NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1195543308|ref|XP_021052002|]
View 

dolichyl-phosphate beta-glucosyltransferase [Mus pahari]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
69-289 1.23e-122

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: 350.33  E-value: 1.23e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMDEALNYLEKRQKhdctFTYEVIVVDDGSEDQTSKVALKYSQKYGSDkVRVITLVQNRGKGGAVR 148
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPS----FSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 149 MGVFSSRGEKILMADADGATKFPDVEKLEKglsdlQPWPEQMAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLCV 228
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEE-----ALKTSGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195543308 229 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQFLQIPITEVAVNWTEIEGSK 289
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 ...
69-289 1.23e-122

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: 350.33  E-value: 1.23e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMDEALNYLEKRQKhdctFTYEVIVVDDGSEDQTSKVALKYSQKYGSDkVRVITLVQNRGKGGAVR 148
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPS----FSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 149 MGVFSSRGEKILMADADGATKFPDVEKLEKglsdlQPWPEQMAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLCV 228
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEE-----ALKTSGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195543308 229 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQFLQIPITEVAVNWTEIEGSK 289
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
66-318 5.96e-120

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 348.30  E-value: 5.96e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  66 QLSVVVPSYNEEKRLPVMMDEALNYLEKRQKHDCTFTYEVIVVDDGSEDQTSKVALKYSQKYGSDKV--RVITLVQNRGK 143
Cdd:PTZ00260   71 DLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdiRLLSLLRNKGK 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 144 GGAVRMGVFSSRGEKILMADADGATKFPDVEKLEKGLsdLQPWPEQMAIACGSRAHLEK-ESIAQRSYFRTFLMYGFHFL 222
Cdd:PTZ00260  151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIM--LKIEQNGLGIVFGSRNHLVDsDVVAKRKWYRNILMYGFHFI 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 223 VWFLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQFLQIPITEVAVNWTEIEGSKLVPFWSWLQMGKD 302
Cdd:PTZ00260  229 VNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISASIQMARD 308
                         250
                  ....*....|....*.
gi 1195543308 303 LLFIRLRYLTGAWRLK 318
Cdd:PTZ00260  309 ILLVRSFYLLGIWKVK 324
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
64-288 1.88e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.11  E-value: 1.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  64 TKQLSVVVPSYNEEKRLPVMMDEALNYLekrqkhdcTFTYEVIVVDDGSEDQTSKVALKYSQKYgsDKVRVITLVQNRGK 143
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQT--------YPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 144 GGAVRMGVFSSRGEKILMADADGatkFPDVEKLEKGLSDLQPWPEqmAIACGSRAHLEKESIaqrsyFRTFLMYGFHFLV 223
Cdd:COG0463    71 GAARNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEGPA--DLVYGSRLIREGESD-----LRRLGSRLFNLVR 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195543308 224 WFLCvkgIRDTQCGFKLLTREAAARTFSSlhiERWAFDVELLYIAQfLQIPITEVAVNWTEIEGS 288
Cdd:COG0463   141 LLTN---LPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALR-HGFRIAEVPVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
68-245 1.73e-25

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: 100.16  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  68 SVVVPSYNEEKRLPVMMDEALNylekrQKHDctfTYEVIVVDDGSEDQTSKVALKYSQKYgsDKVRVITLVQNRGKGGAV 147
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN-----QTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGAR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 148 RMGVFSSRGEKILMADADGATKFPDVEKLEKGLSDLQPwpeqmAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLC 227
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGA-----DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145
                         170
                  ....*....|....*...
gi 1195543308 228 VKGIRDTQCGFKLLTREA 245
Cdd:pfam00535 146 GLNLPFLIGGFALYRREA 163
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
67-182 2.81e-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: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  67 LSVVVPSYNEEKRLPvmmdEALNYLeKRQKHDCtftyEVIVVDDGSEDQTSKVAlkysqkyGSDKVRVITLVQNRgkggA 146
Cdd:TIGR04283   1 LSIIIPVLNEAATLP----ELLADL-QALRGDA----EVIVVDGGSTDGTVEIA-------RSLGAKVIHSPKGR----A 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1195543308 147 VRM--GVFSSRGEKILMADADgaTKFPD--VEKLEKGLSD 182
Cdd:TIGR04283  61 RQMnaGAALAKGDILLFLHAD--TRLPKdfLEAIRRALAK 98
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
67-127 1.28e-06

