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Conserved domains on  [gi|1583828758|emb|VCV20930|]
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Putative glycosyltransferase EpsE [Roseburia intestinalis L1-82]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-206 2.67e-43

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.


The actual alignment was detected with superfamily member cd04195:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 201  Bit Score: 145.92  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEKKKEQVEMAISSILNQSYSNFEFIICDDG---SSEEFFL--WLQEYcktDERIHLLrnEKNEGLSKALNRC 80
Cdd:cd04195     1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGpvtQSLNEVLeeFKRKL---PLKVVPL--EKNRGLGKALNEG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  81 LKYAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDE-GGIWGERKPSerPQKTDFL----WTSPFIHP 155
Cdd:cd04195    76 LKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSdGNDIGKRRLP--TSHDDILkfarRRSPFNHP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1583828758 156 SIMMKTSVLQNMNGYTTadyAERTEDYDLFMRLYAAGEKGYNLQEKLFLYR 206
Cdd:cd04195   154 TVMFRKSKVLAVGGYQD---LPLVEDYALWARMLANGARFANLPEILVKAR 201
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 6-206 2.67e-43

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: 145.92  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEKKKEQVEMAISSILNQSYSNFEFIICDDG---SSEEFFL--WLQEYcktDERIHLLrnEKNEGLSKALNRC 80
Cdd:cd04195     1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGpvtQSLNEVLeeFKRKL---PLKVVPL--EKNRGLGKALNEG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  81 LKYAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDE-GGIWGERKPSerPQKTDFL----WTSPFIHP 155
Cdd:cd04195    76 LKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSdGNDIGKRRLP--TSHDDILkfarRRSPFNHP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1583828758 156 SIMMKTSVLQNMNGYTTadyAERTEDYDLFMRLYAAGEKGYNLQEKLFLYR 206
Cdd:cd04195   154 TVMFRKSKVLAVGGYQD---LPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-217 7.56e-39

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 134.83  E-value: 7.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKkkEQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCLK 82
Cdd:COG0463     2 PLVSVVIPTYNEE--EYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  83 YAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVslIDEGGIWGERKPSERPQKTDFLWTSPFIHPS-IMMKT 161
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRL--IREGESDLRRLGSRLFNLVRLLTNLPDSTSGfRLFRR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1583828758 162 SVLQNMNgyttadYAER-TEDYDLFmrlyAAGEKGYNLQEKLFLYREDRNAFAKRKY 217
Cdd:COG0463   158 EVLEELG------FDEGfLEDTELL----RALRHGFRIAEVPVRYRAGESKLNLRDL 204
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-165 5.08e-34

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: 120.96  E-value: 5.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEKKKeqVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCLKYAK 85
Cdd:pfam00535   1 SVIIPTYNEEKY--LLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  86 GEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDEGG-------IWGERKPSERPQKTDFLWTSPFIHPSIM 158
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGeyrrasrITLSRLPFFLGLRLLGLNLPFLIGGFAL 158


                  ....*..
gi 1583828758 159 MKTSVLQ 165
Cdd:pfam00535 159 YRREALE 165
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-147 3.58e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 65.45  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKKKEQVEMAisSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLrNEKNEGLSKALNRCLK 82
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFME--SLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTGLA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1583828758  83 YAKGEYIARMDADDISLPERFEKQV-MFLKTHPEYAfTGSAVSLIDEGGIWGERKPSERPQKTDFL 147
Cdd:PRK10073   83 VATGKYVAFPDADDVVYPTMYETLMtMALEDDLDVA-QCNADWCFRDTGETWQSIPSDRLRSTGVL 147
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 28-135 3.28e-03

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 38.05  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  28 LNQSYSNFEFIICDdGSSEEFFLWLQEYCKTDE--RI-HLLRNEKNEGLSKALNRCLKYAKGEYIARMDADDISLPERFE 104
Cdd:TIGR04440  22 YSDFGCDYRIIIAD-SSDEKFNENNLKVFKNYSnpNItYLHYPDLGVPFYEKLLDALEQVETPYVVICADDDFIIPSGLT 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1583828758 105 KQVMFLKTHPEYAFT-GSAVSLIDEG-GIWGER 135
Cdd:TIGR04440 101 ECLSFLEANPDYSAAqGRYVYFEDRGdRVYGDQ 133
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 6-206 2.67e-43

