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Conserved domains on  [gi|947264866|gb|ALM48404|]
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glycosyl transferase family 2 [Flavobacterium psychrophilum]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135621)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  12691742|9445404|16037492|10521532
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-187 9.05e-79

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: 237.76  E-value: 9.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELHQWIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKAQ 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  85 GDVIITMDADLQDSPDEIPGLYAMItGENYDLVSGWKKKRYDSVVaKNLPSKLFNWAARKTSGVKLNDFNCGLKAYKNVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKW-EEGYDVVYGVRKNRKESWL-KRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKV 158

                        170       180
                 ....*....|....*....|...
gi 947264866 165 VKNIEVSGEMHRYIPVLAKNSGF 187
Cdd:cd04187  159 VDALLLLPERHRFLRGLIAWVGF 181
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-187 9.05e-79

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: 237.76  E-value: 9.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELHQWIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKAQ 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  85 GDVIITMDADLQDSPDEIPGLYAMItGENYDLVSGWKKKRYDSVVaKNLPSKLFNWAARKTSGVKLNDFNCGLKAYKNVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKW-EEGYDVVYGVRKNRKESWL-KRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKV 158

                        170       180
                 ....*....|....*....|...
gi 947264866 165 VKNIEVSGEMHRYIPVLAKNSGF 187
Cdd:cd04187  159 VDALLLLPERHRFLRGLIAWVGF 181
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-216 4.39e-51

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 167.96  E-value: 4.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   1 MNISIVIPLLNEEESLKELHQWIVKVMAENnfsYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGF 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD---FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  81 AKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSVVAKNLPSKLFNWAARKTsgvKLNDFNCGLKAY 160
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLT---NLPDSTSGFRLF 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 947264866 161 KNVVVKNIEVSGEMHRYIPVLAKNSGFAKIGEKVVIHQArkyGSTKFGMERFVNGF 216
Cdd:COG0463  156 RREVLEELGFDEGFLEDTELLRALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-316 4.06e-49

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 166.45  E-value: 4.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   2 NISIVIPLLNEEESLKELHQWIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQlAAQNPN--IKGIRFQRNYGKSQALHAG 79
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPDshIVAILLNRNYGQHSAIMAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  80 FAKAQGDVIITMDADLQDSPDEIPGLYAmITGENYDLVSGWKKKRYDSVVAKnLPSKLFNWAARKTSGVKLNDFNCGLKA 159
Cdd:PRK10714  86 FSHVTGDLIITLDADLQNPPEEIPRLVA-KADEGYDVVGTVRQNRQDSWFRK-TASKMINRLIQRTTGKAMGDYGCMLRA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866 160 YKNVVVKNIEVSGEMHRYIPVLAkNSGFAKIGEKVVIHQARKYGSTKFGMERFVNGFLDLITIwflsrFGKRPMHLFGAL 239
Cdd:PRK10714 164 YRRHIVDAMLHCHERSTFIPILA-NTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTC-----LTTTPLRLLSLL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866 240 GALMFFIGFGASIYIGAVKLYRLAQHQStilitDNPWFYIALTTMIIGTQLFLAGFLGEIILRTKNN---EERYKISEIL 316
Cdd:PRK10714 238 GSIIAIGGFSLAVLLVVLRLTFGPQWAA-----EGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDvraRPRYFVQQVV 312
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-140 7.68e-32

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: 116.73  E-value: 7.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866    4 SIVIPLLNEEESLKELhqwIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLET---LESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 947264866   84 QGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSVVAKNLPSKLFNW 140
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLS 134
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-94 2.36e-09

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: 56.37  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866    3 ISIVIPLLNEEESLKE----LHQWIVKVmaennfsyEVIFIDDGSTDNSWNTIEQLAAqnpniKGIRFQRnyGKSQALHA 78
Cdd:TIGR04283   1 LSIIIPVLNEAATLPElladLQALRGDA--------EVIVVDGGSTDGTVEIARSLGA-----KVIHSPK--GRARQMNA 65

