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Conserved domains on  [gi|50287043|ref|XP_445951|]
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ALG5 [Nakaseomyces glabratus]

Protein Classification

dolichyl-phosphate beta-glucosyltransferase( domain architecture ID 10135784)

dolichyl-phosphate beta-glucosyltransferase is a glycosyltransferase family 2 protein that catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate

CAZY:  GT2
EC:  2.4.1.117
Gene Ontology:  GO:0004581|GO:0006486
PubMed:  12200473|10521532|12691742|9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 76-300 4.70e-103

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: 301.02  E-value: 4.70e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHVMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAEeyklQPKELRVIKFIENRGKGGAVRQ 155
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARK----NPALIRVLTLPKNRGKGGAVRA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDSIqkleksddeKKPKAAMAIGSRAHMVNtEAVIKRSLLRNCLMYGFHTLVY 235
Cdd:cd04188  77 GMLAARGDYILFADADLATPFEELEKLEEAL---------KTSGYDIAIGSRAHLAS-AAVVKRSWLRNLLGRGFNFLVR 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50287043 236 IFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLANKKAIPVSEIPISWHEVDGSK 300
Cdd:cd04188 147 LLLGLGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 76-300 4.70e-103

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: 301.02  E-value: 4.70e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHVMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAEeyklQPKELRVIKFIENRGKGGAVRQ 155
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARK----NPALIRVLTLPKNRGKGGAVRA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDSIqkleksddeKKPKAAMAIGSRAHMVNtEAVIKRSLLRNCLMYGFHTLVY 235
Cdd:cd04188  77 GMLAARGDYILFADADLATPFEELEKLEEAL---------KTSGYDIAIGSRAHLAS-AAVVKRSWLRNLLGRGFNFLVR 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50287043 236 IFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLANKKAIPVSEIPISWHEVDGSK 300
Cdd:cd04188 147 LLLGLGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 71-327 1.22e-92

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 278.96  E-value: 1.22e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   71 DILISVVVPAYNETDRIHVMLDDTIKYLRSQF---PN-RWEILIVDDGSKDGTTEYCLKLAaEEYKLQPKELRVIKFIEN 146
Cdd:PTZ00260  69 DVDLSIVIPAYNEEDRLPKMLKETIKYLESRSrkdPKfKYEIIIVNDGSKDKTLKVAKDFW-RQNINPNIDIRLLSLLRN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  147 RGKGGAVRQGLLHIRGKYGLFADADGASKFSDISKLIDSIQKLEKSDdekkpkAAMAIGSRAHMVNTEAVIKRSLLRNCL 226
Cdd:PTZ00260 148 KGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQNG------LGIVFGSRNHLVDSDVVAKRKWYRNIL 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  227 MYGFHTLVYIFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLANKKAIPVSEIPISWHEVDGSKMALALD 306
Cdd:PTZ00260 222 MYGFHFIVNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISA 301

                        250       260
                 ....*....|....*....|.
gi 50287043  307 SIKMAIDLVVIRMAYILGIYN 327
Cdd:PTZ00260 302 SIQMARDILLVRSFYLLGIWK 322
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 73-303 3.87e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 3.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  73 LISVVVPAYNETDRIHvmldDTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAEEyklqpKELRVIKFIENRGKGGA 152
Cdd:COG0463   3 LVSVVIPTYNEEEYLE----EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKD-----PRIRVIRLERNRGKGAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 153 VRQGLLHIRGKYGLFADADGASKFSDISKLIDSIQkleksddekKPKAAMAIGSRaHMVNTEAVIKRSLLRNCLMYGFht 232
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALE---------EGPADLVYGSR-LIREGESDLRRLGSRLFNLVRL-- 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50287043 233 lvyifgIRSIKDTQCGFKLFNRPAID-LIFPymhtEGWIFDVEiLLLANKKAIPVSEIPISWHEvDGSKMAL 303
Cdd:COG0463 142 ------LTNLPDSTSGFRLFRREVLEeLGFD----EGFLEDTE-LLRALRHGFRIAEVPVRYRA-GESKLNL 201
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 75-258 5.53e-27

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: 104.01  E-value: 5.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043    75 SVVVPAYNETDrihvMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYclklaAEEYKLQPKELRVIKFIENRGKGGAVR 154
Cdd:pfam00535   1 SVIIPTYNEEK----YLLETLESLLNQTYPNFEIIVVDDGSTDGTVEI-----AEEYAKKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   155 QGLLHIRGKYGLFADADGASKFSDISKLIDSIQKLEksddekkpkAAMAIGSRAHmVNTEAVIKRSLLRNCLMYGFHTLV 234
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDG---------ADVVVGSRYV-IFGETGEYRRASRITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....
gi 50287043   235 YIFGIRSIKDTQCGFKLFNRPAID 258
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALE 165
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
74-121 2.02e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 39.39  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 50287043   74 ISVVVPAYNETDRIHVMLDDtikyLRSQFPN---RWEILIVDDGSKDGTTE 121
Cdd:NF038302   3 FTVAIPTYNGANRLPEVLER----LRSQIGTeslSWEIIVVDNNSTDNTAQ 49
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 76-300 4.70e-103

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: 301.02  E-value: 4.70e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHVMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAEeyklQPKELRVIKFIENRGKGGAVRQ 155
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARK----NPALIRVLTLPKNRGKGGAVRA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDSIqkleksddeKKPKAAMAIGSRAHMVNtEAVIKRSLLRNCLMYGFHTLVY 235
Cdd:cd04188  77 GMLAARGDYILFADADLATPFEELEKLEEAL---------KTSGYDIAIGSRAHLAS-AAVVKRSWLRNLLGRGFNFLVR 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50287043 236 IFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLANKKAIPVSEIPISWHEVDGSK 300
Cdd:cd04188 147 LLLGLGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 71-327 1.22e-92

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 278.96  E-value: 1.22e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   71 DILISVVVPAYNETDRIHVMLDDTIKYLRSQF---PN-RWEILIVDDGSKDGTTEYCLKLAaEEYKLQPKELRVIKFIEN 146
Cdd:PTZ00260  69 DVDLSIVIPAYNEEDRLPKMLKETIKYLESRSrkdPKfKYEIIIVNDGSKDKTLKVAKDFW-RQNINPNIDIRLLSLLRN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  147 RGKGGAVRQGLLHIRGKYGLFADADGASKFSDISKLIDSIQKLEKSDdekkpkAAMAIGSRAHMVNTEAVIKRSLLRNCL 226
Cdd:PTZ00260 148 KGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQNG------LGIVFGSRNHLVDSDVVAKRKWYRNIL 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  227 MYGFHTLVYIFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLANKKAIPVSEIPISWHEVDGSKMALALD 306
Cdd:PTZ00260 222 MYGFHFIVNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISA 301

                        250       260
                 ....*....|....*....|.
gi 50287043  307 SIKMAIDLVVIRMAYILGIYN 327
Cdd:PTZ00260 302 SIQMARDILLVRSFYLLGIWK 322
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 76-279 7.99e-51

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: 166.98  E-value: 7.99e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHVMLDDTIKYLRSQFPnrWEILIVDDGSKDGTTEYCLKLAAEEyklqpKELRVIKFIENRGKGGAVRQ 155
Cdd:cd04179   1 VVIPAYNEEENIPELVERLLAVLEEGYD--YEIIVVDDGSTDGTAEIARELAARV-----PRVRVIRLSRNFGKGAAVRA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDSIqkleksddeKKPKAAMAIGSRAHmvnTEAVIKRSLLRNCLMYGFHTLVY 235
Cdd:cd04179  74 GFKAARGDIVVTMDADLQHPPEDIPKLLEKL---------LEGGADVVIGSRFV---RGGGAGMPLLRRLGSRLFNFLIR 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50287043 236 IFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLA 279
Cdd:cd04179 142 LLLGVRISDTQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 73-303 3.87e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 3.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  73 LISVVVPAYNETDRIHvmldDTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAEEyklqpKELRVIKFIENRGKGGA 152
Cdd:COG0463   3 LVSVVIPTYNEEEYLE----EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKD-----PRIRVIRLERNRGKGAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 153 VRQGLLHIRGKYGLFADADGASKFSDISKLIDSIQkleksddekKPKAAMAIGSRaHMVNTEAVIKRSLLRNCLMYGFht 232
Cdd:COG0463  74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALE---------EGPADLVYGSR-LIREGESDLRRLGSRLFNLVRL-- 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50287043 233 lvyifgIRSIKDTQCGFKLFNRPAID-LIFPymhtEGWIFDVEiLLLANKKAIPVSEIPISWHEvDGSKMAL 303
Cdd:COG0463 142 ------LTNLPDSTSGFRLFRREVLEeLGFD----EGFLEDTE-LLRALRHGFRIAEVPVRYRA-GESKLNL 201
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 75-258 5.53e-27

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: 104.01  E-value: 5.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043    75 SVVVPAYNETDrihvMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYclklaAEEYKLQPKELRVIKFIENRGKGGAVR 154
Cdd:pfam00535   1 SVIIPTYNEEK----YLLETLESLLNQTYPNFEIIVVDDGSTDGTVEI-----AEEYAKKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   155 QGLLHIRGKYGLFADADGASKFSDISKLIDSIQKLEksddekkpkAAMAIGSRAHmVNTEAVIKRSLLRNCLMYGFHTLV 234
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDG---------ADVVVGSRYV-IFGETGEYRRASRITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....
gi 50287043   235 YIFGIRSIKDTQCGFKLFNRPAID 258
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 76-301 1.80e-24

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: 99.14  E-value: 1.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHVMLDDTIKYLRsqfPNRWEILIVDDGSKDGTTEYCLKLAAEEYklqpkELRVIKFIENRGKGGAVRQ 155
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAALK---GIDYEIIVVDDNSPDGTAEIVRELAKEYP-----RVRLIVRPGKRGLGSAYIE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDSIqkleksddeKKPKAAMAIGSRahMVNTEAVIKRSLLRNCLMYGFHTLVY 235
Cdd:cd06442  73 GFKAARGDVIVVMDADLSHPPEYIPELLEAQ---------LEGGADLVIGSR--YVEGGGVEGWGLKRKLISRGANLLAR 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50287043 236 IFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLANKKAIPVSEIPISWHE-VDG-SKM 301
Cdd:cd06442 142 LLLGRKVSDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDrEHGeSKL 209
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 76-171 1.03e-18

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: 82.28  E-value: 1.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHvmldDTIKYLRSQFPNRWEILIVDDGSKDGTTEyclkLAAEEYKLQPKELRVIKFIENRGKGGAVRQ 155
Cdd:cd06423   1 IIVPAYNEEAVIE----RTIESLLALDYPKLEVIVVDDGSTDDTLE----ILEELAALYIRRVLVVRDKENGGKAGALNA 72

                        90
                ....*....|....*.
gi 50287043 156 GLLHIRGKYGLFADAD 171
Cdd:cd06423  73 GLRHAKGDIVVVLDAD 88
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 76-218 1.82e-18

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 81.01  E-value: 1.82e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDrihvMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYclklaAEEYKLQPKELRVIKFIENRGKGGAVRQ 155
Cdd:cd00761   1 VIIPAYNEEP----YLERCLESLLAQTYPNFEVIVVDDGSTDGTLEI-----LEEYAKKDPRVIRVINEENQGLAAARNA 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDsiqkleksDDEKKPKAAMAIGSRAHMVNTEAVIK 218
Cdd:cd00761  72 GLKAARGEYILFLDADDLLLPDWLERLVA--------ELLADPEADAVGGPGNLLFRRELLEE 126
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 74-171 5.33e-17

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: 80.17  E-value: 5.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  74 ISVVVPAYNETDrihvMLDDTIKYLRSQ-FPN-RWEILIVDDGSKDGTTEyclklAAEEYKLQPKELRVIKFIENRGKGG 151
Cdd:COG1215  31 VSVIIPAYNEEA----VIEETLRSLLAQdYPKeKLEVIVVDDGSTDETAE-----IARELAAEYPRVRVIERPENGGKAA 101

                        90       100
                ....*....|....*....|
gi 50287043 152 AVRQGLLHIRGKYGLFADAD 171
Cdd:COG1215 102 ALNAGLKAARGDIVVFLDAD 121
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 76-258 3.37e-15

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: 72.51  E-value: 3.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHVMLDdTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAEEyklqpKELRVIKFIENRGKGGAVRQ 155
Cdd:cd04187   1 IVVPVYNEEENLPELYE-RLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARD-----PRVKVIRLSRNFGQQAALLA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDSIQklEKSDdekkpkaaMAIGSRAhmvNTEAVIKRSLLRNcLMYGFHTLvy 235
Cdd:cd04187  75 GLDHARGDAVITMDADLQDPPELIPEMLAKWE--EGYD--------VVYGVRK---NRKESWLKRLTSK-LFYRLINK-- 138

                       170       180
                ....*....|....*....|...
gi 50287043 236 IFGIRsIKDTQCGFKLFNRPAID 258
Cdd:cd04187 139 LSGVD-IPDNGGDFRLMDRKVVD 160
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 71-297 4.67e-14

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 70.50  E-value: 4.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   71 DILISVVVPAYNETDRIHVMLDDTIKYLRSqfPNRWEILIVDDGSKDGTTEYCLKLAA--EEYKLQ----PKELrvikfi 144
Cdd:PLN02726   8 AMKYSIIVPTYNERLNIALIVYLIFKALQD--VKDFEIIVVDDGSPDGTQDVVKQLQKvyGEDRILlrprPGKL------ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  145 enrGKGGAVRQGLLHIRGKYGLFADADgaskFSDISKLIDSIqkLEKSDDEkkpKAAMAIGSRahMVNTEAVIKRSLLRN 224
Cdd:PLN02726  80 ---GLGTAYIHGLKHASGDFVVIMDAD----LSHHPKYLPSF--IKKQRET---GADIVTGTR--YVKGGGVHGWDLRRK 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50287043  225 CLMYGFHTLVYIFGIRSIKDTQCGFKLFNRPAIDLIFPYMHTEGWIFDVEILLLANKKAIPVSEIPISWheVD 297
Cdd:PLN02726 146 LTSRGANVLAQTLLWPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITF--VD 216
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
74-171 6.82e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 69.25  E-value: 6.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  74 ISVVVPAYNETDrihvMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAEeyklqpkELRVIKFIENRGKGGAV 153
Cdd:COG1216   5 VSVVIPTYNRPE----LLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFP-------RVRVIRNPENLGFAAAR 73

                        90
                ....*....|....*...
gi 50287043 154 RQGLLHIRGKYGLFADAD 171
Cdd:COG1216  74 NLGLRAAGGDYLLFLDDD 91
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 74-171 1.08e-11

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: 63.76  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  74 ISVVVPAYNETDRIhvmlDDTIKYLRSQ-FPN-RWEILIVDDGSKDGTTEyclklAAEEYklQPKELRVIKFIENRGKGG 151
Cdd:cd06439  31 VTIIIPAYNEEAVI----EAKLENLLALdYPRdRLEIIVVSDGSTDGTAE-----IAREY--ADKGVKLLRFPERRGKAA 99

                        90       100
                ....*....|....*....|
gi 50287043 152 AVRQGLLHIRGKYGLFADAD 171
Cdd:cd06439 100 ALNRALALATGEIVVFTDAN 119
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 76-171 3.91e-09

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: 56.14  E-value: 3.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIHVMLDDTIK--YLRSQFpnrwEILIVDDGSKDGTTEYclkLAAEEYKLQPKeLRVIKFIE--NRGKGG 151
Cdd:cd04192   1 VVIAARNEAENLPRLLQSLSAldYPKEKF----EVILVDDHSTDGTVQI---LEFAAAKPNFQ-LKILNNSRvsISGKKN 72

                        90       100
                ....*....|....*....|
gi 50287043 152 AVRQGLLHIRGKYGLFADAD 171
Cdd:cd04192  73 ALTTAIKAAKGDWIVTTDAD 92
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 73-188 2.27e-08

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: 54.16  E-value: 2.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  73 LISVVVPAYNETDRIHVMLDDtikYLRSQFP-NRWEILIVDDGSKDGTTEyclkLAAEEYKLQPKelrvIKFIENRGK-- 149
Cdd:cd02525   1 FVSIIIPVRNEEKYIEELLES---LLNQSYPkDLIEIIVVDGGSTDGTRE----IVQEYAAKDPR----IRLIDNPKRiq 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 50287043 150 GGAVRQGLLHIRGKYGLFADADgaSKFSD--ISKLIDSIQK 188
Cdd:cd02525  70 SAGLNIGIRNSRGDIIIRVDAH--AVYPKdyILELVEALKR 108
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 76-208 3.23e-08

