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Conserved domains on  [gi|1011320527|ref|WP_062234890|]
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glycosyltransferase family 2 protein [Aureimonas sp. N4]

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 ...
5-185 1.30e-81

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: 244.69  E-value: 1.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVGMFHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHAS 84
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  85 GDAVIPIDVDLQDPIDVVPRLIEKWQEGADVVLAKRVDRsSDTHLKRRTAEMFYRLHNQISRPKIEENVGDFRLMSREVV 164
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNR-KESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|.
gi 1011320527 165 ETIKLMKERNLFMKGILSWVG 185
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 ...
5-185 1.30e-81

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: 244.69  E-value: 1.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVGMFHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHAS 84
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  85 GDAVIPIDVDLQDPIDVVPRLIEKWQEGADVVLAKRVDRsSDTHLKRRTAEMFYRLHNQISRPKIEENVGDFRLMSREVV 164
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNR-KESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|.
gi 1011320527 165 ETIKLMKERNLFMKGILSWVG 185
Cdd:cd04187   160 DALLLLPERHRFLRGLIAWVG 180
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-311 4.23e-51

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 171.46  E-value: 4.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   2 KISLVVPVFNEEETVGMFHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGlSANDP--LVVPIRFTRNFGKETALIAG 79
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPdsHIVAILLNRNYGQHSAIMAG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  80 IEHASGDAVIPIDVDLQDPIDVVPRLIEKWQEGADVVLAKRVDRSSDthLKRRTAEmfyRLHNQISRPKIEENVGDFRLM 159
Cdd:PRK10714   86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDS--WFRKTAS---KMINRLIQRTTGKAMGDYGCM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527 160 ----SREVVETIKLMKERNLFMKGILSWVGGEVAVIEYVRAERTAGRSKFNGWALWNLALEGITSFSTVPLRIWTYIGLT 235
Cdd:PRK10714  161 lrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011320527 236 VASFAFLYGVWMILDKLIWGN--AVPGYpSLLVSVLFLG-GIQLIGIGVLGEYIGRIYIETKQRPRYVIRREPGSRSLS 311
Cdd:PRK10714  241 IAIGGFSLAVLLVVLRLTFGPqwAAEGV-FMLFAVLFTFiGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTS 318
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 1.71e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 145.62  E-value: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   1 MKISLVVPVFNEEETVGmfhRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGI 80
Cdd:COG0463     2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  81 EHASGDAVIPIDVDLQDPIDVVPRLIEKWQE-GADVVLAKRVDRSSDTHLKRRTAEMFYrLHNQISrpKIEENVGDFRLM 159
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011320527 160 SREVVETIKLmkERNLFMKGILSWVGGEVAVIEYVRAERTAGRSKFNGWALWNLA 214
Cdd:COG0463   156 RREVLEELGF--DEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 2.97e-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: 117.50  E-value: 2.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   4 SLVVPVFNEEETVgmfHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYL---LETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  84 SGDAVIPIDVDLQDPIDVVPRLIEKWQE-GADVVLAKRVDRSSDTHLKRRT-----AEMFYRLHNQISRPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 1011320527 158 LMSREVVE 165
Cdd:pfam00535 158 LYRREALE 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 ...
5-185 1.30e-81

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: 244.69  E-value: 1.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVGMFHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHAS 84
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  85 GDAVIPIDVDLQDPIDVVPRLIEKWQEGADVVLAKRVDRsSDTHLKRRTAEMFYRLHNQISRPKIEENVGDFRLMSREVV 164
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNR-KESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170       180
                  ....*....|....*....|.
gi 1011320527 165 ETIKLMKERNLFMKGILSWVG 185
Cdd:cd04187   160 DALLLLPERHRFLRGLIAWVG 180
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
5-185 2.14e-56

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: 180.46  E-value: 2.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVGMFHRTVRDFFRSsDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHAS 84
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  85 GDAVIPIDVDLQDPIDVVPRLIEK-WQEGADVVLAKRVDRSSDTH---LKRRTAEMFYRLHNQISRPKIEENVGDFRLMS 160
Cdd:cd04179    80 GDIVVTMDADLQHPPEDIPKLLEKlLEGGADVVIGSRFVRGGGAGmplLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159
                         170       180
                  ....*....|....*....|....*
gi 1011320527 161 REVVETIKLMKERNLFMKGILSWVG 185
Cdd:cd04179   160 REVLEALLSLLESNGFEFGLELLVG 184
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-311 4.23e-51

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 171.46  E-value: 4.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   2 KISLVVPVFNEEETVGMFHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGlSANDP--LVVPIRFTRNFGKETALIAG 79
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPdsHIVAILLNRNYGQHSAIMAG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  80 IEHASGDAVIPIDVDLQDPIDVVPRLIEKWQEGADVVLAKRVDRSSDthLKRRTAEmfyRLHNQISRPKIEENVGDFRLM 159
Cdd:PRK10714   86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDS--WFRKTAS---KMINRLIQRTTGKAMGDYGCM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527 160 ----SREVVETIKLMKERNLFMKGILSWVGGEVAVIEYVRAERTAGRSKFNGWALWNLALEGITSFSTVPLRIWTYIGLT 235
Cdd:PRK10714  161 lrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011320527 236 VASFAFLYGVWMILDKLIWGN--AVPGYpSLLVSVLFLG-GIQLIGIGVLGEYIGRIYIETKQRPRYVIRREPGSRSLS 311
Cdd:PRK10714  241 IAIGGFSLAVLLVVLRLTFGPqwAAEGV-FMLFAVLFTFiGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTS 318
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 1.71e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 145.62  E-value: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   1 MKISLVVPVFNEEETVGmfhRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGI 80
Cdd:COG0463     2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  81 EHASGDAVIPIDVDLQDPIDVVPRLIEKWQE-GADVVLAKRVDRSSDTHLKRRTAEMFYrLHNQISrpKIEENVGDFRLM 159
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011320527 160 SREVVETIKLmkERNLFMKGILSWVGGEVAVIEYVRAERTAGRSKFNGWALWNLA 214
Cdd:COG0463   156 RREVLEELGF--DEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 2.97e-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: 117.50  E-value: 2.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   4 SLVVPVFNEEETVgmfHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYL---LETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  84 SGDAVIPIDVDLQDPIDVVPRLIEKWQE-GADVVLAKRVDRSSDTHLKRRT-----AEMFYRLHNQISRPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 1011320527 158 LMSREVVE 165
Cdd:pfam00535 158 LYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
5-214 1.61e-23

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: 96.06  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVGMFHRTVRDFFrsSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHAS 84
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAAL--KGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  85 GDAVIPIDVDLQDPIDVVPRLIEK-WQEGADVVLAKR-VDRSSDTH--LKR----RTAEMFYRLhnqISRPKIEENVGDF 156
Cdd:cd06442    79 GDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRyVEGGGVEGwgLKRklisRGANLLARL---LLGRKVSDPTSGF 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011320527 157 RLMSREVVETI---------KLMKErnlfMKGILSWVGGEVAVIEYVRAERTAGRSKFNGW----ALWNLA 214
Cdd:cd06442   156 RAYRREVLEKLidslvskgyKFQLE----LLVRARRLGYRIVEVPITFVDREHGESKLGGKeiveYLKGLL 222
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
5-131 9.97e-19

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: 82.62  E-value: 9.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVGMFHRTVRDFFRSS-DFAVEIVFVDDGSQDQTYPIISGLSANDPLVVP-IRFTRNFGKETALIAGIEH 82
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERpSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRvLTLPKNRGKGGAVRAGMLA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1011320527  83 ASGDAVIPIDVDLQDPIDVVPRLIE-KWQEGADVVLAKRVDRSSDTHLKR 131
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEEaLKTSGYDIAIGSRAHLASAAVVKR 130
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-156 3.07e-16

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: 74.46  E-value: 3.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   6 VVPVFNEEEtvgMFHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIAGIEHASG 85
Cdd:cd00761     2 IIPAYNEEP---YLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011320527  86 DAVIPIDVDlqdpidvvprliekwqegaDVVLAKRVDRSSDTHLKRRTAEMFYRLHNQISRPKIEENVGDF 156
Cdd:cd00761    79 EYILFLDAD-------------------DLLLPDWLERLVAELLADPEADAVGGPGNLLFRRELLEEIGGF 130
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-167 9.81e-16

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 75.12  E-value: 9.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   1 MKISLVVPVFNEEETVGMFHRTVRDFFRS-SDFavEIVFVDDGSQDQTYPIISGLSA---NDPLVVPIRfTRNFGKETAL 76
Cdd:PLN02726    9 MKYSIIVPTYNERLNIALIVYLIFKALQDvKDF--EIIVVDDGSPDGTQDVVKQLQKvygEDRILLRPR-PGKLGLGTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  77 IAGIEHASGDAVIPIDVDLQDPIDVVPRLIEKWQE-GADVVLAKRVDRSSDTH---LKRR-TAEMFYRLHNQISRPKIEE 151
Cdd:PLN02726   86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVTGTRYVKGGGVHgwdLRRKlTSRGANVLAQTLLWPGVSD 165
                         170
                  ....*....|....*.
gi 1011320527 152 NVGDFRLMSREVVETI 167
Cdd:PLN02726  166 LTGSFRLYKRSALEDL 181
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-94 4.18e-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: 74.39  E-value: 4.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   1 MKISLVVPVFNEEETVGmfhRTVRDFFRSS--DFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRFTRNFGKETALIA 78
Cdd:COG1215    29 PRVSVIIPAYNEEAVIE---ETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNA 105
                          90
                  ....*....|....*.
gi 1011320527  79 GIEHASGDAVIPIDVD 94
Cdd:COG1215   106 GLKAARGDIVVFLDAD 121
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-147 1.69e-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: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVgmfHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSAN-DPLVVPIRFTRNFGKETALIAGIEHA 83
Cdd:cd06423     1 IIVPAYNEEAVI---ERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALyIRRVLVVRDKENGGKAGALNAGLRHA 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011320527  84 SGDAVIPIDVDLQDPIDVVPRLIEKWQEGADV--VLAKRVDRSSDTHLKRRTAEMFYRLHNQISRP 147
Cdd:cd06423    78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVgaVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRR 143
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
2-106 1.62e-09

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: 57.21  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   2 KISLVVPVFNEEETVGmfhRTVRDFFrSSDF---AVEIVFVDDGSQDQTYPIISGLSANDplVVPIRFTRNFGKETALIA 78
Cdd:cd06439    30 TVTIIIPAYNEEAVIE---AKLENLL-ALDYprdRLEIIVVSDGSTDGTAEIAREYADKG--VKLLRFPERRGKAAALNR 103
                          90       100
                  ....*....|....*....|....*...
gi 1011320527  79 GIEHASGDAVIPIDVDLQDPIDVVPRLI 106
Cdd:cd06439   104 ALALATGEIVVFTDANALLDPDALRLLV 131
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-107 1.80e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 56.54  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   1 MKISLVVPVFNEEETVgmfHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLsaNDPLVVPIRFTRNFGKETALIAGI 80
Cdd:COG1216     3 PKVSVVIPTYNRPELL---RRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGL 77
                          90       100
                  ....*....|....*....|....*..
gi 1011320527  81 EHASGDAVIPIDVDLQDPIDVVPRLIE 107
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLERLLA 104
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-116 3.00e-09

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: 56.47  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   2 KISLVVPVFNEEETVGmfhRTVRDFFRSSD--FAVEIVFVDDGSQDQTYPIISGLSANDPlvvPIRFTRNFGK--ETALI 77
Cdd:cd02525     1 FVSIIIPVRNEEKYIE---ELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDP---RIRLIDNPKRiqSAGLN 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1011320527  78 AGIEHASGDAVIPIDVDLQDPIDVVPRLIEKWQE-GADVV 116
Cdd:cd02525    75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRtGADNV 114
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
3-167 9.77e-08

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 52.46  E-value: 9.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   3 ISLVVPVFNEEETVG-MFHRTVRDFFRSSD----FAVEIVFVDDGSQDQTYPIISGLSANDplVVP------IRFTRNFG 71
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPkMLKETIKYLESRSRkdpkFKYEIIIVNDGSKDKTLKVAKDFWRQN--INPnidirlLSLLRNKG 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  72 KETALIAGIEHASGDAVIPIDVDLQDPIDVVPRL----IEKWQEGADVVLAKR-VDRSSDTHLKRR-----TAEMFYRLH 141
Cdd:PTZ00260  150 KGGAVRIGMLASRGKYILMVDADGATDIDDFDKLedimLKIEQNGLGIVFGSRnHLVDSDVVAKRKwyrniLMYGFHFIV 229
                         170       180
                  ....*....|....*....|....*.
gi 1011320527 142 NQISRPKIEENVGDFRLMSREVVETI 167
Cdd:PTZ00260  230 NTICGTNLKDTQCGFKLFTRETARII 255
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
3-86 4.84e-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: 49.49  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   3 ISLVVPVFNEEETVGmfhRTVRDFFRSSDFAVEIVFVDDGSQDQTypiisGLSANDPLVVPIRFTRNFGKEtaLIAGIEH 82
Cdd:cd02522     1 LSIIIPTLNEAENLP---RLLASLRRLNPLPLEIIVVDGGSTDGT-----VAIARSAGVVVISSPKGRARQ--MNAGAAA 70

                  ....
gi 1011320527  83 ASGD 86
Cdd:cd02522    71 ARGD 74
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
1-119 8.84e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 46.45  E-value: 8.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   1 MKISLVVPVFNEEETVGMFHRTVRDfFRSSDFAVEIVFVDDGSQDQTYPIISG-----LSAND--PLVVPIRftrnfGKE 73
Cdd:PRK13915   31 RTVSVVLPALNEEETVGKVVDSIRP-LLMEPLVDELIVIDSGSTDATAERAAAagarvVSREEilPELPPRP-----GKG 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1011320527  74 TALIAGIEHASGDAVIPIDVDLQDP-IDVVPRLIEKWQEGADVVLAK 119
Cdd:PRK13915  105 EALWRSLAATTGDIVVFVDADLINFdPMFVPGLLGPLLTDPGVHLVK 151
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-98 1.04e-05

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 45.74  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   5 LVVPVFNEEETVgmfHRTVRDFFRSS--DFAVEIVFVDDGSQDQTYPIISGLSA-NDPLVVPIRFTR--NFGKETALIAG 79
Cdd:cd04192     1 VVIAARNEAENL---PRLLQSLSALDypKEKFEVILVDDHSTDGTVQILEFAAAkPNFQLKILNNSRvsISGKKNALTTA 77
                          90
                  ....*....|....*....
gi 1011320527  80 IEHASGDAVIPIDVDLQDP 98
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVP 96
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
3-146 1.20e-04

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: 42.63  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   3 ISLVVPVFNEEETVgmFHRTVRDFFRSSDfaVEIVFVDDGSqDQTYPIISGLSANDPLVVpIRFTRNFGKETALIAGIEH 82
Cdd:cd06434     2 VTVIIPVYDEDPDV--FRECLRSILRQKP--LEIIVVTDGD-DEPYLSILSQTVKYGGIF-VITVPHPGKRRALAEGIRH 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011320527  83 ASGDAVIPIDVDLQDPIDVVPRLI---EKWQEGAdVVLAKRVDRSSDTHLKRRTAEMFYRLHNQISR 146
Cdd:cd06434    76 VTTDIVVLLDSDTVWPPNALPEMLkpfEDPKVGG-VGTNQRILRPRDSKWSFLAAEYLERRNEEIRA 141
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
2-94 1.33e-04

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: 42.28  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   2 KISLVVPVFNEEetvgmfhRTVRDFFRSSDFAV-EIVFVDDGSQDQTYPIISGLSANdplVVPIRFtRNFGKETAliAGI 80
Cdd:cd02511     1 TLSVVIITKNEE-------RNIERCLESVKWAVdEIIVVDSGSTDRTVEIAKEYGAK---VYQRWW-DGFGAQRN--FAL 67
                          90
                  ....*....|....
gi 1011320527  81 EHASGDAVIPIDVD 94
Cdd:cd02511    68 ELATNDWVLSLDAD 81
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-107 8.27e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 40.41  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   2 KISLVVPVFNEEEtvgMFHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIRfTRNFGKETALIAGIE 81
Cdd:PRK10073    7 KLSIIIPLYNAGK---DFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLA 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1011320527  82 HASGDAVIPIDVDlqdpiDVV-----PRLIE 107
Cdd:PRK10073   83 VATGKYVAFPDAD-----DVVyptmyETLMT 108
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
3-143 1.03e-03

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: 39.66  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   3 ISLVVPVFNEEETVGmfhRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDP--LVVPIRFTRNFG---KETALI 77
Cdd:pfam13641   4 VSVVVPAFNEDSVLG---RVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNARLLGptgKSRGLN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011320527  78 AGIEHASGDAVIPIDVDlqdpiDVV-PRLIEK---WQEGADV-VLAKRVDRSSDTHLKRRTAEMFYRLHNQ 143
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDD-----SVLhPGTLKKyvqYFDSPKVgAVGTPVFSLNRSTMLSALGALEFALRHL 146
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-94 1.93e-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: 39.18  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   4 SLVVPVFNEEETVGMFHRtVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANDPLV-VPIRFTRNFGKETALIAGIEH 82
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQER-ILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVyYPNAPDTTYSLAASRNRGTSH 79
                          90
                  ....*....|..
gi 1011320527  83 ASGDAVIPIDVD 94
Cdd:pfam10111  80 AIGEYISFIDGD 91
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-86 2.86e-03

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: 37.92  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527   6 VVPVFNEEETVgmfHRTVRDFFRSSDFAVEIVFVDDGSQDQTYPIISGLSANdplVVPIRFTRNFGKETALIAGIEHASG 85
Cdd:cd04186     2 IIVNYNSLEYL---KACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE---VRLIRNGENLGFGAGNNQGIREAKG 75

                  .
gi 1011320527  86 D 86
Cdd:cd04186    76 D 76
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
30-138 6.66e-03

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 37.22  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011320527  30 SDFAVEIVFVDDGSQDQTYPIISGLSANDPLVVPIR-------FTRNFgketalIAGIEHASGDAVIPIDvdlQDpiDVv 102
Cdd:cd04196    24 TYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIrngknlgVARNF------ESLLQAADGDYVFFCD---QD--DI- 91
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1011320527 103 prliekWQEGadvvlakRVDRSSDTHLKRRTAEMFY 138
Cdd:cd04196    92 ------WLPD-------KLERLLKAFLKDDKPLLVY 114
 
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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