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Conserved domains on  [gi|24582769|ref|NP_609202|]
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wollknaeuel [Drosophila melanogaster]

Protein Classification

dolichyl-phosphate beta-glucosyltransferase( domain architecture ID 10135784)

dolichyl-phosphate beta-glucosyltransferase is a glycosyltransferase family 2 protein that catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate

CAZY:  GT2
EC:  2.4.1.117
Gene Ontology:  GO:0004581|GO:0006486
PubMed:  12200473|10521532|12691742|9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 70-290 1.98e-118

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: 339.93  E-value: 1.98e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFLEQKsagtPNFTYEVIVVSDGSQDATVSVALGYSKKHGAEkVRVLELIENRGKGGAVR 149
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEER----PSFSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 150 MGMLSARGRNLLFADADGATKFPDYDKLEVALKQlapewRDDGIAIGSRAHLENDAIATRSFFRTILMHGFHFLVWLFAV 229
Cdd:cd04188  76 AGMLAARGDYILFADADLATPFEELEKLEEALKT-----SGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582769 230 RSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAENLKLPMSEVAVRWTEIDGSK 290
Cdd:cd04188 151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 70-290 1.98e-118

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: 339.93  E-value: 1.98e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFLEQKsagtPNFTYEVIVVSDGSQDATVSVALGYSKKHGAEkVRVLELIENRGKGGAVR 149
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEER----PSFSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 150 MGMLSARGRNLLFADADGATKFPDYDKLEVALKQlapewRDDGIAIGSRAHLENDAIATRSFFRTILMHGFHFLVWLFAV 229
Cdd:cd04188  76 AGMLAARGDYILFADADLATPFEELEKLEEALKT-----SGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582769 230 RSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAENLKLPMSEVAVRWTEIDGSK 290
Cdd:cd04188 151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 36-325 1.17e-115

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 337.51  E-value: 1.17e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   36 NIKRHKDEETFLDPHTIKTVTFPSLEDSPS-LELSVIVPAYNEEQRLPSMLDECLAFLEQKSAGTPNFTYEVIVVSDGSQ 114
Cdd:PTZ00260  39 VIRQVKSSVIHEKSKEVDKENYINNILKDSdVDLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  115 DATVSVALGYSKKHGAEKV--RVLELIENRGKGGAVRMGMLSARGRNLLFADADGATKFPDYDKLEVALKQLapEWRDDG 192
Cdd:PTZ00260 119 DKTLKVAKDFWRQNINPNIdiRLLSLLRNKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKI--EQNGLG 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  193 IAIGSRAHL-ENDAIATRSFFRTILMHGFHFLVWLFAVRSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAEN 271
Cdd:PTZ00260 197 IVFGSRNHLvDSDVVAKRKWYRNILMYGFHFIVNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQK 276

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24582769  272 LKLPMSEVAVRWTEIDGSKLTPFWSWLQMGRDLFMIWVRYLVGAWRIASIQKKE 325
Cdd:PTZ00260 277 LNLPIAEVPVNWTEVEGSKLNVISASIQMARDILLVRSFYLLGIWKVKDPSLLG 330
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 68-289 3.51e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 3.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  68 LSVIVPAYNEEQRLPSMLDECLAFLeqksagtpNFTYEVIVVSDGSQDATVSVALGYSKKHgaEKVRVLELIENRGKGGA 147
Cdd:COG0463   4 VSVVIPTYNEEEYLEEALESLLAQT--------YPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 148 VRMGMLSARGRNLLFADADGatkFPDYDKLEVALKQLAPEwrDDGIAIGSRAHLENDaiatrSFFRTILMHGFHFLVWLF 227
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEG--PADLVYGSRLIREGE-----SDLRRLGSRLFNLVRLLT 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582769 228 avrSIRDTQCGFKLFTRTTARKLFTSlhvERWAFDVELLYLAENlKLPMSEVAVRWTEIDGS 289
Cdd:COG0463 144 ---NLPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALRH-GFRIAEVPVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 69-244 5.90e-23

