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Conserved domains on  [gi|1833197664|ref|WP_168694789|]
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glycosyltransferase family 2 protein [Dolichospermum flos-aquae]

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
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 ...
13-193 1.54e-77

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: 234.68  E-value: 1.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYAT 92
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  93 AKVIVTLDADLQNDPADIPMLLAKLEEGYDLVSGWRQNRQDGALnRLLPSKIANWLIRRATSVYIHDYGCSLKAYRSELV 172
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWL-KRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|.
gi 1833197664 173 ADMNLYGELHRFLPALAYIEG 193
Cdd:cd04187   160 DALLLLPERHRFLRGLIAWVG 180
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
13-193 1.54e-77

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: 234.68  E-value: 1.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYAT 92
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  93 AKVIVTLDADLQNDPADIPMLLAKLEEGYDLVSGWRQNRQDGALnRLLPSKIANWLIRRATSVYIHDYGCSLKAYRSELV 172
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWL-KRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|.
gi 1833197664 173 ADMNLYGELHRFLPALAYIEG 193
Cdd:cd04187   160 DALLLLPERHRFLRGLIAWVG 180
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
11-322 2.93e-73

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 228.85  E-value: 2.93e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVESLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQT-RTDLKAIILRRNYGQTAAMSAGFN 89
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIMAGFS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  90 YATAKVIVTLDADLQNDPADIPMLLAKLEEGYDLVSGWRQNRQDgALNRLLPSKIANWLIRRATSVYIHDYGCSLKAYRS 169
Cdd:PRK10714   88 HVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD-SWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664 170 ELVADMNLYGELHRFLPALAYIEGARITEVPVRHHARRFGKSKYGISRTFRVLMDLLTILfmkkfLTRPMHVFGLLGLIS 249
Cdd:PRK10714  167 HIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCL-----TTTPLRLLSLLGSII 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833197664 250 MVSGGGIGIYLTVIKLAFHVD-IGSRPLLILAVLLLVTGVQLFCFGLLAELLMRTYHESQGRPIYRVREVVAKN 322
Cdd:PRK10714  242 AIGGFSLAVLLVVLRLTFGPQwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPS 315
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
10-222 6.01e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 162.56  E-value: 6.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  10 DVSIVVPIKDEVESLPLLLEAIsttLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFN 89
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESL---LAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  90 YATAKVIVTLDADLQNDPADIPMLLAKLEE-GYDLVSGWRQNRQDGALNRLLPSKIANWlirRATSVYIHDYGCSLKAYR 168
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNL---VRLLTNLPDSTSGFRLFR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1833197664 169 SELVADMNL---YGELHRFLPALAYieGARITEVPVRHHArrfGKSKYGISRTFRVL 222
Cdd:COG0463   157 REVLEELGFdegFLEDTELLRALRH--GFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
12-174 2.65e-28

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: 107.48  E-value: 2.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  12 SIVVPIKDEvesLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYA 91
Cdd:pfam00535   1 SVIIPTYNE---EKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  92 TAKVIVTLDADLQNDPADIPMLLAKLEE-GYDLVSGWRQNRQDGALNRLLPSKIANW-----LIRRATSVYIHDYGCSLK 165
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRASRITLSrlpffLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 1833197664 166 AYRSELVAD 174
Cdd:pfam00535 158 LYRREALEE 166
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
13-193 1.54e-77

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: 234.68  E-value: 1.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYAT 92
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  93 AKVIVTLDADLQNDPADIPMLLAKLEEGYDLVSGWRQNRQDGALnRLLPSKIANWLIRRATSVYIHDYGCSLKAYRSELV 172
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWL-KRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|.
gi 1833197664 173 ADMNLYGELHRFLPALAYIEG 193
Cdd:cd04187   160 DALLLLPERHRFLRGLIAWVG 180
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
11-322 2.93e-73

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 228.85  E-value: 2.93e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVESLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQT-RTDLKAIILRRNYGQTAAMSAGFN 89
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIMAGFS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  90 YATAKVIVTLDADLQNDPADIPMLLAKLEEGYDLVSGWRQNRQDgALNRLLPSKIANWLIRRATSVYIHDYGCSLKAYRS 169
Cdd:PRK10714   88 HVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD-SWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664 170 ELVADMNLYGELHRFLPALAYIEGARITEVPVRHHARRFGKSKYGISRTFRVLMDLLTILfmkkfLTRPMHVFGLLGLIS 249
Cdd:PRK10714  167 HIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCL-----TTTPLRLLSLLGSII 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833197664 250 MVSGGGIGIYLTVIKLAFHVD-IGSRPLLILAVLLLVTGVQLFCFGLLAELLMRTYHESQGRPIYRVREVVAKN 322
Cdd:PRK10714  242 AIGGFSLAVLLVVLRLTFGPQwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPS 315
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
13-194 7.40e-60

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: 189.71  E-value: 7.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAISTTLtASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYAT 92
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVL-EEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  93 AKVIVTLDADLQNDPADIPMLLAKL-EEGYDLVSGWRQNRQDGA---LNRLLPSKIANWLIRRATSVYIHDYGCSLKAYR 168
Cdd:cd04179    80 GDIVVTMDADLQHPPEDIPKLLEKLlEGGADVVIGSRFVRGGGAgmpLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159
                         170       180
                  ....*....|....*....|....*.
gi 1833197664 169 SELVADMNLYGELHRFLPALAYIEGA 194
Cdd:cd04179   160 REVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
10-222 6.01e-49

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 162.56  E-value: 6.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  10 DVSIVVPIKDEVESLPLLLEAIsttLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFN 89
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESL---LAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  90 YATAKVIVTLDADLQNDPADIPMLLAKLEE-GYDLVSGWRQNRQDGALNRLLPSKIANWlirRATSVYIHDYGCSLKAYR 168
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNL---VRLLTNLPDSTSGFRLFR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1833197664 169 SELVADMNL---YGELHRFLPALAYieGARITEVPVRHHArrfGKSKYGISRTFRVL 222
Cdd:COG0463   157 REVLEELGFdegFLEDTELLRALRH--GFRIAEVPVRYRA---GESKLNLRDLLRLL 208
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
13-216 6.50e-36

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: 129.19  E-value: 6.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAISTTLtaSELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYAT 92
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAAL--KGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  93 AKVIVTLDADLQNDPADIP-MLLAKLEEGYDLVSGWRQ----NRQDGALNRLLPSKIANWLIRRATSVYIHDYGCSLKAY 167
Cdd:cd06442    79 GDVIVVMDADLSHPPEYIPeLLEAQLEGGADLVIGSRYveggGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFRAY 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1833197664 168 RSELVADMN--LYGELHRFLPAL---AYIEGARITEVPVRHHARRFGKSKYGIS 216
Cdd:cd06442   159 RREVLEKLIdsLVSKGYKFQLELlvrARRLGYRIVEVPITFVDREHGESKLGGK 212
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
12-174 2.65e-28

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: 107.48  E-value: 2.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  12 SIVVPIKDEvesLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYA 91
Cdd:pfam00535   1 SVIIPTYNE---EKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  92 TAKVIVTLDADLQNDPADIPMLLAKLEE-GYDLVSGWRQNRQDGALNRLLPSKIANW-----LIRRATSVYIHDYGCSLK 165
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRASRITLSrlpffLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 1833197664 166 AYRSELVAD 174
Cdd:pfam00535 158 LYRREALEE 166
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
13-202 5.75e-25

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: 99.95  E-value: 5.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLL-EAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAII-LRRNYGQTAAMSAGFNY 90
Cdd:cd04188     1 VVIPAYNEEKRLPPTLeEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLtLPKNRGKGGAVRAGMLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  91 ATAKVIVTLDADLQNDPADIPMLLAKLE-EGYDLVSGWRQNRQDGALN-----RLLPSKIANWLIRRATSVYIHDYGCSL 164
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEEALKtSGYDIAIGSRAHLASAAVVkrswlRNLLGRGFNFLVRLLLGLGIKDTQCGF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1833197664 165 KAYRSELVADmnLYGELH--RF-----LPALAYIEGARITEVPVR 202
Cdd:cd04188   161 KLFTRDAARR--LFPRLHleRWafdveLLVLARRLGYPIEEVPVR 203
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
11-230 6.53e-23

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 95.15  E-value: 6.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVESLPLLLEAISTTLTASElNYEIICVDDGSSDGTAEFLKAQAQTRTDlKAIILR---RNYGQTAAMSAG 87
Cdd:PLN02726   11 YSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGE-DRILLRprpGKLGLGTAYIHG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  88 FNYATAKVIVTLDADLQNDPADIPMLLAK-LEEGYDLVSGWRQNRQDGA----LNRLLPSKIANWLIRRATSVYIHDYGC 162
Cdd:PLN02726   89 LKHASGDFVVIMDADLSHHPKYLPSFIKKqRETGADIVTGTRYVKGGGVhgwdLRRKLTSRGANVLAQTLLWPGVSDLTG 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833197664 163 SLKAYRSELVADMnlygeLHRF----------LPALAYIEGARITEVPVRHHARRFGKSKYGISRTFRVLMDLLTILF 230
Cdd:PLN02726  169 SFRLYKRSALEDL-----VSSVvskgyvfqmeIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLL 241
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
13-127 2.49e-15

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: 72.15  E-value: 2.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAIsttLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNYAT 92
Cdd:cd00761     1 VIIPAYNEEPYLERCLESL---LAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1833197664  93 AKVIVTLDADLQNDPADIPMLLAKLEE--GYDLVSGW 127
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELLAdpEADAVGGP 114
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
5-102 6.20e-15

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: 74.01  E-value: 6.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664   5 QSPTLDVSIVVPIKDEVESLPLLLEAIsTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAM 84
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIEETLRSL-LAQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAAL 103
                          90
                  ....*....|....*...
gi 1833197664  85 SAGFNYATAKVIVTLDAD 102
Cdd:COG1215   104 NAGLKAARGDIVVFLDAD 121
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
10-152 1.23e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 71.56  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  10 DVSIVVPIKDEVESLPLLLEAIsttLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLkaIILRRNYGQTAAMSAGFN 89
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESL---LAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRV--IRNPENLGFAAARNLGLR 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833197664  90 YATAKVIVTLDADlqndpaDIPmllakleegydlvsgwrqnrQDGALNRLLpsKIANWLIRRA 152
Cdd:COG1216    79 AAGGDYLLFLDDD------TVV--------------------EPDWLERLL--AAACLLIRRE 113
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
9-201 7.59e-12

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 65.17  E-value: 7.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664   9 LDVSIVVPIKDEVESLPLLLEAISTTLTAS-----ELNYEIICVDDGSSDGTAE----FLKAQAQTRTDLKAIILRRNYG 79
Cdd:PTZ00260   70 VDLSIVIPAYNEEDRLPKMLKETIKYLESRsrkdpKFKYEIIIVNDGSKDKTLKvakdFWRQNINPNIDIRLLSLLRNKG 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  80 QTAAMSAGFNYATAKVIVTLDADLQNDPADIPMLLAKLEE----GYDLVSGWRQNRQDGALN------RLLPSKIANWLI 149
Cdd:PTZ00260  150 KGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKieqnGLGIVFGSRNHLVDSDVVakrkwyRNILMYGFHFIV 229
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1833197664 150 RRATSVYIHDYGCSLKAYRSELVADmnLYGELH--RF-----LPALAYIEGARITEVPV 201
Cdd:PTZ00260  230 NTICGTNLKDTQCGFKLFTRETARI--IFPSLHleRWafdieIVMIAQKLNLPIAEVPV 286
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
13-102 1.59e-11

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: 62.24  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAIsttLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNY-GQTAAMSAGFNYA 91
Cdd:cd06423     1 IIVPAYNEEAVIERTIESL---LALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENgGKAGALNAGLRHA 77
                          90
                  ....*....|.
gi 1833197664  92 TAKVIVTLDAD 102
Cdd:cd06423    78 KGDIVVVLDAD 88
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
11-138 9.61e-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: 58.01  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVESLPLLLEAISTTLTASElNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAII-LRRNygQTAAMSAGFN 89
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKD-LIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDnPKRI--QSAGLNIGIR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1833197664  90 YATAKVIVTLDADLQNDPADIPMLLAKLEE-GYDLVSGWRQNRQDGALNR 138
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYILELVEALKRtGADNVGGPMETIGESKFQK 128
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
13-119 1.19e-08

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 53.72  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAIsttLTASELNYEIICVDDGSSDGTAEFLKAQAQtrtDLKAIILRRNYGQTAAMSAGFNYAT 92
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSL---LAQTYPDFEVIVVDNASTDGSVELLRELFP---EVRLIRNGENLGFGAGNNQGIREAK 74
                          90       100
                  ....*....|....*....|....*..
gi 1833197664  93 AKVIVTLDADLQNDPADIPMLLAKLEE 119
Cdd:cd04186    75 GDYVLLLNPDTVVEPGALLELLDAAEQ 101
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
13-102 1.43e-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: 54.22  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  13 IVVPIKDEVESLPLLLEAISttltasELNY-----EIICVDDGSSDGTAEFLKAQAQtRTDLKAIILRRNY----GQTAA 83
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLS------ALDYpkekfEVILVDDHSTDGTVQILEFAAA-KPNFQLKILNNSRvsisGKKNA 73
                          90
                  ....*....|....*....
gi 1833197664  84 MSAGFNYATAKVIVTLDAD 102
Cdd:cd04192    74 LTTAIKAAKGDWIVTTDAD 92
PRK10073 PRK10073
putative glycosyl transferase; Provisional
5-102 3.65e-08

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 53.90  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664   5 QSPTLDVSIVVPIKDEVESLPLLLEAIST-TLTAselnYEIICVDDGSSDGTAEFLKAQAQTRTDLKaIILRRNYGQTAA 83
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLIAqTWTA----LEIIIVNDGSTDNSVEIAKHYAENYPHVR-LLHQANAGVSVA 76
                          90
                  ....*....|....*....
gi 1833197664  84 MSAGFNYATAKVIVTLDAD 102
Cdd:PRK10073   77 RNTGLAVATGKYVAFPDAD 95
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
11-102 7.85e-07

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: 49.11  E-value: 7.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVESLPLLLEAISTtltASELNYEIICVDDGSSDGTAEflkaqaqTRTDLKAIILRRNYGQTAAMSAGFNY 90
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRR---LNPLPLEIIVVDGGSTDGTVA-------IARSAGVVVISSPKGRARQMNAGAAA 70
                          90
                  ....*....|..
gi 1833197664  91 ATAKVIVTLDAD 102
Cdd:cd02522    71 ARGDWLLFLHAD 82
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
11-126 5.69e-06

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: 46.81  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVP-------IKDEVESLpllleaisttltaSELNY-----EIICVDDGSSDGTAEflKAQAQTRTDLKAIILRRNY 78
Cdd:cd06439    31 VTIIIPayneeavIEAKLENL-------------LALDYprdrlEIIVVSDGSTDGTAE--IAREYADKGVKLLRFPERR 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1833197664  79 GQTAAMSAGFNYATAKVIVTLDADLQNDPADIPMLLAKLE-EGYDLVSG 126
Cdd:cd06439    96 GKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHFAdPSVGAVSG 144
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
12-101 9.91e-06

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: 46.43  E-value: 9.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  12 SIVVPIKDEVESLplLLEAISTTL--TASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNY--GQTAAMSAG 87
Cdd:cd02510     1 SVIIIFHNEALST--LLRTVHSVInrTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKreGLIRARIAG 78
                          90
                  ....*....|....
gi 1833197664  88 FNYATAKVIVTLDA 101
Cdd:cd02510    79 ARAATGDVLVFLDS 92
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
10-184 4.85e-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: 43.78  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  10 DVSIVVPIKDEveSLPLLLEAISTTLtaSELNYEIICVDDGSSDGTAEFLKAQAqtRTDLKAIILRRNYGQTAAMSAGFN 89
Cdd:cd06434     1 DVTVIIPVYDE--DPDVFRECLRSIL--RQKPLEIIVVTDGDDEPYLSILSQTV--KYGGIFVITVPHPGKRRALAEGIR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  90 YATAKVIVTLDADLQNDPADIPMLLAKLE-EGYDLVSGwRQ---NRQDGALNRLLPSKI--ANWLIRRATSVyihdYGC- 162
Cdd:cd06434    75 HVTTDIVVLLDSDTVWPPNALPEMLKPFEdPKVGGVGT-NQrilRPRDSKWSFLAAEYLerRNEEIRAAMSY----DGGv 149
                         170       180
                  ....*....|....*....|....*..
gi 1833197664 163 -----SLKAYRSELVADmnlYGELHRF 184
Cdd:cd06434   150 pclsgRTAAYRTEILKD---FLFLEEF 173
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
11-102 5.28e-05

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: 43.35  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEveSLPLLLEAISTTLTASELNYEIICVDDGSSD-GTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFN 89
Cdd:cd04184     3 ISIVMPVYNT--PEKYLREAIESVRAQTYPNWELCIADDASTDpEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80
                          90
                  ....*....|...
gi 1833197664  90 YATAKVIVTLDAD 102
Cdd:cd04184    81 LATGEFVALLDHD 93
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
11-131 6.82e-05

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: 43.43  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVESLPLLLEAISTtltASElnyEIICVDDGSSDGTAEFLKAqaqtrtdLKAIILRR---NYGqtAAMSAG 87
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKW---AVD---EIIVVDSGSTDRTVEIAKE-------YGAKVYQRwwdGFG--AQRNFA 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1833197664  88 FNYATAKVIVTLDADLQNDPADIP-MLLAKLEEGYDLVSGWRQNR 131
Cdd:cd02511    67 LELATNDWVLSLDADERLTPELADeILALLATDDYDGYYVPRRNF 111
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
11-126 8.59e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 40.67  E-value: 8.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVESLPLLLEAISTTLTASeLNYEIICVDDGSSDGTAEfLKAQAQTRTDLKAIILRR---NYGQTAAMSAG 87
Cdd:PRK13915   33 VSVVLPALNEEETVGKVVDSIRPLLMEP-LVDELIVIDSGSTDATAE-RAAAAGARVVSREEILPElppRPGKGEALWRS 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1833197664  88 FNYATAKVIVTLDADLQN-DPADIPMLLAKL--EEGYDLVSG 126
Cdd:PRK13915  111 LAATTGDIVVFVDADLINfDPMFVPGLLGPLltDPGVHLVKA 152
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
26-102 9.86e-04

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 39.54  E-value: 9.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833197664  26 LLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQaqtrTDLKAIILRRNYGQTAAmSAGFnYATAKVIVTLDAD 102
Cdd:cd04185    11 LLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSL----GDLDNIVYLRLPENLGG-AGGF-YEGVRRAYELGYD 81
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
12-102 1.63e-03

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 39.57  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  12 SIVVPIKDEvESLPLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTR-TDLKAIILRRNYGQTAAMSAGFNY 90
Cdd:pfam10111   1 SVVIPVYNG-EKTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNlQVYYPNAPDTTYSLAASRNRGTSH 79
                          90
                  ....*....|..
gi 1833197664  91 ATAKVIVTLDAD 102
Cdd:pfam10111  80 AIGEYISFIDGD 91
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
24-107 3.98e-03

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: 37.75  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  24 LPLLLEA--ISTT---LTASELNYEIICVDDGSSDGTAEFLKAQAQtrtDLKAIILRR-----NYGQTAAMSAGFNY--- 90
Cdd:cd06436     3 VPCLNEEavIQRTlasLLRNKPNFLVLVIDDASDDDTAGIVRLAIT---DSRVHLLRRhlpnaRTGKGDALNAAYDQirq 79
                          90       100
                  ....*....|....*....|....*
gi 1833197664  91 -------ATAKVIVT-LDADLQNDP 107
Cdd:cd06436    80 ilieegaDPERVIIAvIDADGRLDP 104
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
41-126 4.35e-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: 37.91  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  41 NYEIICVDDGSSDGTAEFLKAQAQTRTDlkaIILRRNYGQTAAMSAGFNYATAKVIVTLDAD--LQNDPADIPMLLAKLE 118
Cdd:cd06433    27 NIEYIVIDGGSTDGTVDIIKKYEDKITY---WISEPDKGIYDAMNKGIALATGDIIGFLNSDdtLLPGALLAVVAAFAEH 103

                  ....*...
gi 1833197664 119 EGYDLVSG 126
Cdd:cd06433   104 PEVDVVYG 111
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
11-184 5.02e-03

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: 37.68  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  11 VSIVVPIKDEVEslpLLLEAISTTLTASELNYEIICVDDGSSDGTAEFLKAQAQTRTDLKAIILRRNYGQTAAMSAGFNY 90
Cdd:cd04195     2 VLMSVYIKEKPE---FLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833197664  91 ATAKVIVTLDADLQNDPADIPMLLAKLEE--GYDLVSGWRQN-RQDGA--LNRLLP---SKIANWLIRRatSVYIHdygc 162
Cdd:cd04195    79 CTYDWVARMDTDDISLPDRFEKQLDFIEKnpEIDIVGGGVLEfDSDGNdiGKRRLPtshDDILKFARRR--SPFNH---- 152
                         170       180
                  ....*....|....*....|..
gi 1833197664 163 SLKAYRSELVADMNLYGELHRF 184
Cdd:cd04195   153 PTVMFRKSKVLAVGGYQDLPLV 174
 
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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