                          90
                  ....*....|....*.
gi 947264866   79 GFAKAQGDVIITMDAD 94
Cdd:TIGR04283  66 GAALAKGDILLFLHAD 81
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-187 9.05e-79

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: 237.76  E-value: 9.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELHQWIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKAQ 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  85 GDVIITMDADLQDSPDEIPGLYAMItGENYDLVSGWKKKRYDSVVaKNLPSKLFNWAARKTSGVKLNDFNCGLKAYKNVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKW-EEGYDVVYGVRKNRKESWL-KRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKV 158

                        170       180
                 ....*....|....*....|...
gi 947264866 165 VKNIEVSGEMHRYIPVLAKNSGF 187
Cdd:cd04187  159 VDALLLLPERHRFLRGLIAWVGF 181
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 5-181 3.19e-62

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: 195.48  E-value: 3.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELHQWIVKVMAENnFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKAQ 84
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEG-YDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  85 GDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSV---VAKNLPSKLFNWAARKTSGVKLNDFNCGLKAYK 161
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAgmpLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159

                        170       180
                 ....*....|....*....|
gi 947264866 162 NVVVKNIEVSGEMHRYIPVL 181
Cdd:cd04179  160 REVLEALLSLLESNGFEFGL 179
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-216 4.39e-51

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 167.96  E-value: 4.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   1 MNISIVIPLLNEEESLKELHQWIVKVMAENnfsYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGF 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD---FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  81 AKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSVVAKNLPSKLFNWAARKTsgvKLNDFNCGLKAY 160
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLT---NLPDSTSGFRLF 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 947264866 161 KNVVVKNIEVSGEMHRYIPVLAKNSGFAKIGEKVVIHQArkyGSTKFGMERFVNGF 216
Cdd:COG0463  156 RREVLEELGFDEGFLEDTELLRALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-316 4.06e-49

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 166.45  E-value: 4.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   2 NISIVIPLLNEEESLKELHQWIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQlAAQNPN--IKGIRFQRNYGKSQALHAG 79
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPDshIVAILLNRNYGQHSAIMAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  80 FAKAQGDVIITMDADLQDSPDEIPGLYAmITGENYDLVSGWKKKRYDSVVAKnLPSKLFNWAARKTSGVKLNDFNCGLKA 159
Cdd:PRK10714  86 FSHVTGDLIITLDADLQNPPEEIPRLVA-KADEGYDVVGTVRQNRQDSWFRK-TASKMINRLIQRTTGKAMGDYGCMLRA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866 160 YKNVVVKNIEVSGEMHRYIPVLAkNSGFAKIGEKVVIHQARKYGSTKFGMERFVNGFLDLITIwflsrFGKRPMHLFGAL 239
Cdd:PRK10714 164 YRRHIVDAMLHCHERSTFIPILA-NTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTC-----LTTTPLRLLSLL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866 240 GALMFFIGFGASIYIGAVKLYRLAQHQStilitDNPWFYIALTTMIIGTQLFLAGFLGEIILRTKNN---EERYKISEIL 316
Cdd:PRK10714 238 GSIIAIGGFSLAVLLVVLRLTFGPQWAA-----EGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDvraRPRYFVQQVV 312
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-140 7.68e-32

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: 116.73  E-value: 7.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866    4 SIVIPLLNEEESLKELhqwIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLET---LESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 947264866   84 QGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSVVAKNLPSKLFNW 140
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLS 134
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 5-222 1.63e-31

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: 117.25  E-value: 1.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELHQWIVKVMAENNfsYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKAQ 84
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGID--YEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  85 GDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGwkkKRY-DSVVAKNLP------SKLFNWAARKTSGVKLNDFNCGL 157
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIG---SRYvEGGGVEGWGlkrkliSRGANLLARLLLGRKVSDPTSGF 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866 158 KAYKNVVVKNIEVSGEMHRY-----IPVLAKNSGFaKIGEKVVIHQARKYGSTKFGMERFVNGFLDLITI 222
Cdd:cd06442  156 RAYRREVLEKLIDSLVSKGYkfqleLLVRARRLGY-RIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-168 1.09e-27

