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Conserved domains on  [gi|490366019|ref|WP_004245683|]
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MULTISPECIES: glycosyltransferase [Proteus]

Protein Classification

glycosyltransferase( domain architecture ID 11484566)

glycosyltransferase that may be involved in cell wall biosynthesis; similar to Escherichia coli glycosyltransferase YibD

CAZY:  GT2
Gene Ontology:  GO:0016020|GO:0016757

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-329 0e+00

putative glycosyl transferase; Provisional


:

Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 601.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   1 MSSSFPQLSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQGVSVARNTG 80
Cdd:PRK10073   1 MMNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  81 FAVAKGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVATCNGNYVYDDkNRPTRPIFPSTRLTTTEVLTGPQWLERALES 160
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRD-TGETWQSIPSDRLRSTGVLSGPDWLRMALSS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019 161 KKFLHVTWLNIYRRQFLLEHGYYFEPGLHHQDIPWTTEVLLTAKRVKYIDERYYDYFIHSGSVSHTTPDDRIHVRTIYNY 240
Cdd:PRK10073 160 RRWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019 241 MKILEMLDAINQRHAEIAKTINACYWQIAKEGLGIIHSIDAISSPETKKQIVKVFFERGIWALIWKNAKDFRLKWRLGRR 320
Cdd:PRK10073 240 IKITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLW 319

                 ....*....
gi 490366019 321 YFRLKKILA 329
Cdd:PRK10073 320 SFRLWQWRD 328
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-329 0e+00

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 601.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   1 MSSSFPQLSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQGVSVARNTG 80
Cdd:PRK10073   1 MMNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  81 FAVAKGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVATCNGNYVYDDkNRPTRPIFPSTRLTTTEVLTGPQWLERALES 160
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRD-TGETWQSIPSDRLRSTGVLSGPDWLRMALSS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019 161 KKFLHVTWLNIYRRQFLLEHGYYFEPGLHHQDIPWTTEVLLTAKRVKYIDERYYDYFIHSGSVSHTTPDDRIHVRTIYNY 240
Cdd:PRK10073 160 RRWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019 241 MKILEMLDAINQRHAEIAKTINACYWQIAKEGLGIIHSIDAISSPETKKQIVKVFFERGIWALIWKNAKDFRLKWRLGRR 320
Cdd:PRK10073 240 IKITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLW 319

                 ....*....
gi 490366019 321 YFRLKKILA 329
Cdd:PRK10073 320 SFRLWQWRD 328
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-215 2.15e-39

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 137.91  E-value: 2.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   6 PQLSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILT-QENQGVSVARNTGFAVA 84
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRlERNRGKGAARNAGLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  85 KGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVATcnGNYVYDDKNRPTRPiFPSTRLTTTEVLTGPQWleraleskkfl 164
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY--GSRLIREGESDLRR-LGSRLFNLVRLLTNLPD----------- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490366019 165 HVTWLNIYRRQFL----LEHGYYFEPGLhhqdipwtTEVLLTAKRVKYIDERYYD 215
Cdd:COG0463  148 STSGFRLFRREVLeelgFDEGFLEDTEL--------LRALRHGFRIAEVPVRYRA 194
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
9-138 4.07e-32

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: 117.50  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019    9 SIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQE-NQGVSVARNTGFAVAKGE 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490366019   88 YVAFPDIDDVIDKRMYPRLLEIAKADNLDVATCNGNYVYDDKNRPTRPIFP 138
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRI 131
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
10-127 8.94e-31

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: 113.76  E-value: 8.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVT-ILTQENQGVSVARNTGFAVAKGEY 88
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIrVINEENQGLAAARNAGLKAARGEY 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490366019  89 VAFPDIDDVIDKRMYPRLLEIAKAD-NLDVATCNGNYVYD 127
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADpEADAVGGPGNLLFR 120
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
8-98 4.65e-12

