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Conserved domains on  [gi|556485319|ref|WP_023333737|]
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MULTISPECIES: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase [Enterobacter]

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

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List of domain hits

Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-327 0e+00

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


:

Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 656.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   3 SAPPVQKVSVVIPVYNEQESLPELIRRTTAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNYGQHS 82
Cdd:PRK10714   1 EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSLFRKLASRTINRLIQRTTGKAMGDYGCM 162
Cdd:PRK10714  81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319 163 LRAYRRHIVDAMLHCHERSTFIPILANTFARKATEIPVLHAEREHGESKYSFMRLINLMYDLITCLTTTPLRLLSVFGSI 242
Cdd:PRK10714 161 LRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319 243 IAVAGFALSVLLVVLRLVFGPQWAAEGVFMLFAVLFMFIGAQFVGMGLLGEYIGRIYNDVRARPRYFIQRVVRQEHKASQ 322
Cdd:PRK10714 241 IAIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSNN 320

                 ....*
gi 556485319 323 EEIHP 327
Cdd:PRK10714 321 EKENE 325
 
Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-327 0e+00

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 656.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   3 SAPPVQKVSVVIPVYNEQESLPELIRRTTAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNYGQHS 82
Cdd:PRK10714   1 EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSLFRKLASRTINRLIQRTTGKAMGDYGCM 162
Cdd:PRK10714  81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319 163 LRAYRRHIVDAMLHCHERSTFIPILANTFARKATEIPVLHAEREHGESKYSFMRLINLMYDLITCLTTTPLRLLSVFGSI 242
Cdd:PRK10714 161 LRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319 243 IAVAGFALSVLLVVLRLVFGPQWAAEGVFMLFAVLFMFIGAQFVGMGLLGEYIGRIYNDVRARPRYFIQRVVRQEHKASQ 322
Cdd:PRK10714 241 IAIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSNN 320

                 ....*
gi 556485319 323 EEIHP 327
Cdd:PRK10714 321 EKENE 325
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
12-188 3.18e-84

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


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 252.01  E-value: 3.18e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRRTTAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEgSHIVAVLLNRNYGQHSAIMAGFSHV 91
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARD-PRVKVIRLSRNFGQQAALLAGLDHA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  92 TGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSLFRKLASRTINRLIQRTTGKAMGDYGCMLRAYRRHIV 171
Cdd:cd04187   80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170
                 ....*....|....*..
gi 556485319 172 DAMLHCHERSTFIPILA 188
Cdd:cd04187  160 DALLLLPERHRFLRGLI 176
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
9-221 1.49e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 156.40  E-value: 1.49e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQESLPELIRRTTAACdtmGKAYEILLVDDGSSDNSALMLTEAAqAEGSHIVAVLLNRNYGQHSAIMAGF 88
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQT---YPDFEIIVVDDGSTDGTAEILRELA-AKDPRIRVIRLERNRGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  89 SHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSLFRKLASRTINRLIQRTTGkaMGDYGCMLRAYR 167
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSGFRLFR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556485319 168 RHIVDAMLHCHERSTFIPIL-ANTFARKATEIPVLHAErehGESKYSFMRLINLM 221
Cdd:COG0463  157 REVLEELGFDEGFLEDTELLrALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
11-172 1.36e-33

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: 121.35  E-value: 1.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   11 SVVIPVYNEQESLPELIRrttAACDTMGKAYEILLVDDGSSDNSALMLTEAAQaEGSHIVAVLLNRNYGQHSAIMAGFSH 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLE---SLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAK-KDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   91 VTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSLFRK------LASRTINRLIQRTTGKAMGDYGCML 163
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYrrasriTLSRLPFFLGLRLLGLNLPFLIGGF 156

                  ....*....
gi 556485319  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 ...
10-153 2.55e-08