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: 106.88  E-value: 1.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEE----SLKELHQWIVKVMAennFSYEVIFIDDGSTDNSWNTIEQLAAQNP-NIKGIRFQRNYGKSQALHAG 79
Cdd:cd04188    1 VVIPAYNEEKrlppTLEEAVEYLEERPS---FSYEIIVVDDGSKDGTAEVARKLARKNPaLIRVLTLPKNRGKGGAVRAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  80 FAKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSVVAK-----NLPSKLFNWAARKTSGVKLNDFN 154
Cdd:cd04188   78 MLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASAAVVKrswlrNLLGRGFNFLVRLLLGLGIKDTQ 157

                        170
                 ....*....|....
gi 947264866 155 CGLKAYKNVVVKNI 168
Cdd:cd04188  158 CGFKLFTRDAARRL 171
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-282 1.74e-20

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 89.42  E-value: 1.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLNEEESLKELhqwIVKVMAEN--NFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGF 80
Cdd:COG1215   31 VSVIIPAYNEEAVIEET---LRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  81 AKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLV---SGWKKKRYDSVvaKNLPSKL------FNWAARKtsgvkln 151
Cdd:COG1215  108 KAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASganLAFRREALEEV--GGFDEDTlgedldLSLRLLR------- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866 152 dfncglKAYKNVVVKNIEVSGEMHRyipvlaknsgfakiGEKVVIHQARKYGSTKFGMERFVNGFLDLITIWFLSRFGKR 231
Cdd:COG1215  179 ------AGYRIVYVPDAVVYEEAPE--------------TLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 947264866 232 PMHLFGALGALMFFIGFGASIYIGAVKLYRlaqHQSTILITDNPWFYIALT 282
Cdd:COG1215  239 PLLLLLLLLALLALLLLLLPALLLALLLAL---RRRRLLLPLLHLLYGLLL 286
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 5-120 4.43e-18

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: 79.47  E-value: 4.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELhqwIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKAQ 84
Cdd:cd00761    1 VIIPAYNEEPYLERC---LESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 947264866  85 GDVIITMDADLQDSPDEIP-GLYAMITGENYDLVSGW 120
Cdd:cd00761   78 GEYILFLDADDLLLPDWLErLVAELLADPEADAVGGP 114
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-213 3.77e-16

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 76.27  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   1 MNISIVIPLLNEEESLKELHQWIVKVMAENNfSYEVIFIDDGSTDNSWNTIEQLAA--QNPNIKGIRFQRNYGKSQALHA 78
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKvyGEDRILLRPRPGKLGLGTAYIH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  79 GFAKAQGDVIITMDADLQDSPDEIPGLYA--------MITGENYDL---VSGWKKKRydsvvakNLPSKLFNWAARKTSG 147
Cdd:PLN02726  88 GLKHASGDFVVIMDADLSHHPKYLPSFIKkqretgadIVTGTRYVKgggVHGWDLRR-------KLTSRGANVLAQTLLW 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 947264866 148 VKLNDFNCGLKAYKNVVVKNIEVSGEMHRY-----IPVLAKNSGFaKIGEKVVIHQARKYGSTKFGMERFV 213
Cdd:PLN02726 161 PGVSDLTGSFRLYKRSALEDLVSSVVSKGYvfqmeIIVRASRKGY-RIEEVPITFVDRVYGESKLGGSEIV 230
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-106 2.04e-15

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 75.47  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLNEEESLKelhQWIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRfQRNYGKSQALHAGFAK 82
Cdd:PRK10073   8 LSIIIPLYNAGKDFR---AFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAV 83

