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Conserved domains on  [gi|492247268|ref|WP_005788964|]
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MULTISPECIES: polyprenol monophosphomannose synthase [Bacteroides]

Protein Classification

polyprenol monophosphomannose synthase( domain architecture ID 10157756)

polyprenol monophosphomannose synthase transfers mannose from GDP-mannose to lipid acceptors, such as dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
8-234 6.94e-106

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: 305.23  E-value: 6.94e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLEK--TFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWALE 85
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKgiDYEIIVVDDNSPDGTAEIVRELAKEYP-RVRLIVRPGKRGLGSAYIEGFKAARG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  86 hsyEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAGFK 165
Cdd:cd06442   80 ---DVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492247268 166 CYRRQVLETIDlDHIRFKGYAFQIEMKFTAYKCGFKIIEVPVIFINRELGTSKMNSSIFGEAVFGVIKL 234
Cdd:cd06442  157 AYRREVLEKLI-DSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
 
Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
8-234 6.94e-106

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: 305.23  E-value: 6.94e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLEK--TFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWALE 85
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKgiDYEIIVVDDNSPDGTAEIVRELAKEYP-RVRLIVRPGKRGLGSAYIEGFKAARG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  86 hsyEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAGFK 165
Cdd:cd06442   80 ---DVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492247268 166 CYRRQVLETIDlDHIRFKGYAFQIEMKFTAYKCGFKIIEVPVIFINRELGTSKMNSSIFGEAVFGVIKL 234
Cdd:cd06442  157 AYRREVLEKLI-DSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
8-234 1.20e-59

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 188.75  E-value: 1.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENI---IRAVFGLEKTFHILIIEDGSPDGTAAIVKTLQQEF-PDRLFMIERKGKLGLGTAYITGFKWA 83
Cdd:PLN02726  13 IIVPTYNERLNIALIvylIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYgEDRILLRPRPGKLGLGTAYIHGLKHA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  84 lehSYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAG 163
Cdd:PLN02726  93 ---SGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSDLTGS 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492247268 164 FKCYRRQVLETIdLDHIRFKGYAFQIEMKFTAYKCGFKIIEVPVIFINRELGTSKMNSSIFGEAVFGVIKL 234
Cdd:PLN02726 170 FRLYKRSALEDL-VSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYL 239
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-220 4.71e-45

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 150.24  E-value: 4.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLE-KTFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWAleh 86
Cdd:COG0463    6 VVIPTYNEEEYLEEALESLLAQTyPDFEIIVVDDGSTDGTAEILRELAAKDP-RIRVIRLERNRGKGAARNAGLAAA--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  87 SYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVvnwpMGRVLMSYFASKYVRIvtgLPIHDTTAGFKC 166
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLL---TNLPDSTSGFRL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492247268 167 YRRQVLETIDLDHirfkGYAFQIEMkFTAYKCGFKIIEVPVIFINrelGTSKMN 220
Cdd:COG0463  155 FRREVLEELGFDE----GFLEDTEL-LRALRHGFRIAEVPVRYRA---GESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-173 1.52e-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: 111.33  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268    8 VIIPTYNERENIENIIRAVFGLE-KTFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWAleh 86
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTyPNFEIIVVDDGSTDGTVEIAEEYAKKDP-RVRVIRLPENRGKAGARNAGLRAA--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   87 SYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYV-SGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAGFK 165
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYViFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 492247268  166 CYRRQVLE 173
Cdd:pfam00535 158 LYRREALE 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
8-53 3.53e-07

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


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 49.43  E-value: 3.53e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 492247268    8 VIIPTYNERENIENIIRAVFGLEKTFHILIIEDGSPDGTAAIVKTL 53
Cdd:TIGR04283   3 IIIPVLNEAATLPELLADLQALRGDAEVIVVDGGSTDGTVEIARSL 48
 
Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
8-234 6.94e-106

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: 305.23  E-value: 6.94e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLEK--TFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWALE 85
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKgiDYEIIVVDDNSPDGTAEIVRELAKEYP-RVRLIVRPGKRGLGSAYIEGFKAARG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  86 hsyEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAGFK 165
Cdd:cd06442   80 ---DVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492247268 166 CYRRQVLETIDlDHIRFKGYAFQIEMKFTAYKCGFKIIEVPVIFINRELGTSKMNSSIFGEAVFGVIKL 234
Cdd:cd06442  157 AYRREVLEKLI-DSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
8-195 1.63e-61

