NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1929625352|gb|QPA16031|]
View 

undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase( domain architecture ID 11484884)

undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-321 0e+00

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


:

Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 675.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   3 EIHPVKKVSVVIPVYNEQESLPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHS 82
Cdd:PRK10714    1 EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 162
Cdd:PRK10714   81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352 163 LRAYRRHIVDAMLHCHERSTFIPILANIFARRAIEIPVHHAEREFGESKYSFMRLINLMYDLVTCLTTTPLRMLSLLGSI 242
Cdd:PRK10714  161 LRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929625352 243 IAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYTDVRARPRYFVQQVIRPSSKEN 321
Cdd:PRK10714  241 IAIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSN 319
 
Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-321 0e+00

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 675.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   3 EIHPVKKVSVVIPVYNEQESLPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHS 82
Cdd:PRK10714    1 EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 162
Cdd:PRK10714   81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352 163 LRAYRRHIVDAMLHCHERSTFIPILANIFARRAIEIPVHHAEREFGESKYSFMRLINLMYDLVTCLTTTPLRMLSLLGSI 242
Cdd:PRK10714  161 LRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929625352 243 IAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYTDVRARPRYFVQQVIRPSSKEN 321
Cdd:PRK10714  241 IAIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSN 319
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
12-188 8.75e-86

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: 255.48  E-value: 8.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEAsQAENSHIVSILLNRNYGQHSAIMAGFSHV 91
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILREL-AARDPRVKVIRLSRNFGQQAALLAGLDHA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  92 TGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIV 171
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170
                  ....*....|....*..
gi 1929625352 172 DAMLHCHERSTFIPILA 188
Cdd:cd04187   160 DALLLLPERHRFLRGLI 176
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
9-221 8.19e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 157.17  E-value: 8.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIRRtttACESLGKEYEILLIDDGSSDNSAHmLVEASQAENSHIVSILLNRNYGQHSAIMAGF 88
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALES---LLAQTYPDFEIIVVDDGSTDGTAE-ILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  89 SHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGkaMGDYGCMLRAYR 167
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSGFRLFR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1929625352 168 RHIVDAmLHCHERSTFIPILANIFAR--RAIEIPVHHAErefGESKYSFMRLINLM 221
Cdd:COG0463   157 REVLEE-LGFDEGFLEDTELLRALRHgfRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
11-172 1.75e-34

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: 123.66  E-value: 1.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  11 SVVIPVYNEQESLPELIRRtttACESLGKEYEILLIDDGSSDNSAHMLVEASQaENSHIVSILLNRNYGQHSAIMAGFSH 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLES---LLNQTYPNFEIIVVDDGSTDGTVEIAEEYAK-KDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  91 VTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSWFRK------TASKMINRLIQRTTGKAMGDYGCML 163
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYrrasriTLSRLPFFLGLRLLGLNLPFLIGGF 156

                  ....*....
gi 1929625352 164 RAYRRHIVD 172
Cdd:pfam00535 157 ALYRREALE 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
10-165 4.13e-07

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: 49.82  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  10 VSVVIPVYNEQESLPELIRRTttacESLGKEYEILLIDDGSSDNSAHMlveASQAENSHIVSillNRNYGQHsaiM-AGF 88
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADL----QALRGDAEVIVVDGGSTDGTVEI---ARSLGAKVIHS---PKGRARQ---MnAGA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  89 SHVTGDLIITLDADL---QNPPEEIPRLVAKadEGYdVVGT--VRQNRQDSWFRKTASKMINRLiqRTTGKAMGDYGCML 163
Cdd:TIGR04283  68 ALAKGDILLFLHADTrlpKDFLEAIRRALAK--PGY-VAGAfdLRFDGPGLLLRLIEWGVNLRS--RLTGIPYGDQGLFV 142

                  ..
gi 1929625352 164 RA 165
Cdd:TIGR04283 143 RR 144
 
Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-321 0e+00

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 675.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   3 EIHPVKKVSVVIPVYNEQESLPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHS 82
Cdd:PRK10714    1 EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 162
Cdd:PRK10714   81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352 163 LRAYRRHIVDAMLHCHERSTFIPILANIFARRAIEIPVHHAEREFGESKYSFMRLINLMYDLVTCLTTTPLRMLSLLGSI 242
Cdd:PRK10714  161 LRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929625352 243 IAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYTDVRARPRYFVQQVIRPSSKEN 321
Cdd:PRK10714  241 IAIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSN 319
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
12-188 8.75e-86

