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Conserved domains on  [gi|298235808|gb|ADI66940|]
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glycosyltransferase, group 2 family protein [Mobiluncus curtisii ATCC 43063]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135280)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  12691742|9445404|12200473|10508766
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 20-178 1.56e-23

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: 94.18  E-value: 1.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRASKALPRADL---FVVIDDGSTDNTGEAARSAGA-----VVVRHSVNRGKASAMETGAKvVAM 91
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYdyeIIVVDDGSTDGTAEIARELAArvprvRVIRLSRNFGKGAAVRAGFK-AAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  92 RDpedgprrLILFLDADLGDSAAQTFPLVEAVMQGRTDCAIAAlpRQAGAGGHG------FVTGLSRRAIRWATGWEPLQ 165
Cdd:cd04179   80 GD-------IVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGS--RFVRGGGAGmpllrrLGSRLFNFLIRLLLGVRISD 150

                        170
                 ....*....|...
gi 298235808 166 PLSGQRCLNAEAF 178
Cdd:cd04179  151 TQSGFRLFRREVL 163
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 20-178 1.56e-23

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: 94.18  E-value: 1.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRASKALPRADL---FVVIDDGSTDNTGEAARSAGA-----VVVRHSVNRGKASAMETGAKvVAM 91
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYdyeIIVVDDGSTDGTAEIARELAArvprvRVIRLSRNFGKGAAVRAGFK-AAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  92 RDpedgprrLILFLDADLGDSAAQTFPLVEAVMQGRTDCAIAAlpRQAGAGGHG------FVTGLSRRAIRWATGWEPLQ 165
Cdd:cd04179   80 GD-------IVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGS--RFVRGGGAGmpllrrLGSRLFNFLIRLLLGVRISD 150

                        170
                 ....*....|...
gi 298235808 166 PLSGQRCLNAEAF 178
Cdd:cd04179  151 TQSGFRLFRREVL 163
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 17-228 1.01e-22

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 92.46  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  17 KVAVVIPAKDEGDSIGATIRASKALPRADL-FVVIDDGSTDNTGEAARSAGA-----VVVRHSVNRGKASAMETGAKVVa 90
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFeIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAAA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  91 mrdpeDGprRLILFLDADLGDSAAQTFPLVEAVMQGRTDCAIAAlpRQAGAGGHGFVTGLSRRAIRWATGWEPLQPLSGQ 170
Cdd:COG0463   82 -----RG--DYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS--RLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 298235808 171 RCLNAEaFFDCLPLAHKWGVETGMtIDLLVKGYSVQEVPcdlTHRATGNDMAGYRHRL 228
Cdd:COG0463  153 RLFRRE-VLEELGFDEGFLEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNLRDLL 205
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 20-185 7.11e-16

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: 73.20  E-value: 7.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808   20 VVIPAKDEGDSIGATIRASKALPRADL-FVVIDDGSTDNTGEAARSA-----GAVVVRHSVNRGKASAMETGAKVVamrd 93
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFeIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808   94 peDGPrrLILFLDADlgDSAAQTF--PLVEAVMQGRTDCAIAALPRqagaggHGFVTGLSRRAIRWatGWEPLQPLSGQR 171
Cdd:pfam00535  78 --TGD--YIAFLDAD--DEVPPDWleKLVEALEEDGADVVVGSRYV------IFGETGEYRRASRI--TLSRLPFFLGLR 143

                         170
                  ....*....|....
gi 298235808  172 CLNAEAFFDCLPLA 185
Cdd:pfam00535 144 LLGLNLPFLIGGFA 157
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 15-199 4.67e-14

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 70.72  E-value: 4.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  15 DQKVAVVIPAKDEGDSIG---ATIRASKALPRADLFVVIDDGSTDNTGEAARSAGAVVV-------RHSVNRGKASAMET 84
Cdd:PRK13915  30 GRTVSVVLPALNEEETVGkvvDSIRPLLMEPLVDELIVIDSGSTDATAERAAAAGARVVsreeilpELPPRPGKGEALWR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  85 GAKVVamrdpeDGprRLILFLDADLGDSAAQTFP-LVEAVMqgrTDCAIA----------ALPRQAGAGGHGFVTGLSRR 153
Cdd:PRK13915 110 SLAAT------TG--DIVVFVDADLINFDPMFVPgLLGPLL---TDPGVHlvkafyrrplRVSGGVDATGGGRVTELVAR 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 298235808 154 AIrWATGWEPL----QPLSGQRCLNAEAFFDcLPLAHKWGVETGMTIDLL 199
Cdd:PRK13915 179 PL-LNLLRPELagfvQPLGGEYAGRRELLES-LPFVPGYGVEIGLLIDTL 226
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 18-108 1.86e-08

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


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 53.28  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808   18 VAVVIPAKDEGDSIGATIRASKALPRADLFVVIDDGSTDNTGEAARSAGAVVVrHSvNRGKASAMETGAKvVAMRDpedg 97
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGDAEVIVVDGGSTDGTVEIARSLGAKVI-HS-PKGRARQMNAGAA-LAKGD---- 73

                          90
                  ....*....|.
gi 298235808   98 prrLILFLDAD 108
Cdd:TIGR04283  74 ---ILLFLHAD 81
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 20-178 1.56e-23

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: 94.18  E-value: 1.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRASKALPRADL---FVVIDDGSTDNTGEAARSAGA-----VVVRHSVNRGKASAMETGAKvVAM 91
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYdyeIIVVDDGSTDGTAEIARELAArvprvRVIRLSRNFGKGAAVRAGFK-AAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  92 RDpedgprrLILFLDADLGDSAAQTFPLVEAVMQGRTDCAIAAlpRQAGAGGHG------FVTGLSRRAIRWATGWEPLQ 165
Cdd:cd04179   80 GD-------IVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGS--RFVRGGGAGmpllrrLGSRLFNFLIRLLLGVRISD 150

                        170
                 ....*....|...
gi 298235808 166 PLSGQRCLNAEAF 178
Cdd:cd04179  151 TQSGFRLFRREVL 163
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 17-228 1.01e-22

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 92.46  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  17 KVAVVIPAKDEGDSIGATIRASKALPRADL-FVVIDDGSTDNTGEAARSAGA-----VVVRHSVNRGKASAMETGAKVVa 90
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFeIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAAA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  91 mrdpeDGprRLILFLDADLGDSAAQTFPLVEAVMQGRTDCAIAAlpRQAGAGGHGFVTGLSRRAIRWATGWEPLQPLSGQ 170
Cdd:COG0463   82 -----RG--DYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS--RLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 298235808 171 RCLNAEaFFDCLPLAHKWGVETGMtIDLLVKGYSVQEVPcdlTHRATGNDMAGYRHRL 228
Cdd:COG0463  153 RLFRRE-VLEELGFDEGFLEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNLRDLL 205
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 12-163 1.70e-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: 77.47  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  12 PHPDQKVAVVIPAKDEGDSIGATIRASKAL--PRADL-FVVIDDGSTDNTGEAARSAGA-----VVVRHSVNRGKASAME 83
Cdd:COG1215   25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQdyPKEKLeVIVVDDGSTDETAEIARELAAeyprvRVIERPENGGKAAALN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  84 TGAKVVamrdpeDGPrrLILFLDADlgdsaaqTFPLVEAVMQgrtdcAIAALpRQAGAGGHGFVTGLSRRAIRWATGWEP 163
Cdd:COG1215  105 AGLKAA------RGD--IVVFLDAD-------TVLDPDWLRR-----LVAAF-ADPGVGASGANLAFRREALEEVGGFDE 163
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 20-108 1.95e-16

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 74.96  E-value: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRASKAL--PRADLfVVIDDGSTDNTGEAARSAGA------VVVRHSVNRGKASAMETGAKVVam 91
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALdyPKLEV-IVVDDGSTDDTLEILEELAAlyirrvLVVRDKENGGKAGALNAGLRHA-- 77

                         90
                 ....*....|....*..
gi 298235808  92 rdpeDGPrrLILFLDAD 108
Cdd:cd06423   78 ----KGD--IVVVLDAD 88
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 20-185 7.11e-16

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: 73.20  E-value: 7.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808   20 VVIPAKDEGDSIGATIRASKALPRADL-FVVIDDGSTDNTGEAARSA-----GAVVVRHSVNRGKASAMETGAKVVamrd 93
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFeIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808   94 peDGPrrLILFLDADlgDSAAQTF--PLVEAVMQGRTDCAIAALPRqagaggHGFVTGLSRRAIRWatGWEPLQPLSGQR 171
Cdd:pfam00535  78 --TGD--YIAFLDAD--DEVPPDWleKLVEALEEDGADVVVGSRYV------IFGETGEYRRASRI--TLSRLPFFLGLR 143

                         170
                  ....*....|....
gi 298235808  172 CLNAEAFFDCLPLA 185
Cdd:pfam00535 144 LLGLNLPFLIGGFA 157
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 15-199 4.67e-14

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 70.72  E-value: 4.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  15 DQKVAVVIPAKDEGDSIG---ATIRASKALPRADLFVVIDDGSTDNTGEAARSAGAVVV-------RHSVNRGKASAMET 84
Cdd:PRK13915  30 GRTVSVVLPALNEEETVGkvvDSIRPLLMEPLVDELIVIDSGSTDATAERAAAAGARVVsreeilpELPPRPGKGEALWR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  85 GAKVVamrdpeDGprRLILFLDADLGDSAAQTFP-LVEAVMqgrTDCAIA----------ALPRQAGAGGHGFVTGLSRR 153
Cdd:PRK13915 110 SLAAT------TG--DIVVFVDADLINFDPMFVPgLLGPLL---TDPGVHlvkafyrrplRVSGGVDATGGGRVTELVAR 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 298235808 154 AIrWATGWEPL----QPLSGQRCLNAEAFFDcLPLAHKWGVETGMTIDLL 199
Cdd:PRK13915 179 PL-LNLLRPELagfvQPLGGEYAGRRELLES-LPFVPGYGVEIGLLIDTL 226
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 20-108 1.07e-12

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: 64.93  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRASKAL----PRADLFVVIDDgSTDNTGEAARSAGA-VVVRH-SVNRGKASAMETG-AKVVAMR 92
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQdyprELYRIFVVADN-CTDDTAQVARAAGAtVLERHdPERRGKGYALDFGfRHLLNLA 79

                         90
                 ....*....|....*.
gi 298235808  93 DPEDGprrlILFLDAD 108
Cdd:cd06438   80 DDPDA----VVVFDAD 91
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 17-110 1.78e-12

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: 65.30  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  17 KVAVVIPAKDEGDSIGATIRASKAL--PRADL-FVVIDDGSTDNTGEAARSAGA---VVVRHSVNRGKASAMETGAK--- 87
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKLENLLALdyPRDRLeIIVVSDGSTDGTAEIAREYADkgvKLLRFPERRGKAAALNRALAlat 109

                         90       100       110
                 ....*....|....*....|....*....|.
gi 298235808  88 --VVAMRD-----PEDGPRRLI-LFLDADLG 110
Cdd:cd06439  110 geIVVFTDanallDPDALRLLVrHFADPSVG 140
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 20-133 5.48e-12

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: 63.36  E-value: 5.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATI-RASKALPRADLF----VVIDDGSTDNTGEAARSAGA------VVVRHSVNRGKASAMETGakV 88
Cdd:cd04188    1 VVIPAYNEEKRLPPTLeEAVEYLEERPSFsyeiIVVDDGSKDGTAEVARKLARknpaliRVLTLPKNRGKGGAVRAG--M 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 298235808  89 VAMRDpedgprRLILFLDADLGDSAAQTFPLVEAVMQGRTDCAIA 133
Cdd:cd04188   79 LAARG------DYILFADADLATPFEELEKLEEALKTSGYDIAIG 117
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 20-108 3.75e-11

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: 59.83  E-value: 3.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRASKALPRADL-FVVIDDGSTDNTGEAARSAGA-----VVVRHSVNRGKASAMETGAKVVamrd 93
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFeVIVVDDGSTDGTLEILEEYAKkdprvIRVINEENQGLAAARNAGLKAA---- 76

                         90
                 ....*....|....*
gi 298235808  94 peDGprRLILFLDAD 108
Cdd:cd00761   77 --RG--EYILFLDAD 87
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 18-108 2.69e-10

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: 58.74  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  18 VAVVIPAKDEGDSIGATIRASKALPRADL-FVVIDDGSTDNTGEAARSAGAVVVRHsvNRGKASAMETGAKVVAmrdped 96
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLeIIVVDGGSTDGTVAIARSAGVVVISS--PKGRARQMNAGAAAAR------ 72

                         90
                 ....*....|..
gi 298235808  97 gpRRLILFLDAD 108
Cdd:cd02522   73 --GDWLLFLHAD 82
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 20-209 7.34e-09

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: 54.46  E-value: 7.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRA-SKALPRADL-FVVIDDGSTDNTGEAARS----AGAVVVRHSVN-RGKASAMETGAKVVAmr 92
Cdd:cd06442    1 IIIPTYNERENIPELIERlDAALKGIDYeIIVVDDNSPDGTAEIVRElakeYPRVRLIVRPGkRGLGSAYIEGFKAAR-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  93 dpedGPrrLILFLDADLGDSAAQTFPLVEAVMQGRTDCAIAAlpRQAGAGG-HGFvtGLSRRAI--------RWATGWEP 163
Cdd:cd06442   79 ----GD--VIVVMDADLSHPPEYIPELLEAQLEGGADLVIGS--RYVEGGGvEGW--GLKRKLIsrganllaRLLLGRKV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 298235808 164 LQPLSGQRCLNAEAFFD----CLPLAHKWGVEtgMTIDLLVKGYSVQEVP 209
Cdd:cd06442  149 SDPTSGFRAYRREVLEKlidsLVSKGYKFQLE--LLVRARRLGYRIVEVP 196
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 20-109 1.70e-08

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: 52.86  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRA-SKALPRADL---FVVIDDGSTDNTGE-----AARSAGAVVVRHSVNRGKASAMETGAKVVa 90
Cdd:cd04187    1 IVVPVYNEEENLPELYERlKAVLESLGYdyeIIFVDDGSTDRTLEilrelAARDPRVKVIRLSRNFGQQAALLAGLDHA- 79

                         90
                 ....*....|....*....
gi 298235808  91 mrdpeDGprRLILFLDADL 109
Cdd:cd04187   80 -----RG--DAVITMDADL 91
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 18-108 1.86e-08

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


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 53.28  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808   18 VAVVIPAKDEGDSIGATIRASKALPRADLFVVIDDGSTDNTGEAARSAGAVVVrHSvNRGKASAMETGAKvVAMRDpedg 97
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGDAEVIVVDGGSTDGTVEIARSLGAKVI-HS-PKGRARQMNAGAA-LAKGD---- 73

                          90
                  ....*....|.
gi 298235808   98 prrLILFLDAD 108
Cdd:TIGR04283  74 ---ILLFLHAD 81
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 17-108 2.26e-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: 53.45  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  17 KVAVVIPAKDEGDSIGATIRASKALprADLFVVIDDGSTDNTGEAARSAGAVVVRH-----SVNRGKASAMETGakvvam 91
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWA--VDEIIVVDSGSTDRTVEIAKEYGAKVYQRwwdgfGAQRNFALELATN------ 72

                         90
                 ....*....|....*..
gi 298235808  92 rdpedgprRLILFLDAD 108
Cdd:cd02511   73 --------DWVLSLDAD 81
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
17-108 3.91e-08

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 52.30  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  17 KVAVVIPAKDEGDSIGATIRASKALPRADL-FVVIDDGSTDNTGEAARS---AGAVVVRHSVNRGKASAMETGAKVVamr 92
Cdd:COG1216    4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFeVIVVDNGSTDGTAELLAAlafPRVRVIRNPENLGFAAARNLGLRAA--- 80

                         90
                 ....*....|....*.
gi 298235808  93 dpeDGPrrLILFLDAD 108
Cdd:COG1216   81 ---GGD--YLLFLDDD 91
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 12-126 7.13e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 49.35  E-value: 7.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  12 PHPDQKVAVVIPAKDEGDSIGATIR----ASKALPRADLFVVIDDGSTDNTG----EAARSAGAVVVRHSVNR--GKASA 81
Cdd:PRK10714   2 IHPIKKVSVVIPVYNEQESLPELIRrttaACESLGKEYEILLIDDGSSDNSAemlvEAAQAPDSHIVAILLNRnyGQHSA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 298235808  82 METGAKVVamrdpeDGPrrLILFLDADLGDSAAQTFPLVEAVMQG 126
Cdd:PRK10714  82 IMAGFSHV------TGD--LIITLDADLQNPPEEIPRLVAKADEG 118
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 20-108 1.49e-06

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: 47.38  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  20 VVIPAKDEGDSIGATIRASKALPRADLFVVIDDGSTDNTGEAARSAGA-----VVVRHSVN--RGKASAMETG-AKVVAM 91
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNKPNFLVLVIDDASDDDTAGIVRLAITdsrvhLLRRHLPNarTGKGDALNAAyDQIRQI 80

                         90
                 ....*....|....*....
gi 298235808  92 RDPEDGPRR--LILFLDAD 108
Cdd:cd06436   81 LIEEGADPErvIIAVIDAD 99
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 25-108 1.03e-05

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 43.39  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808   25 KDEGDSIGATIRASKALpRADLFVVIDDGSTDNTGEAARSAGAVVVRHSVNRGKASAMETGAKVVAMRDPEDGprRLILF 104
Cdd:pfam13704   1 RNEADILPQWLAHHLAL-GFDHIYVYDNGSDDGTAEILARLPDVSILRSDLSYKDARFQVDWRNALLARYAEA--DWVLV 77


                  ....
gi 298235808  105 LDAD 108
Cdd:pfam13704  78 VDAD 81
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 19-109 1.15e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 42.83  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  19 AVVIPAKDEGDSIGATIRAS-KALPRADLF--------VVIDDGSTDNTGEAARS---------AGAVVVRHSVNRGKAS 80
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETiKYLESRSRKdpkfkyeiIIVNDGSKDKTLKVAKDfwrqninpnIDIRLLSLLRNKGKGG 152

                         90       100
                 ....*....|....*....|....*....
gi 298235808  81 AMETGakVVAMRDpedgprRLILFLDADL 109
Cdd:PTZ00260 153 AVRIG--MLASRG------KYILMVDADG 173
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 17-108 1.56e-04

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: 42.22  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298235808  17 KVAVVIPAKDEGDSIGATIRASKA--LPRADL-FVVIDDGSTDNTGEAARS----AGAVVVRHSVNRGKASAMETGAKvV 89
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNqsYPKDLIeIIVVDGGSTDGTREIVQEyaakDPRIRLIDNPKRIQSAGLNIGIR-N 79

                         90
                 ....*....|....*....
gi 298235808  90 AMRDpedgprrLILFLDAD 108
Cdd:cd02525   80 SRGD-------IIIRVDAH 91
 
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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