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Conserved domains on  [gi|18394881|ref|NP_564118|]
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Nucleotide-diphospho-sugar transferases superfamily protein [Arabidopsis thaliana]

Protein Classification

polyprenol monophosphomannose synthase( domain architecture ID 11477088)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
5-246 0e+00

dolichyl-phosphate beta-D-mannosyltransferase


:

Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 507.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    5 METKGEKKYKYSIIIPTYNERLNIAIIVYLIFKHLRDV-DFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLG 83
Cdd:PLN02726   1 MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVkDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   84 LGTAYIHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLTSRGANVLAQTLLW 163
Cdd:PLN02726  81 LGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  164 PGVSDLTGSFRLYKKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVDRVFGTSKLGGSEIVEYLKGLVYLL 243
Cdd:PLN02726 161 PGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLL 240

                 ...
gi 18394881  244 LTT 246
Cdd:PLN02726 241 LTT 243
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
5-246 0e+00

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 507.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    5 METKGEKKYKYSIIIPTYNERLNIAIIVYLIFKHLRDV-DFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLG 83
Cdd:PLN02726   1 MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVkDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   84 LGTAYIHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLTSRGANVLAQTLLW 163
Cdd:PLN02726  81 LGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  164 PGVSDLTGSFRLYKKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVDRVFGTSKLGGSEIVEYLKGLVYLL 243
Cdd:PLN02726 161 PGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLL 240

                 ...
gi 18394881  244 LTT 246
Cdd:PLN02726 241 LTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
17-242 3.92e-137

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: 384.19  E-value: 3.92e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVYLIFKHLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRAraKKLGLGTAYIHGLKHAT 96
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRP--GKRGLGSAYIEGFKAAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  97 GDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLTSRGANVLAQTLLWPGVSDLTGSFRLY 176
Cdd:cd06442  79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFRAY 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394881 177 KKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVDRVFGTSKLGGSEIVEYLKGLVYL 242
Cdd:cd06442 159 RREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
14-236 6.20e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 159.87  E-value: 6.20e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  14 KYSIIIPTYNERLNIAIIVYLIFKHlRDVDFEIIVVDDGSPDGTQEIVKQLQQLYgeDRILLRARAKKLGLGTAYIHGLK 93
Cdd:COG0463   3 LVSVVIPTYNEEEYLEEALESLLAQ-TYPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAARNAGLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  94 HATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVhgwnLMRKLTSRGANVLAqtlLWPGVSDLTGSF 173
Cdd:COG0463  80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVR---LLTNLPDSTSGF 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18394881 174 RLYKKSALEDVIsscVSKGYVFQMEMIvRATRKGYHIEEVPITFVDrvfGTSKLGGSEIVEYL 236
Cdd:COG0463 153 RLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
16-183 3.74e-42

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 140.99  E-value: 3.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    16 SIIIPTYNERLNIAIIVYLIFKHLRDvDFEIIVVDDGSPDGTQEIVKQLQQLYgeDRILLRARAKKLGLGTAYIHGLKHA 95
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    96 TGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLT-SRGANVLAQTLLWPGVSDLTGSFR 174
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 18394881   175 LYKKSALED 183
Cdd:pfam00535 158 LYRREALEE 166
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
16-106 8.55e-14

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: 68.31  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    16 SIIIPTYNERLNIAiivyLIFKHLR--DVDFEIIVVDDGSPDGTQEIVKQLqqlygEDRILLRA--RAKKLglgtayIHG 91
Cdd:TIGR04283   2 SIIIPVLNEAATLP----ELLADLQalRGDAEVIVVDGGSTDGTVEIARSL-----GAKVIHSPkgRARQM------NAG 66
                          90
                  ....*....|....*
gi 18394881    92 LKHATGDFVVIMDAD 106
Cdd:TIGR04283  67 AALAKGDILLFLHAD 81
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
16-106 3.50e-07

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 50.18  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   16 SIIIPTYN---------ERLNIAIivylifkHLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLGLGT 86
Cdd:NF038302   4 TVAIPTYNganrlpevlERLRSQI-------GTESLSWEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLRYCFEPQQGAAF 76
                         90       100
                 ....*....|....*....|
gi 18394881   87 AYIHGLKHATGDFVVIMDAD 106
Cdd:NF038302  77 ARQRAIQEAKGELIGFLDDD 96
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
5-246 0e+00

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 507.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    5 METKGEKKYKYSIIIPTYNERLNIAIIVYLIFKHLRDV-DFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLG 83
Cdd:PLN02726   1 MEAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVkDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   84 LGTAYIHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLTSRGANVLAQTLLW 163
Cdd:PLN02726  81 LGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  164 PGVSDLTGSFRLYKKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVDRVFGTSKLGGSEIVEYLKGLVYLL 243
Cdd:PLN02726 161 PGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLL 240

                 ...
gi 18394881  244 LTT 246
Cdd:PLN02726 241 LTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
17-242 3.92e-137

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: 384.19  E-value: 3.92e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVYLIFKHLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRAraKKLGLGTAYIHGLKHAT 96
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRP--GKRGLGSAYIEGFKAAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  97 GDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLTSRGANVLAQTLLWPGVSDLTGSFRLY 176
Cdd:cd06442  79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFRAY 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394881 177 KKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVDRVFGTSKLGGSEIVEYLKGLVYL 242
Cdd:cd06442 159 RREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
17-203 1.26e-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: 222.06  E-value: 1.26e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVYLIFKHL-RDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARakKLGLGTAYIHGLKHA 95
Cdd:cd04179   1 VVIPAYNEEENIPELVERLLAVLeEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSR--NFGKGAAVRAGFKAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  96 TGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVhGWNLMRKLTSRGANVLAQTLLWPGVSDLTGSFRL 175
Cdd:cd04179  79 RGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGA-GMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157
                       170       180
                ....*....|....*....|....*...
gi 18394881 176 YKKSALEDVISSCVSKGYVFQMEMIVRA 203
Cdd:cd04179 158 FRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
14-236 6.20e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 159.87  E-value: 6.20e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  14 KYSIIIPTYNERLNIAIIVYLIFKHlRDVDFEIIVVDDGSPDGTQEIVKQLQQLYgeDRILLRARAKKLGLGTAYIHGLK 93
Cdd:COG0463   3 LVSVVIPTYNEEEYLEEALESLLAQ-TYPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAARNAGLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  94 HATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVhgwnLMRKLTSRGANVLAqtlLWPGVSDLTGSF 173
Cdd:COG0463  80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVR---LLTNLPDSTSGF 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18394881 174 RLYKKSALEDVIsscVSKGYVFQMEMIvRATRKGYHIEEVPITFVDrvfGTSKLGGSEIVEYL 236
Cdd:COG0463 153 RLFRREVLEELG---FDEGFLEDTELL-RALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
17-226 1.10e-42

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: 143.86  E-value: 1.10e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNE--RLNIAIIVYLIFKHLR-DVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRaRAKKLGLGTAYIHGLK 93
Cdd:cd04188   1 VVIPAYNEekRLPPTLEEAVEYLEERpSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLT-LPKNRGKGGAVRAGML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  94 HATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGG--GVHGwNLMRKLTSRGANVLAQTLLWPGVSDLTG 171
Cdd:cd04188  80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASaaVVKR-SWLRNLLGRGFNFLVRLLLGLGIKDTQC 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18394881 172 SFRLYKKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVDrvFGTSK 226
Cdd:cd04188 159 GFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVE--IPGSK 211
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
16-183 3.74e-42

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 140.99  E-value: 3.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    16 SIIIPTYNERLNIAIIVYLIFKHLRDvDFEIIVVDDGSPDGTQEIVKQLQQLYgeDRILLRARAKKLGLGTAYIHGLKHA 95
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    96 TGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLT-SRGANVLAQTLLWPGVSDLTGSFR 174
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 18394881   175 LYKKSALED 183
Cdd:pfam00535 158 LYRREALEE 166
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
17-186 3.32e-32

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: 116.04  E-value: 3.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVYLIFKHLR--DVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARakKLGLGTAYIHGLKH 94
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAVLEslGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSR--NFGQQAALLAGLDH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  95 ATGDFVVIMDADLSHHPKYLPSFIKKqLETNASIVTGTRYVKGGGvhgwnLMRKLTSRGANVLAQTLLWPGVSDLTGSFR 174
Cdd:cd04187  79 ARGDAVITMDADLQDPPELIPEMLAK-WEEGYDVVYGVRKNRKES-----WLKRLTSKLFYRLINKLSGVDIPDNGGDFR 152
                       170
                ....*....|..
gi 18394881 175 LYKKSALEDVIS 186
Cdd:cd04187 153 LMDRKVVDALLL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
17-132 3.59e-23

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: 91.80  E-value: 3.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVYLIFKHLRDvDFEIIVVDDGSPDGTQEIVKQLQQLYgeDRILLRARAKKLGLGTAYIHGLKHAT 96
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARNAGLKAAR 77
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 18394881  97 GDFVVIMDADLSHHPKYLPSFIKK-QLETNASIVTGT 132
Cdd:cd00761  78 GEYILFLDADDLLLPDWLERLVAElLADPEADAVGGP 114
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
14-218 1.94e-22

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: 93.27  E-value: 1.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  14 KYSIIIPTYNERLNIAIIVYLIFK-HLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYgeDRILLRARAKKLGLGTAYIHGL 92
Cdd:COG1215  30 RVSVIIPAYNEEAVIEETLRSLLAqDYPKEKLEVIVVDDGSTDETAEIARELAAEY--PRVRVIERPENGGKAAALNAGL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  93 KHATGDFVVIMDADLSHHPKYLpsfikkqletnasivtgtryvkgggvhgWNLMRKLTSRGAnvlaqtllwpgvsDLTGS 172
Cdd:COG1215 108 KAARGDIVVFLDADTVLDPDWL----------------------------RRLVAAFADPGV-------------GASGA 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18394881 173 FRLYKKSALEDVisscvsKGYVFQ-----MEMIVRATRKGYHIEEVPITFV 218
Cdd:COG1215 147 NLAFRREALEEV------GGFDEDtlgedLDLSLRLLRAGYRIVYVPDAVV 191
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
17-184 3.54e-20

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: 84.59  E-value: 3.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVylifKHLRDVD---FEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKlGLGTAYIHGLK 93
Cdd:cd06423   1 IIVPAYNEEAVIERTI----ESLLALDypkLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENG-GKAGALNAGLR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  94 HATGDFVVIMDADlSHHPKYLPSFIKKQLETNASI--VTGTRYVKGGGVHGWNLMRKL---TSRGANVLAQTLLWpGVSD 168
Cdd:cd06423  76 HAKGDIVVVLDAD-TILEPDALKRLVVPFFADPKVgaVQGRVRVRNGSENLLTRLQAIeylSIFRLGRRAQSALG-GVLV 153
                       170
                ....*....|....*.
gi 18394881 169 LTGSFRLYKKSALEDV 184
Cdd:cd06423 154 LSGAFGAFRREALREV 169
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
16-184 7.70e-18

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: 79.97  E-value: 7.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYNERLNI-AIIVYLIFKHLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRaraKKLGLGTAYIHGLKH 94
Cdd:cd02525   3 SIIIPVRNEEKYIeELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDN---PKRIQSAGLNIGIRN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  95 ATGDFVVIMDADlSHHPK-YLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLTSRGANVLA---QTLLWPGVSDlT 170
Cdd:cd02525  80 SRGDIIIRVDAH-AVYPKdYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSPLGSGGSayrGGAVKIGYVD-T 157
                       170
                ....*....|....
gi 18394881 171 GSFRLYKKSALEDV 184
Cdd:cd02525 158 VHHGAYRREVFEKV 171
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
14-114 9.87e-17

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.80  E-value: 9.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  14 KYSIIIPTYNERlniAIIVYLI--FKHLRDVDFEIIVVDDGSPDGTQEIVKQLQqlygEDRILLRARAKKLGLGTAYIHG 91
Cdd:COG1216   4 KVSVVIPTYNRP---ELLRRCLesLLAQTYPPFEVIVVDNGSTDGTAELLAALA----FPRVRVIRNPENLGFAAARNLG 76
                        90       100
                ....*....|....*....|...
gi 18394881  92 LKHATGDFVVIMDADLSHHPKYL 114
Cdd:COG1216  77 LRAAGGDYLLFLDDDTVVEPDWL 99
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
10-219 1.12e-14

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 72.11  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   10 EKKYKYSIIIPTYNERLNIAIIVYLIFKHLRD-------VDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLR--ARAK 80
Cdd:PTZ00260  67 DSDVDLSIVIPAYNEEDRLPKMLKETIKYLESrsrkdpkFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIDIRllSLLR 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   81 KLGLGTAYIHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNA---SIVTGTR--YVKGGGVHGWNLMRKLTSRGAN 155
Cdd:PTZ00260 147 NKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQnglGIVFGSRnhLVDSDVVAKRKWYRNILMYGFH 226
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18394881  156 VLAQTLLWPGVSDLTGSFRLYKKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVD 219
Cdd:PTZ00260 227 FIVNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTE 290
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
16-106 8.55e-14

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: 68.31  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    16 SIIIPTYNERLNIAiivyLIFKHLR--DVDFEIIVVDDGSPDGTQEIVKQLqqlygEDRILLRA--RAKKLglgtayIHG 91
Cdd:TIGR04283   2 SIIIPVLNEAATLP----ELLADLQalRGDAEVIVVDGGSTDGTVEIARSL-----GAKVIHSPkgRARQM------NAG 66
                          90
                  ....*....|....*
gi 18394881    92 LKHATGDFVVIMDAD 106
Cdd:TIGR04283  67 AALAKGDILLFLHAD 81
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
16-106 1.53e-12

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: 64.57  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYN-ERlniaiivYL------IFKHLrDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRArAKKLGLGTAY 88
Cdd:cd04196   1 AVLMATYNgEK-------YLreqldsILAQT-YKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRN-GKNLGVARNF 71
                        90
                ....*....|....*...
gi 18394881  89 IHGLKHATGDFVVIMDAD 106
Cdd:cd04196  72 ESLLQAADGDYVFFCDQD 89
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
14-106 5.92e-12

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: 63.37  E-value: 5.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  14 KYSIIIPTYNERLNIAiivylifKHLRDV--------DFEIIVVDDGSPDGTQEIVKQlqqlYGEDRILLRARAKKLGLG 85
Cdd:cd06439  30 TVTIIIPAYNEEAVIE-------AKLENLlaldyprdRLEIIVVSDGSTDGTAEIARE----YADKGVKLLRFPERRGKA 98
                        90       100
                ....*....|....*....|.
gi 18394881  86 TAYIHGLKHATGDFVVIMDAD 106
Cdd:cd06439  99 AALNRALALATGEIVVFTDAN 119
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
15-225 7.23e-12

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: 63.16  E-value: 7.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    15 YSIIIPTYNERlniAIIVYLIFKHLRDV--DFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLGLG---TAYI 89
Cdd:pfam13641   4 VSVVVPAFNED---SVLGRVLEAILAQPypPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgksRGLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    90 HGLKHATGDFVVIMDADLSHHP----KYLPSFIKKQletnASIVTGTRYVKGGGvHGWNLM--RKLTSRGANVLAQTLLw 163
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPgtlkKYVQYFDSPK----VGAVGTPVFSLNRS-TMLSALgaLEFALRHLRMMSLRLA- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394881   164 PGVSDLTGSFRLYKKSALED----VISSCVSKGYvfqmEMIVRATRKGYHIEEVPITFVDRVFGTS 225
Cdd:pfam13641 155 LGVLPLSGAGSAIRREVLKElglfDPFFLLGDDK----SLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
10-246 7.83e-12

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 63.99  E-value: 7.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   10 EKKYKYSIIIPTYNERLNIAIIVYLIFKHLRDV--DFEIIVVDDGSPDGTQEIVKQLQQLYGED--RILLRaraKKLGLG 85
Cdd:PRK10714   3 HPIKKVSVVIPVYNEQESLPELIRRTTAACESLgkEYEILLIDDGSSDNSAEMLVEAAQAPDSHivAILLN---RNYGQH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   86 TAYIHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLEtnASIVTGTRYVKGGGvhgwNLMRKLTSRGANVLAQTLLWPG 165
Cdd:PRK10714  80 SAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADE--GYDVVGTVRQNRQD----SWFRKTASKMINRLIQRTTGKA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  166 VSDLTGSFRLYKKSALeDVISSCVSKGYVFQMEMIVRATRKgyhiEEVPITFVDRVFGTSKLGGSEIVEYLKGLVYLLLT 245
Cdd:PRK10714 154 MGDYGCMLRAYRRHIV-DAMLHCHERSTFIPILANTFARRA----IEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTT 228

                 .
gi 18394881  246 T 246
Cdd:PRK10714 229 T 229
PRK10073 PRK10073
putative glycosyl transferase; Provisional
14-153 9.03e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.53  E-value: 9.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   14 KYSIIIPTYN-ERLNIAIIVYLIFKHLRDvdFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAkklGLGTAYIHGL 92
Cdd:PRK10073   7 KLSIIIPLYNaGKDFRAFMESLIAQTWTA--LEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANA---GVSVARNTGL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18394881   93 KHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVT--GTRYVKGGGvHGWNLM--RKLTSRG 153
Cdd:PRK10073  82 AVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQcnADWCFRDTG-ETWQSIpsDRLRSTG 145
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
17-139 1.39e-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: 62.31  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAiivyLIFKHLRDVD-----FEIIVVDDGSPDGTQEIV-----KQLQQLYGEDRILLRARAKKLGLGT 86
Cdd:cd04192   1 VVIAARNEAENLP----RLLQSLSALDypkekFEVILVDDHSTDGTVQILefaaaKPNFQLKILNNSRVSISGKKNALTT 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18394881  87 AyihgLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTG-TRYVKGGG 139
Cdd:cd04192  77 A----IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGpVIYFKGKS 126
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
16-106 3.76e-11

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: 60.77  E-value: 3.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYNERLNIAiivylifKHLRDVDF---EIIVVDDGSPDGTQEIVKQlqqlYGeDRILLRaraKKLGLGTAYIHGL 92
Cdd:cd02511   3 SVVIITKNEERNIE-------RCLESVKWavdEIIVVDSGSTDRTVEIAKE----YG-AKVYQR---WWDGFGAQRNFAL 67
                        90
                ....*....|....
gi 18394881  93 KHATGDFVVIMDAD 106
Cdd:cd02511  68 ELATNDWVLSLDAD 81
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
15-106 4.47e-11

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: 60.66  E-value: 4.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  15 YSIIIPTYNERLNIAIivyLI--FKHLRDVDFEIIVVDDGSPDGTQEIVKQL--QQLYGEdrillRARAKKLglgtayIH 90
Cdd:cd02522   1 LSIIIPTLNEAENLPR---LLasLRRLNPLPLEIIVVDGGSTDGTVAIARSAgvVVISSP-----KGRARQM------NA 66
                        90
                ....*....|....*.
gi 18394881  91 GLKHATGDFVVIMDAD 106
Cdd:cd02522  67 GAAAARGDWLLFLHAD 82
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
17-155 2.04e-09

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


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 55.28  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYN--ERLNIaiiVYLIFKHLRDVDFEIIVVDDGSPDGTQEIVKQ--------LQQLYGEDrillrarakkLGLGT 86
Cdd:cd06420   1 LIITTYNrpEALEL---VLKSVLNQSILPFEVIIADDGSTEETKELIEEfksqfpipIKHVWQED----------EGFRK 67
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18394881  87 AYI--HGLKHATGDFVVIMDADLSHHPKylpsFIKK--QLETNASIVTGTRYvkgggvhgwNLMRKLTSRGAN 155
Cdd:cd06420  68 AKIrnKAIAAAKGDYLIFIDGDCIPHPD----FIADhiELAEPGVFLSGSRV---------LLNEKLTERGIR 127
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
16-137 5.24e-09

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 55.31  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   16 SIIIPTYNERLNIAIIVYLIFKHL--RDVDfEIIVVDDGSPDGTQEIVKQlqqlYGEDRI----LLRARAKKLGLGTAYI 89
Cdd:PRK13915  34 SVVLPALNEEETVGKVVDSIRPLLmePLVD-ELIVIDSGSTDATAERAAA----AGARVVsreeILPELPPRPGKGEALW 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 18394881   90 HGLKHATGDFVVIMDADL-SHHPKYLPSFIKKQLEtnasiVTGTRYVKG 137
Cdd:PRK13915 109 RSLAATTGDIVVFVDADLiNFDPMFVPGLLGPLLT-----DPGVHLVKA 152
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
17-106 1.06e-08

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 52.95  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVYLIFKHLRDvDFEIIVVDDGSPDGTQEIVKQLQQlygeDRILLRArAKKLGLGTAYIHGLKHAT 96
Cdd:cd04186   1 IIIVNYNSLEYLKACLDSLLAQTYP-DFEVIVVDNASTDGSVELLRELFP----EVRLIRN-GENLGFGAGNNQGIREAK 74
                        90
                ....*....|
gi 18394881  97 GDFVVIMDAD 106
Cdd:cd04186  75 GDYVLLLNPD 84
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
17-114 4.59e-08

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


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 52.19  E-value: 4.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIaiiVYLIFKHLRDVD-----FEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAK-KLGlgtAYIH 90
Cdd:cd06421   5 VFIPTYNEPLEI---VRKTLRAALAIDyphdkLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHaKAG---NLNN 78
                        90       100
                ....*....|....*....|....
gi 18394881  91 GLKHATGDFVVIMDADLSHHPKYL 114
Cdd:cd06421  79 ALAHTTGDFVAILDADHVPTPDFL 102
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
16-139 9.63e-08

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 51.01  E-value: 9.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYNerlNIAIIVYLI--FKHLRDVDFEIIVVDDGSPDGTQEIVKQLqqlygEDRILlrarakKL------GLGTA 87
Cdd:cd06433   1 SIITPTYN---QAETLEETIdsVLSQTYPNIEYIVIDGGSTDGTVDIIKKY-----EDKIT------YWisepdkGIYDA 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18394881  88 YIHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLE-TNASIVTG-TRYVKGGG 139
Cdd:cd06433  67 MNKGIALATGDIIGFLNSDDTLLPGALLAVVAAFAEhPEVDVVYGdVLLVDENG 120
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
16-106 3.50e-07

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 50.18  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881   16 SIIIPTYN---------ERLNIAIivylifkHLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLGLGT 86
Cdd:NF038302   4 TVAIPTYNganrlpevlERLRSQI-------GTESLSWEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLRYCFEPQQGAAF 76
                         90       100
                 ....*....|....*....|
gi 18394881   87 AYIHGLKHATGDFVVIMDAD 106
Cdd:NF038302  77 ARQRAIQEAKGELIGFLDDD 96
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
16-185 5.30e-07

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 49.17  E-value: 5.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYNERLNIaiivyliFKH-----LRDVDFEIIVVDDGSPDGTQEIVKQlQQLYGEDRILLRARAKKLGlgtAYIH 90
Cdd:cd06434   3 TVIIPVYDEDPDV-------FREclrsiLRQKPLEIIVVTDGDDEPYLSILSQ-TVKYGGIFVITVPHPGKRR---ALAE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  91 GLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLM--RKLTSRGANVLAQTLLWPGVSD 168
Cdd:cd06434  72 GIRHVTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTNQRILRPRDSKWSFLaaEYLERRNEEIRAAMSYDGGVPC 151
                       170
                ....*....|....*..
gi 18394881 169 LTGSFRLYKKSALEDVI 185
Cdd:cd06434 152 LSGRTAAYRTEILKDFL 168
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
16-106 6.46e-07

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: 49.20  E-value: 6.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    16 SIIIPTYNERLNIAIIVYLIFK-HLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRiLLRARAKKLGLGTAYIHGLKH 94
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQtFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVY-YPNAPDTTYSLAASRNRGTSH 79
                          90
                  ....*....|..
gi 18394881    95 ATGDFVVIMDAD 106
Cdd:pfam10111  80 AIGEYISFIDGD 91
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
18-138 6.85e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 48.40  E-value: 6.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  18 IIPTYNeRLNIAIIVyliFKHLRDVDF---EIIVVDDGSPDGTQEIvkqLQQLYGEDRILLRARAKKLGlGTAYIH-GLK 93
Cdd:cd04185   2 VVVTYN-RLDLLKEC---LDALLAQTRppdHIIVIDNASTDGTAEW---LTSLGDLDNIVYLRLPENLG-GAGGFYeGVR 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18394881  94 HA--TG-DFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGG 138
Cdd:cd04185  74 RAyeLGyDWIWLMDDDAIPDPDALEKLLAYADKDNPQFLAPLVLDPDG 121
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
16-106 1.19e-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: 47.58  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYNerlniAIIVYLIfKHLRDV------DFEIIVVDDGSPDgtqEIVKQLQQLYGED--RILLRARAKKLGLGTA 87
Cdd:cd04184   4 SIVMPVYN-----TPEKYLR-EAIESVraqtypNWELCIADDASTD---PEVKRVLKKYAAQdpRIKVVFREENGGISAA 74
                        90
                ....*....|....*....
gi 18394881  88 YIHGLKHATGDFVVIMDAD 106
Cdd:cd04184  75 TNSALELATGEFVALLDHD 93
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
45-119 2.51e-06

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


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 46.92  E-value: 2.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  45 EIIVVDDGS-PDGTQEIVKQLQQLYGEDRILLRaraKKLGLGTAYIHGLKHATGDFVVIMDADLSHHP----KYLPSFIK 119
Cdd:cd04195  31 EVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPLE---KNRGLGKALNEGLKHCTYDWVARMDTDDISLPdrfeKQLDFIEK 107
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
16-148 1.34e-05

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: 45.27  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYNERLNIAI-IVYLIF-----KHLRdvdfEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLGLGTAYI 89
Cdd:cd02510   1 SVIIIFHNEALSTLLrTVHSVInrtppELLK----EIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARI 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18394881  90 HGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIV---------TGTRYVKGGGVHG----WNLMRK 148
Cdd:cd02510  77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVcpiidvidaDTFEYRGSSGDARggfdWSLHFK 148
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
16-114 1.55e-05

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


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 44.61  E-value: 1.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  16 SIIIPTYNERLniaiIVYLIFKHLRDVDF-----EIIVVDDGSPDGTQEIVKQLQQLYGED-RILLRARAKKLGL-GTAY 88
Cdd:cd06437   4 TVQLPVFNEKY----VVERLIEAACALDYpkdrlEIQVLDDSTDETVRLAREIVEEYAAQGvNIKHVRRADRTGYkAGAL 79
                        90       100
                ....*....|....*....|....*.
gi 18394881  89 IHGLKHATGDFVVIMDADLSHHPKYL 114
Cdd:cd06437  80 AEGMKVAKGEYVAIFDADFVPPPDFL 105
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
89-184 4.03e-05

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


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 43.04  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    89 IHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYvkGGGVHGW--NLMRKLTSRGANVLAQTLLwpGV 166
Cdd:pfam13506  23 LQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTSPPV--GSDPKGLaaALEAAFFNTLAGVLQAALS--GI 98
                          90
                  ....*....|....*...
gi 18394881   167 SDLTGSFRLYKKSALEDV 184
Cdd:pfam13506  99 GFAVGMSMAFRRADLERI 116
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
22-118 5.40e-04

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 38.38  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881    22 YNErlniAIIVYLIFKHLRDVDFE-IIVVDDGSPDGTQEIvkqLQQLYGEDRILLRARAKKLGLGTAYIHGLK--HATGD 98
Cdd:pfam13704   1 RNE----ADILPQWLAHHLALGFDhIYVYDNGSDDGTAEI---LARLPDVSILRSDLSYKDARFQVDWRNALLarYAEAD 73
                          90       100
                  ....*....|....*....|....
gi 18394881    99 FVVIMDAD----LSHHPKYLPSFI 118
Cdd:pfam13704  74 WVLVVDADeflvYPPGDRSLRALL 97
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
17-136 1.24e-03

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 38.74  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  17 IIIPTYNERLNIAIIVylifKHLRDVD-----FEIIVVDDGSPDGTQEIVKQLqqlygEDRILLRARAKKLGLGTAYIHG 91
Cdd:cd06438   1 ILIPAHNEEAVIGNTV----RSLKAQDyprelYRIFVVADNCTDDTAQVARAA-----GATVLERHDPERRGKGYALDFG 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18394881  92 LKHATG-----DFVVIMDADLSHHPKYLPSFiKKQLETNASIVTGTRYVK 136
Cdd:cd06438  72 FRHLLNladdpDAVVVFDADNLVDPNALEEL-NARFAAGARVVQAYYNSK 120
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
43-158 3.33e-03

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


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 37.58  E-value: 3.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394881  43 DFEII-VVDDGSpDGTQEIVKQLQQLYGEDRILLRARAKKLG-------LGTAYihglKHATGDFVVIMDADLSHHPKYL 114
Cdd:cd02520  30 KYEILfCVQDED-DPAIPVVRKLIAKYPNVDARLLIGGEKVGinpkvnnLIKGY----EEARYDILVISDSDISVPPDYL 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18394881 115 PSFIKKQLETNASIVTGTrYVKGGGvhgwNLMRK--LTSRG-----ANVLA 158
Cdd:cd02520 105 RRMVAPLMDPGVGLVTCL-CAFGKS----MALRRevLDAIGgfeafADYLA 150
 
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.
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