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: 53.67  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   10 VSVVIPVYNEQESLPELIRRtTAACDTmgkAYEILLVDDGSSDNSAlmltEAAQAEGSHIV------AVLLNrnygqhsa 83
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRG---DAEVIVVDGGSTDGTV----EIARSLGAKVIhspkgrARQMN-------- 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556485319   84 imAGFSHVTGDLIITLDADL---QNPPEEIPRLVAKadEGYdVVGT--VRQNRQDSLFRkLASRTIN---RLIQRTTG 153
Cdd:TIGR04283  65 --AGAALAKGDILLFLHADTrlpKDFLEAIRRALAK--PGY-VAGAfdLRFDGPGLLLR-LIEWGVNlrsRLTGIPYG 136
 
Name Accession Description Interval E-value
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-327 0e+00

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 656.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   3 SAPPVQKVSVVIPVYNEQESLPELIRRTTAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNYGQHS 82
Cdd:PRK10714   1 EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSLFRKLASRTINRLIQRTTGKAMGDYGCM 162
Cdd:PRK10714  81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319 163 LRAYRRHIVDAMLHCHERSTFIPILANTFARKATEIPVLHAEREHGESKYSFMRLINLMYDLITCLTTTPLRLLSVFGSI 242
Cdd:PRK10714 161 LRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLLGSI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319 243 IAVAGFALSVLLVVLRLVFGPQWAAEGVFMLFAVLFMFIGAQFVGMGLLGEYIGRIYNDVRARPRYFIQRVVRQEHKASQ 322
Cdd:PRK10714 241 IAIGGFSLAVLLVVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRPSSTSNN 320

                 ....*
gi 556485319 323 EEIHP 327
Cdd:PRK10714 321 EKENE 325
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
12-188 3.18e-84

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


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 252.01  E-value: 3.18e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRRTTAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEgSHIVAVLLNRNYGQHSAIMAGFSHV 91
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARD-PRVKVIRLSRNFGQQAALLAGLDHA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  92 TGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSLFRKLASRTINRLIQRTTGKAMGDYGCMLRAYRRHIV 171
Cdd:cd04187   80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170
                 ....*....|....*..
gi 556485319 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 3.34e-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: 3.34e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRRTTAACDTmGKAYEILLVDDGSSDNSALMLTEAAqAEGSHIVAVLLNRNYGQHSAIMAGFSHV 91
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVDDGSTDGTAEIARELA-ARVPRVRVIRLSRNFGKGAAVRAGFKAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  92 TGDLIITLDADLQNPPEEIPRLVAKA-DEGYDVVGTVRQNRQ----DSLFRKLASRTINRLIQRTTGKAMGDYGCMLRAY 166
Cdd:cd04179   79 RGDIVVTMDADLQHPPEDIPKLLEKLlEGGADVVIGSRFVRGggagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158
                        170
                 ....*....|....*....
gi 556485319 167 RRHIVDAMLHCHERSTFIP 185
Cdd:cd04179  159 RREVLEALLSLLESNGFEF 177
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
9-221 1.49e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 156.40  E-value: 1.49e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQESLPELIRRTTAACdtmGKAYEILLVDDGSSDNSALMLTEAAqAEGSHIVAVLLNRNYGQHSAIMAGF 88
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQT---YPDFEIIVVDDGSTDGTAEILRELA-AKDPRIRVIRLERNRGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  89 SHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSLFRKLASRTINRLIQRTTGkaMGDYGCMLRAYR 167
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSGFRLFR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556485319 168 RHIVDAMLHCHERSTFIPIL-ANTFARKATEIPVLHAErehGESKYSFMRLINLM 221
Cdd:COG0463  157 REVLEELGFDEGFLEDTELLrALRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
12-211 5.90e-36

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: 129.58  E-value: 5.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRRTTAACDtmGKAYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNyGQHSAIMAGFSHV 91
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKR-GLGSAYIEGFKAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  92 TGDLIITLDADLQNPPEEIPRLVAKA-DEGYDVV-------GTVRQNRqdSLFRKLASRTINRLIQRTTGKAMGDY--GC 161
Cdd:cd06442   78 RGDVIVVMDADLSHPPEYIPELLEAQlEGGADLVigsryveGGGVEGW--GLKRKLISRGANLLARLLLGRKVSDPtsGF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556485319 162 mlRAYRRHIVDAMLHcHERST----FIPILANTFARKAT--EIPVLHAEREHGESK 211
Cdd:cd06442  156 --RAYRREVLEKLID-SLVSKgykfQLELLVRARRLGYRivEVPITFVDREHGESK 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
11-172 1.36e-33

