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Conserved domains on  [gi|1279228389|gb|PJE69797.1|]
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hypothetical protein COU98_00215, partial [Candidatus Staskawiczbacteria bacterium CG10_big_fil_rev_8_21_14_0_10_38_10]

Protein Classification

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

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

CAZY:  GT2
EC:  2.4.1.117
Gene Ontology:  GO:0004581|GO:0006486
PubMed:  12200473|10521532|12691742|9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-221 2.49e-78

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: 234.00  E-value: 2.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIDKYLRnqnypsaGSGQASYEIIVVNDGSKDKTAEAVKDLT-PVIKNLKLIDNKENRGKGFV 83
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLE-------ERPSFSYEIIVVDDGSKDGTAEVARKLArKNPALIRVLTLPKNRGKGGA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  84 VRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIVIGSRGVKGAEILVSQFWIRRRLGNIFNLLAQVIIGLwG 162
Cdd:cd04188    74 VRAGMLAARGDYILFADADLATPFEELEKLEEALKTSgYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLGL-G 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1279228389 163 VWDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALIIGKKMGHKFKEIPVVWENNSVSK 221
Cdd:cd04188   153 IKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-221 2.49e-78

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: 234.00  E-value: 2.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIDKYLRnqnypsaGSGQASYEIIVVNDGSKDKTAEAVKDLT-PVIKNLKLIDNKENRGKGFV 83
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLE-------ERPSFSYEIIVVDDGSKDGTAEVARKLArKNPALIRVLTLPKNRGKGGA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  84 VRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIVIGSRGVKGAEILVSQFWIRRRLGNIFNLLAQVIIGLwG 162
Cdd:cd04188    74 VRAGMLAARGDYILFADADLATPFEELEKLEEALKTSgYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLGL-G 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1279228389 163 VWDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALIIGKKMGHKFKEIPVVWENNSVSK 221
Cdd:cd04188   153 IKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 1-221 6.23e-55

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 178.42  E-value: 6.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   1 MFLSVVIPAYNEEKKLPKTLNEIDKYLRNQNypsAGSGQASYEIIVVNDGSKDKTAEAVKDL-----TPVIkNLKLIDNK 75
Cdd:PTZ00260   70 VDLSIVIPAYNEEDRLPKMLKETIKYLESRS---RKDPKFKYEIIIVNDGSKDKTLKVAKDFwrqniNPNI-DIRLLSLL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  76 ENRGKGFVVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEAYD----IVIGSRGVKGAEILVSQ-FWIRRRLGNIF 150
Cdd:PTZ00260  146 RNKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQnglgIVFGSRNHLVDSDVVAKrKWYRNILMYGF 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279228389 151 NLLAQVIIGLwGVWDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALIIGKKMGHKFKEIPVVWENNSVSK 221
Cdd:PTZ00260  226 HFIVNTICGT-NLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSK 295
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-220 1.85e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 137.14  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   1 MFLSVVIPAYNEEKKLPKTLNEIdkylRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGK 80
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESL----LAQTYPD-------FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  81 GFVVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIVIGSRGVKGAEIlvsqfWIRRRLGNIFNLLAQviig 159
Cdd:COG0463    71 GAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGpADLVYGSRLIREGES-----DLRRLGSRLFNLVRL---- 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279228389 160 LWGVWDTQCGFKa**aGAAKDIFPKCTID-GWGFDPEALIIGKKmGHKFKEIPVVWENNSVS 220
Cdd:COG0463   142 LTNLPDSTSGFR----LFRREVLEELGFDeGFLEDTELLRALRH-GFRIAEVPVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-171 7.16e-28

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: 103.63  E-value: 7.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKKLPKTLNEidkyLRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGKGFV 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLES----LLNQTYPN-------FEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  84 VRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIVIGSRGVKGAEIlVSQFWIRRRLGNIFNLLAQVIIGLWG 162
Cdd:pfam00535  70 RNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDgADVVVGSRYVIFGET-GEYRRASRITLSRLPFFLGLRLLGLN 148


                  ....*....
gi 1279228389 163 VWDTQCGFK 171
Cdd:pfam00535 149 LPFLIGGFA 157
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-102 1.91e-10

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: 58.29  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYNEEKKLPKTLNEidkyLRNQNYPSagsgqasyEIIVVNDGSKDKTAEAVKDLtpvikNLKLIDNKENRGkgf 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD----LQALRGDA--------EVIVVDGGSTDGTVEIARSL-----GAKVIHSPKGRA--- 60