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: 255.48  E-value: 8.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEAsQAENSHIVSILLNRNYGQHSAIMAGFSHV 91
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILREL-AARDPRVKVIRLSRNFGQQAALLAGLDHA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  92 TGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIV 171
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                         170
                  ....*....|....*..
gi 1929625352 172 DAMLHCHERSTFIPILA 188
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 ...
12-185 2.41e-60

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: 190.86  E-value: 2.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRRTTTACESlGKEYEILLIDDGSSDNSAHMLVEAsQAENSHIVSILLNRNYGQHSAIMAGFSHV 91
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVDDGSTDGTAEIAREL-AARVPRVRVIRLSRNFGKGAAVRAGFKAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  92 TGDLIITLDADLQNPPEEIPRLVAKA-DEGYDVVGTVRQNRQ----DSWFRKTASKMINRLIQRTTGKAMGDYGCMLRAY 166
Cdd:cd04179    79 RGDIVVTMDADLQHPPEDIPKLLEKLlEGGADVVIGSRFVRGggagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158
                         170
                  ....*....|....*....
gi 1929625352 167 RRHIVDAMLHCHERSTFIP 185
Cdd:cd04179   159 RREVLEALLSLLESNGFEF 177
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
9-221 8.19e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 157.17  E-value: 8.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIRRtttACESLGKEYEILLIDDGSSDNSAHmLVEASQAENSHIVSILLNRNYGQHSAIMAGF 88
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALES---LLAQTYPDFEIIVVDDGSTDGTAE-ILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  89 SHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGkaMGDYGCMLRAYR 167
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSGFRLFR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1929625352 168 RHIVDAmLHCHERSTFIPILANIFAR--RAIEIPVHHAErefGESKYSFMRLINLM 221
Cdd:COG0463   157 REVLEE-LGFDEGFLEDTELLRALRHgfRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
11-172 1.75e-34

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: 123.66  E-value: 1.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  11 SVVIPVYNEQESLPELIRRtttACESLGKEYEILLIDDGSSDNSAHMLVEASQaENSHIVSILLNRNYGQHSAIMAGFSH 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLES---LLNQTYPNFEIIVVDDGSTDGTVEIAEEYAK-KDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  91 VTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSWFRK------TASKMINRLIQRTTGKAMGDYGCML 163
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYrrasriTLSRLPFFLGLRLLGLNLPFLIGGF 156

                  ....*....
gi 1929625352 164 RAYRRHIVD 172
Cdd:pfam00535 157 ALYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
12-211 1.58e-32

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: 120.33  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRRTTTACEslGKEYEILLIDDGSSDNSAHmLVEASQAENSHIVSILLNRNYGQHSAIMAGFSHV 91
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAE-IVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  92 TGDLIITLDADLQNPPEEIPRLVAKA-DEGYDVV-------GTVRQNRqdSWFRKTASKMINRLIQRTTGKAMGDY--GC 161
Cdd:cd06442    78 RGDVIVVMDADLSHPPEYIPELLEAQlEGGADLVigsryveGGGVEGW--GLKRKLISRGANLLARLLLGRKVSDPtsGF 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352 162 mlRAYRRHIVDAMLhcherSTFIP----ILANIFAR------RAIEIPVHHAEREFGESK 211
Cdd:cd06442   156 --RAYRREVLEKLI-----DSLVSkgykFQLELLVRarrlgyRIVEVPITFVDREHGESK 208
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
12-211 1.61e-28

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: 109.19  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRRTT-TACESLGKEYEILLIDDGSSDNSAHmLVEASQAENSHIVSIL-LNRNYGQHSAIMAGFS 89
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVeYLEERPSFSYEIIVVDDGSKDGTAE-VARKLARKNPALIRVLtLPKNRGKGGAVRAGML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  90 HVTGDLIITLDADLQNPPEEIPRLVAKAD-EGYDVVGTVR------QNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 162
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKtSGYDIAIGSRahlasaAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1929625352 163 LRAYRRHIVDAML-HCH-ERSTF---IPILANIFARRAIEIPVHHaeREFGESK 211
Cdd:cd04188   160 FKLFTRDAARRLFpRLHlERWAFdveLLVLARRLGYPIEEVPVRW--VEIPGSK 211
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
9-211 7.19e-21