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: 121.35  E-value: 1.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   11 SVVIPVYNEQESLPELIRrttAACDTMGKAYEILLVDDGSSDNSALMLTEAAQaEGSHIVAVLLNRNYGQHSAIMAGFSH 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLE---SLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAK-KDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   91 VTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQDSLFRK------LASRTINRLIQRTTGKAMGDYGCML 163
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYrrasriTLSRLPFFLGLRLLGLNLPFLIGGF 156

                  ....*....
gi 556485319  164 RAYRRHIVD 172
Cdd:pfam00535 157 ALYRREALE 165
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
12-200 2.04e-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: 2.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRRTTAACD-TMGKAYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNYGQHSAIMAGFSH 90
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEeRPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGKGGAVRAGMLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  91 VTGDLIITLDADLQNPPEEIPRLVAKAD-EGYDVVGTVR------QNRQDSLFRKLASRTINRLIQRTTGKAMGDYGCML 163
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEALKtSGYDIAIGSRahlasaAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCGF 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 556485319 164 RAYRRHIVDAML-HCH-ERSTF---IPILANTFARKATEIPV 200
Cdd:cd04188  161 KLFTRDAARRLFpRLHlERWAFdveLLVLARRLGYPIEEVPV 202
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
9-211 3.84e-23

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 95.92  E-value: 3.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQESLP---ELIRRTTAACdtmgKAYEILLVDDGSSDNSALMLTEAAQAEG-SHIVAVLLNRNYGQHSAI 84
Cdd:PLN02726  10 KYSIIVPTYNERLNIAlivYLIFKALQDV----KDFEIIVVDDGSPDGTQDVVKQLQKVYGeDRILLRPRPGKLGLGTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  85 MAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGTVRQNRQD-----SLFRKLASRTINRLIQRTTGKAMGD 158
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVTGTRYVKGGgvhgwDLRRKLTSRGANVLAQTLLWPGVSD 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556485319 159 YGCMLRAYRRHIVDAMLH-CHERS-TF---IPILANTFARKATEIPVLHAEREHGESK 211
Cdd:PLN02726 166 LTGSFRLYKRSALEDLVSsVVSKGyVFqmeIIVRASRKGYRIEEVPITFVDRVYGESK 223
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
3-283 3.37e-19

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: 86.33  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   3 SAPPVQKVSVVIPVYNEQESLPELIRRTTAAcDTMGKAYEILLVDDGSSDNSALMLtEAAQAEGSHIVAVLLNRNYGQHS 82
Cdd:COG1215   24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQ-DYPKEKLEVIVVDDGSTDETAEIA-RELAAEYPRVRVIERPENGGKAA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAK-ADEGYDVVGTVrqnrqdSLFRKLASRTINRLIQRTTGkamGDYGC 161
Cdd:COG1215  102 ALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAfADPGVGASGAN------LAFRREALEEVGGFDEDTLG---EDLDL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319 162 MLRAYRR-----HIVDAMLHCHERSTFIPILA--NTFARKATEIPVLHAEREHGESKYSFMRLInlmydlitcltTTPLR 234
Cdd:COG1215  173 SLRLLRAgyrivYVPDAVVYEEAPETLRALFRqrRRWARGGLQLLLKHRPLLRPRRLLLFLLLL-----------LLPLL 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 556485319 235 LLSVFGSIIAVAGFALSVLLVVLRLVFGPQWAAEGVFMLFAVLFMFIGA 283
Cdd:COG1215  242 LLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAA 290
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
12-173 4.57e-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: 80.35  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRrttAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNYGQHSAIMAGFSHV 91
Cdd:cd06423    1 IIVPAYNEEAVIERTIE---SLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  92 TGDLIITLDADLQNPPEEIPRLVAKADEGYDVV---GTVR-QNRQDSLFRKLAS---RTINRLIQRTTGkAMGDYGCM-- 162
Cdd:cd06423   78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGavqGRVRvRNGSENLLTRLQAieyLSIFRLGRRAQS-ALGGVLVLsg 156
                        170
                 ....*....|..
gi 556485319 163 -LRAYRRHIVDA 173
Cdd:cd06423  157 aFGAFRREALRE 168
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
12-127 1.30e-17

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: 78.70  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRRTTAACDtmgKAYEILLVDDGSSDNSALMLtEAAQAEGSHIVAVLLNRNYGQHSAIMAGFSHV 91
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTY---PNFEVIVVDDGSTDGTLEIL-EEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 556485319  92 TGDLIITLDADLQNPPEEIPRLVA--KADEGYDVVGTV 127
Cdd:cd00761   77 RGEYILFLDADDLLLPDWLERLVAelLADPEADAVGGP 114
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-117 4.27e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 66.94  E-value: 4.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQESLPELIRrttAACDTMGKAYEILLVDDGSSDNSALMLtEAAQAEGSHIVAVLLNRNYGqhSAIMAGF 88
Cdd:COG1216    4 KVSVVIPTYNRPELLRRCLE---SLLAQTYPPFEVIVVDNGSTDGTAELL-AALAFPRVRVIRNPENLGFA--AARNLGL 77
                         90       100
                 ....*....|....*....|....*....
gi 556485319  89 SHVTGDLIITLDADLQNPPEEIPRLVAKA 117
Cdd:COG1216   78 RAAGGDYLLFLDDDTVVEPDWLERLLAAA 106
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
12-141 5.01e-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: 67.31  E-value: 5.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIRrTTAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNR--NYGQHSAIMAGFS 89
Cdd:cd04192    1 VVIAARNEAENLPRLLQ-SLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRvsISGKKNALTTAIK 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556485319  90 HVTGDLIITLDADLQNPPEEIPRLVAKADEG--YDVVGTVRQNRQDSLFRKLAS 141
Cdd:cd04192   80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEqiGLVAGPVIYFKGKSLLAKFQR 133
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
9-134 8.11e-13

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: 67.22  E-value: 8.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQESLPELIrRTTAACDTMGKAYEILLVDDGSSDNSAlmltEAAQAEGSHIVAVLLN-RNYGQHSAIMAG 87
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKL-ENLLALDYPRDRLEIIVVSDGSTDGTA----EIAREYADKGVKLLRFpERRGKAAALNRA 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 556485319  88 FSHVTGDLIITLDADLQNPPEEIPRLVAK-ADEGYDVV-GTVRQNRQDS 134
Cdd:cd06439  105 LALATGEIVVFTDANALLDPDALRLLVRHfADPSVGAVsGELVIVDGGG 153
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
10-179 1.07e-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: 63.81  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  10 VSVVIPVYNEQeslPELIRRTTAACDTMGKAyEILLVDDGSSDNSALMLTEAAQAEGshiVAVLLNRNYGQHSAIMAGFS 89
Cdd:cd06434    2 VTVIIPVYDED---PDVFRECLRSILRQKPL-EIIVVTDGDDEPYLSILSQTVKYGG---IFVITVPHPGKRRALAEGIR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  90 HVTGDLIITLDADLQNPPEEIPRLVAK-ADEGYDVVGTvRQNRQDSLFRKLASRTINRL-----IQRTTGKAMGDYGCM- 162
Cdd:cd06434   75 HVTTDIVVLLDSDTVWPPNALPEMLKPfEDPKVGGVGT-NQRILRPRDSKWSFLAAEYLerrneEIRAAMSYDGGVPCLs 153
                        170
                 ....*....|....*....
gi 556485319 163 --LRAYRRHIVDAMLHCHE 179
Cdd:cd06434  154 grTAAYRTEILKDFLFLEE 172
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
9-138 4.58e-11