                          90       100
                  ....*....|....*....|...
gi 1279228389  83 vvRQ---GMLAAEGEYRLFTDAD 102
Cdd:TIGR04283  61 --RQmnaGAALAKGDILLFLHAD 81
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-221 2.49e-78

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: 234.00  E-value: 2.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIDKYLRnqnypsaGSGQASYEIIVVNDGSKDKTAEAVKDLT-PVIKNLKLIDNKENRGKGFV 83
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLE-------ERPSFSYEIIVVDDGSKDGTAEVARKLArKNPALIRVLTLPKNRGKGGA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  84 VRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIVIGSRGVKGAEILVSQFWIRRRLGNIFNLLAQVIIGLwG 162
Cdd:cd04188    74 VRAGMLAARGDYILFADADLATPFEELEKLEEALKTSgYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLGL-G 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1279228389 163 VWDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALIIGKKMGHKFKEIPVVWENNSVSK 221
Cdd:cd04188   153 IKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 1-221 6.23e-55

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 178.42  E-value: 6.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   1 MFLSVVIPAYNEEKKLPKTLNEIDKYLRNQNypsAGSGQASYEIIVVNDGSKDKTAEAVKDL-----TPVIkNLKLIDNK 75
Cdd:PTZ00260   70 VDLSIVIPAYNEEDRLPKMLKETIKYLESRS---RKDPKFKYEIIIVNDGSKDKTLKVAKDFwrqniNPNI-DIRLLSLL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  76 ENRGKGFVVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEAYD----IVIGSRGVKGAEILVSQ-FWIRRRLGNIF 150
Cdd:PTZ00260  146 RNKGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQnglgIVFGSRNHLVDSDVVAKrKWYRNILMYGF 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279228389 151 NLLAQVIIGLwGVWDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALIIGKKMGHKFKEIPVVWENNSVSK 221
Cdd:PTZ00260  226 HFIVNTICGT-NLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSK 295
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 5-198 1.22e-50

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: 162.74  E-value: 1.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIDKYLRNQNypsagsgqaSYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGKGFVV 84
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGY---------DYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  85 RQGMLAAEGEYRLFTDADNSTSINQIEKMW-PYFEEAYDIVIGSRGVKGAEILVSqfWIRRRLGNIFNLLAQVIIGlWGV 163
Cdd:cd04179    72 RAGFKAARGDIVVTMDADLQHPPEDIPKLLeKLLEGGADVVIGSRFVRGGGAGMP--LLRRLGSRLFNFLIRLLLG-VRI 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1279228389 164 WDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALI 198
Cdd:cd04179   149 SDTQSGFRLFRREVLEALLSLLESNGFEFGLELLV 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-220 1.85e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 137.14  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   1 MFLSVVIPAYNEEKKLPKTLNEIdkylRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGK 80
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESL----LAQTYPD-------FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  81 GFVVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIVIGSRGVKGAEIlvsqfWIRRRLGNIFNLLAQviig 159
Cdd:COG0463    71 GAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGpADLVYGSRLIREGES-----DLRRLGSRLFNLVRL---- 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279228389 160 LWGVWDTQCGFKa**aGAAKDIFPKCTID-GWGFDPEALIIGKKmGHKFKEIPVVWENNSVS 220
Cdd:COG0463   142 LTNLPDSTSGFR----LFRREVLEELGFDeGFLEDTELLRALRH-GFRIAEVPVRYRAGESK 198
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-119 9.39e-29

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: 109.45  E-value: 9.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   1 MFLSVVIPAYNEEKKLPKTLneidKYLRNQNYPsagsgQASYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGK 80
Cdd:COG1215    29 PRVSVIIPAYNEEAVIEETL----RSLLAQDYP-----KEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGK 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1279228389  81 GFVVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEE 119
Cdd:COG1215   100 AAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAD 138
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 5-213 2.00e-28

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: 106.46  E-value: 2.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIDKYLRNQNYpsagsgqasyEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGKGFVV 84
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGIDY----------EIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  85 RQGMLAAEGEYRLFTDADNSTSINQIEKMW-PYFEEAYDIVIGSRGVKGAEIlVSQFWIRRRLGNIFNLLAQVIIGLwGV 163
Cdd:cd06442    71 IEGFKAARGDVIVVMDADLSHPPEYIPELLeAQLEGGADLVIGSRYVEGGGV-EGWGLKRKLISRGANLLARLLLGR-KV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1279228389 164 WDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALIIGKKMGHKFKEIPVV 213
Cdd:cd06442   149 SDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPIT 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-171 7.16e-28

