERENLPIIIWLIIKyLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMklgLGTAYIHGIQ 93
Cdd:cd02525    3 SIIIPVRNEEKYIEELLESLLN-QSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRI---QSAGLNIGIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  94 QASGNFIIIMDADlSHHPK-FIPEFIKLQLKYDYDIVSG---TRYKGS-GGVYGWDFKRKLISRGANFltqlmlRPGVSD 168
Cdd:cd02525   79 NSRGDIIIRVDAH-AVYPKdYILELVEALKRTGADNVGGpmeTIGESKfQKAIAVAQSSPLGSGGSAY------RGGAVK 151

                        170       180
                 ....*....|....*....|
gi 827549293 169 L----TGSFRLYKKEVLEKL 184
Cdd:cd02525  152 IgyvdTVHHGAYRREVFEKV 171
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
12-119 1.01e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 65.01  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  12 KYSILLPTYNEREnlpiiiwLIIKYLD----ESGVDYEVIIIDDGSPDGTSEVARQLQklYGSSKIVLRPREmkLGLGTA 87
Cdd:COG1216    4 KVSVVIPTYNRPE-------LLRRCLEsllaQTYPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPEN--LGFAAA 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 827549293  88 YIHGIQQASGNFIIIMDADLSHHPKFIPEFIK 119
Cdd:COG1216   73 RNLGLRAAGGDYLLFLDDDTVVEPDWLERLLA 104
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 15-193 6.71e-11

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 60.38  E-value: 6.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIII--WLIIKYLDESgvdYEVIIIDDGSPDGTSE-VARQLQKLYGSSKIVLRPREMKLGLGTAYIHG 91
Cdd:cd04192    1 VVIAARNEAENLPRLLqsLSALDYPKEK---FEVILVDDHSTDGTVQiLEFAAAKPNFQLKILNNSRVSISGKKNALTTA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  92 IQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGtrykGSGGVYGWDFKRKLISrgANFLTQLMLRPGVSDL-- 169
Cdd:cd04192   78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAG----PVIYFKGKSLLAKFQR--LDWLSLLGLIAGSFGLgk 151

                        170       180
                 ....*....|....*....|....*...
gi 827549293 170 --TGSFR--LYKKEVLEKlilscvSKGY 193
Cdd:cd04192  152 pfMCNGAnmAYRKEAFFE------VGGF 173
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 14-115 2.77e-09

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 56.46  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNERENLPIIIWLIIKYLDESGVDyEVIIIDDGSPDGTSEVARQlqklYG----SSKIVLRPREMKLGLGTAYI 89
Cdd:PRK13915  34 SVVLPALNEEETVGKVVDSIRPLLMEPLVD-ELIVIDSGSTDATAERAAA----AGarvvSREEILPELPPRPGKGEALW 108

                         90       100
                 ....*....|....*....|....*..
gi 827549293  90 HGIQQASGNFIIIMDADL-SHHPKFIP 115
Cdd:PRK13915 109 RSLAATTGDIVVFVDADLiNFDPMFVP 135
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 11-184 5.47e-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: 54.68  E-value: 5.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   11 DKYSILLPTYNERENLPIIIWLIIKYldeSGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREMKLGLG---TA 87
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQ---PYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgksRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   88 YIHGIQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDIVSGTRYKGSGGVYgWDF--KRKLISRGANFLtQLMLRPG 165
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTM-LSAlgALEFALRHLRMM-SLRLALG 156

                         170
                  ....*....|....*....
gi 827549293  166 VSDLTGSFRLYKKEVLEKL 184
Cdd:pfam13641 157 VLPLSGAGSAIRREVLKEL 175
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 15-135 1.77e-08

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: 52.58  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWliiKYLDESGVDYEVIIIDDGSPDGTSEVARQLQKlygSSKIVLRP-REMKLGLGTAYI--HG 91
Cdd:cd06420    1 LIITTYNRPEALELVLK---SVLNQSILPFEVIIADDGSTEETKELIEEFKS---QFPIPIKHvWQEDEGFRKAKIrnKA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 827549293  92 IQQASGNFIIIMDADLSHHPKFIPEFIKLqLKYDYdIVSGTRYK 135
Cdd:cd06420   75 IAAAKGDYLIFIDGDCIPHPDFIADHIEL-AEPGV-FLSGSRVL 116
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 14-106 6.45e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 51.74  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   14 SILLPTYNERENLPiiiwLIIKYLDESGVDYEVIIIDDGSPDGTSEVARQLqklygSSKIVLRPRemklglGTAY--IHG 91
Cdd:TIGR04283   2 SIIIPVLNEAATLP----ELLADLQALRGDAEVIVVDGGSTDGTVEIARSL-----GAKVIHSPK------GRARqmNAG 66

                          90
                  ....*....|....*
gi 827549293   92 IQQASGNFIIIMDAD 106
Cdd:TIGR04283  67 AALAKGDILLFLHAD 81
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 14-106 1.77e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 50.32  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNERenlpiiiwliiKYLDE--------SGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREmKLGLG 85
Cdd:cd04196    1 AVLMATYNGE-----------KYLREqldsilaqTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGK-NLGVA 68

                         90       100
                 ....*....|....*....|.
gi 827549293  86 TAYIHGIQQASGNFIIIMDAD 106
Cdd:cd04196   69 RNFESLLQAADGDYVFFCDQD 89
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 12-106 5.46e-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: 49.12  E-value: 5.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  12 KYSILLPTYNERENlpiiiwlIIKYLDES-GVDY-----EVIIIDDGSPDGTSEVARQlqklYGSSKIVLRPREMKLGLG 85
Cdd:cd06439   30 TVTIIIPAYNEEAV-------IEAKLENLlALDYprdrlEIIVVSDGSTDGTAEIARE----YADKGVKLLRFPERRGKA 98