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 89.37  E-value: 7.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLP---ELIRRTTTACeslgKEYEILLIDDGSSDNSAHmLVEASQA--ENSHIVSILLNRNYGQHSA 83
Cdd:PLN02726   10 KYSIIVPTYNERLNIAlivYLIFKALQDV----KDFEIIVVDDGSPDGTQD-VVKQLQKvyGEDRILLRPRPGKLGLGTA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  84 IMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVV-GT--VRQNRQDSW--FRKTASKMINRLIQRTTGKAMG 157
Cdd:PLN02726   85 YIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVtGTryVKGGGVHGWdlRRKLTSRGANVLAQTLLWPGVS 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1929625352 158 DYGCMLRAYRRHIVDAMLH-CHERSTFIPILANIFARRA----IEIPVHHAEREFGESK 211
Cdd:PLN02726  165 DLTGSFRLYKRSALEDLVSsVVSKGYVFQMEIIVRASRKgyriEEVPITFVDRVYGESK 223
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
9-283 5.94e-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: 88.26  E-value: 5.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIRrtttACESL---GKEYEILLIDDGSSDNSAHmLVEASQAENSHIVSILLNRNYGQHSAIM 85
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLR----SLLAQdypKEKLEVIVVDDGSTDETAE-IARELAAEYPRVRVIERPENGGKAAALN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  86 AGFSHVTGDLIITLDADLQNPPEEIPRLVAK-ADEGYDVVGTVrqnrqdSWFRKTASKMINRLIQRTTGkamGDYGCMLR 164
Cdd:COG1215   105 AGLKAARGDIVVFLDADTVLDPDWLRRLVAAfADPGVGASGAN------LAFRREALEEVGGFDEDTLG---EDLDLSLR 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352 165 AYRR-----HIVDAMLHCHERSTFIPILANIF--ARRAIEIPVHHAEREFGESKYSFMRLInlmydlvtcltTTPLRMLS 237
Cdd:COG1215   176 LLRAgyrivYVPDAVVYEEAPETLRALFRQRRrwARGGLQLLLKHRPLLRPRRLLLFLLLL-----------LLPLLLLL 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1929625352 238 LLGSIIAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGA 283
Cdd:COG1215   245 LLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAA 290
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
12-127 7.24e-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: 79.09  E-value: 7.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRRtttACESLGKEYEILLIDDGSSDNSAHmLVEASQAENSHIVSILLNRNYGQHSAIMAGFSHV 91
Cdd:cd00761     1 VIIPAYNEEPYLERCLES---LLAQTYPNFEVIVVDDGSTDGTLE-ILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1929625352  92 TGDLIITLDADLQNPPEEIPRLVA--KADEGYDVVGTV 127
Cdd:cd00761    77 RGEYILFLDADDLLLPDWLERLVAelLADPEADAVGGP 114
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
12-173 1.25e-16

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: 76.50  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRRtttACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHSAIMAGFSHV 91
Cdd:cd06423     1 IIVPAYNEEAVIERTIES---LLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  92 TGDLIITLDADLQNPPEEIPRLVAKADEGYDVV---GTVR-QNRQDSWFRKTAS---KMINRLIQRTTGkAMGDYGCM-- 162
Cdd:cd06423    78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGavqGRVRvRNGSENLLTRLQAieyLSIFRLGRRAQS-ALGGVLVLsg 156
                         170
                  ....*....|..
gi 1929625352 163 -LRAYRRHIVDA 173
Cdd:cd06423   157 aFGAFRREALRE 168
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
12-141 4.35e-13

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: 67.70  E-value: 4.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIRrtTTACESLGKE-YEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNR--NYGQHSAIMAGF 88
Cdd:cd04192     1 VVIAARNEAENLPRLLQ--SLSALDYPKEkFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRvsISGKKNALTTAI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929625352  89 SHVTGDLIITLDADLQNPPEEIPRLVAKADEG--YDVVGTVRQNRQDSWFRKTAS 141
Cdd:cd04192    79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEqiGLVAGPVIYFKGKSLLAKFQR 133
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
11-240 3.38e-12