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: 61.86  E-value: 4.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQESLPELIrRTTAACDTMGKAYEILLVDDGSSDNSALMLTEAAQAEGshIVAVLLNRNYGQHSAIMAGF 88
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELL-ESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDP--RIRLIDNPKRIQSAGLNIGI 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556485319  89 SHVTGDLIITLDADLQNPPEEIPRLVAKA-DEGYDVVGTVRQNRQDSLFRK 138
Cdd:cd02525   78 RNSRGDIIIRVDAHAVYPKDYILELVEALkRTGADNVGGPMETIGESKFQK 128
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
9-131 5.85e-10

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: 58.45  E-value: 5.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQESLPELIRRTTAACDtmgkayEILLVDDGSSDNSAlmltEAAQAEGSHIVAVlLNRNYGqhSAIMAGF 88
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTV----EIAKEYGAKVYQR-WWDGFG--AQRNFAL 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 556485319  89 SHVTGDLIITLDAD------LQnppEEIPRLvaKADEGYDVVGTVRQNR 131
Cdd:cd02511   68 ELATNDWVLSLDADerltpeLA---DEILAL--LATDDYDGYYVPRRNF 111
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-117 2.56e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 57.75  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   1 MFSAPPvqKVSVVIPVYNEQESLPE----LIRRTTAAcdtmgkaYEILLVDDGSSDNSALMLTEAAQaEGSHiVAVLLNR 76
Cdd:PRK10073   1 MMNSTP--KLSIIIPLYNAGKDFRAfmesLIAQTWTA-------LEIIIVNDGSTDNSVEIAKHYAE-NYPH-VRLLHQA 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 556485319  77 NYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKA 117
Cdd:PRK10073  70 NAGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMA 110
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
11-205 4.85e-09

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 56.70  E-value: 4.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  11 SVVIPVYNEQESLPELIRRTTAACDTMGK-----AYEILLVDDGSSDNS---ALMLTEAAQAEGSHIVAVLLNRNYGQHS 82
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETIKYLESRSRkdpkfKYEIIIVNDGSKDKTlkvAKDFWRQNINPNIDIRLLSLLRNKGKGG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  83 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLvakadegYDVVGTVRQNRQDSLFrklASRTINRLiqrttgkamgDYGCM 162
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADGATDIDDFDKL-------EDIMLKIEQNGLGIVF---GSRNHLVD----------SDVVA 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556485319 163 LRAYRRHIVDAMLHchersTFIPILANT-----------FARKATEI--PVLHAER 205
Cdd:PTZ00260 213 KRKWYRNILMYGFH-----FIVNTICGTnlkdtqcgfklFTRETARIifPSLHLER 263
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
10-108 8.71e-09

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: 54.88  E-value: 8.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  10 VSVVIPVYNEQESLPELIRRTTAAcdtMGKAYEILLVDDGSSDNSAlmltEAAQAEGSHIV------AVLLNrnygqhsa 83
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRL---NPLPLEIIVVDGGSTDGTV----AIARSAGVVVIsspkgrARQMN-------- 65
                         90       100
                 ....*....|....*....|....*
gi 556485319  84 imAGFSHVTGDLIITLDADLQNPPE 108
Cdd:cd02522   66 --AGAAAARGDWLLFLHADTRLPPD 88
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
9-102 9.02e-09

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: 54.89  E-value: 9.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYNEQeslPELIRRTTAACDTM---GKAYEILLVDDGSSDNSAlmltEAAQAEGSHIVAVLLNRNYGQHS--- 82
Cdd:cd06421    2 TVDVFIPTYNEP---LEIVRKTLRAALAIdypHDKLRVYVLDDGRRPELR----ALAAELGVEYGYRYLTRPDNRHAkag 74
                         90       100
                 ....*....|....*....|
gi 556485319  83 AIMAGFSHVTGDLIITLDAD 102
Cdd:cd06421   75 NLNNALAHTTGDFVAILDAD 94
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
10-153 2.55e-08

