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Conserved domains on  [gi|1476679192|gb|AXZ93617|]
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undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase [Pseudomonas aeruginosa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10714 super family cl32562
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
5-319 3.81e-174

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


The actual alignment was detected with superfamily member PRK10714:

Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 486.17  E-value: 3.81e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   5 PIDLVSVVIPVYNEEASLPELLRRTEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRNYGQHAAIL 84
Cdd:PRK10714    4 PIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHSAIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  85 AGFEQSRGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRAERQDSAWRRWPSRLVNLAVQRSTGVAMHDYGCMLRA 164
Cdd:PRK10714   84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192 165 YRRSIVEAMLACRERSTFIPILANGFARHTCEIRVAHAERAHGESKYSAMRLLNLMFDLVTCMTTTPLRLLSLVGGGMAL 244
Cdd:PRK10714  164 YRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSIIAI 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1476679192 245 AGFLFALFLLVLRLAFGAAWAGNGLFVLFAVLFMFSGVQLLGMGLLGEYLGRMYSDVRARPRFFIERVVRATPSA 319
Cdd:PRK10714  244 GGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTS 318
 
Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
5-319 3.81e-174

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 486.17  E-value: 3.81e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   5 PIDLVSVVIPVYNEEASLPELLRRTEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRNYGQHAAIL 84
Cdd:PRK10714    4 PIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHSAIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  85 AGFEQSRGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRAERQDSAWRRWPSRLVNLAVQRSTGVAMHDYGCMLRA 164
Cdd:PRK10714   84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192 165 YRRSIVEAMLACRERSTFIPILANGFARHTCEIRVAHAERAHGESKYSAMRLLNLMFDLVTCMTTTPLRLLSLVGGGMAL 244
Cdd:PRK10714  164 YRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSIIAI 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1476679192 245 AGFLFALFLLVLRLAFGAAWAGNGLFVLFAVLFMFSGVQLLGMGLLGEYLGRMYSDVRARPRFFIERVVRATPSA 319
Cdd:PRK10714  244 GGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTS 318
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
11-187 8.81e-81

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 243.54  E-value: 8.81e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSaVVAVILNRNYGQHAAILAGFEQS 90
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPR-VKVIRLSRNFGQQAALLAGLDHA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  91 RGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRAERQDSAWRRWPSRLVNLAVQRSTGVAMHDYGCMLRAYRRSIV 170
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170
                  ....*....|....*..
gi 1476679192 171 EAMLACRERSTFIPILA 187
Cdd:cd04187   160 DALLLLPERHRFLRGLI 176
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-220 4.13e-48

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 161.02  E-value: 4.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   8 LVSVVIPVYNEEASLPELLRRTEAAcleLGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVaVILNRNYGQHAAILAGF 87
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQ---TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRV-IRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  88 EQSRGDLVITLDADLQNPPEEIPRLVERAAQ-GYDVVGSIRAERQD-SAWRRWPSRLVNLAVQRSTgvaMHDYGCMLRAY 165
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGeSDLRRLGSRLFNLVRLLTN---LPDSTSGFRLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1476679192 166 RRSIVEAMLACRERSTFIPILAngFARHTCEIRVAHAERAHGESKYSAMRLLNLM 220
Cdd:COG0463   156 RREVLEELGFDEGFLEDTELLR--ALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-171 1.30e-35

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: 127.13  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  10 SVVIPVYNEEASLPELLrrtEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVaVILNRNYGQHAAILAGFEQ 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETL---ESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRV-IRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  90 SRGDLVITLDADLQNPPEEIPRLVERAAQ-GYD-VVGSIRAERQDSAWRRWPSRLVNLAV-----QRSTGVAMHDYGCML 162
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADvVVGSRYVIFGETGEYRRASRITLSRLpfflgLRLLGLNLPFLIGGF 156

                  ....*....
gi 1476679192 163 RAYRRSIVE 171
Cdd:pfam00535 157 ALYRREALE 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
9-145 1.72e-12