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 66.33  E-value: 3.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  11 SVVIPVYNEQESLPELIRRTTTACESLGKE-----YEILLIDDGSSDNSAHM---LVEASQAENSHIVSILLNRNYGQHS 82
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKYLESRSRKdpkfkYEIIIVNDGSKDKTLKVakdFWRQNINPNIDIRLLSLLRNKGKGG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYD-----VVGTVRQNRQD------SWFRKTASKMINRLIQRT 151
Cdd:PTZ00260  153 AVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQnglgiVFGSRNHLVDSdvvakrKWYRNILMYGFHFIVNTI 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352 152 TGKAMGDYGCMLRAYRRH---IVDAMLHChERSTF---IPILANIFARRAIEIPVHHAEREfGESKYSFMRLINLMYDLV 225
Cdd:PTZ00260  233 CGTNLKDTQCGFKLFTREtarIIFPSLHL-ERWAFdieIVMIAQKLNLPIAEVPVNWTEVE-GSKLNVISASIQMARDIL 310
                         250
                  ....*....|....*
gi 1929625352 226 TcltttpLRMLSLLG 240
Cdd:PTZ00260  311 L------VRSFYLLG 319
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-117 3.56e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 64.24  E-value: 3.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIRrttTACESLGKEYEILLIDDGSSDNSAHMLvEASQAENSHIVSILLNRNYGqhSAIMAGF 88
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLE---SLLAQTYPPFEVIVVDNGSTDGTAELL-AALAFPRVRVIRNPENLGFA--AARNLGL 77
                          90       100
                  ....*....|....*....|....*....
gi 1929625352  89 SHVTGDLIITLDADLQNPPEEIPRLVAKA 117
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLERLLAAA 106
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
9-141 5.58e-12

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: 64.56  E-value: 5.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIrrtttacESL------GKEYEILLIDDGSSDNSAHmLVEASQAENSHIVsILLNRNYGQHS 82
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELL-------ESLlnqsypKDLIEIIVVDGGSTDGTRE-IVQEYAAKDPRIR-LIDNPKRIQSA 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKA-DEGYDVVGTVRQNRQDSWFRKTAS 141
Cdd:cd02525    72 GLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALkRTGADNVGGPMETIGESKFQKAIA 131
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
10-179 4.51e-11

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: 61.89  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  10 VSVVIPVYNEQeslPELIRRTTTACESLgKEYEILLIDDGSSDNSAHMLveaSQAENSHIVSILLNRNYGQHSAIMAGFS 89
Cdd:cd06434     2 VTVIIPVYDED---PDVFRECLRSILRQ-KPLEIIVVTDGDDEPYLSIL---SQTVKYGGIFVITVPHPGKRRALAEGIR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  90 HVTGDLIITLDADLQNPPEEIPRLVA-KADEGYDVVGT---VRQNRQDSWFRKTASKM-INRLIQRTTGKAMGDYGCM-- 162
Cdd:cd06434    75 HVTTDIVVLLDSDTVWPPNALPEMLKpFEDPKVGGVGTnqrILRPRDSKWSFLAAEYLeRRNEEIRAAMSYDGGVPCLsg 154
                         170
                  ....*....|....*...
gi 1929625352 163 -LRAYRRHIVDAMLHCHE 179
Cdd:cd06434   155 rTAAYRTEILKDFLFLEE 172
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
9-134 2.08e-09

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 57.21  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIrRTTTACESLGKEYEILLIDDGSSDNSAHmLVEASQAENSHIVSILLNRnyGQHSAIMAGF 88
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKL-ENLLALDYPRDRLEIIVVSDGSTDGTAE-IAREYADKGVKLLRFPERR--GKAAALNRAL 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1929625352  89 SHVTGDLIITLDADLQNPPEEIPRLVAK-ADEGYDVV-GTVRQNRQDS 134
Cdd:cd06439   106 ALATGEIVVFTDANALLDPDALRLLVRHfADPSVGAVsGELVIVDGGG 153
PRK10073 PRK10073
putative glycosyl transferase; Provisional
9-117 3.68e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 56.98  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPE----LIRRTTTAceslgkeYEILLIDDGSSDNSAHMLveASQAENSHIVSILLNRNYGQHSAI 84
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAfmesLIAQTWTA-------LEIIIVNDGSTDNSVEIA--KHYAENYPHVRLLHQANAGVSVAR 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1929625352  85 MAGFSHVTGDLIITLDADLQNPPEEIPRLVAKA 117
Cdd:PRK10073   78 NTGLAVATGKYVAFPDADDVVYPTMYETLMTMA 110
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
10-165 3.89e-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: 52.96  E-value: 3.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  10 VSVVIPVYNEQESLPELIRrttTACESLGKEYEILLIDDGSSDNSahmlVEASQAENSHIVSILLNRNYGQHsaimAGFS 89
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLA---SLRRLNPLPLEIIVVDGGSTDGT----VAIARSAGVVVISSPKGRARQMN----AGAA 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929625352  90 HVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQN-RQDSWFRKTASKMIN-RLiqRTTGKAMGDYGCMLRA 165
Cdd:cd02522    70 AARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRfDDPGPRLRLLELGANlRS--RLFGLPYGDQGLFIRR 145
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
9-153 6.95e-08

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: 52.29  E-value: 6.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIRRTTTACEslgkeyEILLIDDGSSDNSahmlVEASQAENSHIVSIlLNRNYGqhSAIMAGF 88
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRT----VEIAKEYGAKVYQR-WWDGFG--AQRNFAL 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929625352  89 SHVTGDLIITLDAD------LQnppEEIPRLvaKADEGYDVVGTVRQNR-QDSWFRKT--ASKMINRLIQRTTG 153
Cdd:cd02511    68 ELATNDWVLSLDADerltpeLA---DEILAL--LATDDYDGYYVPRRNFfLGRWIRHGgwYPDRQLRLFRRGKA 136
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
9-102 2.14e-07

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: 51.03  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQeslPELIRRTTTACESL---GKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYgQHSAIM 85
Cdd:cd06421     2 TVDVFIPTYNEP---LEIVRKTLRAALAIdypHDKLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHA-KAGNLN 77
                          90
                  ....*....|....*..
gi 1929625352  86 AGFSHVTGDLIITLDAD 102
Cdd:cd06421    78 NALAHTTGDFVAILDAD 94
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
10-165 4.13e-07

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: 49.82  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  10 VSVVIPVYNEQESLPELIRRTttacESLGKEYEILLIDDGSSDNSAHMlveASQAENSHIVSillNRNYGQHsaiM-AGF 88
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADL----QALRGDAEVIVVDGGSTDGTVEI---ARSLGAKVIHS---PKGRARQ---MnAGA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  89 SHVTGDLIITLDADL---QNPPEEIPRLVAKadEGYdVVGT--VRQNRQDSWFRKTASKMINRLiqRTTGKAMGDYGCML 163
Cdd:TIGR04283  68 ALAKGDILLFLHADTrlpKDFLEAIRRALAK--PGY-VAGAfdLRFDGPGLLLRLIEWGVNLRS--RLTGIPYGDQGLFV 142

                  ..
gi 1929625352 164 RA 165
Cdd:TIGR04283 143 RR 144
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
11-102 2.68e-06

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: 48.04  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  11 SVVIPVYNEQESlPELIRRTTTACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHSAIMAGFSH 90
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDTTYSLAASRNRGTSH 79
                          90
                  ....*....|..
gi 1929625352  91 VTGDLIITLDAD 102
Cdd:pfam10111  80 AIGEYISFIDGD 91
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
10-134 7.10e-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: 46.21  E-value: 7.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  10 VSVVIPVYNEQESLPELIRrtttacESLGKEY---EILLIDDGSSDNSAHMLVEASQA-ENSHIVSILLNRNYGQHSAIM 85
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLE------AILAQPYppvEVVVVVNPSDAETLDVAEEIAARfPDVRLRVIRNARLLGPTGKSR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1929625352  86 A---GFSHVTGDLIITLDADLQNPPEEIPRLVAKAD-EGYDVVGTVRQNRQDS 134
Cdd:pfam13641  78 GlnhGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDsPKVGAVGTPVFSLNRS 130
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
12-119 7.98e-06

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: 45.24  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEqeslPELIRRTttaCESL----GKEYEILLIDDGSSDNSahmlVEASQAENSHIVSILLNRNYGQHSAIMAG 87
Cdd:cd04186     1 IIIVNYNS----LEYLKAC---LDSLlaqtYPDFEVIVVDNASTDGS----VELLRELFPEVRLIRNGENLGFGAGNNQG 69
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1929625352  88 FSHVTGDLIITLDADLQNPPEEIPRLVAKADE 119
Cdd:cd04186    70 IREAKGDYVLLLNPDTVVEPGALLELLDAAEQ 101
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
10-120 1.11e-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: 45.76  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  10 VSVVIPVYNEQESLPELIRrttTACE-SLGKE-YEILLIDDgSSDNSAHMLVEASQAENSHIVSILL----NRNYGQHSA 83
Cdd:cd06437     3 VTVQLPVFNEKYVVERLIE---AACAlDYPKDrLEIQVLDD-STDETVRLAREIVEEYAAQGVNIKHvrraDRTGYKAGA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1929625352  84 IMAGFSHVTGDLIITLDADLQNPPE---EIPRLVAKADEG 120
Cdd:cd06437    79 LAEGMKVAKGEYVAIFDADFVPPPDflqKTPPYFADPKLG 118
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
9-115 2.11e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 45.29  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYNEQESLPELIrrtTTACESLGKEY--EILLIDDGSSDNSAHMLVEA-----SQAEnshIVSiLLNRNYGQH 81
Cdd:PRK13915   32 TVSVVLPALNEEETVGKVV---DSIRPLLMEPLvdELIVIDSGSTDATAERAAAAgarvvSREE---ILP-ELPPRPGKG 104
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1929625352  82 SAIMAGFSHVTGDLIITLDADLQNP-PEEIPRLVA 115
Cdd:PRK13915  105 EALWRSLAATTGDIVVFVDADLINFdPMFVPGLLG 139
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
9-102 2.16e-05

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: 44.50  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352   9 KVSVVIPVYN-EQESLPELIRrttTACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHSAIMAG 87
Cdd:cd04184     2 LISIVMPVYNtPEKYLREAIE---SVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSA 78
                          90
                  ....*....|....*
gi 1929625352  88 FSHVTGDLIITLDAD 102
Cdd:cd04184    79 LELATGEFVALLDHD 93
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
11-150 1.82e-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: 41.76  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  11 SVVIPVYNEQESLPELIRrtttaceSL----GKEYEILLIDDGSSDNSaHMLVEASQAENSHIVSillNRNYGQHSAIMA 86
Cdd:cd06433     1 SIITPTYNQAETLEETID-------SVlsqtYPNIEYIVIDGGSTDGT-VDIIKKYEDKITYWIS---EPDKGIYDAMNK 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  87 GFSHVTGDLIITLDAD---LQNPPEEIPRLVAKADEGYDVVGTVR---QNRQDSWFRKTASKMINRLIQR 150
Cdd:cd06433    70 GIALATGDIIGFLNSDdtlLPGALLAVVAAFAEHPEVDVVYGDVLlvdENGRVIGRRRPPPFLDKFLLYG 139
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
11-126 6.23e-04

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: 40.38  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  11 SVVIPVYNEQEslPELIRRtttACESLGKEY----EILLIDDGSSDNSAHMLVEaSQAENSHIVSILLNRNYGQHSAIMA 86
Cdd:cd04195     1 SVLMSVYIKEK--PEFLRE---ALESILKQTlppdEVVLVKDGPVTQSLNEVLE-EFKRKLPLKVVPLEKNRGLGKALNE 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1929625352  87 GFSHVTGDLIITLDADLQNPPEEIPRLVA--KADEGYDVVGT 126
Cdd:cd04195    75 GLKHCTYDWVARMDTDDISLPDRFEKQLDfiEKNPEIDIVGG 116
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
11-101 4.13e-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: 38.34  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  11 SVVIPVYNEQESLpeLIRRTTTACESLGKEY--EILLIDDGsSDNSAHMLVEASQAEN-SHIVSIL-LNRNYGQHSAIMA 86
Cdd:cd02510     1 SVIIIFHNEALST--LLRTVHSVINRTPPELlkEIILVDDF-SDKPELKLLLEEYYKKyLPKVKVLrLKKREGLIRARIA 77
                          90
                  ....*....|....*
gi 1929625352  87 GFSHVTGDLIITLDA 101
Cdd:cd02510    78 GARAATGDVLVFLDS 92
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
12-150 8.09e-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: 36.81  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929625352  12 VVIPVYNEQESLPELIrRTTTACESLGKEYEILLIDDGSSDNSAHmLVEASQAenshivsILLNRN----YGQHSAIMAG 87
Cdd:cd06438     1 ILIPAHNEEAVIGNTV-RSLKAQDYPRELYRIFVVADNCTDDTAQ-VARAAGA-------TVLERHdperRGKGYALDFG 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929625352  88 FSHVTG-----DLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQ--NRQDSW---FRKTASKMINRLIQR 150
Cdd:cd06438    72 FRHLLNladdpDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNskNPDDSWitrLYAFAFLVFNRLRPL 144
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH