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Conserved domains on  [gi|1055322813|ref|WP_066988246|]
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glycosyltransferase family 2 protein [Methylomonas lenta]

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 ...
16-204 3.24e-62

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: 195.77  E-value: 3.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHavtqLTSLIHELADEglITKDSYLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:cd04187     1 IVVPVYNEEENLPE----LYERLKAVLES--LGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  96 GLtEVAQNcDAAISIDADLQQDPLAIREFVKELHKGFDVVLGVRNDRNsDGWLKRQTALGFYNLM-RIMGVDIVPNHADY 174
Cdd:cd04187    75 GL-DHARG-DAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLInKLSGVDIPDNGGDF 151
                         170       180       190
                  ....*....|....*....|....*....|
gi 1055322813 175 RLLSKRALEALALFPEPSIFLRATCLQLGF 204
Cdd:cd04187   152 RLMDRKVVDALLLLPERHRFLRGLIAWVGF 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 ...
16-204 3.24e-62

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: 195.77  E-value: 3.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHavtqLTSLIHELADEglITKDSYLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:cd04187     1 IVVPVYNEEENLPE----LYERLKAVLES--LGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  96 GLtEVAQNcDAAISIDADLQQDPLAIREFVKELHKGFDVVLGVRNDRNsDGWLKRQTALGFYNLM-RIMGVDIVPNHADY 174
Cdd:cd04187    75 GL-DHARG-DAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLInKLSGVDIPDNGGDF 151
                         170       180       190
                  ....*....|....*....|....*....|
gi 1055322813 175 RLLSKRALEALALFPEPSIFLRATCLQLGF 204
Cdd:cd04187   152 RLMDRKVVDALLLLPERHRFLRGLIAWVGF 181
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
11-317 3.46e-36

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 132.55  E-value: 3.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  11 VPRIAIVLPCHNESESINHAVTQLTSLIHELadegliTKDSYLFFVDDGSTDNSW-VMIDKLNQNNKAIKGLKLSQNFGH 89
Cdd:PRK10714    5 IKKVSVVIPVYNEQESLPELIRRTTAACESL------GKEYEILLIDDGSSDNSAeMLVEAAQAPDSHIVAILLNRNYGQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  90 QAALLAGLTEVaqNCDAAISIDADLQQDPLAIREFVKELHKGFDVVLGVRNDRNsDGWLkRQTALGFYNLM------RIM 163
Cdd:PRK10714   79 HSAIMAGFSHV--TGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQ-DSWF-RKTASKMINRLiqrttgKAM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813 164 GvdivpnhaDY----RLLSKRALEALALFPEPSIFLraTCLQLGFRVSTVFFDV--SERRFGQTKYSLSKMLRLALHGIT 237
Cdd:PRK10714  155 G--------DYgcmlRAYRRHIVDAMLHCHERSTFI--PILANTFARRAIEIPVhhAEREFGDSKYSFMRLINLMYDLVT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813 238 SFSVVPLRMVAILGFVIFLSSLVMGGYVIWHTLFVGdtiPGWAS------ITLPIYFIGGvQLLCLGVVGEYVGQIYKTV 311
Cdd:PRK10714  225 CLTTTPLRLLSLLGSIIAIGGFSLAVLLVVLRLTFG---PQWAAegvfmlFAVLFTFIGA-QFIGMGLLGEYIGRIYNDV 300

                  ....*.
gi 1055322813 312 KKRPRW 317
Cdd:PRK10714  301 RARPRY 306
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
12-232 2.09e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.11  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  12 PRIAIVLPCHNESESINHAVTQLTSLIHEladeglitkDSYLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQA 91
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYP---------DFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  92 ALLAGLtEVAQNcDAAISIDADLQQDPLAIREFVKELHK-GFDVVLGVRNDRNSDGWLKRqTALGFYNLMRIMgVDIVPN 170
Cdd:COG0463    73 ARNAGL-AAARG-DYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRR-LGSRLFNLVRLL-TNLPDS 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055322813 171 HADYRLLSKRALEALAL---FPEPSIFLRAtcLQLGFRVSTVFFDvseRRFGQTKYSLSKMLRLA 232
Cdd:COG0463   149 TSGFRLFRREVLEELGFdegFLEDTELLRA--LRHGFRIAEVPVR---YRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
16-183 2.28e-18

