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Conserved domains on  [gi|1758257445|ref|XP_030985979|]
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uncharacterized protein PgNI_01733 [Pyricularia grisea]

Protein Classification

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

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

CAZY:  GT2
EC:  2.4.1.117
Gene Ontology:  GO:0004581|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
114-384 3.27e-96

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: 286.77  E-value: 3.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARILPTLEEMVEYLDARFGRDppanptqtallspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFS---------------------------------YEIIVVDDGSKDGTAEV 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 194 ALDFARDRGlhDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLvegcEDVVDGSNRGVAIGSRGH 273
Cdd:cd04188    48 ARKLARKNP--ALIRVLTLPKNRGKGGAVRAGMLAARGDYILFADADLATPFEELEKL----EEALKTSGYDIAIGSRAH 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 274 LvGSEAVVKRSALRNFLMKSFHFVLMILtppATSRIRDTQCGFKLFSRAALPHIIPYMHSEGWIFDIEMLMLAESApatp 353
Cdd:cd04188   122 L-ASAAVVKRSWLRNLLGRGFNFLVRLL---LGLGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRL---- 193
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1758257445 354 vlaadgsvigmspGIKVVEVPIDWHEVEGSK 384
Cdd:cd04188   194 -------------GYPIEEVPVRWVEIPGSK 211
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
114-384 3.27e-96

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: 286.77  E-value: 3.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARILPTLEEMVEYLDARFGRDppanptqtallspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFS---------------------------------YEIIVVDDGSKDGTAEV 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 194 ALDFARDRGlhDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLvegcEDVVDGSNRGVAIGSRGH 273
Cdd:cd04188    48 ARKLARKNP--ALIRVLTLPKNRGKGGAVRAGMLAARGDYILFADADLATPFEELEKL----EEALKTSGYDIAIGSRAH 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 274 LvGSEAVVKRSALRNFLMKSFHFVLMILtppATSRIRDTQCGFKLFSRAALPHIIPYMHSEGWIFDIEMLMLAESApatp 353
Cdd:cd04188   122 L-ASAAVVKRSWLRNLLGRGFNFLVRLL---LGLGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRL---- 193
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1758257445 354 vlaadgsvigmspGIKVVEVPIDWHEVEGSK 384
Cdd:cd04188   194 -------------GYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
108-411 3.94e-83

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 257.77  E-value: 3.94e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 108 AEVAMSVVVPAYNEEARILPTLEEMVEYLDARFGRDPPANptqtallspttpkrlafkmhqavpepltgYEIIIVNDGST 187
Cdd:PTZ00260   68 SDVDLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFK-----------------------------YEIIIVNDGSK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 188 DRTVQVALDFARDRGLHDI-VRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEGCEDVVDgSNRGV 266
Cdd:PTZ00260  119 DKTLKVAKDFWRQNINPNIdIRLLSLLRNKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQ-NGLGI 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 267 AIGSRGHLVGSEAVVKRSALRNFLMKSFHFVLMILtppATSRIRDTQCGFKLFSRAALPHIIPYMHSEGWIFDIEMLMLA 346
Cdd:PTZ00260  198 VFGSRNHLVDSDVVAKRKWYRNILMYGFHFIVNTI---CGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIA 274
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758257445 347 ESApatpvlaadgsvigmspGIKVVEVPIDWHEVEGSKMNLIHDSIKMAIGLAVLRASWMMGVYR 411
Cdd:PTZ00260  275 QKL-----------------NLPIAEVPVNWTEVEGSKLNVISASIQMARDILLVRSFYLLGIWK 322
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
113-395 1.45e-35

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 129.82  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEEMVEYLDARFgrdppanptqtallspttpkrlafkmhqavpepltgyEIIIVNDGSTDRTVQ 192
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYPDF-------------------------------------EIIVVDDGSTDGTAE 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 193 VALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEGCEDvvdgSNRGVAIGSRG 272
Cdd:COG0463    48 ILRELAAK---DPRIRVIRLERNRGKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEE----GPADLVYGSRL 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 273 HLVGseavvkRSALRNFLMKSFHFVLMIltppatSRIRDTQCGFKLFSRAALpHIIPYmhSEGWIFDIEMLMLAESapat 352
Cdd:COG0463   121 IREG------ESDLRRLGSRLFNLVRLL------TNLPDSTSGFRLFRREVL-EELGF--DEGFLEDTELLRALRH---- 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1758257445 353 pvlaadgsvigmspGIKVVEVPIDWHEvEGSKMNLiHDSIKMA 395
Cdd:COG0463   182 --------------GFRIAEVPVRYRA-GESKLNL-RDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
113-324 4.92e-30

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: 114.03  E-value: 4.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEEMVEyldarfgrdppanptQTALLspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQ 192
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---------------QTYPN----------------------FEIIVVDDGSTDGTVE 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 193 VALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEgcedVVDGSNRGVAIGSRG 272
Cdd:pfam00535  44 IAEEYAKK---DPRVRVIRLPENRGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVE----ALEEDGADVVVGSRY 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1758257445 273 HlVGSEAVVKRSALRNFLMKSFHFVLMILTPPAtsrIRDTQCGFKLFSRAAL 324
Cdd:pfam00535 117 V-IFGETGEYRRASRITLSRLPFFLGLRLLGLN---LPFLIGGFALYRREAL 164
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
114-384 3.27e-96

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: 286.77  E-value: 3.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARILPTLEEMVEYLDARFGRDppanptqtallspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFS---------------------------------YEIIVVDDGSKDGTAEV 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 194 ALDFARDRGlhDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLvegcEDVVDGSNRGVAIGSRGH 273
Cdd:cd04188    48 ARKLARKNP--ALIRVLTLPKNRGKGGAVRAGMLAARGDYILFADADLATPFEELEKL----EEALKTSGYDIAIGSRAH 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 274 LvGSEAVVKRSALRNFLMKSFHFVLMILtppATSRIRDTQCGFKLFSRAALPHIIPYMHSEGWIFDIEMLMLAESApatp 353
Cdd:cd04188   122 L-ASAAVVKRSWLRNLLGRGFNFLVRLL---LGLGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRL---- 193
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1758257445 354 vlaadgsvigmspGIKVVEVPIDWHEVEGSK 384
Cdd:cd04188   194 -------------GYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
108-411 3.94e-83

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 257.77  E-value: 3.94e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 108 AEVAMSVVVPAYNEEARILPTLEEMVEYLDARFGRDPPANptqtallspttpkrlafkmhqavpepltgYEIIIVNDGST 187
Cdd:PTZ00260   68 SDVDLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFK-----------------------------YEIIIVNDGSK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 188 DRTVQVALDFARDRGLHDI-VRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEGCEDVVDgSNRGV 266
Cdd:PTZ00260  119 DKTLKVAKDFWRQNINPNIdIRLLSLLRNKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQ-NGLGI 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 267 AIGSRGHLVGSEAVVKRSALRNFLMKSFHFVLMILtppATSRIRDTQCGFKLFSRAALPHIIPYMHSEGWIFDIEMLMLA 346
Cdd:PTZ00260  198 VFGSRNHLVDSDVVAKRKWYRNILMYGFHFIVNTI---CGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIA 274
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758257445 347 ESApatpvlaadgsvigmspGIKVVEVPIDWHEVEGSKMNLIHDSIKMAIGLAVLRASWMMGVYR 411
Cdd:PTZ00260  275 QKL-----------------NLPIAEVPVNWTEVEGSKLNVISASIQMARDILLVRSFYLLGIWK 322
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
114-346 1.08e-55

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: 182.00  E-value: 1.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARILPTLEEMVEYLDARFGrdppanptqtallspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYD-----------------------------------YEIIVVDDGSTDGTAEI 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 194 ALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVE-GCEDVVDgsnrgVAIGSRG 272
Cdd:cd04179    46 ARELAAR---VPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTMDADLQHPPEDIPKLLEkLLEGGAD-----VVIGSRF 117
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758257445 273 HLVGSEAvvkRSALRNFLMKSFHFVLMILTppaTSRIRDTQCGFKLFSRAALPHIIPYMHSEGWIFDIEMLMLA 346
Cdd:cd04179   118 VRGGGAG---MPLLRRLGSRLFNFLIRLLL---GVRISDTQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
113-395 1.45e-35

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 129.82  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEEMVEYLDARFgrdppanptqtallspttpkrlafkmhqavpepltgyEIIIVNDGSTDRTVQ 192
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYPDF-------------------------------------EIIVVDDGSTDGTAE 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 193 VALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEGCEDvvdgSNRGVAIGSRG 272
Cdd:COG0463    48 ILRELAAK---DPRIRVIRLERNRGKGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEE----GPADLVYGSRL 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 273 HLVGseavvkRSALRNFLMKSFHFVLMIltppatSRIRDTQCGFKLFSRAALpHIIPYmhSEGWIFDIEMLMLAESapat 352
Cdd:COG0463   121 IREG------ESDLRRLGSRLFNLVRLL------TNLPDSTSGFRLFRREVL-EELGF--DEGFLEDTELLRALRH---- 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1758257445 353 pvlaadgsvigmspGIKVVEVPIDWHEvEGSKMNLiHDSIKMA 395
Cdd:COG0463   182 --------------GFRIAEVPVRYRA-GESKLNL-RDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
113-324 4.92e-30

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: 114.03  E-value: 4.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEEMVEyldarfgrdppanptQTALLspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQ 192
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---------------QTYPN----------------------FEIIVVDDGSTDGTVE 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 193 VALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEgcedVVDGSNRGVAIGSRG 272
Cdd:pfam00535  44 IAEEYAKK---DPRVRVIRLPENRGKAGARNAGLRAATGDYIAFLDADDEVPPDWLEKLVE----ALEEDGADVVVGSRY 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1758257445 273 HlVGSEAVVKRSALRNFLMKSFHFVLMILTPPAtsrIRDTQCGFKLFSRAAL 324
Cdd:pfam00535 117 V-IFGETGEYRRASRITLSRLPFFLGLRLLGLN---LPFLIGGFALYRREAL 164
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
114-387 2.36e-22

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: 94.52  E-value: 2.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARIlptlEEMVEYLDARFgRDPPanptqtallspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd06442     1 IIIPTYNERENI----PELIERLDAAL-KGID-------------------------------YEIIVVDDNSPDGTAEI 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 194 ALDFARdrgLHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEGCEDvvdgSNRGVAIGSRgH 273
Cdd:cd06442    45 VRELAK---EYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDADLSHPPEYIPELLEAQLE----GGADLVIGSR-Y 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 274 LVGSeAVVKRSALRNFLMKSFHFVLMILTPPatsRIRDTQCGFKLFSRAALPHIIPYMHSEGWIFDIEMLmlaesapatp 353
Cdd:cd06442   117 VEGG-GVEGWGLKRKLISRGANLLARLLLGR---KVSDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELL---------- 182
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1758257445 354 vlaadgsVIGMSPGIKVVEVPIDWHE-VEG-SKMNL 387
Cdd:cd06442   183 -------VRARRLGYRIVEVPITFVDrEHGeSKLGG 211
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
114-330 1.06e-21

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: 91.38  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEArilpTLEEMVEYLdarfgrdppanptqTALLSPTTPKrlafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd04187     1 IVVPVYNEEE----NLPELYERL--------------KAVLESLGYD----------------YEIIFVDDGSTDRTLEI 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 194 ALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLV----EGCeDVVDGSNRgvaig 269
Cdd:cd04187    47 LRELAAR---DPRVKVIRLSRNFGQQAALLAGLDHARGDAVITMDADLQDPPELIPEMLakweEGY-DVVYGVRK----- 117
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758257445 270 SRGHlvgseavvkrSALRNFLMKSFHFVLMILTPPatsRIRDTQCGFKLFSRAALPHIIPY 330
Cdd:cd04187   118 NRKE----------SWLKRLTSKLFYRLINKLSGV---DIPDNGGDFRLMDRKVVDALLLL 165
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
114-240 3.28e-20

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: 87.28  E-value: 3.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARILPTLEemveyldarfgrdppanptqtALLSPTTPKrlafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd06423     1 IIVPAYNEEAVIERTIE---------------------SLLALDYPK----------------LEVIVVDDGSTDDTLEI 43
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1758257445 194 ALDFARDRglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd06423    44 LEELAALY--IRRVLVVRDKENGGKAGALNAGLRHAKGDIVVVLDAD 88
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
113-240 9.93e-20

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 89.03  E-value: 9.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEemveyldarfgrdppanptqtALLSpttpkrlafkmhQAVPEPLtgYEIIIVNDGSTDRTVQ 192
Cdd:COG1215    32 SVIIPAYNEEAVIEETLR---------------------SLLA------------QDYPKEK--LEVIVVDDGSTDETAE 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1758257445 193 VALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:COG1215    77 IARELAAE---YPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDAD 121
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
114-240 1.31e-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: 82.17  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEarilPTLEEMVEYLDArfgrdppanptQTallspttpkrlafkmhqavpepLTGYEIIIVNDGSTDRTVQV 193
Cdd:cd00761     1 VIIPAYNEE----PYLERCLESLLA-----------QT----------------------YPNFEVIVVDDGSTDGTLEI 43
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1758257445 194 ALDFARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd00761    44 LEEYAKK---DPRVIRVINEENQGLAAARNAGLKAARGEYILFLDAD 87
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
84-240 1.86e-15

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: 75.70  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445  84 RWLAEQRRQRQANQDAPDLgliePAevaMSVVVPAYNEEARILPTLEEMVEYldarfgrDPPAnptqtallspttpKRLa 163
Cdd:cd06439    10 KLLARLRPKPPSLPDPAYL----PT---VTIIIPAYNEEAVIEAKLENLLAL-------DYPR-------------DRL- 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1758257445 164 fkmhqavpepltgyEIIIVNDGSTDRTVQVALDFARDRglhdiVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd06439    62 --------------EIIVVSDGSTDGTAEIAREYADKG-----VKLLRFPERRGKAAALNRALALATGEIVVFTDAN 119
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
107-375 6.72e-14

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 70.88  E-value: 6.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 107 PAEVAM--SVVVPAYNEEARIlptleemveyldarfgrdppanptqtALLSpttpkRLAFKMHQAVPEpltgYEIIIVND 184
Cdd:PLN02726    4 PGEGAMkySIIVPTYNERLNI--------------------------ALIV-----YLIFKALQDVKD----FEIIVVDD 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 185 GSTDRTVQVALDFARDRGlHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGA--SKF--SDLGKLVEGCEDVVD 260
Cdd:PLN02726   49 GSPDGTQDVVKQLQKVYG-EDRILLRPRPGKLGLGTAYIHGLKHASGDFVVIMDADLShhPKYlpSFIKKQRETGADIVT 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 261 GS----NRGVA-------IGSRGhlvgseavvkrsalRNFLMksfHFVLMiltpPATSrirDTQCGFKLFSRAALPHIIP 329
Cdd:PLN02726  128 GTryvkGGGVHgwdlrrkLTSRG--------------ANVLA---QTLLW----PGVS---DLTGSFRLYKRSALEDLVS 183
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1758257445 330 YMHSEGWIFDIEMLMLAESApatpvlaadgsvigmspGIKVVEVPI 375
Cdd:PLN02726  184 SVVSKGYVFQMEIIVRASRK-----------------GYRIEEVPI 212
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
112-240 1.12e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 63.47  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 112 MSVVVPAYNEEARILPTLEemveyldarfgrdppanptqtALLSPTTPkrlafkmhqavpepltGYEIIIVNDGSTDRTV 191
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLE---------------------SLLAQTYP----------------PFEVIVVDNGSTDGTA 47
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1758257445 192 QVALDFARDRglhdiVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:COG1216    48 ELLAALAFPR-----VRVIRNPENLGFAAARNLGLRAAGGDYLLFLDDD 91
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
113-241 1.20e-10

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: 61.48  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEemveyldarfgrdppanptqtALLSPTTPKRLafkmhqavpepltgYEIIIVNDGSTDRTVQ 192
Cdd:cd02525     3 SIIIPVRNEEKYIEELLE---------------------SLLNQSYPKDL--------------IEIIVVDGGSTDGTRE 47
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1758257445 193 VALDFArdrGLHDIVRVVtlaKNRGK--GGGVTHGFRHARGEYVVFADADG 241
Cdd:cd02525    48 IVQEYA---AKDPRIRLI---DNPKRiqSAGLNIGIRNSRGDIIIRVDAHA 92
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
114-240 3.92e-10

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: 59.61  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARILPTLEemveyldarfgrdppanptqtALLSPTTPKRLafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd04192     1 VVIAARNEAENLPRLLQ---------------------SLSALDYPKEK--------------FEVILVDDHSTDGTVQI 45
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1758257445 194 aLDFARDrglHDIVRVVTL----AKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd04192    46 -LEFAAA---KPNFQLKILnnsrVSISGKKNALTTAIKAAKGDWIVTTDAD 92
PRK10073 PRK10073
putative glycosyl transferase; Provisional
174-240 1.42e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 58.90  E-value: 1.42e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758257445 174 LTGYEIIIVNDGSTDRTVQVALDFARD----RGLHDIVRVVTLAKNRgkgggvthGFRHARGEYVVFADAD 240
Cdd:PRK10073   33 WTALEIIIVNDGSTDNSVEIAKHYAENyphvRLLHQANAGVSVARNT--------GLAVATGKYVAFPDAD 95
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
177-288 1.17e-08