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 65.61  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPELLRRTEAacleLGRAFEIVLVDDGSRDRSAELLQAAAERdgsaVVAVILNRNYGQHaailAGFE 88
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQA----LRGDAEVIVVDGGSTDGTVEIARSLGAK----VIHSPKGRARQMN----AGAA 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  89 QSRGDLVITLDADLQnPPEEIPRLVERAAQGYDVVG---SIRAERqDSAWRRWPSRLVNL 145
Cdd:TIGR04283  69 LAKGDILLFLHADTR-LPKDFLEAIRRALAKPGYVAgafDLRFDG-PGLLLRLIEWGVNL 126
 
Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
5-319 3.81e-174

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 486.17  E-value: 3.81e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   5 PIDLVSVVIPVYNEEASLPELLRRTEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRNYGQHAAIL 84
Cdd:PRK10714    4 PIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHSAIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  85 AGFEQSRGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRAERQDSAWRRWPSRLVNLAVQRSTGVAMHDYGCMLRA 164
Cdd:PRK10714   84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192 165 YRRSIVEAMLACRERSTFIPILANGFARHTCEIRVAHAERAHGESKYSAMRLLNLMFDLVTCMTTTPLRLLSLVGGGMAL 244
Cdd:PRK10714  164 YRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSIIAI 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1476679192 245 AGFLFALFLLVLRLAFGAAWAGNGLFVLFAVLFMFSGVQLLGMGLLGEYLGRMYSDVRARPRFFIERVVRATPSA 319
Cdd:PRK10714  244 GGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTS 318
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
11-187 8.81e-81

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 243.54  E-value: 8.81e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSaVVAVILNRNYGQHAAILAGFEQS 90
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPR-VKVIRLSRNFGQQAALLAGLDHA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  91 RGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRAERQDSAWRRWPSRLVNLAVQRSTGVAMHDYGCMLRAYRRSIV 170
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170
                  ....*....|....*..
gi 1476679192 171 EAMLACRERSTFIPILA 187
Cdd:cd04187   160 DALLLLPERHRFLRGLI 176
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
11-184 7.38e-61

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: 192.79  E-value: 7.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTEAAcLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSaVVAVILNRNYGQHAAILAGFEQS 90
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAV-LEEGYDYEIIVVDDGSTDGTAEIARELAARVPR-VRVIRLSRNFGKGAAVRAGFKAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  91 RGDLVITLDADLQNPPEEIPRLVERAAQ-GYDVVGSIRAERQ----DSAWRRWPSRLVNLAVQRSTGVAMHDYGCMLRAY 165
Cdd:cd04179    79 RGDIVVTMDADLQHPPEDIPKLLEKLLEgGADVVIGSRFVRGggagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158
                         170
                  ....*....|....*....
gi 1476679192 166 RRSIVEAMLACRERSTFIP 184
Cdd:cd04179   159 RREVLEALLSLLESNGFEF 177
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-220 4.13e-48

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 161.02  E-value: 4.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   8 LVSVVIPVYNEEASLPELLRRTEAAcleLGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVaVILNRNYGQHAAILAGF 87
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQ---TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRV-IRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  88 EQSRGDLVITLDADLQNPPEEIPRLVERAAQ-GYDVVGSIRAERQD-SAWRRWPSRLVNLAVQRSTgvaMHDYGCMLRAY 165
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGeSDLRRLGSRLFNLVRLLTN---LPDSTSGFRLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1476679192 166 RRSIVEAMLACRERSTFIPILAngFARHTCEIRVAHAERAHGESKYSAMRLLNLM 220
Cdd:COG0463   156 RREVLEELGFDEGFLEDTELLR--ALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-171 1.30e-35

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: 127.13  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  10 SVVIPVYNEEASLPELLrrtEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVaVILNRNYGQHAAILAGFEQ 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETL---ESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRV-IRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  90 SRGDLVITLDADLQNPPEEIPRLVERAAQ-GYD-VVGSIRAERQDSAWRRWPSRLVNLAV-----QRSTGVAMHDYGCML 162
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADvVVGSRYVIFGETGEYRRASRITLSRLpfflgLRLLGLNLPFLIGGF 156