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: 80.90  E-value: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAVTQLTSLIHELaDEglitkdsyLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPN-FE--------IIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  96 GLTEVaqNCDAAISIDADLQQDPLAIREFVKELHK-GFDVVLGVRNDRNSDGWLKRQT------ALGFYNLMRIMGVDIV 168
Cdd:pfam00535  73 GLRAA--TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlsRLPFFLGLRLLGLNLP 150
                         170
                  ....*....|....*
gi 1055322813 169 PNHADYRLLSKRALE 183
Cdd:pfam00535 151 FLIGGFALYRREALE 165
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
16-204 3.24e-62

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: 195.77  E-value: 3.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHavtqLTSLIHELADEglITKDSYLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:cd04187     1 IVVPVYNEEENLPE----LYERLKAVLES--LGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  96 GLtEVAQNcDAAISIDADLQQDPLAIREFVKELHKGFDVVLGVRNDRNsDGWLKRQTALGFYNLM-RIMGVDIVPNHADY 174
Cdd:cd04187    75 GL-DHARG-DAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLInKLSGVDIPDNGGDF 151
                         170       180       190
                  ....*....|....*....|....*....|
gi 1055322813 175 RLLSKRALEALALFPEPSIFLRATCLQLGF 204
Cdd:cd04187   152 RLMDRKVVDALLLLPERHRFLRGLIAWVGF 181
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
16-204 2.54e-42

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: 144.64  E-value: 2.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAVTQLTSLIHELADEGLItkdsylfFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYDYEII-------VVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  96 GLTEVAQncDAAISIDADLQQDPLAIREFVKEL-HKGFDVVLGVRNDRNS---DGWLKRQTALGFYNLMRIM-GVDIVPN 170
Cdd:cd04179    74 GFKAARG--DIVVTMDADLQHPPEDIPKLLEKLlEGGADVVIGSRFVRGGgagMPLLRRLGSRLFNFLIRLLlGVRISDT 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1055322813 171 HADYRLLSKRALEALALFPEPSIFLRATCLQLGF 204
Cdd:cd04179   152 QSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
11-317 3.46e-36

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 132.55  E-value: 3.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  11 VPRIAIVLPCHNESESINHAVTQLTSLIHELadegliTKDSYLFFVDDGSTDNSW-VMIDKLNQNNKAIKGLKLSQNFGH 89
Cdd:PRK10714    5 IKKVSVVIPVYNEQESLPELIRRTTAACESL------GKEYEILLIDDGSSDNSAeMLVEAAQAPDSHIVAILLNRNYGQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  90 QAALLAGLTEVaqNCDAAISIDADLQQDPLAIREFVKELHKGFDVVLGVRNDRNsDGWLkRQTALGFYNLM------RIM 163
Cdd:PRK10714   79 HSAIMAGFSHV--TGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQ-DSWF-RKTASKMINRLiqrttgKAM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813 164 GvdivpnhaDY----RLLSKRALEALALFPEPSIFLraTCLQLGFRVSTVFFDV--SERRFGQTKYSLSKMLRLALHGIT 237
Cdd:PRK10714  155 G--------DYgcmlRAYRRHIVDAMLHCHERSTFI--PILANTFARRAIEIPVhhAEREFGDSKYSFMRLINLMYDLVT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813 238 SFSVVPLRMVAILGFVIFLSSLVMGGYVIWHTLFVGdtiPGWAS------ITLPIYFIGGvQLLCLGVVGEYVGQIYKTV 311
Cdd:PRK10714  225 CLTTTPLRLLSLLGSIIAIGGFSLAVLLVVLRLTFG---PQWAAegvfmlFAVLFTFIGA-QFIGMGLLGEYIGRIYNDV 300

                  ....*.
gi 1055322813 312 KKRPRW 317
Cdd:PRK10714  301 RARPRY 306
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
12-232 2.09e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.11  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  12 PRIAIVLPCHNESESINHAVTQLTSLIHEladeglitkDSYLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQA 91
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYP---------DFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  92 ALLAGLtEVAQNcDAAISIDADLQQDPLAIREFVKELHK-GFDVVLGVRNDRNSDGWLKRqTALGFYNLMRIMgVDIVPN 170
Cdd:COG0463    73 ARNAGL-AAARG-DYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRR-LGSRLFNLVRLL-TNLPDS 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055322813 171 HADYRLLSKRALEALAL---FPEPSIFLRAtcLQLGFRVSTVFFDvseRRFGQTKYSLSKMLRLA 232
Cdd:COG0463   149 TSGFRLFRREVLEELGFdegFLEDTELLRA--LRHGFRIAEVPVR---YRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
16-183 2.28e-18

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: 80.90  E-value: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAVTQLTSLIHELaDEglitkdsyLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPN-FE--------IIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  96 GLTEVaqNCDAAISIDADLQQDPLAIREFVKELHK-GFDVVLGVRNDRNSDGWLKRQT------ALGFYNLMRIMGVDIV 168
Cdd:pfam00535  73 GLRAA--TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlsRLPFFLGLRLLGLNLP 150
                         170
                  ....*....|....*
gi 1055322813 169 PNHADYRLLSKRALE 183
Cdd:pfam00535 151 FLIGGFALYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
16-234 6.75e-13

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: 66.79  E-value: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAVTQLTSLIHELADEGLItkdsylffVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGIDYEIIV--------VDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  96 GLTEVAQncDAAISIDADLQQDPLAIREFVKELH-KGFDVVLGVR--NDRNSDGW-LKRQ----TALGFYNLMRIMGV-D 166
Cdd:cd06442    73 GFKAARG--DVIVVMDADLSHPPEYIPELLEAQLeGGADLVIGSRyvEGGGVEGWgLKRKlisrGANLLARLLLGRKVsD 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055322813 167 IVpnhADYRLLSKRALEALA--LFPE-PSIFLR--ATCLQLGFRVSTVFFDVSERRFGQTKYSLSKMLRLALH 234
Cdd:cd06442   151 PT---SGFRAYRREVLEKLIdsLVSKgYKFQLEllVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKG 220
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-128 6.78e-10

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: 58.98  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813   1 MINNQYANSEVPRIAIVLPCHNESESINHAVTQLTSLIHEladeglitKDSY-LFFVDDGSTDNSWVMIDKLNQNNKAIK 79
Cdd:COG1215    18 LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYP--------KEKLeVIVVDDGSTDETAEIARELAAEYPRVR 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1055322813  80 GLKLSQNFGHQAALLAGLTEVaqNCDAAISIDADLQQDPLAIREFVKEL 128
Cdd:COG1215    90 VIERPENGGKAAALNAGLKAA--RGDIVVFLDADTVLDPDWLRRLVAAF 136
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
16-163 2.69e-08

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: 53.00  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAVTQLTSLIHELADeglitkdsyLFFVDDGSTDN-SWVMIDKLNQNNKAIKGLKLSQNFGHQAALL 94
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLE---------VIVVDDGSTDDtLEILEELAALYIRRVLVVRDKENGGKAGALN 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055322813  95 AGLtEVAQNcDAAISIDADLQQDPLAIREFVKELHKGFDVV-----LGVRNdrNSDGWLKRQTALGFYNLMRIM 163
Cdd:cd06423    72 AGL-RHAKG-DIVVVLDADTILEPDALKRLVVPFFADPKVGavqgrVRVRN--GSENLLTRLQAIEYLSIFRLG 141
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
16-165 1.25e-06

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: 48.33  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAVTQLTSLIHELadegliTKDSY-LFFVDDGSTDNSWVMIDKL-NQNNKAIKGLKLSQNFGHQAAL 93
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEER------PSFSYeIIVVDDGSKDGTAEVARKLaRKNPALIRVLTLPKNRGKGGAV 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055322813  94 LAG-LTEVAQNCdaaISIDADLQQDPLAIREFVKEL-HKGFDVVLGVRNDRNSDGWLKRQTA-----LGFYNLMRIMGV 165
Cdd:cd04188    75 RAGmLAARGDYI---LFADADLATPFEELEKLEEALkTSGYDIAIGSRAHLASAAVVKRSWLrnllgRGFNFLVRLLLG 150
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
12-222 2.12e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 48.16  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  12 PRIAIVLPCHNESESInhAVtqLTSLIHELADEgliTKDSYLFFVDDGSTDNSWVMIDKLNQ--NNKAIKGLKLSQNFGH 89
Cdd:PLN02726    9 MKYSIIVPTYNERLNI--AL--IVYLIFKALQD---VKDFEIIVVDDGSPDGTQDVVKQLQKvyGEDRILLRPRPGKLGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  90 QAALLAGLTEVAQncDAAISIDADLQQDPLAIREFV-KELHKGFDVVLGVRNDRNSD--GWlkrqtalgfyNLMR---IM 163
Cdd:PLN02726   82 GTAYIHGLKHASG--DFVVIMDADLSHHPKYLPSFIkKQRETGADIVTGTRYVKGGGvhGW----------DLRRkltSR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055322813 164 GVDIV------PNHAD----YRLLSKRALEALA--------LFpEPSIFLRATclQLGFRVSTVFFDVSERRFGQTK 222
Cdd:PLN02726  150 GANVLaqtllwPGVSDltgsFRLYKRSALEDLVssvvskgyVF-QMEIIVRAS--RKGYRIEEVPITFVDRVYGESK 223
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
16-136 1.06e-05

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: 44.80  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAvtqLTSLIHeladegLITKDSYLFFVDDGSTDNSWVMIDKLNQNNKAIKGLKLSQNFGHQAALLA 95
Cdd:cd00761     1 VIIPAYNEEPYLERC---LESLLA------QTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNA 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1055322813  96 GLTEVaqNCDAAISIDADLQQDPLAIREFVKELHKGFDVVL 136
Cdd:cd00761    72 GLKAA--RGEYILFLDADDLLLPDWLERLVAELLADPEADA 110
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
16-164 2.11e-04

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 41.43  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  16 IVLPCHNESESINHAVTQLTSL--IHELADeglitkdsyLFFVDDGSTDNS--------WVMIDKLNQNNKAiKGLKLSQ 85
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQdyPRELYR---------IFVVADNCTDDTaqvaraagATVLERHDPERRG-KGYALDF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  86 NFGHQAALlagltevAQNCDAAISIDADLQQDPLAIREFVKELHKGFDVVLGVRNDRN-SDGWLKRQTALGF--YNLMRI 162
Cdd:cd06438    71 GFRHLLNL-------ADDPDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNSKNpDDSWITRLYAFAFlvFNRLRP 143

                  ..
gi 1055322813 163 MG 164
Cdd:cd06438   144 LG 145
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
2-189 1.91e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 39.37  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813   2 INNQYANSEVpRIAIVLPCHNESESINhavTQLTSLIHELadEGLITKD---SY-LFFVDDGSTDNSWVMIDKLNQNNKA 77
Cdd:PTZ00260   61 INNILKDSDV-DLSIVIPAYNEEDRLP---KMLKETIKYL--ESRSRKDpkfKYeIIIVNDGSKDKTLKVAKDFWRQNIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322813  78 ----IKGLKLSQNFGHQAALLAGLteVAQNCDAAISIDADLQQDplaIREFVK---ELHK----GFDVVLGVRND-RNSD 145
Cdd:PTZ00260  135 pnidIRLLSLLRNKGKGGAVRIGM--LASRGKYILMVDADGATD---IDDFDKledIMLKieqnGLGIVFGSRNHlVDSD 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1055322813 146 -----GWLKRQTALGFYNLMRIM-GVDIVPNHADYRLLSKRAleALALFP 189
Cdd:PTZ00260  210 vvakrKWYRNILMYGFHFIVNTIcGTNLKDTQCGFKLFTRET--ARIIFP 257
 
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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