                         90       100
                 ....*....|....*....|....*
gi 947264866  83 AQGDVIITMDADlqdspDEI-PGLY 106
Cdd:PRK10073  84 ATGKYVAFPDAD-----DVVyPTMY 103
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 3-133 4.38e-15

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: 73.42  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLNEEESLKELhqwIVKVMAE--NNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIrfqRNYGKSQ--ALHA 78
Cdd:cd02525    2 VSIIIPVRNEEKYIEEL---LESLLNQsyPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLI---DNPKRIQsaGLNI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 947264866  79 GFAKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSVVAKNL 133
Cdd:cd02525   76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAI 130
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-100 3.42e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 70.02  E-value: 3.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   1 MNISIVIPLLNEEESLKELhqwIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLaaQNPNIKGIRFQRNYGKSQALHAGF 80
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRC---LESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGL 77

                         90       100
                 ....*....|....*....|
gi 947264866  81 AKAQGDVIITMDADLQDSPD 100
Cdd:COG1216   78 RAAGGDYLLFLDDDTVVEPD 97
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-119 5.46e-14

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: 70.01  E-value: 5.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELHQWIVKvMAENNFSYEVIFIDDGSTDNSWNTIEQLAA-QNPNIKGIRFQR--NYGKSQALHAGFA 81
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSA-LDYPKEKFEVILVDDHSTDGTVQILEFAAAkPNFQLKILNNSRvsISGKKNALTTAIK 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 947264866  82 KAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSG 119
Cdd:cd04192   80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAG 117
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 5-94 1.89e-12

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: 64.56  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELHQWIVKVMAENnfsYEVIFIDDGSTDNSWNTIEQLAA-QNPNIKGIRFQRNYGKSQALHAGFAKA 83
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPK---LEVIVVDDGSTDDTLEILEELAAlYIRRVLVVRDKENGGKAGALNAGLRHA 77

                         90
                 ....*....|.
gi 947264866  84 QGDVIITMDAD 94
Cdd:cd06423   78 KGDIVVVLDAD 88
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 3-158 7.10e-12

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 65.17  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLNEEE----SLKELHQWI-VKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQ----NPNIKGIRFQRNYGKS 73
Cdd:PTZ00260  72 LSIVIPAYNEEDrlpkMLKETIKYLeSRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQninpNIDIRLLSLLRNKGKG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  74 QALHAGFAKAQGDVIITMDADLQDSPDEIPGLYAM---ITGENYDLVSGWKKKRYDS-VVAK-----NLPSKLFNWAARK 144
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDADGATDIDDFDKLEDImlkIEQNGLGIVFGSRNHLVDSdVVAKrkwyrNILMYGFHFIVNT 231

                        170
                 ....*....|....
gi 947264866 145 TSGVKLNDFNCGLK 158
Cdd:PTZ00260 232 ICGTNLKDTQCGFK 245
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-94 2.36e-09

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: 56.37  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866    3 ISIVIPLLNEEESLKE----LHQWIVKVmaennfsyEVIFIDDGSTDNSWNTIEQLAAqnpniKGIRFQRnyGKSQALHA 78
Cdd:TIGR04283   1 LSIIIPVLNEAATLPElladLQALRGDA--------EVIVVDGGSTDGTVEIARSLGA-----KVIHSPK--GRARQMNA 65

                          90
                  ....*....|....*.
gi 947264866   79 GFAKAQGDVIITMDAD 94
Cdd:TIGR04283  66 GAALAKGDILLFLHAD 81
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-119 1.63e-08

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: 54.51  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLNEEeslkelhqwivKVMAE--NNFS--------YEVIFIDDGSTDNSWNTIEQLAAQNpnIKGIRFQRNYGK 72
Cdd:cd06439   31 VTIIIPAYNEE-----------AVIEAklENLLaldyprdrLEIIVVSDGSTDGTAEIAREYADKG--VKLLRFPERRGK 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 947264866  73 SQALHAGFAKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSG 119
Cdd:cd06439   98 AAALNRALALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSG 144
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-119 3.10e-08