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 49.02  E-value: 1.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195543308  67 LSVVVPSYNEEKRLPVMMDeALnyleKRQKHDCTFTYEVIVVDDGSEDQTSKVALKYSQKY 127
Cdd:NF038302    3 FTVAIPTYNGANRLPEVLE-RL----RSQIGTESLSWEIIVVDNNSTDNTAQVVQEYQKNW 58
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
69-289 1.23e-122

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: 350.33  E-value: 1.23e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMDEALNYLEKRQKhdctFTYEVIVVDDGSEDQTSKVALKYSQKYGSDkVRVITLVQNRGKGGAVR 148
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPS----FSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 149 MGVFSSRGEKILMADADGATKFPDVEKLEKglsdlQPWPEQMAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLCV 228
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEE-----ALKTSGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195543308 229 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQFLQIPITEVAVNWTEIEGSK 289
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
66-318 5.96e-120

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 348.30  E-value: 5.96e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  66 QLSVVVPSYNEEKRLPVMMDEALNYLEKRQKHDCTFTYEVIVVDDGSEDQTSKVALKYSQKYGSDKV--RVITLVQNRGK 143
Cdd:PTZ00260   71 DLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdiRLLSLLRNKGK 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 144 GGAVRMGVFSSRGEKILMADADGATKFPDVEKLEKGLsdLQPWPEQMAIACGSRAHLEK-ESIAQRSYFRTFLMYGFHFL 222
Cdd:PTZ00260  151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIM--LKIEQNGLGIVFGSRNHLVDsDVVAKRKWYRNILMYGFHFI 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 223 VWFLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQFLQIPITEVAVNWTEIEGSKLVPFWSWLQMGKD 302
Cdd:PTZ00260  229 VNTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISASIQMARD 308
                         250
                  ....*....|....*.
gi 1195543308 303 LLFIRLRYLTGAWRLK 318
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 ...
69-268 5.03e-58

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: 185.08  E-value: 5.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMDEALNYLEKrqkhdcTFTYEVIVVDDGSEDQTSKVALKYSQKYGsdKVRVITLVQNRGKGGAVR 148
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE------GYDYEIIVVDDGSTDGTAEIARELAARVP--RVRVIRLSRNFGKGAAVR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 149 MGVFSSRGEKILMADADGATKFPDVEKLEKGLsdlqpWPEQMAIACGSRAHleKESIAQRSYFRTFLMYGFHFLVWFLCV 228
Cdd:cd04179    73 AGFKAARGDIVVTMDADLQHPPEDIPKLLEKL-----LEGGADVVIGSRFV--RGGGAGMPLLRRLGSRLFNFLIRLLLG 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1195543308 229 KGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIA 268
Cdd:cd04179   146 VRISDTQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
64-288 1.88e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.11  E-value: 1.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  64 TKQLSVVVPSYNEEKRLPVMMDEALNYLekrqkhdcTFTYEVIVVDDGSEDQTSKVALKYSQKYgsDKVRVITLVQNRGK 143
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQT--------YPDFEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 144 GGAVRMGVFSSRGEKILMADADGatkFPDVEKLEKGLSDLQPWPEqmAIACGSRAHLEKESIaqrsyFRTFLMYGFHFLV 223
Cdd:COG0463    71 GAARNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEGPA--DLVYGSRLIREGESD-----LRRLGSRLFNLVR 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195543308 224 WFLCvkgIRDTQCGFKLLTREAAARTFSSlhiERWAFDVELLYIAQfLQIPITEVAVNWTEIEGS 288
Cdd:COG0463   141 LLTN---LPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALR-HGFRIAEVPVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
68-245 1.73e-25

