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Conserved domains on  [gi|1907151770|ref|XP_036019115|]
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dolichyl-phosphate beta-glucosyltransferase isoform X1 [Mus musculus]

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

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 ...
 52-272 2.98e-124

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: 353.80  E-value: 2.98e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMDEALNYLEKRQKhdctFTYEVIVVDDGSEDQTSKVALKYCQKYGSDkVRVITLVRNRGKGGAVR 131
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPS----FSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 132 MGVFSSRGEKILMADADGATKFPDVEKLEKglsdlQPWPEQMAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLCV 211
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEE-----ALKTSGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907151770 212 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQCLQIPIAEVAVNWTEIEGSK 272
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 52-272 2.98e-124

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: 353.80  E-value: 2.98e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMDEALNYLEKRQKhdctFTYEVIVVDDGSEDQTSKVALKYCQKYGSDkVRVITLVRNRGKGGAVR 131
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPS----FSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 132 MGVFSSRGEKILMADADGATKFPDVEKLEKglsdlQPWPEQMAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLCV 211
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEE-----ALKTSGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907151770 212 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQCLQIPIAEVAVNWTEIEGSK 272
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 49-301 1.78e-119

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 346.37  E-value: 1.78e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  49 QLSVVVPSYNEEKRLPVMMDEALNYLEKRQKHDCTFTYEVIVVDDGSEDQTSKVALKYCQKYGSDKV--RVITLVRNRGK 126
Cdd:PTZ00260   71 DLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdiRLLSLLRNKGK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 127 GGAVRMGVFSSRGEKILMADADGATKFPDVEKLEKGLsdLQPWPEQMAIACGSRAHLEK-ESIAQRSYFRTFLMYGFHFL 205
Cdd:PTZ00260  151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIM--LKIEQNGLGIVFGSRNHLVDsDVVAKRKWYRNILMYGFHFI 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 206 VWFLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQCLQIPIAEVAVNWTEIEGSKLVPFWSWLQMGKD 285
Cdd:PTZ00260  229 VNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISASIQMARD 308

                         250
                  ....*....|....*.
gi 1907151770 286 LLFIRLRYLTGAWRLK 301
Cdd:PTZ00260  309 ILLVRSFYLLGIWKVK 324
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 47-271 2.05e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 2.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  47 TKQLSVVVPSYNEEKRLPVMMDEALNYLekrqkhdcTFTYEVIVVDDGSEDQTSKVALKYCQKYgsDKVRVITLVRNRGK 126
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQT--------YPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 127 GGAVRMGVFSSRGEKILMADADGatkFPDVEKLEKGLSDLQPWPEqmAIACGSRAHLEKESIaqrsyFRTFLMYGFHFLV 206
Cdd:COG0463    71 GAARNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEGPA--DLVYGSRLIREGESD-----LRRLGSRLFNLVR 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907151770 207 WFLCvkgIRDTQCGFKLLTREAAARTFSSlhiERWAFDVELLYIAQcLQIPIAEVAVNWTEIEGS 271
Cdd:COG0463   141 LLTN---LPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALR-HGFRIAEVPVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 51-228 7.53e-26

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: 100.55  E-value: 7.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEKRLPVMMDEALNylekrQKHDctfTYEVIVVDDGSEDQTSKVALKYCQKYgsDKVRVITLVRNRGKGGAV 130
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN-----QTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGAR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 131 RMGVFSSRGEKILMADADGATKFPDVEKLEKGLSDLQPwpeqmAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLC 210
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGA-----DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145

                         170
                  ....*....|....*...
gi 1907151770 211 VKGIRDTQCGFKLLTREA 228
Cdd:pfam00535 146 GLNLPFLIGGFALYRREA 163
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 50-165 2.78e-09

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: 56.37  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  50 LSVVVPSYNEEKRLPvmmdEALNYLeKRQKHDCtftyEVIVVDDGSEDQTSKVAlkycqkyGSDKVRVITLVRNRgkggA 129
Cdd:TIGR04283   1 LSIIIPVLNEAATLP----ELLADL-QALRGDA----EVIVVDGGSTDGTVEIA-------RSLGAKVIHSPKGR----A 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907151770 130 VRM--GVFSSRGEKILMADADgaTKFPD--VEKLEKGLSD 165
Cdd:TIGR04283  61 RQMnaGAALAKGDILLFLHAD--TRLPKdfLEAIRRALAK 98
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
50-107 2.31e-06

