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Conserved domains on  [gi|446626280|ref|WP_000703626|]
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MULTISPECIES: glycosyltransferase family 2 protein [Enterobacteriaceae]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135621)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-185 1.39e-84

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: 252.40  E-value: 1.39e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPIFYKTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  85 GDAVIPIDVDLQDPIEVIPQLIEKWQAGADMVLAKRSDRStDGRLKRKTAEWFYKLHNKISNPQIEENVGDFRLMSREVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                        170       180
                 ....*....|....*....|.
gi 446626280 165 ENIKLLPERNLFMKGILSWVG 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 1.39e-84

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: 252.40  E-value: 1.39e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPIFYKTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  85 GDAVIPIDVDLQDPIEVIPQLIEKWQAGADMVLAKRSDRStDGRLKRKTAEWFYKLHNKISNPQIEENVGDFRLMSREVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                        170       180
                 ....*....|....*....|.
gi 446626280 165 ENIKLLPERNLFMKGILSWVG 185
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVG 180
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-303 2.71e-49

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 166.83  E-value: 2.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   2 KISLVVPVFNEEDAIP-IFYKTVREFEEL-KPYdvEIVFINDGSKDATESIInVLAVSDP--LVVPLSFTRNFGKEPALF 77
Cdd:PRK10714   7 KVSVVIPVYNEQESLPeLIRRTTAACESLgKEY--EILLIDDGSSDNSAEML-VEAAQAPdsHIVAILLNRNYGQHSAIM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  78 AGLDHATGDAVIPIDVDLQDPIEVIPQLIEKWQAGADMVLAKRSDRSTdgrlkrktaEWFYKLHNKISNPQIE----ENV 153
Cdd:PRK10714  84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD---------SWFRKTASKMINRLIQrttgKAM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280 154 GDFRLM----SREVVENIKLLPERNLFMKGILSWVGGDTDVVEYVRAERVAGSTKFNGWKLWNLALEGITSFSTFPLRIW 229
Cdd:PRK10714 155 GDYGCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLL 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446626280 230 TYIGLLVAGVSFLYGAWMIIDTLAFGN--AVRGYPSLLVSILFLGGIQLIGIGVLGEYIGRIYVEAKHRPRY-IKKI 303
Cdd:PRK10714 235 SLLGSIIAIGGFSLAVLLVVLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYfVQQV 311
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-214 9.68e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 138.30  E-value: 9.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   1 MKISLVVPVFNEEDAIPifyKTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  81 DHATGDAVIPIDVDLQDPIEVIPQLIEKWQA-GADMVLAKRSDRSTDGRLKRKTAEWFYkLHNKISNpqIEENVGDFRLM 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446626280 160 SREVVENIkLLPERNLFMKGILsWVGGDTDVVEYVRAERVAGSTKFNGWKLWNLA 214
Cdd:COG0463  156 RREVLEEL-GFDEGFLEDTELL-RALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-165 4.20e-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: 106.71  E-value: 4.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280    4 SLVVPVFNEEDAIPIFYKTVREfeeLKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   84 TGDAVIPIDVDLQDPIEVIPQLIEKWQA-GADMVLAKRSDRSTDGRLKRKT-----AEWFYKLHNKISNPQIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 446626280  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 1.39e-84

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: 252.40  E-value: 1.39e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPIFYKTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  85 GDAVIPIDVDLQDPIEVIPQLIEKWQAGADMVLAKRSDRStDGRLKRKTAEWFYKLHNKISNPQIEENVGDFRLMSREVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                        170       180
                 ....*....|....*....|.
gi 446626280 165 ENIKLLPERNLFMKGILSWVG 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 3.15e-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: 180.08  E-value: 3.15e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPIFYKTVREFEElKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLE-EGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  85 GDAVIPIDVDLQDPIEVIPQLIEK-WQAGADMVLAKRSDR---STDGRLKRKTAEWFYKLHNKISNPQIEENVGDFRLMS 160
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKlLEGGADVVIGSRFVRgggAGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159

                        170       180
                 ....*....|....*....|....*
gi 446626280 161 REVVENIKLLPERNLFMKGILSWVG 185
Cdd:cd04179  160 REVLEALLSLLESNGFEFGLELLVG 184
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-303 2.71e-49