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: 100.16  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  68 SVVVPSYNEEKRLPVMMDEALNylekrQKHDctfTYEVIVVDDGSEDQTSKVALKYSQKYgsDKVRVITLVQNRGKGGAV 147
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN-----QTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGAR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 148 RMGVFSSRGEKILMADADGATKFPDVEKLEKGLSDLQPwpeqmAIACGSRAHLEKESIAQRSYFRTFLMYGFHFLVWFLC 227
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGA-----DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145
                         170
                  ....*....|....*...
gi 1195543308 228 VKGIRDTQCGFKLLTREA 245
Cdd:pfam00535 146 GLNLPFLIGGFALYRREA 163
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
69-317 1.09e-21

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: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMDEALNYLEKrqkhdctFTYEVIVVDDGSEDQTSKVALKYSQKYGsdKVRVITLVQNRGKGGAVR 148
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKG-------IDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 149 MGVFSSRGEKILMADADG--ATKF-PD-VEKLEKGLSDlqpwpeqmaIACGSRaHLEKESIAQRSYFRTFLMYGFHFLVW 224
Cdd:cd06442    72 EGFKAARGDVIVVMDADLshPPEYiPElLEAQLEGGAD---------LVIGSR-YVEGGGVEGWGLKRKLISRGANLLAR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 225 FLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQFLQIPITEVAVNWTE-IEG-SKLvpfwSWLQMgkd 302
Cdd:cd06442   142 LLLGRKVSDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDrEHGeSKL----GGKEI--- 214
                         250
                  ....*....|....*
gi 1195543308 303 llfirLRYLTGAWRL 317
Cdd:cd06442   215 -----VEYLKGLLRL 224
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
69-165 2.29e-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: 80.63  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMDEALNYLEKRqkhdctftYEVIVVDDGSEDQTSKVALKYSQKYgsDKVRVITLVQNRGKGGAVR 148
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPN--------FEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARN 70
                          90
                  ....*....|....*..
gi 1195543308 149 MGVFSSRGEKILMADAD 165
Cdd:cd00761    71 AGLKAARGEYILFLDAD 87
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
61-165 8.91e-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: 82.10  E-value: 8.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  61 DSPTKQLSVVVPSYNEEKRLPvmmdEALNYLeKRQKHDcTFTYEVIVVDDGSEDQTSKVALKYSQKYgsDKVRVITLVQN 140
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIE----ETLRSL-LAQDYP-KEKLEVIVVDDGSTDETAEIARELAAEY--PRVRVIERPEN 96
                          90       100
                  ....*....|....*....|....*
gi 1195543308 141 RGKGGAVRMGVFSSRGEKILMADAD 165
Cdd:COG1215    97 GGKAAALNAGLKAARGDIVVFLDAD 121
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
69-246 2.83e-16

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: 75.59  E-value: 2.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMDEALNYLEKRqkhdcTFTYEVIVVDDGSEDQTSKVALKYSQKYgsDKVRVITLVQNRGKGGAVR 148
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESL-----GYDYEIIFVDDGSTDRTLEILRELAARD--PRVKVIRLSRNFGQQAALL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 149 MGVFSSRGEKILMADADG---ATKFPD-VEKLEKGLSdlqpwpeqmaIACGSRAHlEKESIaqrsyFRTFLMYGFHFLVW 224
Cdd:cd04187    74 AGLDHARGDAVITMDADLqdpPELIPEmLAKWEEGYD----------VVYGVRKN-RKESW-----LKRLTSKLFYRLIN 137
                         170       180
                  ....*....|....*....|..
gi 1195543308 225 FLCVKGIRDTQCGFKLLTREAA 246
Cdd:cd04187   138 KLSGVDIPDNGGDFRLMDRKVV 159
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
69-165 6.28e-15

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: 71.49  E-value: 6.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPvmmdEALNYLeKRQKHDctfTYEVIVVDDGSEDQTSKVALKYSQKYGSDKVRVITLvQNRGKGGAVR 148
Cdd:cd06423     1 IIVPAYNEEAVIE----RTIESL-LALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDK-ENGGKAGALN 71
                          90
                  ....*....|....*..
gi 1195543308 149 MGVFSSRGEKILMADAD 165
Cdd:cd06423    72 AGLRHAKGDIVVVLDAD 88
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
68-278 9.66e-15

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 72.42  E-value: 9.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  68 SVVVPSYNEEKRLPVMMdealnYLEKRQKHDCTfTYEVIVVDDGSEDQTSKVALKYSQKYGSDKVRVITLVQNRGKGGAV 147
Cdd:PLN02726   12 SIIVPTYNERLNIALIV-----YLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308 148 RMGVFSSRGEKILMADADGA--TKF-PDV--EKLEKGLSdlqpwpeqmaIACGSRaHLEKESIAQRSYFRTFLMYGFHFL 222
Cdd:PLN02726   86 IHGLKHASGDFVVIMDADLShhPKYlPSFikKQRETGAD----------IVTGTR-YVKGGGVHGWDLRRKLTSRGANVL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1195543308 223 VWFLCVKGIRDTQCGFKLLTREAAARTFSSLHIERWAFDVELLYIAQFLQIPITEV 278
Cdd:PLN02726  155 AQTLLWPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEV 210
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
49-165 3.11e-12

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 65.30  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  49 AKGQKEALPSIwdsptkqlSVVVPSYNEEKRLPVMMDE--ALNYLEKRqkhdctftYEVIVVDDGSEDQTSKVALKYSQK 126
Cdd:cd06439    21 SLPDPAYLPTV--------TIIIPAYNEEAVIEAKLENllALDYPRDR--------LEIIVVSDGSTDGTAEIAREYADK 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1195543308 127 ygsdKVRVITLVQNRGKGGAVRMGVFSSRGEKILMADAD 165
Cdd:cd06439    85 ----GVKLLRFPERRGKAAALNRALALATGEIVVFTDAN 119
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
63-165 3.32e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 64.63  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  63 PTKQLSVVVPSYNEEKRLpvmmDEALNYLEKRQKHDctftYEVIVVDDGSEDQTskvaLKYSQKYGSDKVRVITLVQNRG 142
Cdd:COG1216     1 MRPKVSVVIPTYNRPELL----RRCLESLLAQTYPP----FEVIVVDNGSTDGT----AELLAALAFPRVRVIRNPENLG 68
                          90       100
                  ....*....|....*....|...
gi 1195543308 143 KGGAVRMGVFSSRGEKILMADAD 165
Cdd:COG1216    69 FAAARNLGLRAAGGDYLLFLDDD 91
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
63-165 1.94e-10

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 60.90  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  63 PTKQLSVVVPSYNEEKRLPVMMDEALNYLEKRQKhdctfTYEVIVVDDGSEDQTSKVALKYSQKYGSDKVRVItLVQNRG 142
Cdd:PRK10714    4 PIKKVSVVIPVYNEQESLPELIRRTTAACESLGK-----EYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAIL-LNRNYG 77
                          90       100
                  ....*....|....*....|...
gi 1195543308 143 KGGAVRMGVFSSRGEKILMADAD 165
Cdd:PRK10714   78 QHSAIMAGFSHVTGDLIITLDAD 100
PRK10073 PRK10073
putative glycosyl transferase; Provisional
61-165 6.32e-10

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 59.29  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  61 DSPTKQLSVVVPSYNEEKRLPVMMDEALnylekRQKHDctfTYEVIVVDDGSEDQTSKVALKYSQKYGsdKVRVITLvQN 140
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLI-----AQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYP--HVRLLHQ-AN 70
                          90       100
                  ....*....|....*....|....*
gi 1195543308 141 RGKGGAVRMGVFSSRGEKILMADAD 165
Cdd:PRK10073   71 AGVSVARNTGLAVATGKYVAFPDAD 95
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
67-182 2.81e-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: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  67 LSVVVPSYNEEKRLPvmmdEALNYLeKRQKHDCtftyEVIVVDDGSEDQTSKVAlkysqkyGSDKVRVITLVQNRgkggA 146
Cdd:TIGR04283   1 LSIIIPVLNEAATLP----ELLADL-QALRGDA----EVIVVDGGSTDGTVEIA-------RSLGAKVIHSPKGR----A 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1195543308 147 VRM--GVFSSRGEKILMADADgaTKFPD--VEKLEKGLSD 182
Cdd:TIGR04283  61 RQMnaGAALAKGDILLFLHAD--TRLPKdfLEAIRRALAK 98
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
69-165 3.45e-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: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPVMMD--EALNYlEKRQkhdctftYEVIVVDDGSEDQTSKVALKYSQKyGSDKVRVITLVQ--NRGKG 144
Cdd:cd04192     1 VVIAARNEAENLPRLLQslSALDY-PKEK-------FEVILVDDHSTDGTVQILEFAAAK-PNFQLKILNNSRvsISGKK 71
                          90       100
                  ....*....|....*....|.
gi 1195543308 145 GAVRMGVFSSRGEKILMADAD 165
Cdd:cd04192    72 NALTTAIKAAKGDWIVTTDAD 92
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
68-166 2.24e-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: 54.16  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  68 SVVVPSYNEEKRLPVMMDEALN--YLEKRqkhdctftYEVIVVDDGSEDQTSKVALKYSQKYGSdkvrvITLVQNRGK-- 143
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLLNqsYPKDL--------IEIIVVDGGSTDGTREIVQEYAAKDPR-----IRLIDNPKRiq 69
                          90       100
                  ....*....|....*....|...
gi 1195543308 144 GGAVRMGVFSSRGEKILMADADG 166
Cdd:cd02525    70 SAGLNIGIRNSRGDIIIRVDAHA 92
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
67-165 2.15e-07

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: 50.83  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  67 LSVVVPSYNEEKRLPVMMDEALNYLEKRqkhdctftYEVIVVDDGSEDQTSKVALKYSQKYGSDKVRVITLVQNRGKGGA 146
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPP--------VEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGK 75
                          90       100
                  ....*....|....*....|..
gi 1195543308 147 VRM--GVFSS-RGEKILMADAD 165
Cdd:pfam13641  76 SRGlnHGFRAvKSDLVVLHDDD 97
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
67-172 2.51e-07

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


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 50.65  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  67 LSVVVPSYNEEKRLPvmmdEALNYLEKRQKHDCtftyEVIVVDDGSEDQTSKVAlkysQKYGsdkVRVITlvQNRGKGGA 146
Cdd:cd02522     1 LSIIIPTLNEAENLP----RLLASLRRLNPLPL----EIIVVDGGSTDGTVAIA----RSAG---VVVIS--SPKGRARQ 63
                          90       100
                  ....*....|....*....|....*.
gi 1195543308 147 VRMGVFSSRGEKILMADADgaTKFPD 172
Cdd:cd02522    64 MNAGAAAARGDWLLFLHAD--TRLPP 87
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
67-127 1.28e-06

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 49.02  E-value: 1.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195543308  67 LSVVVPSYNEEKRLPVMMDeALnyleKRQKHDCTFTYEVIVVDDGSEDQTSKVALKYSQKY 127
Cdd:NF038302    3 FTVAIPTYNGANRLPEVLE-RL----RSQIGTESLSWEIIVVDNNSTDNTAQVVQEYQKNW 58
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
68-148 9.72e-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: 43.00  E-value: 9.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  68 SVVVPSYNEEKrlpvmmdealnYLEK------RQKHDCTftyEVIVVDDGSEDQTSKVALKYSQKYGsdkvRVITLVQNR 141
Cdd:cd04196     1 AVLMATYNGEK-----------YLREqldsilAQTYKND---ELIISDDGSTDGTVEIIKEYIDKDP----FIIILIRNG 62

                  ....*..
gi 1195543308 142 GKGGAVR 148
Cdd:cd04196    63 KNLGVAR 69
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
67-165 1.63e-04

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: 42.28  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  67 LSVVVPSYNEEKRLPvmmdEALNYLEKrqkhdctFTYEVIVVDDGSEDQTSKVALKYsqkygsdKVRVITlVQNRGKGGA 146
Cdd:cd02511     2 LSVVIITKNEERNIE----RCLESVKW-------AVDEIIVVDSGSTDRTVEIAKEY-------GAKVYQ-RWWDGFGAQ 62
                          90
                  ....*....|....*....
gi 1195543308 147 VRMGVFSSRGEKILMADAD 165
Cdd:cd02511    63 RNFALELATNDWVLSLDAD 81
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
69-183 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: 41.39  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  69 VVVPSYNEEKRLPvmmdEALNYLEKRQKHDctftYEVIVVDDGSEDQTSKVALKYSQkygsdKVRVITLVQNRGKGGAVR 148
Cdd:cd04186     1 IIIVNYNSLEYLK----ACLDSLLAQTYPD----FEVIVVDNASTDGSVELLRELFP-----EVRLIRNGENLGFGAGNN 67
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1195543308 149 MGVFSSRGEKILMADadgatkfPDVEKLEKGLSDL 183
Cdd:cd04186    68 QGIREAKGDYVLLLN-------PDTVVEPGALLEL 95
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
104-142 3.52e-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: 41.81  E-value: 3.52e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1195543308 104 EVIVVDDGSEDQTSKVALKYSQKYGSDKVRVITLVQNRG 142
Cdd:cd02510    32 EIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREG 70
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
68-165 2.38e-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: 38.45  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  68 SVVVPSYNEEKrlPVMMDEALNYLEKRQkhdcTFTYEVIVVDDG--SEDQTSkVALKYSQKYGsdkVRVITLVQNRGKGG 145
Cdd:cd04195     1 SVLMSVYIKEK--PEFLREALESILKQT----LPPDEVVLVKDGpvTQSLNE-VLEEFKRKLP---LKVVPLEKNRGLGK 70
                          90       100
                  ....*....|....*....|
gi 1195543308 146 AVRMGVFSSRGEKILMADAD 165
Cdd:cd04195    71 ALNEGLKHCTYDWVARMDTD 90
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
68-126 5.90e-03

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: 37.52  E-value: 5.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1195543308  68 SVVVPSYNEEKRLPvmmdEALNYLEKrQKHDctfTYEVIVVDDGSEDQTSKVALKYSQK 126
Cdd:cd06433     1 SIITPTYNQAETLE----ETIDSVLS-QTYP---NIEYIVIDGGSTDGTVDIIKKYEDK 51
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
67-165 6.25e-03

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: 37.62  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195543308  67 LSVVVPSYneekrlpvmmDEALNYLEK------RQKHDctftyEVIVVDDGSEDqtsKVALKYSQKYGSDKVRVITlVQN 140
Cdd:cd06434     2 VTVIIPVY----------DEDPDVFREclrsilRQKPL-----EIIVVTDGDDE---PYLSILSQTVKYGGIFVIT-VPH 62
                          90       100
                  ....*....|....*....|....*
gi 1195543308 141 RGKGGAVRMGVFSSRGEKILMADAD 165
Cdd:cd06434    63 PGKRRALAEGIRHVTTDIVVLLDSD 87
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH