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Conserved domains on  [gi|492128771|ref|WP_005756394|]
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glycosyltransferase [Pasteurella multocida]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135928)

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

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-203 8.22e-115

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: 327.73  E-value: 8.22e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   4 SVLMSLYVKENPLYLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLHCS 83
Cdd:cd04195    1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  84 YDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSLDEIVSYRnVPLSKADIVQFTRKRCPFNHMTVAYQK 163
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 492128771 164 QAVLACGGYED--LQEDYYLWIKLVASGHNVANLPDILVYAR 203
Cdd:cd04195  160 SKVLAVGGYQDlpLVEDYALWARMLANGARFANLPEILVKAR 201
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-203 8.22e-115

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: 327.73  E-value: 8.22e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   4 SVLMSLYVKENPLYLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLHCS 83
Cdd:cd04195    1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  84 YDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSLDEIVSYRnVPLSKADIVQFTRKRCPFNHMTVAYQK 163
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 492128771 164 QAVLACGGYED--LQEDYYLWIKLVASGHNVANLPDILVYAR 203
Cdd:cd04195  160 SKVLAVGGYQDlpLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-216 4.78e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 114.41  E-value: 4.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   1 MKFSVLMSLYvkeN-PLYLRECFESLQQQTLPADEIVLVFDGPvSEELEAIVQQFEMRLP-IKTVKLAQNRGLGKALNEG 78
Cdd:COG0463    2 PLVSVVIPTY---NeEEYLEEALESLLAQTYPDFEIIVVDDGS-TDGTAEILRELAAKDPrIRVIRLERNRGKGAARNAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  79 LLHCSYDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSLdeivsYRNVPLSKADIVQFTRKRCPFNHMT 158
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESD-----LRRLGSRLFNLVRLLTNLPDSTSGF 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492128771 159 VAYQKQAVLACGGYEDLQEDYYLwIKLVASGHNVANLPdilVYARVGNGMVGRRRGLA 216
Cdd:COG0463  153 RLFRREVLEELGFDEGFLEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNLRDLLR 206
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-125 5.33e-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: 97.47  E-value: 5.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771    4 SVLMSLYVKENplYLRECFESLQQQTLPADEIVLVFDGPvSEELEAIVQQF-EMRLPIKTVKLAQNRGLGKALNEGLLHC 82
Cdd:pfam00535   1 SVIIPTYNEEK--YLLETLESLLNQTYPNFEIIVVDDGS-TDGTVEIAEEYaKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 492128771   83 SYDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFG 125
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFG 120
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-103 4.45e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 56.21  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   2 KFSVLMSLYVKENplYLRECFESLQQQTLPADEIVLVFDGPVSEELEaIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLH 81
Cdd:PRK10073   7 KLSIIIPLYNAGK--DFRAFMESLIAQTWTALEIIIVNDGSTDNSVE-IAKHYAENYPHVRLLHQANAGVSVARNTGLAV 83
                         90       100
                 ....*....|....*....|..
gi 492128771  82 CSYDWVFRMDTDDICVPTRFEK 103
Cdd:PRK10073  84 ATGKYVAFPDADDVVYPTMYET 105
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-203 8.22e-115

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: 327.73  E-value: 8.22e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   4 SVLMSLYVKENPLYLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLHCS 83
Cdd:cd04195    1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  84 YDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSLDEIVSYRnVPLSKADIVQFTRKRCPFNHMTVAYQK 163
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 492128771 164 QAVLACGGYED--LQEDYYLWIKLVASGHNVANLPDILVYAR 203
Cdd:cd04195  160 SKVLAVGGYQDlpLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-216 4.78e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 114.41  E-value: 4.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   1 MKFSVLMSLYvkeN-PLYLRECFESLQQQTLPADEIVLVFDGPvSEELEAIVQQFEMRLP-IKTVKLAQNRGLGKALNEG 78
Cdd:COG0463    2 PLVSVVIPTY---NeEEYLEEALESLLAQTYPDFEIIVVDDGS-TDGTAEILRELAAKDPrIRVIRLERNRGKGAARNAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  79 LLHCSYDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSLdeivsYRNVPLSKADIVQFTRKRCPFNHMT 158
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESD-----LRRLGSRLFNLVRLLTNLPDSTSGF 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492128771 159 VAYQKQAVLACGGYEDLQEDYYLwIKLVASGHNVANLPdilVYARVGNGMVGRRRGLA 216
Cdd:COG0463  153 RLFRREVLEELGFDEGFLEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNLRDLLR 206
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-242 1.87e-26