                  ....*....
gi 1476679192 163 RAYRRSIVE 171
Cdd:pfam00535 157 ALYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
11-210 1.02e-30

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: 115.71  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTEAACLELgrAFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRNyGQHAAILAGFEQS 90
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGI--DYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKR-GLGSAYIEGFKAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  91 RGDLVITLDADLQNPPEEIPRLVERAAQ-GYD-VVGSIRAE----RQDSAWRRWPSRLVNLAVQRSTGVAMHDY--GCml 162
Cdd:cd06442    78 RGDVIVVMDADLSHPPEYIPELLEAQLEgGADlVIGSRYVEgggvEGWGLKRKLISRGANLLARLLLGRKVSDPtsGF-- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1476679192 163 RAYRRSIVEAML-ACRER--STFIPILANGFARHTC--EIRVAHAERAHGESK 210
Cdd:cd06442   156 RAYRREVLEKLIdSLVSKgyKFQLELLVRARRLGYRivEVPITFVDREHGESK 208
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
11-172 8.71e-27

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: 104.96  E-value: 8.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRT-EAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRNYGQHAAILAGFEQ 89
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAvEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGKGGAVRAGMLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  90 SRGDLVITLDADLQNPPEEIPRLVERA-AQGYDVV-GSiRAERQD------SAWRRWPSRLVNLAVQRSTGVAMHDYGCM 161
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEEALkTSGYDIAiGS-RAHLASaavvkrSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159
                         170
                  ....*....|.
gi 1476679192 162 LRAYRRSIVEA 172
Cdd:cd04188   160 FKLFTRDAARR 170
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
9-137 3.43e-20

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: 89.03  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPELLRrteaACLEL---GRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVaVILNRNYGQHAAILA 85
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLR----SLLAQdypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRV-IERPENGGKAAALNA 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1476679192  86 GFEQSRGDLVITLDADLQNPPEEIPRLVERAAQ-GYDVVGSIraerqdSAWRR 137
Cdd:COG1215   106 GLKAARGDIVVFLDADTVLDPDWLRRLVAAFADpGVGASGAN------LAFRR 152
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
11-125 4.76e-20

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: 85.25  E-value: 4.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRrteaACLELG-RAFEIVLVDDGSRDRSAELLQAAAERDGSAVVaVILNRNYGQHAAILAGFEQ 89
Cdd:cd00761     1 VIIPAYNEEPYLERCLE----SLLAQTyPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIR-VINEENQGLAAARNAGLKA 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1476679192  90 SRGDLVITLDADLQNPPEEIPRLVERAAQ--GYDVVGS 125
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLERLVAELLAdpEADAVGG 113
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
11-172 1.87e-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: 81.50  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRrteaACLELGR-AFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRNYGQHAAILAGFEQ 89
Cdd:cd06423     1 IIVPAYNEEAVIERTIE----SLLALDYpKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  90 SRGDLVITLDADLQNPPEEIPRLVERAAQGYDVV---GSIRAERQDsawRRWPSRLVNLAVQRSTGV---AMHDYGCMLR 163
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGavqGRVRVRNGS---ENLLTRLQAIEYLSIFRLgrrAQSALGGVLV 153
                         170
                  ....*....|....*
gi 1476679192 164 ------AYRRSIVEA 172
Cdd:cd06423   154 lsgafgAFRREALRE 168
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
8-210 3.72e-16

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 76.66  E-value: 3.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   8 LVSVVIPVYNEEASLP---ELLRRTEAACLElgraFEIVLVDDGSRDRSAELLQAAAERDGSA-VVAVILNRNYGQHAAI 83
Cdd:PLN02726   10 KYSIIVPTYNERLNIAlivYLIFKALQDVKD----FEIIVVDDGSPDGTQDVVKQLQKVYGEDrILLRPRPGKLGLGTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  84 LAGFEQSRGDLVITLDADLQNPPEEIPRLVE-RAAQGYDVVGSIRAERQD--SAW---RRWPSRLVNLAVQRSTGVAMHD 157
Cdd:PLN02726   86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKkQRETGADIVTGTRYVKGGgvHGWdlrRKLTSRGANVLAQTLLWPGVSD 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1476679192 158 YGCMLRAYRRSIVEAMLA-CRERS-TF---IPILANGFARHTCEIRVAHAERAHGESK 210
Cdd:PLN02726  166 LTGSFRLYKRSALEDLVSsVVSKGyVFqmeIIVRASRKGYRIEEVPITFVDRVYGESK 223
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-137 4.40e-15