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: 93.23  E-value: 5.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769    69 SVIVPAYNEEQRLPSMLDECLAFLEQKsagtpnftYEVIVVSDGSQDATVSVALGYSKKHGaeKVRVLELIENRGKGGAV 148
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN--------FEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPENRGKAGAR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   149 RMGMLSARGRNLLFADADGatkFPDYDKLEVALKQLapEWRDDGIAIGSRAHLENDAIATRSFFRTILMHGFHFLVWLFA 228
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADD---EVPPDWLEKLVEAL--EEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145

                         170
                  ....*....|....*.
gi 24582769   229 VRSIRDTQCGFKLFTR 244
Cdd:pfam00535 146 GLNLPFLIGGFALYRR 161
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 68-189 5.58e-11

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: 61.37  E-value: 5.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769    68 LSVIVPAYNEEQRLPSMLDECLAFLEqksagtpnfTYEVIVVSDGSQDATVSVAlgysKKHGAeKVrvleLIENRGKGGA 147
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRG---------DAEVIVVDGGSTDGTVEIA----RSLGA-KV----IHSPKGRARQ 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 24582769   148 VRMGMLSARGRNLLFADADgaTKFPDyDKLEVALKQLAPEWR 189
Cdd:TIGR04283  63 MNAGAALAKGDILLFLHAD--TRLPK-DFLEAIRRALAKPGY 101
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 70-290 1.98e-118

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: 339.93  E-value: 1.98e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFLEQKsagtPNFTYEVIVVSDGSQDATVSVALGYSKKHGAEkVRVLELIENRGKGGAVR 149
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEER----PSFSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 150 MGMLSARGRNLLFADADGATKFPDYDKLEVALKQlapewRDDGIAIGSRAHLENDAIATRSFFRTILMHGFHFLVWLFAV 229
Cdd:cd04188  76 AGMLAARGDYILFADADLATPFEELEKLEEALKT-----SGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582769 230 RSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAENLKLPMSEVAVRWTEIDGSK 290
Cdd:cd04188 151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 36-325 1.17e-115

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 337.51  E-value: 1.17e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   36 NIKRHKDEETFLDPHTIKTVTFPSLEDSPS-LELSVIVPAYNEEQRLPSMLDECLAFLEQKSAGTPNFTYEVIVVSDGSQ 114
Cdd:PTZ00260  39 VIRQVKSSVIHEKSKEVDKENYINNILKDSdVDLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  115 DATVSVALGYSKKHGAEKV--RVLELIENRGKGGAVRMGMLSARGRNLLFADADGATKFPDYDKLEVALKQLapEWRDDG 192
Cdd:PTZ00260 119 DKTLKVAKDFWRQNINPNIdiRLLSLLRNKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKI--EQNGLG 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  193 IAIGSRAHL-ENDAIATRSFFRTILMHGFHFLVWLFAVRSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAEN 271
Cdd:PTZ00260 197 IVFGSRNHLvDSDVVAKRKWYRNILMYGFHFIVNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQK 276

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24582769  272 LKLPMSEVAVRWTEIDGSKLTPFWSWLQMGRDLFMIWVRYLVGAWRIASIQKKE 325
Cdd:PTZ00260 277 LNLPIAEVPVNWTEVEGSKLNVISASIQMARDILLVRSFYLLGIWKVKDPSLLG 330
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 70-269 1.51e-57

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: 183.93  E-value: 1.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFLEQksagtpNFTYEVIVVSDGSQDATVSVALGYSKKHGaeKVRVLELIENRGKGGAVR 149
Cdd:cd04179   1 VVIPAYNEEENIPELVERLLAVLEE------GYDYEIIVVDDGSTDGTAEIARELAARVP--RVRVIRLSRNFGKGAAVR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 150 MGMLSARGRNLLFADADGATKFPDYDKLevalkqLAPEWRDDG-IAIGSRAHLENDAiaTRSFFRTILMHGFHFLVWLFA 228
Cdd:cd04179  73 AGFKAARGDIVVTMDADLQHPPEDIPKL------LEKLLEGGAdVVIGSRFVRGGGA--GMPLLRRLGSRLFNFLIRLLL 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24582769 229 VRSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLA 269
Cdd:cd04179 145 GVRISDTQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 68-289 3.51e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 3.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  68 LSVIVPAYNEEQRLPSMLDECLAFLeqksagtpNFTYEVIVVSDGSQDATVSVALGYSKKHgaEKVRVLELIENRGKGGA 147
Cdd:COG0463   4 VSVVIPTYNEEEYLEEALESLLAQT--------YPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 148 VRMGMLSARGRNLLFADADGatkFPDYDKLEVALKQLAPEwrDDGIAIGSRAHLENDaiatrSFFRTILMHGFHFLVWLF 227
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEG--PADLVYGSRLIREGE-----SDLRRLGSRLFNLVRLLT 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582769 228 avrSIRDTQCGFKLFTRTTARKLFTSlhvERWAFDVELLYLAENlKLPMSEVAVRWTEIDGS 289
Cdd:COG0463 144 ---NLPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALRH-GFRIAEVPVRYRAGESK 198
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 70-318 6.55e-25

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: 99.92  E-value: 6.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFLEqksagtpNFTYEVIVVSDGSQDATVSVALGYSKKHGaeKVRVLELIENRGKGGAVR 149
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALK-------GIDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 150 MGMLSARGRNLLFADADGATKfPDYdklevaLKQLAPEWRDDG--IAIGSRaHLENDAIATRSFFRTILMHGFHFLVWLF 227
Cdd:cd06442  72 EGFKAARGDVIVVMDADLSHP-PEY------IPELLEAQLEGGadLVIGSR-YVEGGGVEGWGLKRKLISRGANLLARLL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 228 AVRSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAENLKLPMSEVAVRWTE-IDG-SKLTpfwswlqmgrdlF 305
Cdd:cd06442 144 LGRKVSDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDrEHGeSKLG------------G 211

                       250
                ....*....|...
gi 24582769 306 MIWVRYLVGAWRI 318
Cdd:cd06442 212 KEIVEYLKGLLRL 224
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 69-244 5.90e-23

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: 93.23  E-value: 5.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769    69 SVIVPAYNEEQRLPSMLDECLAFLEQKsagtpnftYEVIVVSDGSQDATVSVALGYSKKHGaeKVRVLELIENRGKGGAV 148
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN--------FEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPENRGKAGAR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   149 RMGMLSARGRNLLFADADGatkFPDYDKLEVALKQLapEWRDDGIAIGSRAHLENDAIATRSFFRTILMHGFHFLVWLFA 228
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADD---EVPPDWLEKLVEAL--EEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145

                         170
                  ....*....|....*.
gi 24582769   229 VRSIRDTQCGFKLFTR 244
Cdd:pfam00535 146 GLNLPFLIGGFALYRR 161
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 70-242 4.84e-19

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 82.55  E-value: 4.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDeclAFLEQksaGTPNFtyEVIVVSDGSQDATVSVALGYSKKHgaEKVRVLELIENRGKGGAVR 149
Cdd:cd00761   1 VIIPAYNEEPYLERCLE---SLLAQ---TYPNF--EVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARN 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 150 MGMLSARGRNLLFADADGatkFPDYDKLEVALKQLapEWRDDGIAIGSRAHLendaIATRSFFRTILMHGFHFLVWLFAV 229
Cdd:cd00761  71 AGLKAARGEYILFLDADD---LLLPDWLERLVAEL--LADPEADAVGGPGNL----LFRRELLEEIGGFDEALLSGEEDD 141