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: 103.63  E-value: 7.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKKLPKTLNEidkyLRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGKGFV 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLES----LLNQTYPN-------FEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  84 VRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIVIGSRGVKGAEIlVSQFWIRRRLGNIFNLLAQVIIGLWG 162
Cdd:pfam00535  70 RNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDgADVVVGSRYVIFGET-GEYRRASRITLSRLPFFLGLRLLGLN 148


                  ....*....
gi 1279228389 163 VWDTQCGFK 171
Cdd:pfam00535 149 LPFLIGGFA 157
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-157 2.28e-25

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: 97.55  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIDKYLRNQNYpsagsgqaSYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGKGFVV 84
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGY--------DYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAAL 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279228389  85 RQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEAYDIVIGSRGVKgaeilvSQFWIRRRLGNIFNLLAQVI 157
Cdd:cd04187    73 LAGLDHARGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNR------KESWLKRLTSKLFYRLINKL 139
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 5-126 7.81e-23

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: 90.26  E-value: 7.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNeidkYLRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGKGFVV 84
Cdd:cd00761     1 VIIPAYNEEPYLERCLE----SLLAQTYPN-------FEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAAR 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1279228389  85 RQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA--YDIVIG 126
Cdd:cd00761    70 NAGLKAARGEYILFLDADDLLLPDWLERLVAELLADpeADAVGG 113
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 5-152 7.43e-22

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: 88.44  E-value: 7.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLneidKYLRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTP-VIKNLKLIDNKENRGKGFV 83
Cdd:cd06423     1 IIVPAYNEEAVIERTI----ESLLALDYPK-------LEVIVVDDGSTDDTLEILEELAAlYIRRVLVVRDKENGGKAGA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  84 VRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEAYDIVIGSRGVK-------------GAEILVSQFWIRR---RLG 147
Cdd:cd06423    70 LNAGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRvrngsenlltrlqAIEYLSIFRLGRRaqsALG 149


                  ....*
gi 1279228389 148 NIFNL 152
Cdd:cd06423   150 GVLVL 154
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 4-213 1.33e-20

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 86.68  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKKLPKTLNEIDKYLRNQNypsagsgqaSYEIIVVNDGSKDKTAEAVKDLTPVIKN--LKLIDNKENRGKG 81
Cdd:PLN02726   12 SIIVPTYNERLNIALIVYLIFKALQDVK---------DFEIIVVDDGSPDGTQDVVKQLQKVYGEdrILLRPRPGKLGLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  82 FVVRQGMLAAEGEYRLFTDADNSTSinqiEKMWPYF-----EEAYDIVIGSRGVKGAEilVSQFWIRRRL-GNIFNLLAQ 155
Cdd:PLN02726   83 TAYIHGLKHASGDFVVIMDADLSHH----PKYLPSFikkqrETGADIVTGTRYVKGGG--VHGWDLRRKLtSRGANVLAQ 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1279228389 156 VIigLW-GVWDTQCGFKA**AGAAKDIFPKCTIDGWGFDPEALIIGKKMGHKFKEIPVV 213
Cdd:PLN02726  157 TL--LWpGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPIT 213
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 4-102 2.02e-20

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: 86.10  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKKLPKTLNEIdkylRNQNYPsagsgQASYEIIVVNDGSKDKTAEAVKDLTPviKNLKLIDNKENRGKGFV 83
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENL----LALDYP-----RDRLEIIVVSDGSTDGTAEIAREYAD--KGVKLLRFPERRGKAAA 100

                          90
                  ....*....|....*....
gi 1279228389  84 VRQGMLAAEGEYRLFTDAD 102
Cdd:cd06439   101 LNRALALATGEIVVFTDAN 119
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-140 5.02e-20

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: 84.65  E-value: 5.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEidkyLRNQNYPsagsgQASYEIIVVNDGSKDKTAEAVKDLT-PVIKNLKLIDNKE--NRGKG 81
Cdd:cd04192     1 VVIAARNEAENLPRLLQS----LSALDYP-----KEKFEVILVDDHSTDGTVQILEFAAaKPNFQLKILNNSRvsISGKK 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  82 FVVRQGMLAAEGEYRLFTDADNSTSINQIEK-MWPYFEEAYDIVIGSRGVKGAEILVSQF 140
Cdd:cd04192    72 NALTTAIKAAKGDWIVTTDADCVVPSNWLLTfVAFIQKEQIGLVAGPVIYFKGKSLLAKF 131
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 2-113 2.23e-16