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: 73.48  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTEaaCLELGRA-FEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNR--NYGQHAAILAGF 87
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLS--ALDYPKEkFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRvsISGKKNALTTAI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1476679192  88 EQSRGDLVITLDADLQNPPEEIPRLVERAAQG--YDVVGSIRAERQDSAWRR 137
Cdd:cd04192    79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEqiGLVAGPVIYFKGKSLLAK 130
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
8-124 1.09e-14

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: 72.65  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   8 LVSVVIPVYNEEASLPELLRRTEAACLELGRaFEIVLVDDGSRDRSAELLQAAAERDGSavVAVILNRNYGQHAAILAGF 87
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDL-IEIIVVDGGSTDGTREIVQEYAAKDPR--IRLIDNPKRIQSAGLNIGI 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1476679192  88 EQSRGDLVITLDADLQNPPEEIPRLVE-RAAQGYDVVG 124
Cdd:cd02525    78 RNSRGDIIIRVDAHAVYPKDYILELVEaLKRTGADNVG 115
PRK10073 PRK10073
putative glycosyl transferase; Provisional
8-153 3.54e-14

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 72.39  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   8 LVSVVIPVYNEEASLPELLRRTEAACLElgrAFEIVLVDDGSRDRSAELLQAAAERDGSavVAVILNRNYGQHAAILAGF 87
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLLHQANAGVSVARNTGL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1476679192  88 EQSRGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRAER----QDSAWRRWPS-RLvnlavqRSTGV 153
Cdd:PRK10073   82 AVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWcfrdTGETWQSIPSdRL------RSTGV 146
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-117 7.67e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 69.25  E-value: 7.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPELLRRTEAAClelGRAFEIVLVDDGSRDRSAELLQAAAERDgsaVVAVILNRNYGQHAAILAGFE 88
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQT---YPPFEVIVVDNGSTDGTAELLAALAFPR---VRVIRNPENLGFAAARNLGLR 78
                          90       100
                  ....*....|....*....|....*....
gi 1476679192  89 QSRGDLVITLDADLQNPPEEIPRLVERAA 117
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDWLERLLAAAC 107
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
9-145 1.72e-12

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 65.61  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPELLRRTEAacleLGRAFEIVLVDDGSRDRSAELLQAAAERdgsaVVAVILNRNYGQHaailAGFE 88
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQA----LRGDAEVIVVDGGSTDGTVEIARSLGAK----VIHSPKGRARQMN----AGAA 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  89 QSRGDLVITLDADLQnPPEEIPRLVERAAQGYDVVG---SIRAERqDSAWRRWPSRLVNL 145
Cdd:TIGR04283  69 LAKGDILLFLHADTR-LPKDFLEAIRRALAKPGYVAgafDLRFDG-PGLLLRLIEWGVNL 126
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
9-145 1.11e-11

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: 63.36  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPELLRRTEAAcleLGRAFEIVLVDDGSRDRSAELLQAAAerdgsavvAVILNRNYGQHAAILAGFE 88
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRL---NPLPLEIIVVDGGSTDGTVAIARSAG--------VVVISSPKGRARQMNAGAA 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1476679192  89 QSRGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIR-AERQDSAWRRWPSRLVNL 145
Cdd:cd02522    70 AARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRlRFDDPGPRLRLLELGANL 127
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
9-142 3.26e-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: 62.60  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPELLRRteaaCLEL---GRAFEIVLVDDGSRDRSAELLQAAAERDgsaVVAVILNRNYGQHAAILA 85
Cdd:cd06439    31 VTIIIPAYNEEAVIEAKLEN----LLALdypRDRLEIIVVSDGSTDGTAEIAREYADKG---VKLLRFPERRGKAAALNR 103
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1476679192  86 GFEQSRGDLVITLDADLQNPPEEIPRLVERAAQ---GYdVVGSIRAERQDSA-------W------RRWPSRL 142
Cdd:cd06439   104 ALALATGEIVVFTDANALLDPDALRLLVRHFADpsvGA-VSGELVIVDGGGSgsgeglyWkyenwlKRAESRL 175
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
9-158 7.93e-11

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: 61.15  E-value: 7.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPEllrrteaaCLE-LGRAF-EIVLVDDGSRDRSAELLQAAaerdgSAVVAVILNRNYGqhAAILAG 86
Cdd:cd02511     2 LSVVIITKNEERNIER--------CLEsVKWAVdEIIVVDSGSTDRTVEIAKEY-----GAKVYQRWWDGFG--AQRNFA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  87 FEQSRGDLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRaeRQDSAWRRW----------PSRLVNLAVQRSTGVAMH 156
Cdd:cd02511    67 LELATNDWVLSLDADERLTPELADEILALLATDDYDGYYVP--RRNFFLGRWirhggwypdrQLRLFRRGKARFEDGRVH 144

                  ..
gi 1476679192 157 DY 158
Cdd:cd02511   145 EQ 146
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
9-101 1.57e-10

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 60.28  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEaslPELLRRTEAACLEL---GRAFEIVLVDDGSRDRsaelLQAAAERDGSAVVAVILNRNYGQHA---A 82
Cdd:cd06421     3 VDVFIPTYNEP---LEIVRKTLRAALAIdypHDKLRVYVLDDGRRPE----LRALAAELGVEYGYRYLTRPDNRHAkagN 75
                          90
                  ....*....|....*....
gi 1476679192  83 ILAGFEQSRGDLVITLDAD 101
Cdd:cd06421    76 LNNALAHTTGDFVAILDAD 94
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
6-171 8.23e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 59.40  E-value: 8.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   6 IDLvSVVIPVYNEEASLPELLRRT-----EAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVV---AVILNRNY 77
Cdd:PTZ00260   70 VDL-SIVIPAYNEEDRLPKMLKETikyleSRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdirLLSLLRNK 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  78 GQHAAILAGFEQSRGDLVITLDADLQNPPEEIPRLVERAAQGYD-----VVGS--IRAERQDSAWRRWPSRLV----NLA 146
Cdd:PTZ00260  149 GKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQnglgiVFGSrnHLVDSDVVAKRKWYRNILmygfHFI 228
                         170       180
                  ....*....|....*....|....*
gi 1476679192 147 VQRSTGVAMHDYGCMLRAYRRSIVE 171
Cdd:PTZ00260  229 VNTICGTNLKDTQCGFKLFTRETAR 253
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
7-142 4.36e-08

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: 53.14  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   7 DLVSVVIPVYNEEASLPELLRrtEAACLELGRaFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRN----YGQHAA 82
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLE--AILAQPYPP-VEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARllgpTGKSRG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1476679192  83 ILAGFEQSRGDLVITLDADLQNPPEEIPRLVERAAQ-GYDVVGSIRAERQDSAWRRWPSRL 142
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSpKVGAVGTPVFSLNRSTMLSALGAL 139
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-118 6.33e-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: 51.41  E-value: 6.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTEAaclELGRAFEIVLVDDGSRDRSAELLqaaaERDGSAVVAVILNRNYGQHAAILAGFEQS 90
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLA---QTYPDFEVIVVDNASTDGSVELL----RELFPEVRLIRNGENLGFGAGNNQGIREA 73
                          90       100
                  ....*....|....*....|....*...
gi 1476679192  91 RGDLVITLDADLQNPPEEIPRLVERAAQ 118
Cdd:cd04186    74 KGDYVLLLNPDTVVEPGALLELLDAAEQ 101
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
9-170 1.49e-07