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 52.18  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDrihvMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEYClklaaeeyKLQPKELRVIKFIENRGKGGAVRQ 155
Cdd:cd04186   1 IIIVNYNSLE----YLKACLDSLLAQTYPDFEVIVVDNASTDGSVELL--------RELFPEVRLIRNGENLGFGAGNNQ 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 50287043 156 GLLHIRGKYGLFADADGASKFSDISKLIDSIqkleksddEKKPKAAMaIGSRA 208
Cdd:cd04186  69 GIREAKGDYVLLLNPDTVVEPGALLELLDAA--------EQDPDVGI-VGPKV 112
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 73-171 4.84e-08

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 52.59  E-value: 4.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  73 LISVVVPAYNeTDRIHvmLDDTIKYLRSQ-FPNrWEILIVDDGSkdgtTEYCLKLAAEEYKLQPKELRVIKFIENRGKGG 151
Cdd:cd04184   2 LISIVMPVYN-TPEKY--LREAIESVRAQtYPN-WELCIADDAS----TDPEVKRVLKKYAAQDPRIKVVFREENGGISA 73

                        90       100
                ....*....|....*....|
gi 50287043 152 AVRQGLLHIRGKYGLFADAD 171
Cdd:cd04184  74 ATNSALELATGEFVALLDHD 93
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 74-171 6.15e-08

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 52.57  E-value: 6.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  74 ISVVVPAYNETDRIHvmldDTIKYLRSQFPNRWEILIVDDGSKDGTTEYCLKLAAeeyklqpkelRVIKfiENRGKGGAV 153
Cdd:cd02522   1 LSIIIPTLNEAENLP----RLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGV----------VVIS--SPKGRARQM 64

                        90
                ....*....|....*...
gi 50287043 154 RQGLLHIRGKYGLFADAD 171
Cdd:cd02522  65 NAGAAAARGDWLLFLHAD 82
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 96-265 7.32e-08

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 52.25  E-value: 7.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  96 KYLRSQ--------FPNrWEILIVDDGSKDGTTEYClklaaEEYklQPKELRVIKFIENRGKGGAVR---QGLLHIRGKY 164
Cdd:cd04196  11 KYLREQldsilaqtYKN-DELIISDDGSTDGTVEII-----KEY--IDKDPFIIILIRNGKNLGVARnfeSLLQAADGDY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043 165 GLFADADgaskfsDI---SKLIDSIQKLEKSDDekkpkaAMAIGSRAHMVNTE-AVIKRSLL--RNCLMYGFHTLVYIFG 238
Cdd:cd04196  83 VFFCDQD------DIwlpDKLERLLKAFLKDDK------PLLVYSDLELVDENgNPIGESFFeyQKIKPGTSFNNLLFQN 150

                       170       180       190
                ....*....|....*....|....*....|...
gi 50287043 239 IRsikdTQCGFkLFNRPAIDLIFPY------MH 265
Cdd:cd04196 151 VV----TGCTM-AFNRELLELALPFpdadviMH 178
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 73-171 1.09e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 52.74  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   73 LISVVVPAYNETDrihvMLDDTIKYLRSQFPNRWEILIVDDGSKDGTTEyclklAAEEYKLQPKELRVIKfIENRGKGGA 152
Cdd:PRK10073   7 KLSIIIPLYNAGK----DFRAFMESLIAQTWTALEIIIVNDGSTDNSVE-----IAKHYAENYPHVRLLH-QANAGVSVA 76

                         90
                 ....*....|....*....
gi 50287043  153 VRQGLLHIRGKYGLFADAD 171
Cdd:PRK10073  77 RNTGLAVATGKYVAFPDAD 95
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 74-184 8.21e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 50.12  E-value: 8.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   74 ISVVVPAYNETDRIHVMLDDTIKYLRsQFPNRWEILIVDDGSKDGTTEYcLKLAAEEyklqpKELRVIKFIENR--GKGG 151
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRRTTAACE-SLGKEYEILLIDDGSSDNSAEM-LVEAAQA-----PDSHIVAILLNRnyGQHS 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 50287043  152 AVRQGLLHIRGKYGLFADADGASKFSDISKLID 184
Cdd:PRK10714  81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVA 113
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 74-171 1.70e-06