                       170
                ....*....|...
gi 24582769 230 RSIRDTQCGFKLF 242
Cdd:cd00761 142 DFLLRLLRGGKVA 154
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 55-196 2.58e-17

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: 80.94  E-value: 2.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  55 VTFPSLEDSPSLELSVIVPAYNEEQRLPSMLDeclAFLEQKsagTPNFTYEVIVVSDGSQDATVSVALGYSKKHGaeKVR 134
Cdd:COG1215  18 LARRRRAPADLPRVSVIIPAYNEEAVIEETLR---SLLAQD---YPKEKLEVIVVDDGSTDETAEIARELAAEYP--RVR 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582769 135 VLELIENRGKGGAVRMGMLSARGRNLLFADADgaTKFPDYdklevALKQLAPEWRDDGIAIG 196
Cdd:COG1215  90 VIERPENGGKAAALNAGLKAARGDIVVFLDAD--TVLDPD-----WLRRLVAAFADPGVGAS 144
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 70-244 3.40e-16

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: 75.21  E-value: 3.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFLEQksagtPNFTYEVIVVSDGSQDATVSVALGYSKKHgaEKVRVLELIENRGKGGAVR 149
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAVLES-----LGYDYEIIFVDDGSTDRTLEILRELAARD--PRVKVIRLSRNFGQQAALL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769 150 MGMLSARGRNLLFADADGAtkfpdyDKLEVaLKQLAPEWRDD-GIAIGSRahlendaiATR--SFFRTILMHGFHFLVWL 226
Cdd:cd04187  74 AGLDHARGDAVITMDADLQ------DPPEL-IPEMLAKWEEGyDVVYGVR--------KNRkeSWLKRLTSKLFYRLINK 138

                       170
                ....*....|....*...
gi 24582769 227 FAVRSIRDTQCGFKLFTR 244
Cdd:cd04187 139 LSGVDIPDNGGDFRLMDR 156
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 70-203 4.30e-16

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: 74.96  E-value: 4.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQrlpsMLDECL-AFLEQKSagtPNftYEVIVVSDGSQDATVSVALGYSKKHGAEKVRVLELiENRGKGGAV 148
Cdd:cd06423   1 IIVPAYNEEA----VIERTIeSLLALDY---PK--LEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDK-ENGGKAGAL 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582769 149 RMGMLSARGRNLLFADADGatkFPDYDklevALKQLAPEWRDDG--IAIGSRAHLEN 203
Cdd:cd06423  71 NAGLRHAKGDIVVVLDADT---ILEPD----ALKRLVVPFFADPkvGAVQGRVRVRN 120
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 57-166 7.59e-16

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: 75.70  E-value: 7.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  57 FPSLEDSPSL-ELSVIVPAYNEEQRLPSMLDECLAfLEQksagtPNFTYEVIVVSDGSQDATVSVALGYSKKhgaeKVRV 135
Cdd:cd06439  19 PPSLPDPAYLpTVTIIIPAYNEEAVIEAKLENLLA-LDY-----PRDRLEIIVVSDGSTDGTAEIAREYADK----GVKL 88

                        90       100       110
                ....*....|....*....|....*....|.
gi 24582769 136 LELIENRGKGGAVRMGMLSARGRNLLFADAD 166
Cdd:cd06439  89 LRFPERRGKAAALNRALALATGEIVVFTDAN 119
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
68-166 9.24e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 66.17  E-value: 9.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  68 LSVIVPAYNEeqrlPSMLDECLAFLEQKSAGTpnftYEVIVVSDGSQDATVSVAlgysKKHGAEKVRVLELIENRGKGGA 147
Cdd:COG1216   5 VSVVIPTYNR----PELLRRCLESLLAQTYPP----FEVIVVDNGSTDGTAELL----AALAFPRVRVIRNPENLGFAAA 72

                        90
                ....*....|....*....
gi 24582769 148 VRMGMLSARGRNLLFADAD 166
Cdd:COG1216  73 RNLGLRAAGGDYLLFLDDD 91
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 62-183 2.60e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.53  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   62 DSPSLELSVIVPAYNEEQRLPsmldeclAFLEQKSAGTPNfTYEVIVVSDGSQDATVSVALGYSKKHGaeKVRVLELiEN 141
Cdd:PRK10073   2 MNSTPKLSIIIPLYNAGKDFR-------AFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYP--HVRLLHQ-AN 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24582769  142 RGKGGAVRMGMLSARGRNLLFADADGATKFPDYDKL-EVALKQ 183
Cdd:PRK10073  71 AGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLmTMALED 113
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 68-189 5.58e-11

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: 61.37  E-value: 5.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769    68 LSVIVPAYNEEQRLPSMLDECLAFLEqksagtpnfTYEVIVVSDGSQDATVSVAlgysKKHGAeKVrvleLIENRGKGGA 147
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRG---------DAEVIVVDGGSTDGTVEIA----RSLGA-KV----IHSPKGRARQ 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 24582769   148 VRMGMLSARGRNLLFADADgaTKFPDyDKLEVALKQLAPEWR 189
Cdd:TIGR04283  63 MNAGAALAKGDILLFLHAD--TRLPK-DFLEAIRRALAKPGY 101
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 69-167 6.03e-10

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


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 58.78  E-value: 6.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  69 SVIVPAYNEEQRLPSMLDeclAFLEQksaGTPNFTYEVIVVSDGSQDATVSVALGYSKKHgaEKVRvleLIENRGK--GG 146
Cdd:cd02525   3 SIIIPVRNEEKYIEELLE---SLLNQ---SYPKDLIEIIVVDGGSTDGTREIVQEYAAKD--PRIR---LIDNPKRiqSA 71

                        90       100
                ....*....|....*....|.
gi 24582769 147 AVRMGMLSARGRNLLFADADG 167
Cdd:cd02525  72 GLNIGIRNSRGDIIIRVDAHA 92
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 68-166 7.52e-10

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: 58.15  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769    68 LSVIVPAYNEEQRLPSMLDECLAfleqksagTPNFTYEVIVVSDGSQDATVSVALGYSKKHGAEKVRVLELIENRGKGGA 147
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILA--------QPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGK 75

                          90       100
                  ....*....|....*....|..
gi 24582769   148 VRM--GMLSA-RGRNLLFADAD 166
Cdd:pfam13641  76 SRGlnHGFRAvKSDLVVLHDDD 97
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 68-173 7.91e-10

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: 57.97  E-value: 7.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  68 LSVIVPAYNEEQRLPSmldeCLAFLEQKSAGTPnftyEVIVVSDGSQDATVSVAlgysKKHGaekVRVLEliENRGKGGA 147
Cdd:cd02522   1 LSIIIPTLNEAENLPR----LLASLRRLNPLPL----EIIVVDGGSTDGTVAIA----RSAG---VVVIS--SPKGRARQ 63

                        90       100
                ....*....|....*....|....*.
gi 24582769 148 VRMGMLSARGRNLLFADADgaTKFPD 173
Cdd:cd02522  64 MNAGAAAARGDWLLFLHAD--TRLPP 87
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 67-279 6.98e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 55.47  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   67 ELSVIVPAYNEEQRLPsmldeCLAFLEQKSAGTPNfTYEVIVVSDGSQDATVSVALGYSKKHGAEKVRVLELIENRGKGG 146
Cdd:PLN02726  10 KYSIIVPTYNERLNIA-----LIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  147 AVRMGMLSARGRNLLFADADgATKFPDYDKlEVALKQLApewRDDGIAIGSRaHLENDAIATRSFFRTILMHG----FHF 222
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDAD-LSHHPKYLP-SFIKKQRE---TGADIVTGTR-YVKGGGVHGWDLRRKLTSRGanvlAQT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582769  223 LVWlfavRSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAENLKLPMSEV 279
Cdd:PLN02726 158 LLW----PGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEV 210
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 70-166 5.17e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 52.68  E-value: 5.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLD--ECLAFleqksagtPNFTYEVIVVSDGSQDATVSVaLGYSKKHGAEKVRVLELIE--NRGKG 145
Cdd:cd04192   1 VVIAARNEAENLPRLLQslSALDY--------PKEKFEVILVDDHSTDGTVQI-LEFAAAKPNFQLKILNNSRvsISGKK 71

                        90       100
                ....*....|....*....|.
gi 24582769 146 GAVRMGMLSARGRNLLFADAD 166
Cdd:cd04192  72 NALTTAIKAAKGDWIVTTDAD 92
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 67-166 1.04e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 49.73  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   67 ELSVIVPAYNEEQRLPSMLDECLAFLEQKSAgtpnfTYEVIVVSDGSQDATVSVALGYSKKHGAEKVRVLeLIENRGKGG 146
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGK-----EYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAIL-LNRNYGQHS 80

                         90       100
                 ....*....|....*....|
gi 24582769  147 AVRMGMLSARGRNLLFADAD 166
Cdd:PRK10714  81 AIMAGFSHVTGDLIITLDAD 100
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 70-166 6.42e-06

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 46.30  E-value: 6.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQrlpsMLDECL-AFLEQKSAGtpnfTYEVIVVSDGSQDATVSVALGYSKKhgAEKVRVLELIEN------R 142
Cdd:cd06913   1 IILPVHNGEQ----WLDECLeSVLQQDFEG----TLELSVFNDASTDKSAEIIEKWRKK--LEDSGVIVLVGShnspspK 70

                        90       100
                ....*....|....*....|....
gi 24582769 143 GKGGAVRMGMLSARGRNLLFADAD 166
Cdd:cd06913  71 GVGYAKNQAIAQSSGRYLCFLDSD 94
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 70-199 6.85e-06

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 45.63  E-value: 6.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEeqrlPSMLDECLAFLEQKSagtpNFTYEVIVVSDGSQDATVSVALGYSKkhgaeKVRVLELIENRGKGGAVR 149
Cdd:cd04186   1 IIIVNYNS----LEYLKACLDSLLAQT----YPDFEVIVVDNASTDGSVELLRELFP-----EVRLIRNGENLGFGAGNN 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24582769 150 MGMLSARGRNLLFADADGATKFPDYDKLEVALKQlapewrDDGIAI-GSRA 199
Cdd:cd04186  68 QGIREAKGDYVLLLNPDTVVEPGALLELLDAAEQ------DPDVGIvGPKV 112
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 68-166 8.12e-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: 8.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  68 LSVIVPAYNEEQRLPsmldECLAFLEqksagtpNFTYEVIVVSDGSQDATVSVAlgysKKHGAekvRVLElIENRGKGGA 147
Cdd:cd02511   2 LSVVIITKNEERNIE----RCLESVK-------WAVDEIIVVDSGSTDRTVEIA----KEYGA---KVYQ-RWWDGFGAQ 62

                        90
                ....*....|....*....
gi 24582769 148 VRMGMLSARGRNLLFADAD 166
Cdd:cd02511  63 RNFALELATNDWVLSLDAD 81
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 69-166 2.99e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 44.91  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769   69 SVIVPAYNEEQRLPSMLDECLAFLeqksaGTPNFTyEVIVVSDGSQDATVSVAlgysKKHGAEKVR---VLELIENR-GK 144
Cdd:PRK13915  34 SVVLPALNEEETVGKVVDSIRPLL-----MEPLVD-ELIVIDSGSTDATAERA----AAAGARVVSreeILPELPPRpGK 103

                         90       100
                 ....*....|....*....|..
gi 24582769  145 GGAVRMGMLSARGRNLLFADAD 166
Cdd:PRK13915 104 GEALWRSLAATTGDIVVFVDAD 125
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 67-166 7.62e-05

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: 43.40  E-value: 7.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  67 ELSVIVPAYNEEqrlPSMLDECLaflEQKSAGTPnftYEVIVVSDGSQDATVSvALGYSKKHGaeKVRVLeLIENRGKGG 146
Cdd:cd06434   1 DVTVIIPVYDED---PDVFRECL---RSILRQKP---LEIIVVTDGDDEPYLS-ILSQTVKYG--GIFVI-TVPHPGKRR 67

                        90       100
                ....*....|....*....|
gi 24582769 147 AVRMGMLSARGRNLLFADAD 166
Cdd:cd06434  68 ALAEGIRHVTTDIVVLLDSD 87
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 69-213 9.03e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 43.00  E-value: 9.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  69 SVIVPAYNEEQRLPSMLDEclaFLEQKsagTPNFtyEVIVVSDGSQDATVSVALGYSKKHGaekvRVLELIENRGKGGAV 148
Cdd:cd04196   1 AVLMATYNGEKYLREQLDS---ILAQT---YKND--ELIISDDGSTDGTVEIIKEYIDKDP----FIIILIRNGKNLGVA 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582769 149 R---MGMLSARGRNLLFADADgatkfpDY---DKLEVALKQLApewRDDGIA-IGSRAHL--ENDAIATRSFFR 213
Cdd:cd04196  69 RnfeSLLQAADGDYVFFCDQD------DIwlpDKLERLLKAFL---KDDKPLlVYSDLELvdENGNPIGESFFE 133
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 70-167 3.65e-04

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 40.83  E-value: 3.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFleqksagTPNFTyeVIVVSDGSQDATVSVAlgySKKHGAEKVRVL--ELIENR-GKGG 146
Cdd:cd06436   1 VLVPCLNEEAVIQRTLASLLRN-------KPNFL--VLVIDDASDDDTAGIV---RLAITDSRVHLLrrHLPNARtGKGD 68

                        90       100       110
                ....*....|....*....|....*....|..
gi 24582769 147 AVRMG------MLSARGRNL---LFA--DADG 167
Cdd:cd06436  69 ALNAAydqirqILIEEGADPervIIAviDADG 100
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 69-165 7.22e-04

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: 40.65  E-value: 7.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  69 SVIVPAYNEEqrlPSMLDECLAFLEQKSAgtPNFTYEVIVVSDGSQDATVSVALGYSKKHGAEKVRVLELIENRGKGGAv 148
Cdd:cd02510   1 SVIIIFHNEA---LSTLLRTVHSVINRTP--PELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRA- 74

                        90
                ....*....|....*...
gi 24582769 149 RM-GMLSARGRNLLFADA 165
Cdd:cd02510  75 RIaGARAATGDVLVFLDS 92
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 69-128 2.87e-03

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: 38.30  E-value: 2.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582769  69 SVIVPAYNEEQRLPsmldECLA-FLEQKsagTPNFtyEVIVVSDGSQDATVSVALGYSKKH 128
Cdd:cd06433   1 SIITPTYNQAETLE----ETIDsVLSQT---YPNI--EYIVIDGGSTDGTVDIIKKYEDKI 52
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 70-152 3.63e-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: 37.97  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582769  70 VIVPAYNEEQRLPSMLDECLAFLeqksagTPNFTYEVIVVSDGSQDATVSVALGyskkHGAEkvrVLELI--ENRGKGGA 147
Cdd:cd06438   1 ILIPAHNEEAVIGNTVRSLKAQD------YPRELYRIFVVADNCTDDTAQVARA----AGAT---VLERHdpERRGKGYA 67


                ....*
gi 24582769 148 VRMGM 152
Cdd:cd06438  68 LDFGF 72
 
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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