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: 51.49  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEaslPELLRRTEAACLELGRAfEIVLVDDGSRDRSAELLqAAAERDGSAVvaVILNRNYGQHAAILAGFE 88
Cdd:cd06434     2 VTVIIPVYDED---PDVFRECLRSILRQKPL-EIIVVTDGDDEPYLSIL-SQTVKYGGIF--VITVPHPGKRRALAEGIR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  89 QSRGDLVITLDADLQNPPEEIPRLV---ERAAQGyDVVGSIRAERQDsawRRWPSRLVNLAVQR-----STGVAMHDY-G 159
Cdd:cd06434    75 HVTTDIVVLLDSDTVWPPNALPEMLkpfEDPKVG-GVGTNQRILRPR---DSKWSFLAAEYLERrneeiRAAMSYDGGvP 150
                         170
                  ....*....|....
gi 1476679192 160 CM---LRAYRRSIV 170
Cdd:cd06434   151 CLsgrTAAYRTEIL 164
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
8-101 7.68e-07

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: 49.12  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   8 LVSVVIPVYNeeaSLPELLRRteaaCLELGRA-----FEIVLVDDGSRDRS-AELLQAAAERDGsaVVAVILNR-NYGQH 80
Cdd:cd04184     2 LISIVMPVYN---TPEKYLRE----AIESVRAqtypnWELCIADDASTDPEvKRVLKKYAAQDP--RIKVVFREeNGGIS 72
                          90       100
                  ....*....|....*....|.
gi 1476679192  81 AAILAGFEQSRGDLVITLDAD 101
Cdd:cd04184    73 AATNSALELATGEFVALLDHD 93
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
9-113 2.19e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 48.76  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   9 VSVVIPVYNEEASLPELLRrTEAACLELGRAFEIVLVDDGSRDRSAELLQAAaerdGSAVVA--VILNR---NYGQHAAI 83
Cdd:PRK13915   33 VSVVLPALNEEETVGKVVD-SIRPLLMEPLVDELIVIDSGSTDATAERAAAA----GARVVSreEILPElppRPGKGEAL 107
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1476679192  84 LAGFEQSRGDLVITLDADLQNP-PEEIPRLV 113
Cdd:PRK13915  108 WRSLAATTGDIVVFVDADLINFdPMFVPGLL 138
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
11-142 5.58e-05

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 43.60  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTEAACLELGraFEIVLVDDGSRDRSAELLQAAAER-DGSAVVAVILNRNYGQHAAIlaGF-- 87
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGT--LELSVFNDASTDKSAEIIEKWRKKlEDSGVIVLVGSHNSPSPKGV--GYak 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1476679192  88 ----EQSRGDLVITLDADLQNPPEEIpRLVERAAQGY--DVVG-SIRAERQDSAWR--RWPSRL 142
Cdd:cd06913    77 nqaiAQSSGRYLCFLDSDDVMMPQRI-RLQYEAALQHpnSIIGcQVRRIPEDSTERytRWINTL 139
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
8-107 9.36e-05

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: 43.07  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192   8 LVSVVIPVYNEEASLPELLrrtEAAC-LELGRAFEIVLVDDGSRDRSAELLQAAAER---DGSAVVAVILNRNYGQHA-A 82
Cdd:cd06437     2 MVTVQLPVFNEKYVVERLI---EAACaLDYPKDRLEIQVLDDSTDETVRLAREIVEEyaaQGVNIKHVRRADRTGYKAgA 78
                          90       100
                  ....*....|....*....|....*
gi 1476679192  83 ILAGFEQSRGDLVITLDADLQNPPE 107
Cdd:cd06437    79 LAEGMKVAKGEYVAIFDADFVPPPD 103
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
10-101 1.10e-04

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 42.53  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  10 SVVIPVYNEEASLPELLR----RTeaaclelGRAFEIVLVDDGSRDRSAELLQAAA--------ERDGsavvavilnrny 77
Cdd:cd06433     1 SIITPTYNQAETLEETIDsvlsQT-------YPNIEYIVIDGGSTDGTVDIIKKYEdkitywisEPDK------------ 61
                          90       100
                  ....*....|....*....|....
gi 1476679192  78 GQHAAILAGFEQSRGDLVITLDAD 101
Cdd:cd06433    62 GIYDAMNKGIALATGDIIGFLNSD 85
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
10-101 2.10e-04

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 42.26  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  10 SVVIPVYNEEASlPELLRRTEAACLELGRAFEIVLVDDGSRDRSAELLQAAAERDGSAVVAVILNRNYGQHAAILAGFEQ 89
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDTTYSLAASRNRGTSH 79
                          90
                  ....*....|..
gi 1476679192  90 SRGDLVITLDAD 101
Cdd:pfam10111  80 AIGEYISFIDGD 91
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
11-165 2.81e-04

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: 41.22  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEAslpeLLRRTEAACLELGRAFEIVLVDDGSRDRSAELLQAAAE--------------RDGSAVVaviLNRN 76
Cdd:cd06436     1 VLVPCLNEEA----VIQRTLASLLRNKPNFLVLVIDDASDDDTAGIVRLAITdsrvhllrrhlpnaRTGKGDA---LNAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  77 YGQHAAIL--AGFEQSRgDLVITLDADLQNPpeeiPRLVERAAQGYD---VVGSIRAERQDSAWRRWPSRLVNLAVqRST 151
Cdd:cd06436    74 YDQIRQILieEGADPER-VIIAVIDADGRLD----PNALEAVAPYFSdprVAGTQSRVRMYNRHKNLLTILQDLEF-FII 147
                         170
                  ....*....|....
gi 1476679192 152 GVAMhdygCMLRAY 165
Cdd:cd06436   148 IAAT----QSLRAL 157
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
11-101 5.92e-04

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 40.25  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEeaslPELLRRTEAACLELGR-AFEIVLVDDGSRDRSAELLQAAAERDGSAVVAV-----------ILNRnyg 78
Cdd:cd06420     1 LIITTYNR----PEALELVLKSVLNQSIlPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVwqedegfrkakIRNK--- 73
                          90       100
                  ....*....|....*....|...
gi 1476679192  79 qhaAILAgfeqSRGDLVITLDAD 101
Cdd:cd06420    74 ---AIAA----AKGDYLIFIDGD 89
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
11-136 1.21e-03

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 39.12  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  11 VVIPVYNEEASLPELLRRTeAACLELGRAFEIVLVDDGSRDRSAELLQAAaerdGSAVVAVILNRNYGQHAAILAGFEQS 90
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSL-KAQDYPRELYRIFVVADNCTDDTAQVARAA----GATVLERHDPERRGKGYALDFGFRHL 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1476679192  91 RG-----DLVITLDADLQNPPEEIPRLVERAAQGYDVVGSIRAERQ-DSAWR 136
Cdd:cd06438    76 LNladdpDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNSKNpDDSWI 127
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
10-129 2.07e-03

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 38.84  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  10 SVVIPVYNEEAslPELLRRteaaCLE-----LGRAFEIVLVDDGSRDRSaelLQAAAER--DGSAVVAVILNRNYGQHAA 82
Cdd:cd04195     1 SVLMSVYIKEK--PEFLRE----ALEsilkqTLPPDEVVLVKDGPVTQS---LNEVLEEfkRKLPLKVVPLEKNRGLGKA 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1476679192  83 ILAGFEQSRGDLVITLDADLQNPPEEIPRLVERAAQ--GYDVVGSIRAE 129
Cdd:cd04195    72 LNEGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKnpEIDIVGGGVLE 120
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
10-100 2.08e-03

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 39.49  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476679192  10 SVVIPVYNEEASLpeLLR-------RTEAACLElgrafEIVLVDDGSRDrsAELLQAAAERDGSAVVAVILNRNYGQHAA 82
Cdd:cd02510     1 SVIIIFHNEALST--LLRtvhsvinRTPPELLK-----EIILVDDFSDK--PELKLLLEEYYKKYLPKVKVLRLKKREGL 71
                          90       100
                  ....*....|....*....|.
gi 1476679192  83 I---LAGFEQSRGDLVITLDA 100
Cdd:cd02510    72 IrarIAGARAATGDVLVFLDS 92
 
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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