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: 53.67  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   10 VSVVIPVYNEQESLPELIRRtTAACDTmgkAYEILLVDDGSSDNSAlmltEAAQAEGSHIV------AVLLNrnygqhsa 83
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRG---DAEVIVVDGGSTDGTV----EIARSLGAKVIhspkgrARQMN-------- 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556485319   84 imAGFSHVTGDLIITLDADL---QNPPEEIPRLVAKadEGYdVVGT--VRQNRQDSLFRkLASRTIN---RLIQRTTG 153
Cdd:TIGR04283  65 --AGAALAKGDILLFLHADTrlpKDFLEAIRRALAK--PGY-VAGAfdLRFDGPGLLLR-LIEWGVNlrsRLTGIPYG 136
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
8-173 7.92e-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: 52.37  E-value: 7.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319    8 QKVSVVIPVYNEQESLPELIRrTTAACDTMgkAYEILLVDDGSSDNSALMLTEAAQA-EGSHIVAVLLNRNYGQHSAIMA 86
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLE-AILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARfPDVRLRVIRNARLLGPTGKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   87 ---GFSHVTGDLIITLDADLQNPPEEIPRLVAKAD-EGYDVVGTVRQNRQDSLF------RKLASRTINRLIQRTTGKAM 156
Cdd:pfam13641  79 lnhGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDsPKVGAVGTPVFSLNRSTMlsalgaLEFALRHLRMMSLRLALGVL 158
                         170
                  ....*....|....*..
gi 556485319  157 GDYGCMLrAYRRHIVDA 173
Cdd:pfam13641 159 PLSGAGS-AIRREVLKE 174
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
10-120 7.22e-07

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: 49.23  E-value: 7.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  10 VSVVIPVYNEQESLPELIrRTTAACDTMGKAYEILLVDDgSSDNSALMLTEAAQ---AEGSHIVAVLL-NRNYGQHSAIM 85
Cdd:cd06437    3 VTVQLPVFNEKYVVERLI-EAACALDYPKDRLEIQVLDD-STDETVRLAREIVEeyaAQGVNIKHVRRaDRTGYKAGALA 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 556485319  86 AGFSHVTGDLIITLDADLQNPPE---EIPRLVAKADEG 120
Cdd:cd06437   81 EGMKVAKGEYVAIFDADFVPPPDflqKTPPYFADPKLG 118
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
8-115 3.95e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 47.60  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   8 QKVSVVIPVYNEQESLPELIRRTTAACDTmGKAYEILLVDDGSSDNSAlmltEAAQAEGSHIVA---VL--LNRNYGQHS 82
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIRPLLME-PLVDELIVIDSGSTDATA----ERAAAAGARVVSreeILpeLPPRPGKGE 105
                         90       100       110
                 ....*....|....*....|....*....|....
gi 556485319  83 AIMAGFSHVTGDLIITLDADLQNP-PEEIPRLVA 115
Cdd:PRK13915 106 ALWRSLAATTGDIVVFVDADLINFdPMFVPGLLG 139
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
11-102 5.61e-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: 47.27  E-value: 5.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   11 SVVIPVYNEQES--LPELIRRTTAACDTMgkaYEILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNYGQHSAIMAGF 88
Cdd:pfam10111   1 SVVIPVYNGEKThwIQERILNQTFQYDPE---FELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDTTYSLAASRNRGT 77
                          90
                  ....*....|....
gi 556485319   89 SHVTGDLIITLDAD 102
Cdd:pfam10111  78 SHAIGEYISFIDGD 91
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
12-119 1.95e-05