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 191.25  E-value: 1.63e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENI---IRAVFGLEKTFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWAL 84
Cdd:cd04179    1 VVIPAYNEEENIPELverLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVP-RVRVIRLSRNFGKGAAVRAGFKAAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  85 EhsyEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGvNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAGF 164
Cdd:cd04179   80 G---DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRG-GGAGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGF 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 492247268 165 KCYRRQVLETIdLDHIRFKGYAFQIEMKFTA 195
Cdd:cd04179  156 RLFRREVLEAL-LSLLESNGFEFGLELLVGA 185
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
8-234 1.20e-59

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 188.75  E-value: 1.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENI---IRAVFGLEKTFHILIIEDGSPDGTAAIVKTLQQEF-PDRLFMIERKGKLGLGTAYITGFKWA 83
Cdd:PLN02726  13 IIVPTYNERLNIALIvylIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYgEDRILLRPRPGKLGLGTAYIHGLKHA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  84 lehSYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAG 163
Cdd:PLN02726  93 ---SGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSDLTGS 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492247268 164 FKCYRRQVLETIdLDHIRFKGYAFQIEMKFTAYKCGFKIIEVPVIFINRELGTSKMNSSIFGEAVFGVIKL 234
Cdd:PLN02726 170 FRLYKRSALEDL-VSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYL 239
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-220 4.71e-45

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 150.24  E-value: 4.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLE-KTFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWAleh 86
Cdd:COG0463    6 VVIPTYNEEEYLEEALESLLAQTyPDFEIIVVDDGSTDGTAEILRELAAKDP-RIRVIRLERNRGKGAARNAGLAAA--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  87 SYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVvnwpMGRVLMSYFASKYVRIvtgLPIHDTTAGFKC 166
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES----DLRRLGSRLFNLVRLL---TNLPDSTSGFRL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492247268 167 YRRQVLETIDLDHirfkGYAFQIEMkFTAYKCGFKIIEVPVIFINrelGTSKMN 220
Cdd:COG0463  155 FRREVLEELGFDE----GFLEDTEL-LRALRHGFRIAEVPVRYRA---GESKLN 200
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
8-218 1.30e-36

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: 128.45  E-value: 1.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGL-----EKTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMIERKGKLGLGTAYITGFKw 82
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYleerpSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGKGGAVRAGML- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  83 aleHSY-EYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYV-SGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDT 160
Cdd:cd04188   80 ---AARgDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHlASAAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDT 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492247268 161 TAGFKCYRRQVLETIdLDHIRFKGYAFQIEMKFTAYKCGFKIIEVPVIFinRELGTSK 218
Cdd:cd04188  157 QCGFKLFTRDAARRL-FPRLHLERWAFDVELLVLARRLGYPIEEVPVRW--VEIPGSK 211
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-173 1.52e-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: 111.33  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268    8 VIIPTYNERENIENIIRAVFGLE-KTFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWAleh 86
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTyPNFEIIVVDDGSTDGTVEIAEEYAKKDP-RVRVIRLPENRGKAGARNAGLRAA--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   87 SYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYV-SGVNVVNWPMGRVLMSYFASKYVRIVTGLPIHDTTAGFK 165
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYViFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 492247268  166 CYRRQVLE 173
Cdd:pfam00535 158 LYRREALE 165
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
8-175 4.56e-22

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: 89.46  E-value: 4.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVF----GLEKTFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGfkwa 83
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKavleSLGYDYEIIFVDDGSTDRTLEILRELAARDP-RVKVIRLSRNFGQQAALLAG---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  84 LEHSY-EYIFEMDADFSHNPNDLPRLYEAcAVQGGDVAIGSRYVSGVNVVnwpmgRVLMSYFASKYVRIVTGLPIHDTTA 162
Cdd:cd04187   76 LDHARgDAVITMDADLQDPPELIPEMLAK-WEEGYDVVYGVRKNRKESWL-----KRLTSKLFYRLINKLSGVDIPDNGG 149
                        170
                 ....*....|...
gi 492247268 163 GFKCYRRQVLETI 175
Cdd:cd04187  150 DFRLMDRKVVDAL 162
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
8-111 5.63e-16