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: 75.35  E-value: 2.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   2 FLSVVIPAYNEEKKLPKTLneidKYLRNQNYPsagsgQASYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDN-KENRGK 80
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELL----ESLLNQSYP-----KDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNpKRIQSA 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1279228389  81 GfvVRQGMLAAEGEYRLFTDADNSTSINQIEKM 113
Cdd:cd02525    72 G--LNIGIRNSRGDIIIRVDAHAVYPKDYILEL 102
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-102 8.11e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 72.72  E-value: 8.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   1 MFLSVVIPAYNEEKKLPKTLNEidkyLRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTpvIKNLKLIDNKENRGK 80
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLES----LLAQTYPP-------FEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGF 69

                          90       100
                  ....*....|....*....|..
gi 1279228389  81 GFVVRQGMLAAEGEYRLFTDAD 102
Cdd:COG1216    70 AAARNLGLRAAGGDYLLFLDDD 91
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-103 8.19e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 60.44  E-value: 8.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYNEEKKLPKTLNEidkyLRNQNYpsagsgqASYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDnKENRGKGF 82
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMES----LIAQTW-------TALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSV 75

                          90       100
                  ....*....|....*....|.
gi 1279228389  83 VVRQGMLAAEGEYRLFTDADN 103
Cdd:PRK10073   76 ARNTGLAVATGKYVAFPDADD 96
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 3-102 1.38e-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: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYNEEKKLPKTLneidKYLRNQNYPSAgsgqasyEIIVVNDGSKDKTAEAVKDLtpvikNLKLIDNKENRGkgf 82
Cdd:cd02522     1 LSIIIPTLNEAENLPRLL----ASLRRLNPLPL-------EIIVVDGGSTDGTVAIARSA-----GVVVISSPKGRA--- 61

                          90       100
                  ....*....|....*....|...
gi 1279228389  83 vvRQ---GMLAAEGEYRLFTDAD 102
Cdd:cd02522    62 --RQmnaGAAAARGDWLLFLHAD 82
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-102 1.91e-10

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: 58.29  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYNEEKKLPKTLNEidkyLRNQNYPSagsgqasyEIIVVNDGSKDKTAEAVKDLtpvikNLKLIDNKENRGkgf 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD----LQALRGDA--------EVIVVDGGSTDGTVEIARSL-----GAKVIHSPKGRA--- 60

                          90       100
                  ....*....|....*....|...
gi 1279228389  83 vvRQ---GMLAAEGEYRLFTDAD 102
Cdd:TIGR04283  61 --RQmnaGAALAKGDILLFLHAD 81
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-102 3.44e-09

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 54.10  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEidkyLRNQNYPSagsgqasYEIIVVNDGSKDKTAEAVKDLTPvikNLKLIDNKENRGKGFVV 84
Cdd:cd04186     1 IIIVNYNSLEYLKACLDS----LLAQTYPD-------FEVIVVDNASTDGSVELLRELFP---EVRLIRNGENLGFGAGN 66

                          90
                  ....*....|....*...
gi 1279228389  85 RQGMLAAEGEYRLFTDAD 102
Cdd:cd04186    67 NQGIREAKGDYVLLLNPD 84
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 5-131 1.56e-08

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: 52.60  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIdkylRNQNYPSAGsgqasYEIIVVNDGSKDKTAEAVKDL-TPVIKNlkliDNKENRGKGFV 83
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSL----KAQDYPREL-----YRIFVVADNCTDDTAQVARAAgATVLER----HDPERRGKGYA 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1279228389  84 VRQG---MLAAEGEYRLFT--DADNSTSINQIEKMWPYFEEAYDIVIGSRGVK 131
Cdd:cd06438    68 LDFGfrhLLNLADDPDAVVvfDADNLVDPNALEELNARFAAGARVVQAYYNSK 120
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 3-159 4.38e-08

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 52.43  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYNEEKKLPKTLNEIDKYLRNQNYPsagsgqasYEIIVVNDGSKDKTAEAVKDLTPVIKN--LKLIDNKeNRGK 80
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAACESLGKE--------YEILLIDDGSSDNSAEMLVEAAQAPDShiVAILLNR-NYGQ 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279228389  81 GFVVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEAYDIVIGSRGVKgaeilvSQFWIRRRLGNIFNLLAQVIIG 159
Cdd:PRK10714   79 HSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNR------QDSWFRKTASKMINRLIQRTTG 151
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-102 1.91e-07

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: 49.98  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYNEEKKLPKTLNEIDKylrnqnypsagsgqASYEIIVVNDGSKDKTAEAVKDLTPviknlKLIDNKENrgkGF 82
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKW--------------AVDEIIVVDSGSTDRTVEIAKEYGA-----KVYQRWWD---GF 59

                          90       100
                  ....*....|....*....|..
gi 1279228389  83 V--VRQGMLAAEGEYRLFTDAD 102
Cdd:cd02511    60 GaqRNFALELATNDWVLSLDAD 81
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 5-149 3.36e-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: 45.84  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLNEIDKYLRNqnypsagsgqasYEIIVVNDGSKDKTAEAVKdltPVIKNLKLI---DNKEN--RG 79
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNKPN------------FLVLVIDDASDDDTAGIVR---LAITDSRVHllrRHLPNarTG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389  80 KGFVVRQG------MLAAEGEYR---LFT--DADNSTSINQIEKMWPYFEEAydivigsrGVKGAEILVsqfWIRRRLGN 148
Cdd:cd06436    66 KGDALNAAydqirqILIEEGADPervIIAviDADGRLDPNALEAVAPYFSDP--------RVAGTQSRV---RMYNRHKN 134


                  .
gi 1279228389 149 I 149
Cdd:cd06436   135 L 135
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-113 6.13e-06

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 45.73  E-value: 6.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKKlpktlNEIDKYLRNQnypsAGSGQASYEIIVVNDGSKDKTAEAVKDltpvIKNLKLIDNKENR----- 78
Cdd:pfam10111   1 SVVIPVYNGEKT-----HWIQERILNQ----TFQYDPEFELIIINDGSTDKTLEEVSS----IKDHNLQVYYPNApdtty 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1279228389  79 GKGFVVRQGMLAAEGEYRLFTDADNSTSINQIEKM 113
Cdd:pfam10111  68 SLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQ 102
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 4-102 7.81e-06

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 44.93  E-value: 7.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKKLPKTLNEIdkylRNQNYPSAgsgqasyEIIVVNDGSKDKTAEAVKDLTP-VIKNLKLIDNKENRG--K 80
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSI----LAQTYKND-------ELIISDDGSTDGTVEIIKEYIDkDPFIIILIRNGKNLGvaR 69

                          90       100
                  ....*....|....*....|..
gi 1279228389  81 GFvvRQGMLAAEGEYRLFTDAD 102
Cdd:cd04196    70 NF--ESLLQAADGDYVFFCDQD 89
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 5-103 8.77e-06

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 45.14  E-value: 8.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKklpkTLNEIDKYLRNQNYpsagsgQASYEIIVVNDGSKDKTAEAVKDLTPVIKNLKLI------DNKENR 78
Cdd:cd06913     1 IILPVHNGEQ----WLDECLESVLQQDF------EGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIvlvgshNSPSPK 70

                          90       100
                  ....*....|....*....|....*
gi 1279228389  79 GKGFVVRQGMLAAEGEYRLFTDADN 103
Cdd:cd06913    71 GVGYAKNQAIAQSSGRYLCFLDSDD 95
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 4-102 2.16e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 44.14  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKklpkTLNEIDKYLRnqnyPSAGSGqASYEIIVVNDGSKDKTA--------------EAVKDLTPViknl 69
Cdd:PRK13915   34 SVVLPALNEEE----TVGKVVDSIR----PLLMEP-LVDELIVIDSGSTDATAeraaaagarvvsreEILPELPPR---- 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1279228389  70 klidnkenRGKGFVVRQGMLAAEGEYRLFTDAD 102
Cdd:PRK13915  101 --------PGKGEALWRSLAATTGDIVVFVDAD 125
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 5-102 2.16e-05

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 43.34  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKLPKTLneiDKYLRNQNYPsagsgqasYEIIVVNDGSKDKTAEAVKDLTP-VIKNLKLIDNKENrgkGF- 82
Cdd:cd06420     1 LIITTYNRPEALELVL---KSVLNQSILP--------FEVIIADDGSTEETKELIEEFKSqFPIPIKHVWQEDE---GFr 66