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: 145.92  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEKKKEQVEMAISSILNQSYSNFEFIICDDG---SSEEFFL--WLQEYcktDERIHLLrnEKNEGLSKALNRC 80
Cdd:cd04195     1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGpvtQSLNEVLeeFKRKL---PLKVVPL--EKNRGLGKALNEG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  81 LKYAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDE-GGIWGERKPSerPQKTDFL----WTSPFIHP 155
Cdd:cd04195    76 LKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSdGNDIGKRRLP--TSHDDILkfarRRSPFNHP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1583828758 156 SIMMKTSVLQNMNGYTTadyAERTEDYDLFMRLYAAGEKGYNLQEKLFLYR 206
Cdd:cd04195   154 TVMFRKSKVLAVGGYQD---LPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-217 7.56e-39

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 134.83  E-value: 7.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKkkEQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCLK 82
Cdd:COG0463     2 PLVSVVIPTYNEE--EYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  83 YAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVslIDEGGIWGERKPSERPQKTDFLWTSPFIHPS-IMMKT 161
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRL--IREGESDLRRLGSRLFNLVRLLTNLPDSTSGfRLFRR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1583828758 162 SVLQNMNgyttadYAER-TEDYDLFmrlyAAGEKGYNLQEKLFLYREDRNAFAKRKY 217
Cdd:COG0463   158 EVLEELG------FDEGfLEDTELL----RALRHGFRIAEVPVRYRAGESKLNLRDL 204
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-165 5.08e-34

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: 120.96  E-value: 5.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEKKKeqVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCLKYAK 85
Cdd:pfam00535   1 SVIIPTYNEEKY--LLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  86 GEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDEGG-------IWGERKPSERPQKTDFLWTSPFIHPSIM 158
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGeyrrasrITLSRLPFFLGLRLLGLNLPFLIGGFAL 158


                  ....*..
gi 1583828758 159 MKTSVLQ 165
Cdd:pfam00535 159 YRREALE 165
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 11-196 9.63e-33

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: 117.22  E-value: 9.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  11 IYNEKKkeQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCLKYAKGEYIA 90
Cdd:cd00761     5 AYNEEP--YLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  91 RMDADDISLPERFEKQVMFLKTHPEYAFTGSAvslideggiwgerkpserpqktdflwtspfihPSIMMKTSVLQNMNGY 170
Cdd:cd00761    83 FLDADDLLLPDWLERLVAELLADPEADAVGGP--------------------------------GNLLFRRELLEEIGGF 130

                         170       180
                  ....*....|....*....|....*.
gi 1583828758 171 TTADYAERtEDYDLFMRLYAAGEKGY 196
Cdd:cd00761   131 DEALLSGE-EDDDFLLRLLRGGKVAF 155
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-258 1.05e-32

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: 121.39  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKkkEQVEMAISSILNQSY--SNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRC 80
Cdd:COG1215    29 PRVSVIIPAYNEE--AVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  81 LKYAKGEYIARMDADDISLPERFEKQVMFLKtHPEYAFTGSavslideggiwgerkpserpqktdflwtspfihpSIMMK 160
Cdd:COG1215   107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGASGA----------------------------------NLAFR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758 161 TSVLQNMNGYTTADYaerTEDYDLFMRLYAAGEKGYNLQEKLFLYR--EDRNAFAKRKYRYRINEAKVrYIGFGQLGIRK 238
Cdd:COG1215   152 REALEEVGGFDEDTL---GEDLDLSLRLLRAGYRIVYVPDAVVYEEapETLRALFRQRRRWARGGLQL-LLKHRPLLRPR 227

                         250       260
                  ....*....|....*....|
gi 1583828758 239 GSMKYIIKPLVVGVLPGFVL 258
Cdd:COG1215   228 RLLLFLLLLLLPLLLLLLLL 247
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-194 1.48e-29

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


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 110.37  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNeKKKEQVEMAISSILNQSYSNFEFIICDDGSS-EEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCL 81
Cdd:cd04184     1 PLISIVMPVYN-TPEKYLREAIESVRAQTYPNWELCIADDASTdPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  82 KYAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDEGGIWGER--KPSERPqktDFLWTSPFIHPSIMM 159
Cdd:cd04184    80 ELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPffKPDWSP---DLLLSQNYIGHLLVY 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1583828758 160 KTSVLQNMNGYTTAdyAERTEDYDLFMRLYAAGEK 194
Cdd:cd04184   157 RRSLVRQVGGFREG--FEGAQDYDLVLRVSEHTDR 189
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-216 8.19e-27

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: 103.48  E-value: 8.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYN-EKK-KEQVEmaisSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERI-HLLRNEKNEGLSKALNRCLK 82
Cdd:cd04196     1 AVLMATYNgEKYlREQLD----SILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIiILIRNGKNLGVARNFESLLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  83 YAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDEGG------IWGERKPSERPQKTDFLWTSPFIHPS 156
Cdd:cd04196    77 AADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGnpigesFFEYQKIKPGTSFNNLLFQNVVTGCT 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1583828758 157 IMMKTSVLqnmngyttaDYAERTEDYDLFM------RLYAAGEKGYNLQEKLFLYRE-DRNAFAKRK 216
Cdd:cd04196   157 MAFNRELL---------ELALPFPDADVIMhdwwlaLLASAFGKVVFLDEPLILYRQhGNNVVGANK 214
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 18-206 3.40e-26

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: 101.47  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  18 EQVEMAISSILNQSYSNFEFIICD----DGSSEefflWLQEYcktDERIHLLRNEKNEGLSKALNRCLKYAKGEYIARMD 93
Cdd:cd06433    11 ETLEETIDSVLSQTYPNIEYIVIDggstDGTVD----IIKKY---EDKITYWISEPDKGIYDAMNKGIALATGDIIGFLN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  94 ADDISLPERFEKQVMFLKTHPEYAFTGSAVSLIDEGGIWGERKPSERPQKTDFLWTSPFIHPSIMMKTSVLQNMNGYTTa 173
Cdd:cd06433    84 SDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPICHQATFFRRSLFEKYGGFDE- 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1583828758 174 DYaeRT-EDYDLFMRLYAAGEKGYNLQEKLFLYR 206
Cdd:cd06433   163 SY--RIaADYDLLLRLLLAGKIFKYLPEVLAAFR 194
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 5-219 9.16e-20

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: 85.75  E-value: 9.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   5 ISVLMGIYNEKKkeQVEMAISSILNQSYS--NFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKnEGLSKALNRCLK 82
Cdd:cd02525     2 VSIIIPVRNEEK--YIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPK-RIQSAGLNIGIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  83 YAKGEYIARMDADDiSLPERF-EKQVMFLKTH-------PEYAF----TGSAVSLIDEG----GIWGERKPSERPQKTDf 146
Cdd:cd02525    79 NSRGDIIIRVDAHA-VYPKDYiLELVEALKRTgadnvggPMETIgeskFQKAIAVAQSSplgsGGSAYRGGAVKIGYVD- 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1583828758 147 lwTSPFihpsIMMKTSVLQNMNGYTTADYaeRTEDYDLFMRLYAAGEKGYnLQEKLFLY---REDRNAFAKRKYRY 219
Cdd:cd02525   157 --TVHH----GAYRREVFEKVGGFDESLV--RNEDAELNYRLRKAGYKIW-LSPDIRVYyypRSTLKKLARQYFRY 223
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-192 1.43e-19

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 83.89  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   1 MVPDISVLMGIYNekKKEQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYckTDERIHLLRNEKNEGLSKALNRC 80
Cdd:COG1216     1 MRPKVSVVIPTYN--RPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  81 LKYAKGEYIARMDADDISLPErfekqvmFLKTHPEYAFtgsavslideggiwgerkpserpqktdflwtspfihpsIMMK 160
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEPD-------WLERLLAAAC--------------------------------------LLIR 111

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1583828758 161 TSVLQNMNGYTTaDYAERTEDYDLFMRLYAAG 192
Cdd:COG1216   112 REVFEEVGGFDE-RFFLYGEDVDLCLRLRKAG 142
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 12-95 5.25e-15

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: 71.07  E-value: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  12 YNEKKK-EQVEMAISSILNQSYsNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCLKYAKGEYIA 90
Cdd:cd04179     6 YNEEENiPELVERLLAVLEEGY-DYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVV 84


                  ....*
gi 1583828758  91 RMDAD 95
Cdd:cd04179    85 TMDAD 89
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-102 1.21e-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: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   7 VLMGIYNEKkkEQVEMAISSILNQSYSNFEFIICDDGSSEEFF-LWLQEYCKTDERIHLLRNEKNEGLSKALNRCLKYAK 85
Cdd:cd06423     1 IIVPAYNEE--AVIERTIESLLALDYPKLEVIVVDDGSTDDTLeILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAK 78

                          90
                  ....*....|....*..
gi 1583828758  86 GEYIARMDADdiSLPER 102
Cdd:cd06423    79 GDIVVVLDAD--TILEP 93
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-194 1.65e-12

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: 63.73  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  12 YNekKKEQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYcktDERIHLLRNEKNEGLSKALNRCLKYAKGEYIAR 91
Cdd:cd04186     6 YN--SLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLREL---FPEVRLIRNGENLGFGAGNNQGIREAKGDYVLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  92 MDADDISLPERFEKQVMFLKTHPEYAFTGSAVSlideGGiwgerkpserpqktdflwtspfihpSIMMKTSVLQNMNGYT 171
Cdd:cd04186    81 LNPDTVVEPGALLELLDAAEQDPDVGIVGPKVS----GA-------------------------FLLVRREVFEEVGGFD 131

                         170       180
                  ....*....|....*....|...
gi 1583828758 172 TaDYAERTEDYDLFMRLYAAGEK 194
Cdd:cd04186   132 E-DFFLYYEDVDLCLRARLAGYR 153
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-147 3.58e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 65.45  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKKKEQVEMAisSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLrNEKNEGLSKALNRCLK 82
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFME--SLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTGLA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1583828758  83 YAKGEYIARMDADDISLPERFEKQV-MFLKTHPEYAfTGSAVSLIDEGGIWGERKPSERPQKTDFL 147
Cdd:PRK10073   83 VATGKYVAFPDADDVVYPTMYETLMtMALEDDLDVA-QCNADWCFRDTGETWQSIPSDRLRSTGVL 147
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-191 1.38e-11

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: 63.06  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEKKKEQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLR-NEKNEGLSKALNRCLKYA 84
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNaPDTTYSLAASRNRGTSHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  85 KGEYIARMDADDISLPERFEKQVMF-----LKTHPEYAFTGSAVSLIDEGG----IWGERKPSERPQKTDFLWTSP---F 152
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKIatslaLQENIQAAVVLPVTDLNDESSnflrRGGDLTASGDVLRDLLVFYSPlaiF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1583828758 153 IHPS---IMMKTSVLQNMNGYTTADYAERTEDYDLFMRLYAA 191
Cdd:pfam10111 161 FAPNssnALINRQAFIEVGGFDESFRGHGAEDFDIFLRLAAR 202
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
3-103 1.59e-11

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 63.09  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNekkKEQVEM-AISSILNQSYSNFEFIICDDGSSEefFLWLQEYCK--TDERIHLLRNEKNEGLSKALNR 79
Cdd:PRK10018    5 PLISIYMPTWN---RQQLAIrAIKSVLRQDYSNWEMIIVDDCSTS--WEQLQQYVTalNDPRITYIHNDINSGACAVRNQ 79

                          90       100
                  ....*....|....*....|....
gi 1583828758  80 CLKYAKGEYIARMDADDISLPERF 103
Cdd:PRK10018   80 AIMLAQGEYITGIDDDDEWTPNRL 103
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-192 1.86e-10

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: 59.31  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKKkeQVEMAISSILNQSYSNFEFIICDDGSSEE---FFLWLQEYCKtDERIHLLRNEKNEGL---SKA 76
Cdd:pfam13641   2 PDVSVVVPAFNEDS--VLGRVLEAILAQPYPPVEVVVVVNPSDAEtldVAEEIAARFP-DVRLRVIRNARLLGPtgkSRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  77 LNRCLKYAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAFTGS----------AVSLIDEGGIWGERKPSERPQKtdf 146
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPvfslnrstmlSALGALEFALRHLRMMSLRLAL--- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1583828758 147 lwTSPFIHPSIM-MKTSVLQNMNGYTTADYAerTEDYDLFMRLYAAG 192
Cdd:pfam13641 156 --GVLPLSGAGSaIRREVLKELGLFDPFFLL--GDDKSLGRRLRRHG 198
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-95 2.34e-10

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: 59.52  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKKkeQVEMAISSILNQSYSN--FEFIICDDGSS----EEfflwLQEYckTDERIHLLRNEKNEGLSKA 76
Cdd:cd06439    29 PTVTIIIPAYNEEA--VIEAKLENLLALDYPRdrLEIIVVSDGSTdgtaEI----AREY--ADKGVKLLRFPERRGKAAA 100

                          90
                  ....*....|....*....
gi 1583828758  77 LNRCLKYAKGEYIARMDAD 95
Cdd:cd06439   101 LNRALALATGEIVVFTDAN 119
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 23-95 2.93e-10

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: 57.87  E-value: 2.93e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1583828758  23 AISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALnRC-LKYAKGEYIARMDAD 95
Cdd:cd04187    18 RLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAAL-LAgLDHARGDAVITMDAD 90
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 12-133 4.67e-10

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


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 57.59  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  12 YNekKKEQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYCKTDER--IHLLrnEKNEG--LSKALNRCLKYAKGE 87
Cdd:cd06420     6 YN--RPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIpiKHVW--QEDEGfrKAKIRNKAIAAAKGD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1583828758  88 YIARMDADDISLPErfekqvmFLKTHPEYAFTGSAVS----LIDEG----GIWG 133
Cdd:cd06420    82 YLIFIDGDCIPHPD-------FIADHIELAEPGVFLSgsrvLLNEKlterGIRG 128
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 13-186 9.37e-10

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: 57.30  E-value: 9.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  13 NEKKKeqVEMAISSILNQSY--SNFEFIICDDGSSEEFFLWLQ-EYCKTDERIHLLRN--EKNEGLSKALNRCLKYAKGE 87
Cdd:cd04192     7 NEAEN--LPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEfAAAKPNFQLKILNNsrVSISGKKNALTTAIKAAKGD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  88 YIARMDADDISLPERFEKQVMFLKTHPeYAFTGSAVSLIDEGGIWGERkpserpQKTDFLWTSPFIHPSIMMK---TSVL 164
Cdd:cd04192    85 WIVTTDADCVVPSNWLLTFVAFIQKEQ-IGLVAGPVIYFKGKSLLAKF------QRLDWLSLLGLIAGSFGLGkpfMCNG 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1583828758 165 QNMNgYTTADYAE----------RTEDYDLFM 186
Cdd:cd04192   158 ANMA-YRKEAFFEvggfegndhiASGDDELLL 188
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 3-118 6.64e-09

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 54.89  E-value: 6.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKKkEQVEMAISSILNQSYSNFEF--IICDDGSSEEFFLWLQEYCkTDERIHLLRNEKNEGlSKA--LN 78
Cdd:cd06421     1 PTVDVFIPTYNEPL-EIVRKTLRAALAIDYPHDKLrvYVLDDGRRPELRALAAELG-VEYGYRYLTRPDNRH-AKAgnLN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1583828758  79 RCLKYAKGEYIARMDADDISLPERFEKQVMFLKTHPEYAF 118
Cdd:cd06421    78 NALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVAL 117
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 12-95 2.18e-08

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: 53.31  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  12 YNEKkkEQVEMAISSILNQSYS-NFEFIICDDGSSEEFFLWLQEYCKTDERIHLLRNEKNEGLSKALNRCLKYAKGEYIA 90
Cdd:cd06442     6 YNER--ENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIV 83


                  ....*
gi 1583828758  91 RMDAD 95
Cdd:cd06442    84 VMDAD 88
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 6-94 3.81e-07

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: 50.28  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEkkkeQVEM---AISSILNQSYSNF--EFIICDDGSSEEFFLWLQE--YCKTDERIHLLRNEKNEGLSKALN 78
Cdd:cd02510     1 SVIIIFHNE----ALSTllrTVHSVINRTPPELlkEIILVDDFSDKPELKLLLEeyYKKYLPKVKVLRLKKREGLIRARI 76

                          90
                  ....*....|....*.
gi 1583828758  79 RCLKYAKGEYIARMDA 94
Cdd:cd02510    77 AGARAATGDVLVFLDS 92
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-133 1.30e-06

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 48.02  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  12 YNEKKKeqVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEyCKTDERIHLLRNEKNEGLSKALNRCLKYA---KGEY 88
Cdd:cd04185     6 YNRLDL--LKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTS-LGDLDNIVYLRLPENLGGAGGFYEGVRRAyelGYDW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1583828758  89 IARMDADDISLPERFEKQVMFLKtHPEYAFTGSAVSLIDeGGIWG 133
Cdd:cd04185    83 IWLMDDDAIPDPDALEKLLAYAD-KDNPQFLAPLVLDPD-GSFVG 125
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 12-108 2.89e-06

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: 46.79  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  12 YNEKKK--EQVEMAISSILNQSYSNFEFIICDDGSSEEFFLWLQEYC-KTDERIHLLRNEKNEGLSKALNRCLKYAKGEY 88
Cdd:cd04188     6 YNEEKRlpPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLArKNPALIRVLTLPKNRGKGGAVRAGMLAARGDY 85

                          90       100
                  ....*....|....*....|...
gi 1583828758  89 IARMDAD---DISLPERFEKQVM 108
Cdd:cd04188    86 ILFADADlatPFEELEKLEEALK 108
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 7-211 3.08e-06

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


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 47.07  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   7 VLMGIYNekkKEQ-VEMAISSILNQSYSN-FEFIICDDGSSEEFFLWLQEYCK--TDERIHLLRNEKN----EGLSKALN 78
Cdd:cd06913     1 IILPVHN---GEQwLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKklEDSGVIVLVGSHNspspKGVGYAKN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  79 RCLKYAKGEYIARMDADDISLPERFEKQVMFLKTHPEyAFTGSAVSLIDEGGI-----WGERKPSErpQKTDFLWTSpfi 153
Cdd:cd06913    78 QAIAQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPN-SIIGCQVRRIPEDSTerytrWINTLTRE--QLLTQVYTS--- 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1583828758 154 H-PSIMMKT-----SVLQNMNGYTTADYAErTEDYDLFMRLYAAGEKGYNLQEKLFLYREDRNA 211
Cdd:cd06913   152 HgPTVIMPTwfcsrEWFSHVGPFDEGGKGV-PEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGA 214
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 12-111 3.17e-06

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


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 46.89  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  12 YNEKKKEQVEmAISSILNQSYsnfEFIICDDGSSEEFFLWLQEYcktDERIHLLRNEKNEGLSKALNRCLKYAKG---EY 88
Cdd:cd02526     6 YNPDLSKLKE-LLAALAEQVD---KVVVVDNSSGNDIELRLRLN---SEKIELIHLGENLGIAKALNIGIKAALEngaDY 78

                          90       100
                  ....*....|....*....|...
gi 1583828758  89 IARMDADDISLPERFEKQVMFLK 111
Cdd:cd02526    79 VLLFDQDSVPPPDMVEKLLAYKI 101
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 6-106 1.67e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 45.07  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   6 SVLMGIYNEKKKEQVEMAISSILNQSYSNFEFIICDDGS---SEEFFLWLQEYCKTDeRIHLLRNEKNEGLSKALNRCLK 82
Cdd:PLN02726   12 SIIVPTYNERLNIALIVYLIFKALQDVKDFEIIVVDDGSpdgTQDVVKQLQKVYGED-RILLRPRPGKLGLGTAYIHGLK 90

                          90       100
                  ....*....|....*....|....*....
gi 1583828758  83 YAKGEYIARMDAdDIS-----LPERFEKQ 106
Cdd:PLN02726   91 HASGDFVVIMDA-DLShhpkyLPSFIKKQ 118
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 3-118 1.20e-04

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 42.30  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   3 PDISVLMGIYNEKkkEQVEMAISSILNQSY--SNFEFIICDDGSSEEFFLWLQ---EYCKTDERI-HLLRNEKNEGLSKA 76
Cdd:cd06437     1 PMVTVQLPVFNEK--YVVERLIEAACALDYpkDRLEIQVLDDSTDETVRLAREiveEYAAQGVNIkHVRRADRTGYKAGA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1583828758  77 LNRCLKYAKGEYIARMDADDISLPErFEKQVMFLKTHPEYAF 118
Cdd:cd06437    79 LAEGMKVAKGEYVAIFDADFVPPPD-FLQKTPPYFADPKLGF 119
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 75-192 3.71e-04

CESA_like_2 is a member of 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: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 40.70  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  75 KALNRCLKYAKGEYIARMDADDISLPERFEKQV-MFLKTHPEYAFTGSAVSLIDEGGIWGERKPS-ERPQKTDFL----- 147
Cdd:cd06427    74 KACNYALAFARGEYVVIYDAEDAPDPDQLKKAVaAFARLDDKLACVQAPLNYYNARENWLTRMFAlEYAAWFDYLlpgla 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1583828758 148 -WTSPFihP----SIMMKTSVLQNMNGYttaDYAERTEDYDLFMRLYAAG 192
Cdd:cd06427   154 rLGLPI--PlggtSNHFRTDVLRELGGW---DPFNVTEDADLGLRLARAG 198
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 17-101 7.28e-04

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: 40.08  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  17 KEQVEMAI---SSILNQSYSNFEFIICDDGSSEEfFLW--LQEYCKT-DERIHLLRNEKNEGL-SKALNRCLKYAKG--E 87
Cdd:cd06435     8 EEPPEMVKetlDSLAALDYPNFEVIVIDNNTKDE-ALWkpVEAHCAQlGERFRFFHVEPLPGAkAGALNYALERTAPdaE 86

                          90
                  ....*....|....
gi 1583828758  88 YIARMDADDISLPE 101
Cdd:cd06435    87 IIAVIDADYQVEPD 100
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 39-111 1.38e-03

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 40.01  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1583828758  39 ICDDGSSEEFFLWLQEYcktdeRIHLLRNEKNEGlSKA--LNRCLKYAKGEYIARMDADDIslPER-FEKQVM--FLK 111
Cdd:PRK11498  297 ILDDGGREEFRQFAQEV-----GVKYIARPTHEH-AKAgnINNALKYAKGEFVAIFDCDHV--PTRsFLQMTMgwFLK 366
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 4-137 1.66e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 39.37  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758   4 DISVLMGIYNEKK------KEQVEMAISSILNQSYSNFEFIICDDGSS-------EEFFlwlQEYCKTDERIHLLRNEKN 70
Cdd:PTZ00260   71 DLSIVIPAYNEEDrlpkmlKETIKYLESRSRKDPKFKYEIIIVNDGSKdktlkvaKDFW---RQNINPNIDIRLLSLLRN 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  71 EGLSKALNRCLKYAKGEYIARMDAD---DISLPERFEKqVMFLKTHPEYAFTGSAVSLIDEGGIWGERKP 137
Cdd:PTZ00260  148 KGKGGAVRIGMLASRGKYILMVDADgatDIDDFDKLED-IMLKIEQNGLGIVFGSRNHLVDSDVVAKRKW 216
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 28-135 3.28e-03

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 38.05  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583828758  28 LNQSYSNFEFIICDdGSSEEFFLWLQEYCKTDE--RI-HLLRNEKNEGLSKALNRCLKYAKGEYIARMDADDISLPERFE 104
Cdd:TIGR04440  22 YSDFGCDYRIIIAD-SSDEKFNENNLKVFKNYSnpNItYLHYPDLGVPFYEKLLDALEQVETPYVVICADDDFIIPSGLT 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1583828758 105 KQVMFLKTHPEYAFT-GSAVSLIDEG-GIWGER 135
Cdd:TIGR04440 101 ECLSFLEANPDYSAAqGRYVYFEDRGdRVYGDQ 133
 
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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