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: 75.55  E-value: 5.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGL---EKTFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLGLGTAYITGFKWAl 84
Cdd:COG1215   33 VIIPAYNEEAVIEETLRSLLAQdypKEKLEVIVVDDGSTDETAEIARELAAEYP-RVRVIERPENGGKAAALNAGLKAA- 110
                         90       100
                 ....*....|....*....|....*..
gi 492247268  85 ehSYEYIFEMDADFSHNPNDLPRLYEA 111
Cdd:COG1215  111 --RGDIVVFLDADTVLDPDWLRRLVAA 135
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
8-130 4.49e-15

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: 70.23  E-value: 4.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGL-EKTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFmIERKGKLGLGTAYITGFKWAleh 86
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQtYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIR-VINEENQGLAAARNAGLKAA--- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 492247268  87 SYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVN 130
Cdd:cd00761   77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLLFR 120
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
8-175 1.40e-14

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 70.72  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAV----FGLEKtFHILIIEDGSPDGTAAIVKTLQQEFPdRLFMIERKGKLgLGTAYITGFKwa 83
Cdd:cd02525    4 IIIPVRNEEKYIEELLESLlnqsYPKDL-IEIIVVDGGSTDGTREIVQEYAAKDP-RIRLIDNPKRI-QSAGLNIGIR-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  84 lEHSYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVVNWPMGRVLMSYFA---SKYVRIVTGLPIHDT 160
Cdd:cd02525   79 -NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSPLGsggSAYRGGAVKIGYVDT 157
                        170
                 ....*....|....*
gi 492247268 161 TAgFKCYRRQVLETI 175
Cdd:cd02525  158 VH-HGAYRREVFEKV 171
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
8-176 2.24e-14

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: 69.18  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLE-KTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMI---ERKGKLGlgtayitGFKWA 83
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDyPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVrdkENGGKAG-------ALNAG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  84 LEHS-YEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYVSGVNVVNW-------------PMGRVLMSYFasKYV 149
Cdd:cd06423   74 LRHAkGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLltrlqaieylsifRLGRRAQSAL--GGV 151
                        170       180
                 ....*....|....*....|....*..
gi 492247268 150 RIVTGlpihdtTAGFkcYRRQVLETID 176
Cdd:cd06423  152 LVLSG------AFGA--FRREALREVG 170
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
8-207 6.52e-13

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 67.10  E-value: 6.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVF---------GLEKTFHILIIEDGSPDGTAAIVKTL--QQEFPDR----LFMIERKGKlgl 72
Cdd:PTZ00260  74 IVIPAYNEEDRLPKMLKETIkylesrsrkDPKFKYEIIIVNDGSKDKTLKVAKDFwrQNINPNIdirlLSLLRNKGK--- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  73 GTAYITGFkwaLEHSYEYIFEMDADFSHNPNDLPRLYE---ACAVQGGDVAIGSRYV---SGVNVVNWPMGRVLMSYFaS 146
Cdd:PTZ00260 151 GGAVRIGM---LASRGKYILMVDADGATDIDDFDKLEDimlKIEQNGLGIVFGSRNHlvdSDVVAKRKWYRNILMYGF-H 226
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492247268 147 KYVRIVTGLPIHDTTAGFKCYRRQVLETIdLDHIRFKGYAFQIEMKFTAYKCGFKIIEVPV 207
Cdd:PTZ00260 227 FIVNTICGTNLKDTQCGFKLFTRETARII-FPSLHLERWAFDIEIVMIAQKLNLPIAEVPV 286
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-114 2.02e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 64.24  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLEKT-FHILIIEDGSPDGTAAIVKTLQqefPDRLFMIERKGKLGLGTAYITGFKWAleh 86
Cdd:COG1216    7 VVIPTYNRPELLRRCLESLLAQTYPpFEVIVVDNGSTDGTAELLAALA---FPRVRVIRNPENLGFAAARNLGLRAA--- 80
                         90       100
                 ....*....|....*....|....*...
gi 492247268  87 SYEYIFEMDADFSHNPNDLPRLYEACAV 114
Cdd:COG1216   81 GGDYLLFLDDDTVVEPDWLERLLAAACL 108
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
8-218 1.30e-10

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 60.52  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIR----AVFGLEKTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMIERKGKLGLGTAYITGFKWA 83
Cdd:PRK10714  10 VVIPVYNEQESLPELIRrttaACESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNYGQHSAIMAGFSHV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  84 lehSYEYIFEMDADFSHNPNDLPRLYEAcAVQGGDVaIGSRYVSGVNvvnwPMGRVLMSYFASKYVRIVTGLPIHDTTAG 163
Cdd:PRK10714  90 ---TGDLIITLDADLQNPPEEIPRLVAK-ADEGYDV-VGTVRQNRQD----SWFRKTASKMINRLIQRTTGKAMGDYGCM 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492247268 164 FKCYRRQVLETIDLDHIRfkgyafQIEMKFTAYKCGFKIIEVPVIFINRELGTSK 218
Cdd:PRK10714 161 LRAYRRHIVDAMLHCHER------STFIPILANTFARRAIEIPVHHAEREFGDSK 209
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
8-240 1.44e-08

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 53.83  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNEreNIENIIRAVFGLEKTFHILIIEDGSPDGTAAIVKTLQQEfpdRLFMIERKGKLGLGTAYITGFKWALEHS 87
Cdd:cd02526    1 AVVVTYNP--DLSKLKELLAALAEQVDKVVVVDNSSGNDIELRLRLNSE---KIELIHLGENLGIAKALNIGIKAALENG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  88 YEYIFEMDADFSHNPNDLPRL--YEACAVQGGDV-AIGSRYVSgvnvvnwpmgRVLMSYFASKYVRIVTGLPIHDTTAGF 164
Cdd:cd02526   76 ADYVLLFDQDSVPPPDMVEKLlaYKILSDKNSNIgAVGPRIID----------RRTGENSPGVRKSGYKLRIQKEGEEGL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268 165 K----------CYRRQVLETI-----DL--DHIRFkgyafqiEMKFTAYKCGFKIIEVPVIFINRELGTSKMNssifgea 227
Cdd:cd02526  146 KevdflitsgsLISLEALEKVggfdeDLfiDYVDT-------EWCLRARSKGYKIYVVPDAVLKHELGDKRVK------- 211
                        250
                 ....*....|...
gi 492247268 228 VFGVIKLKVNSWF 240
Cdd:cd02526  212 RLGGVSVPLHSPL 224
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
6-97 9.53e-08

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


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 51.14  E-value: 9.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   6 SIVIIpTYNERENIENIIRAVfgleKTFH--ILIIEDGSPDGTAAIVKTLQQEFPDRLFmierkgkLGLGTAyitgFKWA 83
Cdd:cd02511    3 SVVII-TKNEERNIERCLESV----KWAVdeIIVVDSGSTDRTVEIAKEYGAKVYQRWW-------DGFGAQ----RNFA 66
                         90
                 ....*....|....*
gi 492247268  84 LEH-SYEYIFEMDAD 97
Cdd:cd02511   67 LELaTNDWVLSLDAD 81
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
8-69 1.86e-07

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: 50.66  E-value: 1.86e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492247268   8 VIIPTYNERENIENIIRAVFGLE---KTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMIERKGK 69
Cdd:cd06439   33 IIIPAYNEEAVIEAKLENLLALDyprDRLEIIVVSDGSTDGTAEIAREYADKGVKLLRFPERRGK 97
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-128 3.53e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 48.71  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLEKT-FHILIIEDGSPDGTAAIVKTLQQefpdRLFMIERKGKLGLGTAYITGFKWAleh 86
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPdFEVIVVDNASTDGSVELLRELFP----EVRLIRNGENLGFGAGNNQGIREA--- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492247268  87 SYEYIFEMDADFSHNPNDLPRLYEAcAVQGGDVAIGSRYVSG 128
Cdd:cd04186   74 KGDYVLLLNPDTVVEPGALLELLDA-AEQDPDVGIVGPKVSG 114
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
8-53 3.53e-07

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


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 49.43  E-value: 3.53e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 492247268    8 VIIPTYNERENIENIIRAVFGLEKTFHILIIEDGSPDGTAAIVKTL 53
Cdd:TIGR04283   3 IIIPVLNEAATLPELLADLQALRGDAEVIVVDGGSTDGTVEIARSL 48
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
8-99 7.40e-07

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


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 48.15  E-value: 7.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLEKTFHILIIEDGSPDGTAAIVKT---------LQQEFPDrlfmiERKGKlglGTAyit 78
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNKPNFLVLVIDDASDDDTAGIVRLaitdsrvhlLRRHLPN-----ARTGK---GDA--- 69
                         90       100
                 ....*....|....*....|.
gi 492247268  79 gFKWALEHSYEYIFEMDADFS 99
Cdd:cd06436   70 -LNAAYDQIRQILIEEGADPE 89
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-111 7.52e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 48.44  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLE---KTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMIERKGKLGLGTAyiTGFKWAL 84
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDypkEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVSISGKK--NALTTAI 78
                         90       100
                 ....*....|....*....|....*...
gi 492247268  85 EHS-YEYIFEMDADFSHNPNDLPRLYEA 111
Cdd:cd04192   79 KAAkGDWIVTTDADCVVPSNWLLTFVAF 106
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-159 7.97e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 48.40  E-value: 7.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVfgLEKTF---HILIIEDGSPDGTAAIvktLQQEFPDRLFMIERKGKlGLGTA--YITGFKW 82
Cdd:cd04185    1 AVVVTYNRLDLLKECLDAL--LAQTRppdHIIVIDNASTDGTAEW---LTSLGDLDNIVYLRLPE-NLGGAggFYEGVRR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  83 ALEHSYEYIFEMDADFSHNPNDLPRLYEACAVQGGDVAIGSRYvsgvnvvnWPMGR---VLMSyfaSKYVRIVtGLPIHD 159
Cdd:cd04185   75 AYELGYDWIWLMDDDAIPDPDALEKLLAYADKDNPQFLAPLVL--------DPDGSfvgVLIS---RRVVEKI-GLPDKE 142
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
8-107 4.19e-06

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: 46.53  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLE---KTFHILIIEDgSPDGTaaiVKTLQQefpdrlfMIERKGKLGLGTAYI-----TG 79
Cdd:cd06437    5 VQLPVFNEKYVVERLIEAACALDypkDRLEIQVLDD-STDET---VRLARE-------IVEEYAAQGVNIKHVrradrTG 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 492247268  80 FK-WALEH-----SYEYIFEMDADFSHNPNDLPR 107
Cdd:cd06437   74 YKaGALAEgmkvaKGEYVAIFDADFVPPPDFLQK 107
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
8-53 1.18e-05

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: 44.87  E-value: 1.18e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 492247268   8 VIIPTYNERENIENIIRAVFGL-EKTFHILIIEDGSPDGTAAIVKTL 53
Cdd:cd02522    3 IIIPTLNEAENLPRLLASLRRLnPLPLEIIVVDGGSTDGTVAIARSA 49
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-92 1.28e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 44.93  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFG-LEKTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMIERKGKLGlgtaYITGFKWALEH 86
Cdd:cd04196    2 VLMATYNGEKYLREQLDSILAqTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLG----VARNFESLLQA 77

                 ....*..
gi 492247268  87 S-YEYIF 92
Cdd:cd04196   78 AdGDYVF 84
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
8-178 7.60e-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: 39.12  E-value: 7.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNERENIENIIRAVFGLEKTFH---ILIIEDGSPDGTAAIVKTLQQEFPDRlFMIERKGKlglGTAYITGFK--W 82
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYPRElyrIFVVADNCTDDTAQVARAAGATVLER-HDPERRGK---GYALDFGFRhlL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268  83 ALEHSYEYIFEMDADFSHNPNDLPRLyeACAVQGGDVAIGSRYVSGVNVVNWPMGRVLMSYFASKYV----RIVTGLPIH 158
Cdd:cd06438   77 NLADDPDAVVVFDADNLVDPNALEEL--NARFAAGARVVQAYYNSKNPDDSWITRLYAFAFLVFNRLrplgRSNLGLSCQ 154
                        170       180
                 ....*....|....*....|
gi 492247268 159 DTTAGFkCYRRQVLETIDLD 178
Cdd:cd06438  155 LGGTGM-CFPWAVLRQAPWA 173
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
8-97 1.59e-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: 38.80  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268    8 VIIPTYNEREN---IENIIRAVFGLEKTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMIERKGKLGLGTAYITGFKWAl 84
Cdd:pfam10111   2 VVIPVYNGEKThwiQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDTTYSLAASRNRGTSHA- 80
                          90
                  ....*....|...
gi 492247268   85 eHSyEYIFEMDAD 97
Cdd:pfam10111  81 -IG-EYISFIDGD 91
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
8-98 2.59e-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: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492247268   8 VIIPTYNE-RENIENIIRAVFGLE---KTFHILIIEDGSPDGTAAIVKTLQQEFPDRLFMIERkgklglgtayITGFK-- 81
Cdd:cd06421    5 VFIPTYNEpLEIVRKTLRAALAIDyphDKLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPD----------NRHAKag 74
                         90       100
                 ....*....|....*....|.
gi 492247268  82 ---WALEHS-YEYIFEMDADF 98
Cdd:cd06421   75 nlnNALAHTtGDFVAILDADH 95
 
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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