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 65.59  E-value: 4.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   8 LSIVVAVFNGEKFLPQFFNCLHAQ-QLE--NWELILVDDGSTDNSRQILDKWEKHFPNVTIL---TQENQGVSVARNTGF 81
Cdd:NF038302   3 FTVAIPTYNGANRLPEVLERLRSQiGTEslSWEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLrycFEPQQGAAFARQRAI 82
                         90
                 ....*....|....*..
gi 490366019  82 AVAKGEYVAFPDiDDVI 98
Cdd:NF038302  83 QEAKGELIGFLD-DDNL 98
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
39-179 1.77e-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: 39.20  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   39 ILVDDGSTDNSRQILDKWEKHF--PNVTILTQENQGVSVARNTGFAVA--KGEYVAFPDIDDVIDKRMYPRLLEIAKAdN 114
Cdd:TIGR04440  31 IIIADSSDEKFNENNLKVFKNYsnPNITYLHYPDLGVPFYEKLLDALEqvETPYVVICADDDFIIPSGLTECLSFLEA-N 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490366019  115 LDVATCNGNYVY--DDKNRPTR-PIFPSTRLTTtevLTGPQWLERALESKKFLHVTWLNIYRRQFLLE 179
Cdd:TIGR04440 110 PDYSAAQGRYVYfeDRGDRVYGdQPFQYYPDYS---IEQDDPIERLAQFFSNYMHLWYSVFRTDVIKK 174
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-329 0e+00

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 601.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   1 MSSSFPQLSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQGVSVARNTG 80
Cdd:PRK10073   1 MMNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  81 FAVAKGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVATCNGNYVYDDkNRPTRPIFPSTRLTTTEVLTGPQWLERALES 160
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRD-TGETWQSIPSDRLRSTGVLSGPDWLRMALSS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019 161 KKFLHVTWLNIYRRQFLLEHGYYFEPGLHHQDIPWTTEVLLTAKRVKYIDERYYDYFIHSGSVSHTTPDDRIHVRTIYNY 240
Cdd:PRK10073 160 RRWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019 241 MKILEMLDAINQRHAEIAKTINACYWQIAKEGLGIIHSIDAISSPETKKQIVKVFFERGIWALIWKNAKDFRLKWRLGRR 320
Cdd:PRK10073 240 IKITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLW 319

                 ....*....
gi 490366019 321 YFRLKKILA 329
Cdd:PRK10073 320 SFRLWQWRD 328
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-215 2.15e-39

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 137.91  E-value: 2.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   6 PQLSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILT-QENQGVSVARNTGFAVA 84
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRlERNRGKGAARNAGLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  85 KGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVATcnGNYVYDDKNRPTRPiFPSTRLTTTEVLTGPQWleraleskkfl 164
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY--GSRLIREGESDLRR-LGSRLFNLVRLLTNLPD----------- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490366019 165 HVTWLNIYRRQFL----LEHGYYFEPGLhhqdipwtTEVLLTAKRVKYIDERYYD 215
Cdd:COG0463  148 STSGFRLFRREVLeelgFDEGFLEDTEL--------LRALRHGFRIAEVPVRYRA 194
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
9-138 4.07e-32

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: 117.50  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019    9 SIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQE-NQGVSVARNTGFAVAKGE 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490366019   88 YVAFPDIDDVIDKRMYPRLLEIAKADNLDVATCNGNYVYDDKNRPTRPIFP 138
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRI 131
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
10-127 8.94e-31

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: 113.76  E-value: 8.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVT-ILTQENQGVSVARNTGFAVAKGEY 88
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIrVINEENQGLAAARNAGLKAARGEY 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490366019  89 VAFPDIDDVIDKRMYPRLLEIAKAD-NLDVATCNGNYVYD 127
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADpEADAVGGPGNLLFR 120
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
6-110 2.87e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 92.36  E-value: 2.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   6 PQLSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWekHFPNVTILTQ-ENQGVSVARNTGFAVA 84
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNpENLGFAAARNLGLRAA 80
                         90       100
                 ....*....|....*....|....*.
gi 490366019  85 KGEYVAFPDIDDVIDKRMYPRLLEIA 110
Cdd:COG1216   81 GGDYLLFLDDDTVVEPDWLERLLAAA 106
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-122 3.09e-21

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: 92.11  E-value: 3.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   2 SSSFPQLSIVVAVFNGEKFLPQFFNCLHAQ--QLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQE-NQGVSVARN 78
Cdd:COG1215   25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQdyPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPeNGGKAAALN 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490366019  79 TGFAVAKGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVATCNG 122
Cdd:COG1215  105 AGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL 148
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-97 9.54e-19

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: 83.06  E-value: 9.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   9 SIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQGVSVARNtgF----AVA 84
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARN--FesllQAA 78
                         90
                 ....*....|...
gi 490366019  85 KGEYVAFPDIDDV 97
Cdd:cd04196   79 DGDYVFFCDQDDI 91
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
10-121 1.05e-18

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: 82.24  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHA--QQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILT-QENQGVSVARNTGFAVAKG 86
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRlSRNFGKGAAVRAGFKAARG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490366019  87 EYVAFPDIDDVIDKRMYPRLLEIAKADNLDVATCN 121
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGS 115
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
6-114 3.28e-18

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: 81.48  E-value: 3.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   6 PQLSIVVAVFNG-EKFLPQFFNCLHAQQLENWELILVDDGSTDNS-RQILDKWEKHFPNVTIL-TQENQGVSVARNTGFA 82
Cdd:cd04184    1 PLISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEvKRVLKKYAAQDPRIKVVfREENGGISAATNSALE 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 490366019  83 VAKGEYVAFPDIDDVIDKRMyprLLEIAKADN 114
Cdd:cd04184   81 LATGEFVALLDHDDELAPHA---LYEVVKALN 109
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
10-183 3.40e-18

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: 80.73  E-value: 3.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKW--EKHFPNVTILTQENQGVSVARNTGFAVAKGE 87
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELaaLYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  88 YVAFPDIDDVIDKRMYPRLLEIAKADNlDVATCNGNYVYddKNRPTRPIfpsTRLTTTEVLTGpQWLERALES--KKFLH 165
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADP-KVGAVQGRVRV--RNGSENLL---TRLQAIEYLSI-FRLGRRAQSalGGVLV 153
                        170
                 ....*....|....*....
gi 490366019 166 VTWLN-IYRRQFLLEHGYY 183
Cdd:cd06423  154 LSGAFgAFRREALREVGGW 172
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
9-117 1.13e-17

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: 81.12  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   9 SIVVAVFNGEKFLPQFFNCLHAQQ--LENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQGVSVARNTGFAVAKG 86
Cdd:cd02525    3 SIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRNSRG 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 490366019  87 EYVAFPDIDDVIDKRMYPRLLEIAKADNLDV 117
Cdd:cd02525   83 DIIIRVDAHAVYPKDYILELVEALKRTGADN 113
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
10-120 1.98e-17

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: 78.37  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILdkwEKHFPNVTILTQ-ENQGVSVARNTGFAVAKGEY 88
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELL---RELFPEVRLIRNgENLGFGAGNNQGIREAKGDY 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 490366019  89 VAF--PDIddVIDKRMYPRLLEIAkADNLDVATC 120
Cdd:cd04186   78 VLLlnPDT--VVEPGALLELLDAA-EQDPDVGIV 108
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
10-119 8.16e-17

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: 77.61  E-value: 8.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQF----FNCLHAQQLENWELILVDDGSTDNSRQILDK-WEKHFPNVTILTQE-NQGVSVARNTGFAV 83
Cdd:cd04188    1 VVIPAYNEEKRLPPTleeaVEYLEERPSFSYEIIVVDDGSKDGTAEVARKlARKNPALIRVLTLPkNRGKGGAVRAGMLA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490366019  84 AKGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVAT 119
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEALKTSGYDIAI 116
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
10-95 1.23e-15

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: 73.67  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHA---QQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILT-QENQGVSVARNTGFAVAK 85
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAvleSLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRlSRNFGQQAALLAGLDHAR 80
                         90
                 ....*....|
gi 490366019  86 GEYVAFPDID 95
Cdd:cd04187   81 GDAVITMDAD 90
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
9-229 6.76e-14

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: 69.50  E-value: 6.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   9 SIVVAVFNGEKFLPQffnCLH---AQQLENWELILVDDGSTDNSRQILDKWEkhfPNVTILTQEN-QGVSVARNTGFAVA 84
Cdd:cd06433    1 SIITPTYNQAETLEE---TIDsvlSQTYPNIEYIVIDGGSTDGTVDIIKKYE---DKITYWISEPdKGIYDAMNKGIALA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  85 KGEYVAFPDIDDvidkRMYPRLLE-----IAKADNLDVATCNGNYVYDDKNRPTRPIFPStrltttevltgpqwlerale 159
Cdd:cd06433   75 TGDIIGFLNSDD----TLLPGALLavvaaFAEHPEVDVVYGDVLLVDENGRVIGRRRPPP-------------------- 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490366019 160 skkflhvtwlniYRRQFLLEHGYyfepgLHHQDIPWTTEVLltaKRVKYIDERY-----YDYFI---HSGSVSHTTPD 229
Cdd:cd06433  131 ------------FLDKFLLYGMP-----ICHQATFFRRSLF---EKYGGFDESYriaadYDLLLrllLAGKIFKYLPE 188
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
8-98 4.65e-12

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 65.59  E-value: 4.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   8 LSIVVAVFNGEKFLPQFFNCLHAQ-QLE--NWELILVDDGSTDNSRQILDKWEKHFPNVTIL---TQENQGVSVARNTGF 81
Cdd:NF038302   3 FTVAIPTYNGANRLPEVLERLRSQiGTEslSWEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLrycFEPQQGAAFARQRAI 82
                         90
                 ....*....|....*..
gi 490366019  82 AVAKGEYVAFPDiDDVI 98
Cdd:NF038302  83 QEAKGELIGFLD-DDNL 98
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
10-105 4.91e-11

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: 61.70  E-value: 4.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHAQQLEN-WELILVDDGSTDNSRQILDKWEKHF--PNVTILTQEN-----QGVSVARNTGF 81
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKLedSGVIVLVGSHnspspKGVGYAKNQAI 80
                         90       100
                 ....*....|....*....|....
gi 490366019  82 AVAKGEYVAFPDIDDVidkrMYPR 105
Cdd:cd06913   81 AQSSGRYLCFLDSDDV----MMPQ 100
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
9-97 3.35e-10

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: 58.87  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   9 SIVVAVFNGEK--FLPQFFNCLHAQQLENWELILVDDGS-TDNSRQILDKWEKHFPNVTILTQENQGVSVARNTGFAVAK 85
Cdd:cd04195    1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                         90
                 ....*....|..
gi 490366019  86 GEYVAFPDIDDV 97
Cdd:cd04195   81 YDWVARMDTDDI 92
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
10-95 6.78e-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: 6.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFP-NVTILTQENQG--VSVARNTGFAVAKG 86
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPiPIKHVWQEDEGfrKAKIRNKAIAAAKG 80

                 ....*....
gi 490366019  87 EYVAFPDID 95
Cdd:cd06420   81 DYLIFIDGD 89
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-131 1.33e-09

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: 57.59  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   3 SSFPQLSIVVAVFNGEKFLpqffnclhAQQLEN----------WELILVDDGSTDNSRQILDKWEKHfpNVTILTQE-NQ 71
Cdd:cd06439   26 AYLPTVTIIIPAYNEEAVI--------EAKLENllaldyprdrLEIIVVSDGSTDGTAEIAREYADK--GVKLLRFPeRR 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  72 GVSVARNTGFAVAKGEYVAFPDIDDVIDKRMyPRLLeIAKADNLDVATCNGNYVYDDKNR 131
Cdd:cd06439   96 GKAAALNRALALATGEIVVFTDANALLDPDA-LRLL-VRHFADPSVGAVSGELVIVDGGG 153
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
8-117 2.16e-09

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: 56.91  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   8 LSIVVAVFNGEKFLPqffNCLhaQQLENW--ELILVDDGSTDNSRQILdkwekHFPNVTILTQENQGVSVARNTGFAVAK 85
Cdd:cd02511    2 LSVVIITKNEERNIE---RCL--ESVKWAvdEIIVVDSGSTDRTVEIA-----KEYGAKVYQRWWDGFGAQRNFALELAT 71
                         90       100       110
                 ....*....|....*....|....*....|..
gi 490366019  86 GEYVAFPDIDDVIDKRMYPRLLEIAKADNLDV 117
Cdd:cd02511   72 NDWVLSLDADERLTPELADEILALLATDDYDG 103
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
7-110 1.10e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 52.43  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   7 QLSIVVAVFNGEKFLPQFFNCLHA--QQLE-NWELILVDDGSTDNSRQILDKW----EKHFpnVTILTQENQGVSVARNT 79
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAacESLGkEYEILLIDDGSSDNSAEMLVEAaqapDSHI--VAILLNRNYGQHSAIMA 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 490366019  80 GFAVAKGEYVAFPDIDDVIDKRMYPRLLEIA 110
Cdd:PRK10714  85 GFSHVTGDLIITLDADLQNPPEEIPRLVAKA 115
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
35-119 1.43e-07

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: 51.38  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  35 NWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQ-GVSVARNTGFAVAKGEYVAFPDIDDVIDKRMYPRLLEIAKAD 113
Cdd:cd06442   27 DYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKrGLGSAYIEGFKAARGDVIVVMDADLSHPPEYIPELLEAQLEG 106

                 ....*.
gi 490366019 114 NLDVAT 119
Cdd:cd06442  107 GADLVI 112
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
10-95 1.56e-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: 51.52  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  10 IVVAVFNGEKFLPQFFNCLHAQQL--ENWELILVDDGSTDNSRQILDKWEKH-FPNVTILTQ---ENQGVSVARNTGFAV 83
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAKpNFQLKILNNsrvSISGKKNALTTAIKA 80
                         90
                 ....*....|..
gi 490366019  84 AKGEYVAFPDID 95
Cdd:cd04192   81 AKGDWIVTTDAD 92
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-109 1.32e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 49.38  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   7 QLSIVVAVFNGEKFLP-------QFFNCLHAQQLE-NWELILVDDGSTDNSRQILDKW--EKHFPNVTIL---TQENQGV 73
Cdd:PTZ00260  71 DLSIVIPAYNEEDRLPkmlketiKYLESRSRKDPKfKYEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRllsLLRNKGK 150
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490366019  74 SVARNTGFAVAKGEYVAFPDIDDVIDKRMYPRLLEI 109
Cdd:PTZ00260 151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDI 186
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
37-93 1.58e-06

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: 48.74  E-value: 1.58e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  37 ELILVDDGST-DNSRQILDKWEKHF-PNVTIL-TQENQGVSVARNTGFAVAKGEYVAFPD 93
Cdd:cd02510   32 EIILVDDFSDkPELKLLLEEYYKKYlPKVKVLrLKKREGLIRARIAGARAATGDVLVFLD 91
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
9-115 6.66e-06

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 46.89  E-value: 6.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019    9 SIVVAVFNGEK--FLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTI--LTQENQGVSVARNTGFAVA 84
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYpnAPDTTYSLAASRNRGTSHA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 490366019   85 KGEYVAFPDIDDVIDKRMYPRLLEIAKADNL 115
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKIATSLAL 111
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
8-91 1.44e-05

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


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 45.25  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   8 LSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKwekhfPNVTILTqENQGVSVARNTGFAVAKGE 87
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARS-----AGVVVIS-SPKGRARQMNAGAAAARGD 74

                 ....
gi 490366019  88 YVAF 91
Cdd:cd02522   75 WLLF 78
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
6-96 1.05e-04

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 43.44  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   6 PQLSIVVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTdnSRQILDKW--EKHFPNVTILTQE-NQGVSVARNTGFA 82
Cdd:PRK10018   5 PLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYvtALNDPRITYIHNDiNSGACAVRNQAIM 82
                         90
                 ....*....|....
gi 490366019  83 VAKGEYVAFPDIDD 96
Cdd:PRK10018  83 LAQGEYITGIDDDD 96
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
6-119 5.88e-04

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 40.84  E-value: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   6 PQLSIVVAVFNGEKFLPQFFNCL--HAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQ---GVSVARNTG 80
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIfkALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPgklGLGTAYIHG 88
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490366019  81 FAVAKGEYVAFPDIDDVIDKRMYPRLLEIAKADNLDVAT 119
Cdd:PLN02726  89 LKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVT 127
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
16-95 1.56e-03

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 37.22  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   16 NGEKFLPQFfnCLHAQQLENWELILVDDGSTDNSRQILDKWE--KHFPNVTILTQENQGVSVARNTGFAVAKGEYVAFPD 93
Cdd:pfam13704   2 NEADILPQW--LAHHLALGFDHIYVYDNGSDDGTAEILARLPdvSILRSDLSYKDARFQVDWRNALLARYAEADWVLVVD 79

                  ..
gi 490366019   94 ID 95
Cdd:pfam13704  80 AD 81
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
39-179 1.77e-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: 39.20  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019   39 ILVDDGSTDNSRQILDKWEKHF--PNVTILTQENQGVSVARNTGFAVA--KGEYVAFPDIDDVIDKRMYPRLLEIAKAdN 114
Cdd:TIGR04440  31 IIIADSSDEKFNENNLKVFKNYsnPNITYLHYPDLGVPFYEKLLDALEqvETPYVVICADDDFIIPSGLTECLSFLEA-N 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490366019  115 LDVATCNGNYVY--DDKNRPTR-PIFPSTRLTTtevLTGPQWLERALESKKFLHVTWLNIYRRQFLLE 179
Cdd:TIGR04440 110 PDYSAAQGRYVYfeDRGDRVYGdQPFQYYPDYS---IEQDDPIERLAQFFSNYMHLWYSVFRTDVIKK 174
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-127 4.28e-03

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: 37.61  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366019  11 VVAVFNGEKFLPQFFNCLHAQQLENWELILVDDGSTDNSRQILDKWEKHFPNVTILTQENQGVSVARNTGFAVA---KGE 87
Cdd:cd04185    2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYEGVRRAyelGYD 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490366019  88 YVAFPDiDDVI-DKRMYPRLLEIAKADNLDVATCNgnyVYD 127
Cdd:cd04185   82 WIWLMD-DDAIpDPDALEKLLAYADKDNPQFLAPL---VLD 118
 
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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