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 54.15  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   1 MNISIVIPLLNEEESLKElhqwIVKVMAE---NNFSYEVIFIDDGSTDNswnTIEQLAAQN----------PNIKGIRfq 67
Cdd:PRK13915  31 RTVSVVLPALNEEETVGK----VVDSIRPllmEPLVDELIVIDSGSTDA---TAERAAAAGarvvsreeilPELPPRP-- 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 947264866  68 rnyGKSQALHAGFAKAQGDVIITMDADLQD-SPDEIPGLYA-MITGENYDLVSG 119
Cdd:PRK13915 102 ---GKGEALWRSLAATTGDIVVFVDADLINfDPMFVPGLLGpLLTDPGVHLVKA 152
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 3-94 4.97e-08

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: 52.57  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLNEEESLKELhqwIVKVMAENNFSYEVIFIDDGSTDnswNTIEqlAAQNPNIKGIRFQRnyGKSQALHAGFAK 82
Cdd:cd02522    1 LSIIIPTLNEAENLPRL---LASLRRLNPLPLEIIVVDGGSTD---GTVA--IARSAGVVVISSPK--GRARQMNAGAAA 70

                         90
                 ....*....|..
gi 947264866  83 AQGDVIITMDAD 94
Cdd:cd02522   71 ARGDWLLFLHAD 82
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-94 6.85e-08

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: 51.82  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLN-EEESLKELhqwIVKVMAEnnfSY---EVIFIDDGSTDNSW-NTIEQLAAQNPNIKGIRFQRNYGKSQALH 77
Cdd:cd04184    3 ISIVMPVYNtPEKYLREA---IESVRAQ---TYpnwELCIADDASTDPEVkRVLKKYAAQDPRIKVVFREENGGISAATN 76

                         90
                 ....*....|....*..
gi 947264866  78 AGFAKAQGDVIITMDAD 94
Cdd:cd04184   77 SALELATGEFVALLDHD 93
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-107 2.39e-07

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 49.87  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKELhqwIVKVMAENNFSYEVIFIDDGSTDNSwntIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKAQ 84
Cdd:cd04186    1 IIIVNYNSLEYLKAC---LDSLLAQTYPDFEVIVVDNASTDGS---VELLRELFPEVRLIRNGENLGFGAGNNQGIREAK 74

                         90       100
                 ....*....|....*....|...
gi 947264866  85 GDVIITMDADLQDSPDEIPGLYA 107
Cdd:cd04186   75 GDYVLLLNPDTVVEPGALLELLD 97
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 2-125 6.90e-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: 46.51  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   2 NISIVIPLLNEE-------ESLKelhqWIVKvmaennfsyEVIFIDDGSTDnswNTIEqlAAQNPNIKGIRF-------Q 67
Cdd:cd02511    1 TLSVVIITKNEErnierclESVK----WAVD---------EIIVVDSGSTD---RTVE--IAKEYGAKVYQRwwdgfgaQ 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 947264866  68 RNYgksqalhaGFAKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRY 125
Cdd:cd02511   63 RNF--------ALELATNDWVLSLDADERLTPELADEILALLATDDYDGYYVPRRNFF 112
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-113 1.25e-05

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 46.12  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866    4 SIVIPLLNEEESlkelhQWIVKVMAENNFSY----EVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRF-QRNYGKSQALHA 78
Cdd:pfam10111   1 SVVIPVYNGEKT-----HWIQERILNQTFQYdpefELIIINDGSTDKTLEEVSSIKDHNLQVYYPNApDTTYSLAASRNR 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 947264866   79 GFAKAQGDVIITMDADLQDSPDEIPGLYAMITGEN 113
Cdd:pfam10111  76 GTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLA 110
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-129 1.40e-05

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: 45.44  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866    3 ISIVIPLLNEEESLKE-LHQwivkVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKG--IRFQRN---YGKSQAL 76
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRvLEA----ILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLrvIRNARLlgpTGKSRGL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 947264866   77 HAGFAKAQGDVIITMDADLQDSPDEIPGLYAMITGENYDLVSGWKKKRYDSVV 129
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTM 132
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 3-100 2.98e-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: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   3 ISIVIPLLNEEESLKELHQWIVKVmaennfSY-----EVIFIDDgSTDNSW----NTIEQLAAQNPNIKGI-RFQRNYGK 72
Cdd:cd06437    3 VTVQLPVFNEKYVVERLIEAACAL------DYpkdrlEIQVLDD-STDETVrlarEIVEEYAAQGVNIKHVrRADRTGYK 75

                         90       100
                 ....*....|....*....|....*...
gi 947264866  73 SQALHAGFAKAQGDVIITMDADLQDSPD 100
Cdd:cd06437   76 AGALAEGMKVAKGEYVAIFDADFVPPPD 103
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 26-102 3.91e-05

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: 43.72  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866  26 VMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNP-NIKGIRfQRNYG--KSQALHAGFAKAQGDVIITMDADLQDSPDEI 102
Cdd:cd06420   19 VLNQSILPFEVIIADDGSTEETKELIEEFKSQFPiPIKHVW-QEDEGfrKAKIRNKAIAAAKGDYLIFIDGDCIPHPDFI 97
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 4-93 2.94e-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: 41.81  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   4 SIVIPLLNEEES--LKELHQWIvkvmaenNFS-----YEVIFIDDGSTDNSWNT--IEQLAAQNPNIKGIRFQRNYGKSQ 74
Cdd:cd02510    1 SVIIIFHNEALStlLRTVHSVI-------NRTppellKEIILVDDFSDKPELKLllEEYYKKYLPKVKVLRLKKREGLIR 73

                         90
                 ....*....|....*....
gi 947264866  75 ALHAGFAKAQGDVIITMDA 93
Cdd:cd02510   74 ARIAGARAATGDVLVFLDS 92
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 4-120 4.46e-04

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


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 40.76  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   4 SIVIPLLNEEESLKeLHQWIVKVMAENNFSYEVIFIDDGSTDNSWNTIEQLAAQNPNIKGIRFQRNYGKSQALHAGFAKA 83
Cdd:cd04195    1 SVLMSVYIKEKPEF-LREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHC 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 947264866  84 QGDVIITMDADLQDSPDEIP-GLYAMITGENYDLVSGW 120
Cdd:cd04195   80 TYDWVARMDTDDISLPDRFEkQLDFIEKNPEIDIVGGG 117
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-94 7.88e-04

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: 39.84  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   4 SIVIPLLNEEESLKELHQWIvkvmAENNFS-YEVIFIDDGSTDnswNTIEQLAAQNPNI--------KGIrfqrnygkSQ 74
Cdd:cd06433    1 SIITPTYNQAETLEETIDSV----LSQTYPnIEYIVIDGGSTD---GTVDIIKKYEDKItywisepdKGI--------YD 65

                         90       100
                 ....*....|....*....|
gi 947264866  75 ALHAGFAKAQGDVIITMDAD 94
Cdd:cd06433   66 AMNKGIALATGDIIGFLNSD 85
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 5-99 8.61e-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: 39.67  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947264866   5 IVIPLLNEEESLKElhqwIVKVMAENNFSYEVIFIDDGSTDNSWNTIEqLAAQNPNIKGIRFQR---NYGKSQALHAGFA 81
Cdd:cd06436    1 VLVPCLNEEAVIQR----TLASLLRNKPNFLVLVIDDASDDDTAGIVR-LAITDSRVHLLRRHLpnaRTGKGDALNAAYD 75

                         90       100
                 ....*....|....*....|....*....
gi 947264866  82 ------KAQG----DVIIT-MDADLQDSP 99
Cdd:cd06436   76 qirqilIEEGadpeRVIIAvIDADGRLDP 104
 
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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