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: 48.14  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043    74 ISVVVPAYNETDRIHVMLDDTIKYLRSQFpnrwEILIVDDGSKDGTTEYCLKLAAEeykLQPKELRVIKFIENRGKGGAV 153
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPV----EVVVVVNPSDAETLDVAEEIAAR---FPDVRLRVIRNARLLGPTGKS 76

                          90       100
                  ....*....|....*....|..
gi 50287043   154 RqGLLH----IRGKYGLFADAD 171
Cdd:pfam13641  77 R-GLNHgfraVKSDLVVLHDDD 97
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 74-195 4.55e-06

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 46.90  E-value: 4.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  74 ISVVVPAYNETDRIHvmldDTIKYLRsqfpnrW---EILIVDDGSKDGTTEYCLKLAAEEYklqpkelrvikFIENRGKG 150
Cdd:cd02511   2 LSVVIITKNEERNIE----RCLESVK------WavdEIIVVDSGSTDRTVEIAKEYGAKVY-----------QRWWDGFG 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 50287043 151 GAVRQGLLHIRGKYGLFADADgaSKFSDisKLIDSIQKLEKSDDE 195
Cdd:cd02511  61 AQRNFALELATNDWVLSLDAD--ERLTP--ELADEILALLATDDY 101
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 74-171 7.06e-06

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: 46.48  E-value: 7.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  74 ISVVVPAYNETDRIhvmLDDTIKYLRSQFPNrwEILIVDDGSKDgttEYCLKLAAEEyklqPKELRVIKFIENRGKGGAV 153
Cdd:cd06434   2 VTVIIPVYDEDPDV---FRECLRSILRQKPL--EIIVVTDGDDE---PYLSILSQTV----KYGGIFVITVPHPGKRRAL 69

                        90
                ....*....|....*...
gi 50287043 154 RQGLLHIRGKYGLFADAD 171
Cdd:cd06434  70 AEGIRHVTTDIVVLLDSD 87
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 73-171 7.17e-04

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 40.37  E-value: 7.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  73 LISVVVPAYNETDRIHVMLDDTIKYlrsQFP-NRWEILIVDDgSKDGTTEYcLKLAAEEYKLQPKELRVIKFIENRG-KG 150
Cdd:cd06437   2 MVTVQLPVFNEKYVVERLIEAACAL---DYPkDRLEIQVLDD-STDETVRL-AREIVEEYAAQGVNIKHVRRADRTGyKA 76

                        90       100
                ....*....|....*....|.
gi 50287043 151 GAVRQGLLHIRGKYGLFADAD 171
Cdd:cd06437  77 GALAEGMKVAKGEYVAIFDAD 97
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 74-171 1.78e-03

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 39.52  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043   74 ISVVVPAYNETDRI-HVMldDTIKYLRSQfPNRWEILIVDDGSKDGTTEyclkLAAE-------------EYKLQPkelr 139
Cdd:PRK13915  33 VSVVLPALNEEETVgKVV--DSIRPLLME-PLVDELIVIDSGSTDATAE----RAAAagarvvsreeilpELPPRP---- 101

                         90       100       110
                 ....*....|....*....|....*....|..
gi 50287043  140 vikfienrGKGGAVRQGLLHIRGKYGLFADAD 171
Cdd:PRK13915 102 --------GKGEALWRSLAATTGDIVVFVDAD 125
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
74-121 2.02e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 39.39  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 50287043   74 ISVVVPAYNETDRIHVMLDDtikyLRSQFPN---RWEILIVDDGSKDGTTE 121
Cdd:NF038302   3 FTVAIPTYNGANRLPEVLER----LRSQIGTeslSWEIIVVDNNSTDNTAQ 49
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 76-161 3.55e-03

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 38.13  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50287043  76 VVVPAYNETDRIhvmlDDTIKYLRSQFPNrWEILIVDDGSKDGTTEYcLKLAAEEYKLQpkELRVIKFIENRGKGGAVRQ 155
Cdd:cd06436   1 VLVPCLNEEAVI----QRTLASLLRNKPN-FLVLVIDDASDDDTAGI-VRLAITDSRVH--LLRRHLPNARTGKGDALNA 72


                ....*.
gi 50287043 156 GLLHIR 161
Cdd:cd06436  73 AYDQIR 78
 
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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