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 54.10  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 177 YEIIIVNDGSTDRTVQVALDFARDrglhdiVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEGCE 256
Cdd:cd04186    27 FEVIVVDNASTDGSVELLRELFPE------VRLIRNGENLGFGAGNNQGIREAKGDYVLLLNPDTVVEPGALLELLDAAE 100
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1758257445 257 DvvdgsNRGVAI-GSRghLVGSEAVVKRSALRN 288
Cdd:cd04186   101 Q-----DPDVGIvGPK--VSGAFLLVRREVFEE 126
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
113-240 1.02e-07

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


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 52.19  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEemveylDARFGRDPPAnptqtallspttpkrlafkmhqavpepltgyEIIIVNDGSTDRTVQ 192
Cdd:cd02522     2 SIIIPTLNEAENLPRLLA------SLRRLNPLPL-------------------------------EIIVVDGGSTDGTVA 44
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1758257445 193 VALDFArdrglhdiVRVVTLAKNRGKggGVTHGFRHARGEYVVFADAD 240
Cdd:cd02522    45 IARSAG--------VVVISSPKGRAR--QMNAGAAAARGDWLLFLHAD 82
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
178-240 1.91e-07

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 51.48  E-value: 1.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1758257445 178 EIIIVNDGSTDRTVQVALDFARdrglHDIVRVVTLakNRGKGGGVTHGFRHA----RGEYVVFADAD 240
Cdd:cd04196    29 ELIISDDGSTDGTVEIIKEYID----KDPFIIILI--RNGKNLGVARNFESLlqaaDGDYVFFCDQD 89
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
113-259 1.57e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 49.73  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARiLPTLEEMVEYLDARFGRDppanptqtallspttpkrlafkmhqavpepltgYEIIIVNDGSTDRTVQ 192
Cdd:PRK10714    9 SVVIPVYNEQES-LPELIRRTTAACESLGKE---------------------------------YEILLIDDGSSDNSAE 54
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 193 VALDFARDRGLHDIvrVVTLAKNRGKGGGVTHGFRHARGEYVVFADADGASKFSDLGKLVEGCE---DVV 259
Cdd:PRK10714   55 MLVEAAQAPDSHIV--AILLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADegyDVV 122
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
178-240 6.97e-06

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


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 46.90  E-value: 6.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758257445 178 EIIIVNDGSTDRTVQVALDFardrglhdIVRVVTLaKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd02511    28 EIIVVDSGSTDRTVEIAKEY--------GAKVYQR-WWDGFGAQRNFALELATNDWVLSLDAD 81
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
113-240 2.20e-05

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: 45.44  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 113 SVVVPAYNEEARILPTLEemveyldarfgrdppanptqtallspttpkrlafkMHQAVPEPltGYEIIIVNDGSTDRTVQ 192
Cdd:pfam13641   5 SVVVPAFNEDSVLGRVLE-----------------------------------AILAQPYP--PVEVVVVVNPSDAETLD 47
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1758257445 193 VALDFARDRGlHDIVRVVTLAKN---RGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:pfam13641  48 VAEEIAARFP-DVRLRVIRNARLlgpTGKSRGLNHGFRAVKSDLVVLHDDD 97
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
174-240 2.24e-05

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: 45.32  E-value: 2.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1758257445 174 LTGYEIIIVNDGSTDRTVQVALDFARDRGlhdivRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd06434    26 QKPLEIIVVTDGDDEPYLSILSQTVKYGG-----IFVITVPHPGKRRALAEGIRHVTTDIVVLLDSD 87
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
178-239 4.99e-05

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: 44.89  E-value: 4.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758257445 178 EIIIVNDGSTDRTVQVALDfARDRGLHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADA 239
Cdd:cd02510    32 EIILVDDFSDKPELKLLLE-EYYKKYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDS 92
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
114-240 8.21e-05

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: 42.97  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEARILPTLEemveyldarfgrdppanptqtALLSPTTPKRLafkmhqavpepltgYEIIIVNDGSTDRTVQV 193
Cdd:cd06438     1 ILIPAHNEEAVIGNTVR---------------------SLKAQDYPREL--------------YRIFVVADNCTDDTAQV 45
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1758257445 194 aldfARDRGLHDIVRvvTLAKNRGKGGGVTHGFRHARGE------YVVFaDAD 240
Cdd:cd06438    46 ----ARAAGATVLER--HDPERRGKGYALDFGFRHLLNLaddpdaVVVF-DAD 91
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
179-240 8.46e-05

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


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 43.84  E-value: 8.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758257445 179 IIIVNDGSTDRTVQVALDFA---RDRGLHdiVRVVTLAKNRG-KGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd06437    34 EIQVLDDSTDETVRLAREIVeeyAAQGVN--IKHVRRADRTGyKAGALAEGMKVAKGEYVAIFDAD 97
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
178-240 2.68e-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: 41.92  E-value: 2.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758257445 178 EIIIVNDGS-TDRTVQVALDFARDRGLhdivRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd04195    31 EVVLVKDGPvTQSLNEVLEEFKRKLPL----KVVPLEKNRGLGKALNEGLKHCTYDWVARMDTD 90
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
177-240 6.48e-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: 40.61  E-value: 6.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758257445 177 YEIIIVNDGSTDRTVQVALDFArdrglHDIVRVVTlaknrGKGGGVTH----GFRHARGEYVVFADAD 240
Cdd:cd06433    28 IEYIVIDGGSTDGTVDIIKKYE-----DKITYWIS-----EPDKGIYDamnkGIALATGDIIGFLNSD 85
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
83-240 9.22e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.06  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445  83 DRWLaEQRRQRQANQDAPDLgLIEPAEVAMSVVVPAYNEEArilpTLEEMVEyldarfgrdppanptqtallspttpkrl 162
Cdd:PRK13915    6 EAWL-EDRTWHAPDWTIEEL-VAAKAGRTVSVVLPALNEEE----TVGKVVD---------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 163 afKMHQAVPEPLTGyEIIIVNDGSTDRTVQValdfARDRGlhdiVRVVT-------LAKNRGKGGGVTHGFRHARGEYVV 235
Cdd:PRK13915   52 --SIRPLLMEPLVD-ELIVIDSGSTDATAER----AAAAG----ARVVSreeilpeLPPRPGKGEALWRSLAATTGDIVV 120

                  ....*
gi 1758257445 236 FADAD 240
Cdd:PRK13915  121 FVDAD 125
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
168-283 1.49e-03

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 39.54  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 168 QAVPEPLTgyEIIIVNDGSTDRTVqvalDFARDRGLHDIVRVVTLAKNRGKGGGVTHGFRHA--RG-EYVVFADADGASK 244
Cdd:cd04185    20 LAQTRPPD--HIIVIDNASTDGTA----EWLTSLGDLDNIVYLRLPENLGGAGGFYEGVRRAyeLGyDWIWLMDDDAIPD 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1758257445 245 FSDLGKLVEGcedvVDGSNRGVAIGSR----GHLVG---SEAVVKR 283
Cdd:cd04185    94 PDALEKLLAY----ADKDNPQFLAPLVldpdGSFVGvliSRRVVEK 135
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
178-240 1.57e-03

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: 39.49  E-value: 1.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758257445 178 EIIIVNDGSTDRTVQVALD-FARDrglHDIVRVVTLAKNRGKGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd04184    33 ELCIADDASTDPEVKRVLKkYAAQ---DPRIKVVFREENGGISAATNSALELATGEFVALLDHD 93
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
155-240 2.37e-03

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: 39.57  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 155 SPTTPKRLAFKMHQAVPEPltgyEIIIVNDGSTDRTVQVALDFARDRGL----HDIVRVVTLAKNRGKGggvthgFRHAR 230
Cdd:pfam10111  12 THWIQERILNQTFQYDPEF----ELIIINDGSTDKTLEEVSSIKDHNLQvyypNAPDTTYSLAASRNRG------TSHAI 81
                          90
                  ....*....|
gi 1758257445 231 GEYVVFADAD 240
Cdd:pfam10111  82 GEYISFIDGD 91
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
114-240 6.48e-03

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: 37.94  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758257445 114 VVVPAYNEEarilptlEEMVEyldarfgrdppanPTQTAllspttpkrlAFKMHQavpePLTGYEIIIVNDGSTDRTVQV 193
Cdd:cd06421     5 VFIPTYNEP-------LEIVR-------------KTLRA----------ALAIDY----PHDKLRVYVLDDGRRPELRAL 50
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1758257445 194 ALDFARDRGLHDIVRvvtlAKNRG-KGGGVTHGFRHARGEYVVFADAD 240
Cdd:cd06421    51 AAELGVEYGYRYLTR----PDNRHaKAGNLNNALAHTTGDFVAILDAD 94
 
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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