                         90       100
                 ....*....|....*....|.
gi 827549293  86 TAYIHGIQQASGNFIIIMDAD 106
Cdd:cd06439   99 AALNRALALATGEIVVFTDAN 119
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 12-128 9.53e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 48.89  E-value: 9.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  12 KYSILLPTYNERENLPIIIWLIIKYLDESgvdYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREmklGLGTAYIHG 91
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTWTA---LEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANA---GVSVARNTG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 827549293  92 IQQASGNFIIIMDADLSHHPKFIPEFIKLQLKYDYDI 128
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDV 117
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 13-64 2.77e-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: 46.79  E-value: 2.77e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 827549293  13 YSILLPTYNERENLPIiiwLIIKYLDESGVDYEVIIIDDGSPDGTSEVARQL 64
Cdd:cd02522    1 LSIIIPTLNEAENLPR---LLASLRRLNPLPLEIIVVDGGSTDGTVAIARSA 49
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 14-106 4.41e-06

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: 46.13  E-value: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNERENLP--I--IIWLiikyldesgVDyEVIIIDDGSPDGTSEVARQLqklygSSKIVLRPremKLGLGTAYI 89
Cdd:cd02511    3 SVVIITKNEERNIErcLesVKWA---------VD-EIIVVDSGSTDRTVEIAKEY-----GAKVYQRW---WDGFGAQRN 64

                         90
                 ....*....|....*..
gi 827549293  90 HGIQQASGNFIIIMDAD 106
Cdd:cd02511   65 FALELATNDWVLSLDAD 81
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 14-226 1.17e-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: 44.84  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNERENLPiiiWLIIKYLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYgsSKIVLRPREmklGLGTAYIHGIQ 93
Cdd:cd06433    1 SIITPTYNQAETLE---ETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKI--TYWISEPDK---GIYDAMNKGIA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  94 QASGNFIIIMDA-DLSHHPKFIPEFIKLQLKYDYDIVSGTRYkgsggVYGWDFKRKLISRGANFLTQLMLRPGVSDLTGS 172
Cdd:cd06433   73 LATGDIIGFLNSdDTLLPGALLAVVAAFAEHPEVDVVYGDVL-----LVDENGRVIGRRRPPPFLDKFLLYGMPICHQAT 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 827549293 173 FrlYKKEVLEKLILSCVSKGYVFQMEMIIRARQFDYSIGEVPISFVD-RVYGESK 226
Cdd:cd06433  148 F--FRRSLFEKYGGFDESYRIAADYDLLLRLLLAGKIFKYLPEVLAAfRLGGVSS 200
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 15-131 5.66e-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: 42.16  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNEREnlpiiiwLIIKYLD----ESGVDYEVIIIDDGSPDGTSEVARQLQKlygssKIVLRPREMKLGLGTAYIH 90
Cdd:cd04186    1 IIIVNYNSLE-------YLKACLDsllaQTYPDFEVIVVDNASTDGSVELLRELFP-----EVRLIRNGENLGFGAGNNQ 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 827549293  91 GIQQASGNFIIIMDADLSHHPKFIPEFIKLQLKY-DYDIVSG 131
Cdd:cd04186   69 GIREAKGDYVLLLNPDTVVEPGALLELLDAAEQDpDVGIVGP 110
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 15-116 6.85e-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: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  15 ILLPTYNERENLPIIIWLIIKYLDESGVDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPREM-KLGlgtAYIHGIQ 93
Cdd:cd06421    5 VFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHaKAG---NLNNALA 81

                         90       100
                 ....*....|....*....|...
gi 827549293  94 QASGNFIIIMDADlshhpkFIPE 116
Cdd:cd06421   82 HTTGDFVAILDAD------HVPT 98
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 14-106 2.29e-04

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


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 41.03  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNerenlPIIIWL---IIKYLDESGVDYEVIIIDDGSPDgtSEVARQLQKLYGS-SKIVLRPREMKLGLGTAYI 89
Cdd:cd04184    4 SIVMPVYN-----TPEKYLreaIESVRAQTYPNWELCIADDASTD--PEVKRVLKKYAAQdPRIKVVFREENGGISAATN 76

                         90
                 ....*....|....*..
gi 827549293  90 HGIQQASGNFIIIMDAD 106
Cdd:cd04184   77 SALELATGEFVALLDHD 93
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 14-106 7.84e-04

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: 39.95  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293   14 SILLPTYNERENLPII--IWLIIKYLDEsgvDYEVIIIDDGSPDGTSEVARQLQKLYGSSKIVLRPrEMKLGLGTAYIHG 91
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQerILNQTFQYDP---EFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAP-DTTYSLAASRNRG 76

                          90
                  ....*....|....*
gi 827549293   92 IQQASGNFIIIMDAD 106
Cdd:pfam10111  77 TSHAIGEYISFIDGD 91
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 14-114 1.27e-03

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: 38.83  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827549293  14 SILLPTYNERENLPIIIWLIIKyLDESGVDYEVIIIDDgSPDGTSEVARQLQKLYGSS--KIVLRPREMKLGL-GTAYIH 90
Cdd:cd06437    4 TVQLPVFNEKYVVERLIEAACA-LDYPKDRLEIQVLDD-STDETVRLAREIVEEYAAQgvNIKHVRRADRTGYkAGALAE 81

                         90       100
                 ....*....|....*....|....
gi 827549293  91 GIQQASGNFIIIMDADLSHHPKFI 114
Cdd:cd06437   82 GMKVAKGEYVAIFDADFVPPPDFL 105
 
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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