                          90       100
                  ....*....|....*....|...
gi 1279228389  83 ---VVRQGMLAAEGEYRLFTDAD 102
Cdd:cd06420    67 kakIRNKAIAAAKGDYLIFIDGD 89
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-66 8.78e-05

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 41.76  E-value: 8.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279228389   4 SVVIPAYNEEKKLPKTLNEIdkylRNQNYPsagsgqaSYEIIVVNDGSKDKTAEAVKDLTPVI 66
Cdd:cd06433     1 SIITPTYNQAETLEETIDSV----LSQTYP-------NIEYIVIDGGSTDGTVDIIKKYEDKI 52
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-79 2.02e-04

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: 40.70  E-value: 2.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279228389   5 VVIPAYNEEKKLPKTLNeidkYLRNQNYPSAgsgqasyEIIVVNDGSKDKTAEAVKDLTPViKNLKLIDNKENRG 79
Cdd:cd04185     1 AVVVTYNRLDLLKECLD----ALLAQTRPPD-------HIIVIDNASTDGTAEWLTSLGDL-DNIVYLRLPENLG 63
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 2-120 4.95e-04

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 39.93  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   2 FLSVVIPAYNE-EKKLPKTLNEIdkylrnqnypsagSGQASYEIIVVNDGSKDKTAEAVKDLTPviKNLKLIDNKENRGK 80
Cdd:cd06434     1 DVTVIIPVYDEdPDVFRECLRSI-------------LRQKPLEIIVVTDGDDEPYLSILSQTVK--YGGIFVITVPHPGK 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1279228389  81 GFVVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEA 120
Cdd:cd06434    66 RRALAEGIRHVTTDIVVLLDSDTVWPPNALPEMLKPFEDP 105
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-102 1.13e-03

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 38.72  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYN-EEKKLPKTLNEIdkylRNQNYPsagsgqaSYEIIVVNDGSkdkTAEAVKDltpVIKNLKLID-------N 74
Cdd:cd04184     3 ISIVMPVYNtPEKYLREAIESV----RAQTYP-------NWELCIADDAS---TDPEVKR---VLKKYAAQDprikvvfR 65

                          90       100
                  ....*....|....*....|....*...
gi 1279228389  75 KENRGKGFVVRQGMLAAEGEYRLFTDAD 102
Cdd:cd04184    66 EENGGISAATNSALELATGEFVALLDHD 93
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-124 1.73e-03

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 38.12  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   3 LSVVIPAYNEEKKLPKTLNEIDKylrnQNYPsagsgqaSYEIIVVNDGSKDKT---AEAVKDLTPVIKnLKLIDNKENRG 79
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILA----QPYP-------PVEVVVVVNPSDAETldvAEEIAARFPDVR-LRVIRNARLLG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1279228389  80 KGfVVRQGML----AAEGEYRLFTDADNSTSINQIEKMWPYFEEA-YDIV 124
Cdd:pfam13641  72 PT-GKSRGLNhgfrAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPkVGAV 120
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 4-130 4.20e-03

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 36.91  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   4 SVVIPAYNEEKklPKTLNE-IDKYLRNQNYPSagsgqasyEIIVVNDGSKDKTAEAVKDLTPVIKNLKLIDNKENRGKGF 82
Cdd:cd04195     1 SVLMSVYIKEK--PEFLREaLESILKQTLPPD--------EVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGK 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1279228389  83 VVRQGMLAAEGEYRLFTDADNSTSINQIEKMWPYFEEAYDIVIGSRGV 130
Cdd:cd04195    71 ALNEGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGV 118
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 5-122 7.99e-03

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: 36.49  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279228389   5 VVIPAYNEEKKlpKTLNEIDKYLRNqnypsagsgqaSYEIIVVnDGSKDKTAEAVKDLtpVIKNLKLIDNKENRGKGFVV 84
Cdd:cd02526     1 AVVVTYNPDLS--KLKELLAALAEQ-----------VDKVVVV-DNSSGNDIELRLRL--NSEKIELIHLGENLGIAKAL 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1279228389  85 RQGM--LAAEG-EYRLFTDADNSTSINQIEKMWPYFEEAYD 122
Cdd:cd02526    65 NIGIkaALENGaDYVLLFDQDSVPPPDMVEKLLAYKILSDK 105
 
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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