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 48.25  E-value: 2.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  50 LSVVVPSYNEEKRLPVMMDeALnyleKRQKHDCTFTYEVIVVDDGSEDQTSKV------------ALKYC 107
Cdd:NF038302    3 FTVAIPTYNGANRLPEVLE-RL----RSQIGTESLSWEIIVVDNNSTDNTAQVvqeyqknwpspyPLRYC 67
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 52-272 2.98e-124

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: 353.80  E-value: 2.98e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMDEALNYLEKRQKhdctFTYEVIVVDDGSEDQTSKVALKYCQKYGSDkVRVITLVRNRGKGGAVR 131
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPS----FSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 132 MGVFSSRGEKILMADADGATKFPDVEKLEKglsdlQPWPEQMAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLCV 211
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEE-----ALKTSGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907151770 212 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQCLQIPIAEVAVNWTEIEGSK 272
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 49-301 1.78e-119

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 346.37  E-value: 1.78e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  49 QLSVVVPSYNEEKRLPVMMDEALNYLEKRQKHDCTFTYEVIVVDDGSEDQTSKVALKYCQKYGSDKV--RVITLVRNRGK 126
Cdd:PTZ00260   71 DLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdiRLLSLLRNKGK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 127 GGAVRMGVFSSRGEKILMADADGATKFPDVEKLEKGLsdLQPWPEQMAIACGSRAHLEK-ESIAQRSYFRTFLMYGFHFL 205
Cdd:PTZ00260  151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIM--LKIEQNGLGIVFGSRNHLVDsDVVAKRKWYRNILMYGFHFI 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 206 VWFLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQCLQIPIAEVAVNWTEIEGSKLVPFWSWLQMGKD 285
Cdd:PTZ00260  229 VNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISASIQMARD 308

                         250
                  ....*....|....*.
gi 1907151770 286 LLFIRLRYLTGAWRLK 301
Cdd:PTZ00260  309 ILLVRSFYLLGIWKVK 324
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 52-251 3.22e-59

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: 187.40  E-value: 3.22e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMDEALNYLEKrqkhdcTFTYEVIVVDDGSEDQTSKVALKYCQKYGsdKVRVITLVRNRGKGGAVR 131
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE------GYDYEIIVVDDGSTDGTAEIARELAARVP--RVRVIRLSRNFGKGAAVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 132 MGVFSSRGEKILMADADGATKFPDVEKLEKGLsdlqpWPEQMAIACGSRAHleKESIAQRSYFRTFLMYGFHFLVWFLCV 211
Cdd:cd04179    73 AGFKAARGDIVVTMDADLQHPPEDIPKLLEKL-----LEGGADVVIGSRFV--RGGGAGMPLLRRLGSRLFNFLIRLLLG 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907151770 212 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIA 251
Cdd:cd04179   146 VRISDTQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 47-271 2.05e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 2.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  47 TKQLSVVVPSYNEEKRLPVMMDEALNYLekrqkhdcTFTYEVIVVDDGSEDQTSKVALKYCQKYgsDKVRVITLVRNRGK 126
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQT--------YPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 127 GGAVRMGVFSSRGEKILMADADGatkFPDVEKLEKGLSDLQPWPEqmAIACGSRAHLEKESIaqrsyFRTFLMYGFHFLV 206
Cdd:COG0463    71 GAARNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEGPA--DLVYGSRLIREGESD-----LRRLGSRLFNLVR 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907151770 207 WFLCvkgIRDTQCGFKLLTREAAARTFSSlhiERWAFDVELLYIAQcLQIPIAEVAVNWTEIEGS 271
Cdd:COG0463   141 LLTN---LPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALR-HGFRIAEVPVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 51-228 7.53e-26

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: 100.55  E-value: 7.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEKRLPVMMDEALNylekrQKHDctfTYEVIVVDDGSEDQTSKVALKYCQKYgsDKVRVITLVRNRGKGGAV 130
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN-----QTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGAR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 131 RMGVFSSRGEKILMADADGATKFPDVEKLEKGLSDLQPwpeqmAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLC 210
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGA-----DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145

                         170
                  ....*....|....*...
gi 1907151770 211 VKGIRDTQCGFKLLTREA 228
Cdd:pfam00535 146 GLNLPFLIGGFALYRREA 163
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 52-300 8.67e-22

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


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 91.44  E-value: 8.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMDEALNYLEKrqkhdctFTYEVIVVDDGSEDQTSKVALKYCQKYGsdKVRVITLVRNRGKGGAVR 131
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKG-------IDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 132 MGVFSSRGEKILMADADG--ATKF-PD-VEKLEKGLSDlqpwpeqmaIACGSRaHLEKESIAQRSYFRTFLMYGFHFLVW 207
Cdd:cd06442    72 EGFKAARGDVIVVMDADLshPPEYiPElLEAQLEGGAD---------LVIGSR-YVEGGGVEGWGLKRKLISRGANLLAR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 208 FLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQCLQIPIAEVAVNWTE-IEG-SKLvpfwSWLQMgkd 285
Cdd:cd06442   142 LLLGRKVSDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDrEHGeSKL----GGKEI--- 214

                         250
                  ....*....|....*
gi 1907151770 286 llfirLRYLTGAWRL 300
Cdd:cd06442   215 -----VEYLKGLLRL 224
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 52-229 3.63e-18

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: 80.21  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMDEALNYLEKRqkhdcTFTYEVIVVDDGSEDQTSKVALKYCQKYgsDKVRVITLVRNRGKGGAVR 131
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESL-----GYDYEIIFVDDGSTDRTLEILRELAARD--PRVKVIRLSRNFGQQAALL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 132 MGVFSSRGEKILMADADG---ATKFPD-VEKLEKGLSdlqpwpeqmaIACGSRAHlEKESIaqrsyFRTFLMYGFHFLVW 207
Cdd:cd04187    74 AGLDHARGDAVITMDADLqdpPELIPEmLAKWEEGYD----------VVYGVRKN-RKESW-----LKRLTSKLFYRLIN 137

                         170       180
                  ....*....|....*....|..
gi 1907151770 208 FLCVKGIRDTQCGFKLLTREAA 229
Cdd:cd04187   138 KLSGVDIPDNGGDFRLMDRKVV 159
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 44-148 5.69e-18

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: 82.48  E-value: 5.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  44 DSPTKQLSVVVPSYNEEKRLPvmmdEALNYLeKRQKHDcTFTYEVIVVDDGSEDQTSKVALKYCQKYgsDKVRVITLVRN 123
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIE----ETLRSL-LAQDYP-KEKLEVIVVDDGSTDETAEIARELAAEY--PRVRVIERPEN 96

                          90       100
                  ....*....|....*....|....*
gi 1907151770 124 RGKGGAVRMGVFSSRGEKILMADAD 148
Cdd:COG1215    97 GGKAAALNAGLKAARGDIVVFLDAD 121
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 52-148 7.86e-18

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 78.70  E-value: 7.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMDEALNYLEKRqkhdctftYEVIVVDDGSEDQTSKVALKYCQKYgsDKVRVITLVRNRGKGGAVR 131
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPN--------FEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARN 70

                          90
                  ....*....|....*..
gi 1907151770 132 MGVFSSRGEKILMADAD 148
Cdd:cd00761    71 AGLKAARGEYILFLDAD 87
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 51-261 1.34e-14

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 72.04  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEKRLPVMMdealnYLEKRQKHDCTfTYEVIVVDDGSEDQTSKVALKYCQKYGSDKVRVITLVRNRGKGGAV 130
Cdd:PLN02726   12 SIIVPTYNERLNIALIV-----YLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770 131 RMGVFSSRGEKILMADADGA--TKF-PDV--EKLEKGLSdlqpwpeqmaIACGSRaHLEKESIAQRSYFRTFLMYGFHFL 205
Cdd:PLN02726   86 IHGLKHASGDFVVIMDADLShhPKYlPSFikKQRETGAD----------IVTGTR-YVKGGGVHGWDLRRKLTSRGANVL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907151770 206 VWFLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQCLQIPIAEV 261
Cdd:PLN02726  155 AQTLLWPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEV 210
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 52-148 2.28e-14

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


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 69.95  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPvmmdEALNYLeKRQKHDctfTYEVIVVDDGSEDQTSKVALKYCQKYGSDKVRVITLvRNRGKGGAVR 131
Cdd:cd06423     1 IIVPAYNEEAVIE----RTIESL-LALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDK-ENGGKAGALN 71

                          90
                  ....*....|....*..
gi 1907151770 132 MGVFSSRGEKILMADAD 148
Cdd:cd06423    72 AGLRHAKGDIVVVLDAD 88
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
46-148 7.14e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 66.17  E-value: 7.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  46 PTKQLSVVVPSYNEEKRLpvmmDEALNYLEKRQKHDctftYEVIVVDDGSEDQTskvaLKYCQKYGSDKVRVITLVRNRG 125
Cdd:COG1216     1 MRPKVSVVIPTYNRPELL----RRCLESLLAQTYPP----FEVIVVDNGSTDGT----AELLAALAFPRVRVIRNPENLG 68

                          90       100
                  ....*....|....*....|...
gi 1907151770 126 KGGAVRMGVFSSRGEKILMADAD 148
Cdd:COG1216    69 FAAARNLGLRAAGGDYLLFLDDD 91
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 32-148 7.86e-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: 64.14  E-value: 7.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  32 AKGQKEALPSIwdsptkqlSVVVPSYNEEKRLPVMMDE--ALNYLEKRqkhdctftYEVIVVDDGSEDQTSKVAlkycQK 109
Cdd:cd06439    21 SLPDPAYLPTV--------TIIIPAYNEEAVIEAKLENllALDYPRDR--------LEIIVVSDGSTDGTAEIA----RE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907151770 110 YGSDKVRVITLVRNRGKGGAVRMGVFSSRGEKILMADAD 148
Cdd:cd06439    81 YADKGVKLLRFPERRGKAAALNRALALATGEIVVFTDAN 119
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 46-148 5.50e-11

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 62.45  E-value: 5.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  46 PTKQLSVVVPSYNEEKRLPVMMDEALNYLEKRQKhdctfTYEVIVVDDGSEDQTSKVALKYCQKYGSDKVRVItLVRNRG 125
Cdd:PRK10714    4 PIKKVSVVIPVYNEQESLPELIRRTTAACESLGK-----EYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAIL-LNRNYG 77

                          90       100
                  ....*....|....*....|...
gi 1907151770 126 KGGAVRMGVFSSRGEKILMADAD 148
Cdd:PRK10714   78 QHSAIMAGFSHVTGDLIITLDAD 100
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 50-165 2.78e-09

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: 56.37  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  50 LSVVVPSYNEEKRLPvmmdEALNYLeKRQKHDCtftyEVIVVDDGSEDQTSKVAlkycqkyGSDKVRVITLVRNRgkggA 129
Cdd:TIGR04283   1 LSIIIPVLNEAATLP----ELLADL-QALRGDA----EVIVVDGGSTDGTVEIA-------RSLGAKVIHSPKGR----A 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907151770 130 VRM--GVFSSRGEKILMADADgaTKFPD--VEKLEKGLSD 165
Cdd:TIGR04283  61 RQMnaGAALAKGDILLFLHAD--TRLPKdfLEAIRRALAK 98
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 52-148 3.26e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 56.14  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPVMMD--EALNYlEKRQkhdctftYEVIVVDDGSEDQTSKVaLKYCQKYGSDKVRVITLVR--NRGKG 127
Cdd:cd04192     1 VVIAARNEAENLPRLLQslSALDY-PKEK-------FEVILVDDHSTDGTVQI-LEFAAAKPNFQLKILNNSRvsISGKK 71

                          90       100
                  ....*....|....*....|.
gi 1907151770 128 GAVRMGVFSSRGEKILMADAD 148
Cdd:cd04192    72 NALTTAIKAAKGDWIVTTDAD 92
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 44-148 3.29e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 56.98  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  44 DSPTKQLSVVVPSYNEEKRLPVMMDEALnylekRQKHDctfTYEVIVVDDGSEDQTSKVALKYCQKYGsdKVRVITLvRN 123
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLI-----AQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYP--HVRLLHQ-AN 70

                          90       100
                  ....*....|....*....|....*
gi 1907151770 124 RGKGGAVRMGVFSSRGEKILMADAD 148
Cdd:PRK10073   71 AGVSVARNTGLAVATGKYVAFPDAD 95
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 51-149 1.19e-08

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: 54.55  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEKRLPVMMDEALN--YLEKRqkhdctftYEVIVVDDGSEDQTSKVALKYCQKYGSdkvrvITLVRNRGK-- 126
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLLNqsYPKDL--------IEIIVVDGGSTDGTREIVQEYAAKDPR-----IRLIDNPKRiq 69

                          90       100
                  ....*....|....*....|...
gi 1907151770 127 GGAVRMGVFSSRGEKILMADADG 149
Cdd:cd02525    70 SAGLNIGIRNSRGDIIIRVDAHA 92
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 50-148 7.28e-08

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 52.37  E-value: 7.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  50 LSVVVPSYNEEKRLPVMMDEALNYLEKRqkhdctftYEVIVVDDGSEDQTSKVALKYCQKYGSDKVRVITLVRNRGKGGA 129
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPP--------VEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGK 75

                          90       100
                  ....*....|....*....|..
gi 1907151770 130 VRM--GVFSS-RGEKILMADAD 148
Cdd:pfam13641  76 SRGlnHGFRAvKSDLVVLHDDD 97
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 50-126 9.69e-08

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: 51.80  E-value: 9.69e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907151770  50 LSVVVPSYNEEKRLPvmmdEALNYLEKRQKHDCtftyEVIVVDDGSEDQTSKVAlkycQKYGsdkVRVITLVRNRGK 126
Cdd:cd02522     1 LSIIIPTLNEAENLP----RLLASLRRLNPLPL----EIIVVDGGSTDGTVAIA----RSAG---VVVISSPKGRAR 62
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
50-107 2.31e-06

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 48.25  E-value: 2.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  50 LSVVVPSYNEEKRLPVMMDeALnyleKRQKHDCTFTYEVIVVDDGSEDQTSKV------------ALKYC 107
Cdd:NF038302    3 FTVAIPTYNGANRLPEVLE-RL----RSQIGTESLSWEIIVVDNNSTDNTAQVvqeyqknwpspyPLRYC 67
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 51-131 1.15e-05

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 45.31  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEKrlpvmmdealnYLEK------RQKHDCTftyEVIVVDDGSEDQTSKVALKYCQKYGsdkvRVITLVRNR 124
Cdd:cd04196     1 AVLMATYNGEK-----------YLREqldsilAQTYKND---ELIISDDGSTDGTVEIIKEYIDKDP----FIIILIRNG 62


                  ....*..
gi 1907151770 125 GKGGAVR 131
Cdd:cd04196    63 KNLGVAR 69
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 50-148 9.71e-05

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: 42.66  E-value: 9.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  50 LSVVVPSYNEEKRLPvmmdEALNYLEKrqkhdctFTYEVIVVDDGSEDQTskVALkyCQKYGsdkVRVITlVRNRGKGGA 129
Cdd:cd02511     2 LSVVIITKNEERNIE----RCLESVKW-------AVDEIIVVDSGSTDRT--VEI--AKEYG---AKVYQ-RWWDGFGAQ 62

                          90
                  ....*....|....*....
gi 1907151770 130 VRMGVFSSRGEKILMADAD 148
Cdd:cd02511    63 RNFALELATNDWVLSLDAD 81
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 52-166 2.04e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 41.01  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  52 VVVPSYNEEKRLPvmmdEALNYLEKRQKHDctftYEVIVVDDGSEDQTSKVALKYcqkygSDKVRVITLVRNRGKGGAVR 131
Cdd:cd04186     1 IIIVNYNSLEYLK----ACLDSLLAQTYPD----FEVIVVDNASTDGSVELLREL-----FPEVRLIRNGENLGFGAGNN 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907151770 132 MGVFSSRGEKILMADadgatkfPDVEKLEKGLSDL 166
Cdd:cd04186    68 QGIREAKGDYVLLLN-------PDTVVEPGALLEL 95
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 51-148 3.74e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.44  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEKRLPVMMDEALNYLEKrqkhdcTFTYEVIVVDDGSEDQTSKVAlkycQKYGSdkvRVIT-------LVRN 123
Cdd:PRK13915   34 SVVLPALNEEETVGKVVDSIRPLLME------PLVDELIVIDSGSTDATAERA----AAAGA---RVVSreeilpeLPPR 100

                          90       100
                  ....*....|....*....|....*
gi 1907151770 124 RGKGGAVRMGVFSSRGEKILMADAD 148
Cdd:PRK13915  101 PGKGEALWRSLAATTGDIVVFVDAD 125
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 87-125 5.24e-04

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 41.04  E-value: 5.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907151770  87 EVIVVDDGSEDQTSKVALKYCQKYGSDKVRVITLVRNRG 125
Cdd:cd02510    32 EIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREG 70
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 51-167 1.10e-03

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 39.95  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEKRlPVMMDEALNyleKRQKHDCTFtyEVIVVDDGSEDQTSKVALKYCQ-------KYGSDKVRVITLVRN 123
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILN---QTFQYDPEF--ELIIINDGSTDKTLEEVSSIKDhnlqvyyPNAPDTTYSLAASRN 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907151770 124 RGKGGAVrmgvfssrGEKILMADADgatKFPDVEKLEKGLSDLQ 167
Cdd:pfam10111  75 RGTSHAI--------GEYISFIDGD---CLWSPDKFEKQLKIAT 107
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 51-148 8.93e-03

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 36.99  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151770  51 SVVVPSYNEEkrlPVMMDEALNYLEKRQKHDctftYEVIVVDDGSEDQTSKVAL-KYCQKYGsDKVRVITLVRNRG-KGG 128
Cdd:cd06435     1 SIHVPCYEEP---PEMVKETLDSLAALDYPN----FEVIVIDNNTKDEALWKPVeAHCAQLG-ERFRFFHVEPLPGaKAG 72

                          90       100
                  ....*....|....*....|..
gi 1907151770 129 AVR--MGVFSSRGEKILMADAD 148
Cdd:cd06435    73 ALNyaLERTAPDAEIIAVIDAD 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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