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 166.83  E-value: 2.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   2 KISLVVPVFNEEDAIP-IFYKTVREFEEL-KPYdvEIVFINDGSKDATESIInVLAVSDP--LVVPLSFTRNFGKEPALF 77
Cdd:PRK10714   7 KVSVVIPVYNEQESLPeLIRRTTAACESLgKEY--EILLIDDGSSDNSAEML-VEAAQAPdsHIVAILLNRNYGQHSAIM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  78 AGLDHATGDAVIPIDVDLQDPIEVIPQLIEKWQAGADMVLAKRSDRSTdgrlkrktaEWFYKLHNKISNPQIE----ENV 153
Cdd:PRK10714  84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD---------SWFRKTASKMINRLIQrttgKAM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280 154 GDFRLM----SREVVENIKLLPERNLFMKGILSWVGGDTDVVEYVRAERVAGSTKFNGWKLWNLALEGITSFSTFPLRIW 229
Cdd:PRK10714 155 GDYGCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLL 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446626280 230 TYIGLLVAGVSFLYGAWMIIDTLAFGN--AVRGYPSLLVSILFLGGIQLIGIGVLGEYIGRIYVEAKHRPRY-IKKI 303
Cdd:PRK10714 235 SLLGSIIAIGGFSLAVLLVVLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYfVQQV 311
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-214 9.68e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 138.30  E-value: 9.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   1 MKISLVVPVFNEEDAIPifyKTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  81 DHATGDAVIPIDVDLQDPIEVIPQLIEKWQA-GADMVLAKRSDRSTDGRLKRKTAEWFYkLHNKISNpqIEENVGDFRLM 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446626280 160 SREVVENIkLLPERNLFMKGILsWVGGDTDVVEYVRAERVAGSTKFNGWKLWNLA 214
Cdd:COG0463  156 RREVLEEL-GFDEGFLEDTELL-RALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-165 4.20e-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: 106.71  E-value: 4.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280    4 SLVVPVFNEEDAIPIFYKTVREfeeLKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   84 TGDAVIPIDVDLQDPIEVIPQLIEKWQA-GADMVLAKRSDRSTDGRLKRKT-----AEWFYKLHNKISNPQIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 446626280  158 LMSREVVE 165
Cdd:pfam00535 158 LYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 5-212 1.39e-19

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: 85.28  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPIFykTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd06442    1 IIIPTYNERENIPEL--IERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  85 GDAVIPIDVDLQDPIEVIPQLIEK-WQAGADMVLAKR--SDRSTDGR-LKRK----TAEWFYK--LHNKISNPqieenVG 154
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRyvEGGGVEGWgLKRKlisrGANLLARllLGRKVSDP-----TS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446626280 155 DFRLMSREVVENI--KLLPERNLFMKGILsWVGGD--TDVVE--YVRAERVAGSTKFNGWKLWN 212
Cdd:cd06442  154 GFRAYRREVLEKLidSLVSKGYKFQLELL-VRARRlgYRIVEvpITFVDREHGESKLGGKEIVE 216
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-132 2.97e-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: 84.16  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPIFYKTVREF-EELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVP-LSFTRNFGKEPALFAGLDH 82
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYlEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRvLTLPKNRGKGGAVRAGMLA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446626280  83 ATGDAVIPIDVDLQDPIEVIPQLIE-KWQAGADMVLAKRSDRSTDGRLKRK 132
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEaLKTSGYDIAIGSRAHLASAAVVKRS 131
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-167 1.04e-14

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 72.42  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   1 MKISLVVPVFNEEDAIPIFYKTVRE-FEELKPYdvEIVFINDGSKDATESIINVL--AVSDPLVVPLSFTRNFGKEPALF 77
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKaLQDVKDF--EIIVVDDGSPDGTQDVVKQLqkVYGEDRILLRPRPGKLGLGTAYI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  78 AGLDHATGDAVIPIDVDLQDPIEVIPQLIEKWQA-GADMVLAKRSdRSTDG----RLKRK-TAEWFYKLHNKISNPQIEE 151
Cdd:PLN02726  87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVTGTRY-VKGGGvhgwDLRRKlTSRGANVLAQTLLWPGVSD 165

                        170
                 ....*....|....*.
gi 446626280 152 NVGDFRLMSREVVENI 167
Cdd:PLN02726 166 LTGSFRLYKRSALEDL 181
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-282 1.46e-13

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: 69.77  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   1 MKISLVVPVFNEEDAIPifyKTVREFEELK--PYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFA 78
Cdd:COG1215   29 PRVSVIIPAYNEEAVIE---ETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  79 GLDHATGDAVIPIDvdlqdpievipqliekwqagADMVLAKrsdrstdgrlkrktaEWFYKLHNKISNPQIeENVGDFRL 158
Cdd:COG1215  106 GLKAARGDIVVFLD--------------------ADTVLDP---------------DWLRRLVAAFADPGV-GASGANLA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280 159 MSREVVENIKLLPERN----------LFMKGILSWVGGDTDVVEYVRAERVAGSTKFNGWKLWNLALEGITSFSTFPLRI 228
Cdd:COG1215  150 FRREALEEVGGFDEDTlgedldlslrLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRL 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446626280 229 WTYIGLLVAGVSFLYGAWMIIDTLAF--GNAVRGYPSLLVSILFLGGIQLIGIGVL 282
Cdd:COG1215  230 LLFLLLLLLPLLLLLLLLALLALLLLllPALLLALLLALRRRRLLLPLLHLLYGLL 285
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-109 3.10e-13

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: 66.38  E-value: 3.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   6 VVPVFNEEDAIPIFYKTVREfeeLKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKEPALFAGLDHATG 85
Cdd:cd00761    2 IIPAYNEEPYLERCLESLLA---QTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78

                         90       100
                 ....*....|....*....|....
gi 446626280  86 DAVIPIDVDlqdpIEVIPQLIEKW 109
Cdd:cd00761   79 EYILFLDAD----DLLLPDWLERL 98
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 3-167 8.67e-11

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 61.71  E-value: 8.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   3 ISLVVPVFNEEDAIPIFYK-TVREFEELKPYDV----EIVFINDGSKDATESII------NVLAVSDPLVvpLSFTRNFG 71
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKeTIKYLESRSRKDPkfkyEIIIVNDGSKDKTLKVAkdfwrqNINPNIDIRL--LSLLRNKG 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280  72 KEPALFAGLDHATGDAVIPIDVDLQDPIE----VIPQLIEKWQAGADMVLAKRSD-RSTDGRLKRK-----TAEWFYKLH 141
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDADGATDIDdfdkLEDIMLKIEQNGLGIVFGSRNHlVDSDVVAKRKwyrniLMYGFHFIV 229

                        170       180
                 ....*....|....*....|....*.
gi 446626280 142 NKISNPQIEENVGDFRLMSREVVENI 167
Cdd:PTZ00260 230 NTICGTNLKDTQCGFKLFTRETARII 255
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-94 2.11e-10

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: 59.90  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   2 KISLVVPVFNEEDAIPifyKTVREFEELK-PYD-VEIVFINDGSKDATESIinVLAVSDPLVVPLSFTRNFGKEPALFAG 79
Cdd:cd06439   30 TVTIIIPAYNEEAVIE---AKLENLLALDyPRDrLEIIVVSDGSTDGTAEI--AREYADKGVKLLRFPERRGKAAALNRA 104

                         90
                 ....*....|....*
gi 446626280  80 LDHATGDAVIPIDVD 94
Cdd:cd06439  105 LALATGEIVVFTDAN 119
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 5-94 9.46e-09

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: 54.16  E-value: 9.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPifyKTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDP---LVVPLSftRNFGKEPALFAGLD 81
Cdd:cd06423    1 IIVPAYNEEAVIE---RTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIrrvLVVRDK--ENGGKAGALNAGLR 75

                         90
                 ....*....|...
gi 446626280  82 HATGDAVIPIDVD 94
Cdd:cd06423   76 HAKGDIVVVLDAD 88
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-117 2.62e-08

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 53.07  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   1 MKISLVVPVFNEEDAIPifyKTVREFEELKPYDVEIVFINDGSKDATESIINVLAVSDPLVVPLSFTRNFGKepALFAGL 80
Cdd:COG1216    3 PKVSVVIPTYNRPELLR---RCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNPENLGFAA--ARNLGL 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446626280  81 DHATGDAVIPIDVDlqdpIEVIPQLIEKWQAGADMVL 117
Cdd:COG1216   78 RAAGGDYLLFLDDD----TVVEPDWLERLLAAACLLI 110
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 3-86 3.86e-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: 49.88  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   3 ISLVVPVFNEEDAIPifyKTVREFEELKPYDVEIVFINDGSKDATESIinvlaVSDPLVVPLSFTRNFGKEpaLFAGLDH 82
Cdd:cd02522    1 LSIIIPTLNEAENLP---RLLASLRRLNPLPLEIIVVDGGSTDGTVAI-----ARSAGVVVISSPKGRARQ--MNAGAAA 70


                 ....
gi 446626280  83 ATGD 86
Cdd:cd02522   71 ARGD 74
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 2-92 2.09e-05

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: 44.92  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   2 KISLVVPVFNEEDAIPifyKTVREFEELKPY--DVEIVFINDGSKDATESIINVLAVSDPLVVPLSftrNFGK--EPALF 77
Cdd:cd02525    1 FVSIIIPVRNEEKYIE---ELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLID---NPKRiqSAGLN 74

                         90
                 ....*....|....*
gi 446626280  78 AGLDHATGDAVIPID 92
Cdd:cd02525   75 IGIRNSRGDIIIRVD 89
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-98 3.81e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 44.52  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   1 MKISLVVPVFNEEDAIPIFYKTVRefEELKPYDV-EIVFINDGSKDATESI-----INVLAVSD--PLVVPLSftrnfGK 72
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIR--PLLMEPLVdELIVIDSGSTDATAERaaaagARVVSREEilPELPPRP-----GK 103

                         90       100
                 ....*....|....*....|....*.
gi 446626280  73 EPALFAGLDHATGDAVIPIDVDLQDP 98
Cdd:PRK13915 104 GEALWRSLAATTGDIVVFVDADLINF 129
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-138 1.90e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 41.89  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   5 LVVPVFNEEDAIPifyKTVREFEELK-PYD-VEIVFINDGSKDATESIINV-LAVSDPLVVPLSFTR--NFGKEPALFAG 79
Cdd:cd04192    1 VVIAARNEAENLP---RLLQSLSALDyPKEkFEVILVDDHSTDGTVQILEFaAAKPNFQLKILNNSRvsISGKKNALTTA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446626280  80 LDHATGDAVIPIDVDLQDP---IEVIPQLIEKWQAGadMVLAKRSDRSTDGRL-KRKTAEWFY 138
Cdd:cd04192   78 IKAAKGDWIVTTDADCVVPsnwLLTFVAFIQKEQIG--LVAGPVIYFKGKSLLaKFQRLDWLS 138
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-94 4.61e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 41.18  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   2 KISLVVPVFNEEDAIPIFyktvreFEELKPY---DVEIVFINDGSKDATESIINVLAVSDPLVVPLSfTRNFGKEPALFA 78
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAF------MESLIAQtwtALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNT 79

                         90
                 ....*....|....*.
gi 446626280  79 GLDHATGDAVIPIDVD 94
Cdd:PRK10073  80 GLAVATGKYVAFPDAD 95
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 2-110 1.14e-03

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: 39.58  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   2 KISLVVPVFNEEDAIPIFYKTVREFEElkpydvEIVFINDGSKDATESIINVLAVSdplVVPLSFtRNFGkePALFAGLD 81
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTVEIAKEYGAK---VYQRWW-DGFG--AQRNFALE 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446626280  82 HATGDAVIPIDVD---LQDPIEVIPQLIEKWQ 110
Cdd:cd02511   69 LATNDWVLSLDADerlTPELADEILALLATDD 100
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-210 2.68e-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: 38.51  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280    3 ISLVVPVFNEEDAIpifYKTVREFeeLK-PY-DVEIVFINDGSKDATESIINVLAV--SDPLVVPLSFTRNFG---KEPA 75
Cdd:pfam13641   4 VSVVVPAFNEDSVL---GRVLEAI--LAqPYpPVEVVVVVNPSDAETLDVAEEIAArfPDVRLRVIRNARLLGptgKSRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   76 LFAGLDHATGDAVIPIDVD-LQDP--IEVIPQLIEKWQAGA--DMVLAKRSDRSTDGRLKRKTAEWfyklHNKISNPQIE 150
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDsVLHPgtLKKYVQYFDSPKVGAvgTPVFSLNRSTMLSALGALEFALR----HLRMMSLRLA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446626280  151 ENV----GDFRLMSREVVENIKLLPERNLFMKGILSWV-----GGDTDVVEYVRAERVAGSTKFNGWKL 210
Cdd:pfam13641 155 LGVlplsGAGSAIRREVLKELGLFDPFFLLGDDKSLGRrlrrhGWRVAYAPDAAVRTVFPTYLAASIKQ 223
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 3-94 3.64e-03

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: 38.00  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626280   3 ISLVVPVFNEEdaIPIFYKTVREFEELKPYdvEIVFINDGSKDATESIINVLAVSDPLVVPLsfTRNFGKEPALFAGLDH 82
Cdd:cd06434    2 VTVIIPVYDED--PDVFRECLRSILRQKPL--EIIVVTDGDDEPYLSILSQTVKYGGIFVIT--VPHPGKRRALAEGIRH 75

                         90
                 ....*....|..
gi 446626280  83 ATGDAVIPIDVD 94
Cdd:cd06434   76 VTTDIVVLLDSD 87
 
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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