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: 104.82  E-value: 1.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   1 MKFSVLMSLYvKEnPLYLRECFESLQQQTLPAD--EIVLVFDGPvSEELEAIVQQFEMRLP-IKTVKLAQNRGLGKALNE 77
Cdd:COG1215   29 PRVSVIIPAY-NE-EAVIEETLRSLLAQDYPKEklEVIVVDDGS-TDETAEIARELAAEYPrVRVIERPENGGKAAALNA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  78 GLLHCSYDWVFRMDTDDICVPTRFEKQVGYIQqHPDVIIVGGqiaefgqsldeivsyrnvplskadivqftrkrcpfnhm 157
Cdd:COG1215  106 GLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGASGA-------------------------------------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771 158 TVAYQKQAVLACGGYED--LQEDYYLWIKLVASGHNVANLPDILVYARVGNGMVG-----RRRGLAQAQAEWRLFKLKYR 230
Cdd:COG1215  147 NLAFRREALEEVGGFDEdtLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRAlfrqrRRWARGGLQLLLKHRPLLRP 226
                        250
                 ....*....|..
gi 492128771 231 VKLQGMLSGLFT 242
Cdd:COG1215  227 RRLLLFLLLLLL 238
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-125 5.33e-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: 97.47  E-value: 5.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771    4 SVLMSLYVKENplYLRECFESLQQQTLPADEIVLVFDGPvSEELEAIVQQF-EMRLPIKTVKLAQNRGLGKALNEGLLHC 82
Cdd:pfam00535   1 SVIIPTYNEEK--YLLETLESLLNQTYPNFEIIVVDDGS-TDGTVEIAEEYaKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 492128771   83 SYDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFG 125
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFG 120
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
17-120 3.97e-22

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: 89.49  E-value: 3.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  17 YLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLHCSYDWVFRMDTDDIC 96
Cdd:cd00761   11 YLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDADDLL 90
                         90       100
                 ....*....|....*....|....
gi 492128771  97 VPTRFEKQVGYIQQHPDVIIVGGQ 120
Cdd:cd00761   91 LPDWLERLVAELLADPEADAVGGP 114
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-240 9.04e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 73.49  E-value: 9.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   1 MKFSVLMSLYvkeNPL-YLRECFESLQQQTLPADEIVLVFDGPvSEELEAIVQQFEMRlPIKTVKLAQNRGLGKALNEGL 79
Cdd:COG1216    3 PKVSVVIPTY---NRPeLLRRCLESLLAQTYPPFEVIVVDNGS-TDGTAELLAALAFP-RVRVIRNPENLGFAAARNLGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  80 LHCSYDWVFRMDtDDICVptrfekqvgyiqqHPDviivggqiaefgqSLDEIVSYRNvplskadivqftrkrcpfnhmtV 159
Cdd:COG1216   78 RAAGGDYLLFLD-DDTVV-------------EPD-------------WLERLLAAAC----------------------L 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771 160 AYQKQAVLACGGY-EDL---QEDYYLWIKLVASGHNVANLPDILVYaRVGNGMVGRRRGLAQAQAEWRLFKLKYRVKLQG 235
Cdd:COG1216  109 LIRREVFEEVGGFdERFflyGEDVDLCLRLRKAGYRIVYVPDAVVY-HLGGASSGPLLRAYYLGRNRLLFLRKHGPRPLL 187

                 ....*
gi 492128771 236 MLSGL 240
Cdd:COG1216  188 RLALL 192
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-204 7.34e-12

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: 63.40  E-value: 7.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   2 KFSVLMSLYVKENplYLRECFESLQQQTLPADEI-VLVFDGPVSEELEAIVQQFEMRLPIktVKLAQN--RGLGKALNEG 78
Cdd:cd02525    1 FVSIIIPVRNEEK--YIEELLESLLNQSYPKDLIeIIVVDGGSTDGTREIVQEYAAKDPR--IRLIDNpkRIQSAGLNIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  79 LLHCSYDWVFRMDTDDIcVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSLDEIV--------------SYRNVPLS--KA 142
Cdd:cd02525   77 IRNSRGDIIIRVDAHAV-YPKDYILELVEALKRTGADNVGGPMETIGESKFQKAiavaqssplgsggsAYRGGAVKigYV 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492128771 143 DIVQFtrkrcpfnhmtVAYQKQAVLACGGY-EDL--QEDYYLWIKLVASGHNVANLPDILVYARV 204
Cdd:cd02525  156 DTVHH-----------GAYRREVFEKVGGFdESLvrNEDAELNYRLRKAGYKIWLSPDIRVYYYP 209
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
2-113 2.28e-11

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: 61.45  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   2 KFSVLMSLYvKENPLYLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEMRLP-IKTVKLAQNRGLGKALNEGLL 80
Cdd:cd04184    2 LISIVMPVY-NTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPrIKVVFREENGGISAATNSALE 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 492128771  81 HCSYDWVFRMDTDDICVPTRFEKQVGYIQQHPD 113
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALNEHPD 113
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
18-178 5.23e-11

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: 59.93  E-value: 5.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  18 LRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGlGK--ALNEGLLHCSYDWVFRMDTDDI 95
Cdd:cd06423   12 IERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENG-GKagALNAGLRHAKGDIVVVLDADTI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  96 --------CVPTRFE-KQVGYIQQHPDVIIVGGQIAEFGQSLDEIVSYRnvplskadivQFTRKRCPFNHMTV------A 160
Cdd:cd06423   91 lepdalkrLVVPFFAdPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFR----------LGRRAQSALGGVLVlsgafgA 160
                        170       180
                 ....*....|....*....|
gi 492128771 161 YQKQAVLACGGYED--LQED 178
Cdd:cd06423  161 FRREALREVGGWDEdtLTED 180
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
4-117 5.85e-11

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: 60.34  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   4 SVLMSLYvkeNP-LYLRECFESLQQQTLPADEIVLVFDGPVSEELEaIVQQF--EMRLPIKTVKLAQNRGLGKALNEGLL 80
Cdd:cd04196    1 AVLMATY---NGeKYLREQLDSILAQTYKNDELIISDDGSTDGTVE-IIKEYidKDPFIIILIRNGKNLGVARNFESLLQ 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 492128771  81 HCSYDWVFRMDTDDICVPTRFEKQVGYIQQHPDVIIV 117
Cdd:cd04196   77 AADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLV 113
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
17-205 5.86e-11

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: 60.25  E-value: 5.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  17 YLRECFESLQQQTLPADEIVLVfDGPVSEELEAIVQQFEMRLpiktVKLAQN--RGLGKALNEGLLHCSYDWVFRMDTDD 94
Cdd:cd06433   12 TLEETIDSVLSQTYPNIEYIVI-DGGSTDGTVDIIKKYEDKI----TYWISEpdKGIYDAMNKGIALATGDIIGFLNSDD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  95 ICVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSLDEIVSYRNVPLSKADIvqftRKRCPFNHMTVAYQKQAVLACGGY-E 173
Cdd:cd06433   87 TLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFL----LYGMPICHQATFFRRSLFEKYGGFdE 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 492128771 174 DLQ--EDYYLWIKLVASGHNVANLPDILVYARVG 205
Cdd:cd06433  163 SYRiaADYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-121 9.18e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 56.03  E-value: 9.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  11 VKENPLYLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEmrlPIKTVKLAQNRGLGKALNEGLLHCSYDWVFRM 90
Cdd:cd04186    5 NYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFP---EVRLIRNGENLGFGAGNNQGIREAKGDYVLLL 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 492128771  91 DTDDICVPTRFEKQVGYIQQHPDVIIVGGQI 121
Cdd:cd04186   82 NPDTVVEPGALLELLDAAEQDPDVGIVGPKV 112
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
17-201 1.35e-09

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: 57.00  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   17 YLRECFESLQQQTLPADEIVLVFDgPVSEELEAIVQQFEMRLPIKTVKLAQN------RGLGKALNEGLLHCSYDWVFRM 90
Cdd:pfam13641  16 VLGRVLEAILAQPYPPVEVVVVVN-PSDAETLDVAEEIAARFPDVRLRVIRNarllgpTGKSRGLNHGFRAVKSDLVVLH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   91 DTDDICVPTRFEKQVGYIqQHPDVIIVGGQiaefgqsldEIVSYRNVPLSKADIVQFTR---KRCPFNHM---------T 158
Cdd:pfam13641  95 DDDSVLHPGTLKKYVQYF-DSPKVGAVGTP---------VFSLNRSTMLSALGALEFALrhlRMMSLRLAlgvlplsgaG 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 492128771  159 VAYQKQAVLACGGYED---LQEDYYLWIKLVASGHNVANLPDILVY 201
Cdd:pfam13641 165 SAIRREVLKELGLFDPfflLGDDKSLGRRLRRHGWRVAYAPDAAVR 210
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-103 4.45e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 56.21  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771   2 KFSVLMSLYVKENplYLRECFESLQQQTLPADEIVLVFDGPVSEELEaIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLH 81
Cdd:PRK10073   7 KLSIIIPLYNAGK--DFRAFMESLIAQTWTALEIIIVNDGSTDNSVE-IAKHYAENYPHVRLLHQANAGVSVARNTGLAV 83
                         90       100
                 ....*....|....*....|..
gi 492128771  82 CSYDWVFRMDTDDICVPTRFEK 103
Cdd:PRK10073  84 ATGKYVAFPDADDVVYPTMYET 105
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
17-118 4.56e-08

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: 51.87  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  17 YLRECFESLQQQTLPADEIVLVfDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGLGKALNEGL---LHCSYDWVFRMDTD 93
Cdd:cd04185   11 LLKECLDALLAQTRPPDHIIVI-DNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYEGVrraYELGYDWIWLMDDD 89
                         90       100
                 ....*....|....*....|....*
gi 492128771  94 DICVPTRFEKQVGYIQQHPDVIIVG 118
Cdd:cd04185   90 AIPDPDALEKLLAYADKDNPQFLAP 114
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
18-197 2.13e-07

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: 50.36  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  18 LRECFESLQQQTLPAD--EIVLVFDGpvSEE-----LEAIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLHCSYDWVFRM 90
Cdd:cd04192   12 LPRLLQSLSALDYPKEkfEVILVDDH--STDgtvqiLEFAAAKPNFQLKILNNSRVSISGKKNALTTAIKAAKGDWIVTT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  91 DTDDICVPTRFEKQVGYIQQHPDVIIVGGQIAEFGQSL-DEIVSYRNVPLSKADIVQFTRKRcPF----NHMtvAYQKQA 165
Cdd:cd04192   90 DADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLlAKFQRLDWLSLLGLIAGSFGLGK-PFmcngANM--AYRKEA 166
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 492128771 166 VLACGGYEDLQ-----EDYYLWIKLVASGHNVANLPD 197
Cdd:cd04192  167 FFEVGGFEGNDhiasgDDELLLAKVASKYPKVAYLKN 203
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
15-116 2.95e-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: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  15 PLYLRECFESLQQQTLPADEIVLVFDGPVSEELEaIVQQFEMRLP--IKTVKLAQNRGLGKALNEGLLHCSYDWVFRMDT 92
Cdd:cd04188   13 PPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAE-VARKLARKNPalIRVLTLPKNRGKGGAVRAGMLAARGDYILFADA 91
                         90       100
                 ....*....|....*....|....*
gi 492128771  93 DDICVPTRFEKQVGYIQQ-HPDVII 116
Cdd:cd04188   92 DLATPFEELEKLEEALKTsGYDIAI 116
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
14-118 7.38e-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: 45.74  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  14 NPlYLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEmrlPIKTVKLAQNRGLGKALNEG---LLHCSYDWVFRM 90
Cdd:cd02526    7 NP-DLSKLKELLAALAEQVDKVVVVDNSSGNDIELRLRLNSE---KIELIHLGENLGIAKALNIGikaALENGADYVLLF 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 492128771  91 DTDDICVPTRFEKQVGYI---QQHPDVIIVG 118
Cdd:cd02526   83 DQDSVPPPDMVEKLLAYKilsDKNSNIGAVG 113
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
17-121 1.16e-05

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


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 45.14  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  17 YLRECFESLQQQTLPADEIVLVFDGPVSEELEAIVQQFEMRLPIKTVKL-------AQNRGLGKALNEGLLHCSYDWVFR 89
Cdd:cd06913   11 WLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVlvgshnsPSPKGVGYAKNQAIAQSSGRYLCF 90
                         90       100       110
                 ....*....|....*....|....*....|..
gi 492128771  90 MDTDDICVPTRFEKQVGYIQQHPDVIIvGGQI 121
Cdd:cd06913   91 LDSDDVMMPQRIRLQYEAALQHPNSII-GCQV 121
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
14-190 1.68e-05

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


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 44.11  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  14 NPLYLRECFESLQQQTLPADEIVLVFDGPvSEELEAIVQQFEMRLPIKTVKLAQ-NRG--LGKALNEGLLHCSYDWVFRM 90
Cdd:cd06420    8 RPEALELVLKSVLNQSILPFEVIIADDGS-TEETKELIEEFKSQFPIPIKHVWQeDEGfrKAKIRNKAIAAAKGDYLIFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  91 DTDdiCVPtrfekqvgyiqqHPDVIIVGGQIAEFGQsldeIVSYRNVPLSKadivQFTRKRcpFNHMTVAYQKQAVLACG 170
Cdd:cd06420   87 DGD--CIP------------HPDFIADHIELAEPGV----FLSGSRVLLNE----KLTERG--IRGCNMSFWKKDLLAVN 142
                        170       180
                 ....*....|....*....|....*
gi 492128771 171 GY-EDLQ----EDYYLWIKLVASGH 190
Cdd:cd06420  143 GFdEEFTgwggEDSELVARLLNSGI 167
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
18-93 9.88e-05

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: 42.18  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  18 LRECFESLQQ--QTLPADEIVLVFDGpvS-----EELEAIVQQFEmrlPIKTVKLAQNRGLGKALNEGLLHCSYDWVFRM 90
Cdd:cd04179   12 IPELVERLLAvlEEGYDYEIIVVDDG--StdgtaEIARELAARVP---RVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86

                 ...
gi 492128771  91 DTD 93
Cdd:cd04179   87 DAD 89
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
18-98 1.35e-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: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  18 LRECFESLQQQtlpADEIVLV----FDGPVseeleAIVQQFemrlpikTVKLAQN--RGLGKALNEGLLHCSYDWVFRMD 91
Cdd:cd02511   15 IERCLESVKWA---VDEIIVVdsgsTDRTV-----EIAKEY-------GAKVYQRwwDGFGAQRNFALELATNDWVLSLD 79

                 ....*..
gi 492128771  92 TDDICVP 98
Cdd:cd02511   80 ADERLTP 86
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
11-121 2.90e-04

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 41.09  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  11 VKENPLYLRECFESLQQQTlpADEIVLVFDGPVSEELEAIVQQFemRLPIKTVKLAQNRGLGKALNEGLLHCSYDWVFRM 90
Cdd:cd06434    9 YDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSILSQTV--KYGGIFVITVPHPGKRRALAEGIRHVTTDIVVLL 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 492128771  91 DtDDICVPTRFEKQVGYIQQHPDVIIVGGQI 121
Cdd:cd06434   85 D-SDTVWPPNALPEMLKPFEDPKVGGVGTNQ 114
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
12-201 4.75e-04

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: 40.63  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  12 KENPLYLRECFESLQQQTLPADEI-VLVFDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGlGKA--LNEGLLHCSYDWVF 88
Cdd:cd06421   11 NEPLEIVRKTLRAALAIDYPHDKLrVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRH-AKAgnLNNALAHTTGDFVA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  89 RMDTDDICVPTRFEKQVGYIQQHPDVIIVG----------GQIAEFGQSLDEIVSYRNVPLSKadivqfTRKRCPFNHMT 158
Cdd:cd06421   90 ILDADHVPTPDFLRRTLGYFLDDPKVALVQtpqffynpdpFDWLADGAPNEQELFYGVIQPGR------DRWGAAFCCGS 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492128771 159 -VAYQKQAVLACGGY--EDLQEDYYLWIKLVASGHNVANLPDILVY 201
Cdd:cd06421  164 gAVVRREALDEIGGFptDSVTEDLATSLRLHAKGWRSVYVPEPLAA 209
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
15-93 5.43e-04

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: 39.77  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771  15 PLY-----LRECFESLQQ--QTLPAD-EIVLVFDGPVSEELEAIVQQFEMRLPIKTVKLAQNRGLGKALNEGLLHCSYDW 86
Cdd:cd04187    4 PVYneeenLPELYERLKAvlESLGYDyEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDA 83

                 ....*..
gi 492128771  87 VFRMDTD 93
Cdd:cd04187   84 VITMDAD 90
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-117 1.18e-03

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 39.57  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492128771    4 SVLMSLYVKENPLYLRECFESLQQQTLPADEIVLVFDG---PVSEELEAIVQqfeMRLPIKTVKLAQNR-GLGKALNEGL 79
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTFQYDPEFELIIINDGstdKTLEEVSSIKD---HNLQVYYPNAPDTTySLAASRNRGT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 492128771   80 LHCSYDWVFRMDTDDICVPTRFEKQVGY-----IQQHPDVIIV 117
Cdd:pfam10111  78 SHAIGEYISFIDGDCLWSPDKFEKQLKIatslaLQENIQAAVV 120
 
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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