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 44.09  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPEL---IRRTTaacdtmGKAYEILLVDDGSSDNSAlmltEAAQAEGSHIVAVLLNRNYGQHSAIMAGF 88
Cdd:cd04186    1 IIIVNYNSLEYLKACldsLLAQT------YPDFEVIVVDNASTDGSV----ELLRELFPEVRLIRNGENLGFGAGNNQGI 70
                         90       100       110
                 ....*....|....*....|....*....|.
gi 556485319  89 SHVTGDLIITLDADLQNPPEEIPRLVAKADE 119
Cdd:cd04186   71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQ 101
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
9-102 2.69e-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: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319   9 KVSVVIPVYN-EQESLPELIRRTTAacdtmgKAY---EILLVDDGSSDNSALMLTEAAQAEGSHIVAVLLNRNYGQHSAI 84
Cdd:cd04184    2 LISIVMPVYNtPEKYLREAIESVRA------QTYpnwELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAAT 75
                         90
                 ....*....|....*...
gi 556485319  85 MAGFSHVTGDLIITLDAD 102
Cdd:cd04184   76 NSALELATGEFVALLDHD 93
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
11-101 3.45e-04

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: 41.81  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  11 SVVIPVYNEQESL-------------PELIRrttaacdtmgkayEILLVDDGSSDNSALMLTEAAQAEGSHIVAVL-LNR 76
Cdd:cd02510    1 SVIIIFHNEALSTllrtvhsvinrtpPELLK-------------EIILVDDFSDKPELKLLLEEYYKKYLPKVKVLrLKK 67
                         90       100
                 ....*....|....*....|....*
gi 556485319  77 NYGQHSAIMAGFSHVTGDLIITLDA 101
Cdd:cd02510   68 REGLIRARIAGARAATGDVLVFLDS 92
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
12-150 4.86e-04

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: 40.28  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  12 VVIPVYNEQESLPELIrRTTAACDTMGKAYEILLVDDGSSDNSAlmltEAAQAEGSHIVAVLLNRNYGQHSAIMAGFSHV 91
Cdd:cd06438    1 ILIPAHNEEAVIGNTV-RSLKAQDYPRELYRIFVVADNCTDDTA----QVARAAGATVLERHDPERRGKGYALDFGFRHL 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556485319  92 TG-----DLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQ--NRQDSL---FRKLASRTINRLIQR 150
Cdd:cd06438   76 LNladdpDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNskNPDDSWitrLYAFAFLVFNRLRPL 144
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
11-126 4.35e-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: 37.68  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  11 SVVIPVYNEQ------ESLPELIRRTTAACdtmgkayEILLVDDGSSDNSAL-MLTEAAQAEGshIVAVLLNRNYGQHSA 83
Cdd:cd04195    1 SVLMSVYIKEkpeflrEALESILKQTLPPD-------EVVLVKDGPVTQSLNeVLEEFKRKLP--LKVVPLEKNRGLGKA 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 556485319  84 IMAGFSHVTGDLIITLDADLQNPPEEIPRLVA--KADEGYDVVGT 126
Cdd:cd04195   72 LNEGLKHCTYDWVARMDTDDISLPDRFEKQLDfiEKNPEIDIVGG 116
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
11-169 8.88e-03

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: 36.75  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  11 SVVIPVYNEQESLPELIR----RTTaacdtmgKAYEILLVDDGSSDNSAlmltEAAQAEGSHIVAVLLNRNYGQHSAIMA 86
Cdd:cd06433    1 SIITPTYNQAETLEETIDsvlsQTY-------PNIEYIVIDGGSTDGTV----DIIKKYEDKITYWISEPDKGIYDAMNK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556485319  87 GFSHVTGDLIITLDAD---LQNPPEEIPRLVAKADEGYDVVG------------TVRQNRQDSLFRKLASRTIN------ 145
Cdd:cd06433   70 GIALATGDIIGFLNSDdtlLPGALLAVVAAFAEHPEVDVVYGdvllvdengrviGRRRPPPFLDKFLLYGMPIChqatff 149
                        170       180       190
                 ....*....|....*....|....*....|.
gi 556485319 146 -RLIQRTTG------KAMGDYGCMLRAYRRH 169
Cdd:cd06433  150 rRSLFEKYGgfdesyRIAADYDLLLRLLLAG 180
 
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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