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Conserved domains on  [gi|521289070|ref|WP_020453338|]
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MULTISPECIES: glycosyltransferase family 2 protein [Bacillus]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-193 3.59e-34

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 122.89  E-value: 3.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   1 MNISIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHLKENVKHVKARNIGVKEA 77
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGStdGTAEILRELAAKDPrIRVIRLERNRGKGAARNAGLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  78 SGDVIMLCDDDDFFTPCHMERMLNALET--ADFVYSDAEIvsfeekeDKRIPTSRYLFAYSFNLDE-MRKFSTYVPSGSM 154
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEgpADLVYGSRLI-------REGESDLRRLGSRLFNLVRlLTNLPDSTSGFRL 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 521289070 155 YKRSLHDEIGyFDPAVhnYWDWDFFLRAAERFRVKRVPF 193
Cdd:COG0463  155 FRREVLEELG-FDEGF--LEDTELLRALRHGFRIAEVPV 190
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-193 3.59e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 122.89  E-value: 3.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   1 MNISIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHLKENVKHVKARNIGVKEA 77
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGStdGTAEILRELAAKDPrIRVIRLERNRGKGAARNAGLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  78 SGDVIMLCDDDDFFTPCHMERMLNALET--ADFVYSDAEIvsfeekeDKRIPTSRYLFAYSFNLDE-MRKFSTYVPSGSM 154
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEgpADLVYGSRLI-------REGESDLRRLGSRLFNLVRlLTNLPDSTSGFRL 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 521289070 155 YKRSLHDEIGyFDPAVhnYWDWDFFLRAAERFRVKRVPF 193
Cdd:COG0463  155 FRREVLEELG-FDEGF--LEDTELLRALRHGFRIAEVPV 190
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-162 1.73e-29

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: 109.41  E-value: 1.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070    4 SIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYS-DLPIRVIHLKENVKHVKARNIGVKEASGD 80
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGStdGTVEIAEEYAKkDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   81 VIMLCDDDDFFTPCHMERMLNALETADFVYSDAEIVSFEEKEDKRIPTSRYLFAYSFNLDEMR----KFSTYVPSGSMYK 156
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRllglNLPFLIGGFALYR 160

                  ....*.
gi 521289070  157 RSLHDE 162
Cdd:pfam00535 161 REALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-191 4.10e-24

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: 94.88  E-value: 4.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLPIRVIHLKENVKHV-KARNIGVKEASGDV 81
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGStdGTLEILEEYAKKDPRVIRVINEENQGLaAARNAGLKAARGEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  82 IMLCDDDDFFTPCHMERMLNALETADfvysDAEIVSFeekedkriptsrylfaysfnldemrkfstyvPSGSMYKRSLHD 161
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADP----EADAVGG-------------------------------PGNLLFRRELLE 125
                        170       180       190
                 ....*....|....*....|....*....|.
gi 521289070 162 EIGYFDPAVHNYW-DWDFFLRAAERFRVKRV 191
Cdd:cd00761  126 EIGGFDEALLSGEeDDDFLLRLLRGGKVAFR 156
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-187 1.70e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 57.36  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHlKENVKHVKARNIGVKEASG 79
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGStdNSVEIAKHYAENYPhVRLLH-QANAGVSVARNTGLAVATG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  80 DVIMLCDDDDFFTPCHMERMLNALET---------ADFVYSDAeivsfeEKEDKRIPTSRylFAYSFNLD---------E 141
Cdd:PRK10073  87 KYVAFPDADDVVYPTMYETLMTMALEddldvaqcnADWCFRDT------GETWQSIPSDR--LRSTGVLSgpdwlrmalS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 521289070 142 MRKFsTYVPSGSMYKRSLHDEIGY-FDPAVHNY---WDWDFFLrAAERFR 187
Cdd:PRK10073 159 SRRW-THVVWLGVYRRDFIVKNNIkFEPGLHHQdipWTTEVMF-NALRVR 206
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-193 3.59e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 122.89  E-value: 3.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   1 MNISIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHLKENVKHVKARNIGVKEA 77
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGStdGTAEILRELAAKDPrIRVIRLERNRGKGAARNAGLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  78 SGDVIMLCDDDDFFTPCHMERMLNALET--ADFVYSDAEIvsfeekeDKRIPTSRYLFAYSFNLDE-MRKFSTYVPSGSM 154
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEgpADLVYGSRLI-------REGESDLRRLGSRLFNLVRlLTNLPDSTSGFRL 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 521289070 155 YKRSLHDEIGyFDPAVhnYWDWDFFLRAAERFRVKRVPF 193
Cdd:COG0463  155 FRREVLEELG-FDEGF--LEDTELLRALRHGFRIAEVPV 190
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-201 3.67e-31

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 114.70  E-value: 3.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   1 MNISIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDlPIRVIHLKENVKHVKARNIGVKEAS 78
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGStdGTAELLAALAFP-RVRVIRNPENLGFAAARNLGLRAAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  79 GDVIMLCDDDDFFTPCHMERMLNAletadfvysdaeivsfeekedkriptsrylfaysfnldemrkfstyvpSGSMYKRS 158
Cdd:COG1216   82 GDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------ACLLIRRE 113
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 521289070 159 LHDEIGYFDPAVHNYW-DWDFFLRAAER-FRVKRVPFASVIYAFS 201
Cdd:COG1216  114 VFEEVGGFDERFFLYGeDVDLCLRLRKAgYRIVYVPDAVVYHLGG 158
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-162 1.73e-29

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: 109.41  E-value: 1.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070    4 SIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYS-DLPIRVIHLKENVKHVKARNIGVKEASGD 80
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGStdGTVEIAEEYAKkDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   81 VIMLCDDDDFFTPCHMERMLNALETADFVYSDAEIVSFEEKEDKRIPTSRYLFAYSFNLDEMR----KFSTYVPSGSMYK 156
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRllglNLPFLIGGFALYR 160

                  ....*.
gi 521289070  157 RSLHDE 162
Cdd:pfam00535 161 REALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-191 4.10e-24

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: 94.88  E-value: 4.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLPIRVIHLKENVKHV-KARNIGVKEASGDV 81
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGStdGTLEILEEYAKKDPRVIRVINEENQGLaAARNAGLKAARGEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  82 IMLCDDDDFFTPCHMERMLNALETADfvysDAEIVSFeekedkriptsrylfaysfnldemrkfstyvPSGSMYKRSLHD 161
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADP----EADAVGG-------------------------------PGNLLFRRELLE 125
                        170       180       190
                 ....*....|....*....|....*....|.
gi 521289070 162 EIGYFDPAVHNYW-DWDFFLRAAERFRVKRV 191
Cdd:cd00761  126 EIGGFDEALLSGEeDDDFLLRLLRGGKVAFR 156
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
4-208 1.19e-20

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: 86.83  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   4 SIVVVTHNRVTALCELLESITKQSVAPFEVIIVnDAG---ESVDFVERlYSDLPIRVI--------HlkenvkhvkARNI 72
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVI-DGGstdGTVDIIKK-YEDKITYWIsepdkgiyD---------AMNK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  73 GVKEASGDVIMLCDDDDFFTP---CHMERMLNALETADFVYSDAEIVSfeekEDKRIPTSRYLFAYSFNLdemRKFSTYV 149
Cdd:cd06433   70 GIALATGDIIGFLNSDDTLLPgalLAVVAAFAEHPEVDVVYGDVLLVD----ENGRVIGRRRPPPFLDKF---LLYGMPI 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521289070 150 PSGSM-YKRSLHDEIGYFDPAVHNYWDWDFFLRAAERFRVK-RVPFasVIYAFSDQGDNQS 208
Cdd:cd06433  143 CHQATfFRRSLFEKYGGFDESYRIAADYDLLLRLLLAGKIFkYLPE--VLAAFRLGGVSST 201
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-198 3.14e-19

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: 83.02  E-value: 3.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNR-VTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYS--DLPIRVIHLKENVKHVKARNIGVKEA 77
Cdd:cd04184    3 ISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDAStdPEVKRVLKKYAaqDPRIKVVFREENGGISAATNSALELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  78 SGDVIMLCDDDDFFTP---CHMERMLNALETADFVYSDaeivsfEEKEDKRIPTSRYLFAYSFNLDEMRKFStYVPSGSM 154
Cdd:cd04184   83 TGEFVALLDHDDELAPhalYEVVKALNEHPDADLIYSD------EDKIDEGGKRSEPFFKPDWSPDLLLSQN-YIGHLLV 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 521289070 155 YKRSLHDEIGYFDPAVHNYWDWDFFLRAAERF-RVKRVPfaSVIY 198
Cdd:cd04184  156 YRRSLVRQVGGFREGFEGAQDYDLVLRVSEHTdRIAHIP--RVLY 198
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-197 3.44e-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: 76.83  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDlpIRVIHLKENVKHVKARNIGVKEASGDVI 82
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNAStdGSVELLRELFPE--VRLIRNGENLGFGAGNNQGIREAKGDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  83 MLCDDDDFFTPchmermlNALetadfvysDAEIVSFEEKEDKRIPTSRylfaysfnldemrkfstyVPSGSM-YKRSLHD 161
Cdd:cd04186   79 LLLNPDTVVEP-------GAL--------LELLDAAEQDPDVGIVGPK------------------VSGAFLlVRREVFE 125
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 521289070 162 EIGYFDPAVHNYW-DWDFFLRAAER-FRVKRVPFASVI 197
Cdd:cd04186  126 EVGGFDEDFFLYYeDVDLCLRARLAgYRVLYVPQAVIY 163
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
3-196 1.58e-15

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: 74.78  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNRVTALCELLESITKQS--VAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHLKENVKHVKARNIGVKEA 77
Cdd:COG1215   31 VSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGStdETAEIARELAAEYPrVRVIERPENGGKAAALNAGLKAA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  78 SGDVIMLCDDDDFFTPCHMERMLNALETadfvySDAEIVSfeekedkriptsrylfaysfnldemrkfstyvpSGSMYKR 157
Cdd:COG1215  111 RGDIVVFLDADTVLDPDWLRRLVAAFAD-----PGVGASG---------------------------------ANLAFRR 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 521289070 158 SLHDEIGYFDPaVHNYWDWDFFLRAAER-FRVKRVPFASV 196
Cdd:COG1215  153 EALEEVGGFDE-DTLGEDLDLSLRLLRAgYRIVYVPDAVV 191
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
4-209 9.15e-14

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: 68.43  E-value: 9.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   4 SIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLPIRVIHLKENVKHVKARNI--GVKEASG 79
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGStdGTVEIIKEYIDKDPFIIILIRNGKNLGVARNFesLLQAADG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  80 DVIMLCDDDDFFTPCHMERMLNALETAD---FVYSDAEIVSFEEKE-DKRIPTSRYLFAYSFNLDEMrkFSTYVP-SGSM 154
Cdd:cd04196   81 DYVFFCDQDDIWLPDKLERLLKAFLKDDkplLVYSDLELVDENGNPiGESFFEYQKIKPGTSFNNLL--FQNVVTgCTMA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 521289070 155 YKRSLHDEIGYFDPAVHNYWDWDFFLRAAERFRVKRVPFASVIYAfsdQ-GDNQSG 209
Cdd:cd04196  159 FNRELLELALPFPDADVIMHDWWLALLASAFGKVVFLDEPLILYR---QhGNNVVG 211
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
3-181 1.98e-13

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: 68.03  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNRVTALCELLESITKQSV--APFEVIIVnDAGES---VDFVERLYS-DLPIRVIH-LKENVKhvKARNIGVK 75
Cdd:cd02525    2 VSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVV-DGGSTdgtREIVQEYAAkDPRIRLIDnPKRIQS--AGLNIGIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  76 EASGDVIMLCDDDDFFTPCHMERMLNALETadfvySDAEIVSfeeKEDKRIPTSRYLFAYSFNLDEM-----------RK 144
Cdd:cd02525   79 NSRGDIIIRVDAHAVYPKDYILELVEALKR-----TGADNVG---GPMETIGESKFQKAIAVAQSSPlgsggsayrggAV 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 521289070 145 FSTYVPSG--SMYKRSLHDEIGYFDPA-VHNYwDWDFFLR 181
Cdd:cd02525  151 KIGYVDTVhhGAYRREVFEKVGGFDESlVRNE-DAELNYR 189
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
16-176 3.31e-12

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: 63.87  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  16 LCELLESITKQSVAPFEVIIVNDA--GESVDFV-ERLYSDLPIRVIHLKENVKHVKARNIGVKEASGDVIMLCDDDDFFT 92
Cdd:cd04195   15 LREALESILKQTLPPDEVVLVKDGpvTQSLNEVlEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCTYDWVARMDTDDISL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  93 PCHMERMLNALET-ADFVYSDAEIVSFEEKEDK----RIPTSR---YLFAysfnldemRKFSTYVPSGSMYKRSLHDEIG 164
Cdd:cd04195   95 PDRFEKQLDFIEKnPEIDIVGGGVLEFDSDGNDigkrRLPTSHddiLKFA--------RRRSPFNHPTVMFRKSKVLAVG 166
                        170
                 ....*....|....
gi 521289070 165 -YFD-PAVHNYWDW 176
Cdd:cd04195  167 gYQDlPLVEDYALW 180
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-218 8.97e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 59.96  E-value: 8.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   6 VVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLPIRVIHLKENVKHVKARNIGVK---EASGD 80
Cdd:cd04185    2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNAStdGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYEGVRrayELGYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  81 VIMLCDDDDFFTPchmermlNALETAdFVYSDAEIVSFeekedkrIPTSRYLFAYSFNldemrkfstyvpsGSMYKRSLH 160
Cdd:cd04185   82 WIWLMDDDAIPDP-------DALEKL-LAYADKDNPQF-------LAPLVLDPDGSFV-------------GVLISRRVV 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521289070 161 DEIGYFDPAVHNYW-DWDFFLRAAERFRVKRVPFASVI--YAFSDQGDNQSGDLGGMRQYY 218
Cdd:cd04185  134 EKIGLPDKEFFIWGdDTEYTLRASKAGPGIYVPDAVVVhkTAINKGSSAVVNIDPPWKLYY 194
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
5-139 1.86e-10

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: 58.74  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITK--QSVAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHLKENVKHVKARNIGVKEASG 79
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGStdGTAEIARELAARVPrVRVIRLSRNFGKGAAVRAGFKAARG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521289070  80 DVIMLCDDDDFFTPCHMERMLNAL--ETADFVYSdaeiVSFEEKEDKRIPTSRYLFAYSFNL 139
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLleGGADVVIG----SRFVRGGGAGMPLLRRLGSRLFNF 138
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-187 1.70e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 57.36  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHlKENVKHVKARNIGVKEASG 79
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGStdNSVEIAKHYAENYPhVRLLH-QANAGVSVARNTGLAVATG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  80 DVIMLCDDDDFFTPCHMERMLNALET---------ADFVYSDAeivsfeEKEDKRIPTSRylFAYSFNLD---------E 141
Cdd:PRK10073  87 KYVAFPDADDVVYPTMYETLMTMALEddldvaqcnADWCFRDT------GETWQSIPSDR--LRSTGVLSgpdwlrmalS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 521289070 142 MRKFsTYVPSGSMYKRSLHDEIGY-FDPAVHNY---WDWDFFLrAAERFR 187
Cdd:PRK10073 159 SRRW-THVVWLGVYRRDFIVKNNIkFEPGLHHQdipWTTEVMF-NALRVR 206
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
3-196 2.85e-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: 55.84  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070    3 ISIVVVTHNRVTALCELLESITKQSVAPFEVIIV---NDAG--ESVDFVERLYSDLPIRVIHLKE----NVKhVKARNIG 73
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVvnpSDAEtlDVAEEIAARFPDVRLRVIRNARllgpTGK-SRGLNHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   74 VKEASGDVIMLCDDDDFFTPCHMERMLNALETAD--FVYSDAEIvsfeeKEDKRIPTSRY-LFAYSFNLDEMR-----KF 145
Cdd:pfam13641  83 FRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKvgAVGTPVFS-----LNRSTMLSALGaLEFALRHLRMMSlrlalGV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 521289070  146 STYVPSGSMYKRSLHDEIGYFDPAVHNYWDWDFFLRAAER-FRVKRVPFASV 196
Cdd:pfam13641 158 LPLSGAGSAIRREVLKELGLFDPFFLLGDDKSLGRRLRRHgWRVAYAPDAAV 209
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-168 9.29e-09

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: 53.77  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITKQSVAPFEVIIVNDaGESVDFVERLYS-----DLPIRVIHLKENVKHVKARNIGVKEASG 79
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDD-GSTDDTLEILEElaalyIRRVLVVRDKENGGKAGALNAGLRHAKG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  80 DVIMLCDDDDFFTPCHMERMLNALetadFVYSDAEIVSFE---EKEDKRIPTSRYLFAY--SFNLDEM---RKFSTYVPS 151
Cdd:cd06423   80 DIVVVLDADTILEPDALKRLVVPF----FADPKVGAVQGRvrvRNGSENLLTRLQAIEYlsIFRLGRRaqsALGGVLVLS 155
                        170
                 ....*....|....*....
gi 521289070 152 G--SMYKRSLHDEIGYFDP 168
Cdd:cd06423  156 GafGAFRREALREVGGWDE 174
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
3-181 4.51e-08

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 53.07  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAGESVD----FVERLySDLPIRVIHLKENVKHVKARNIGVKEAS 78
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSWEqlqqYVTAL-NDPRITYIHNDINSGACAVRNQAIMLAQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  79 GDVIMLCDDDDFFTPCHMERML---NALETADFVYSDAEIVSFEEKED-------KRIPTSRYLFaYSFNLDEMRKFSTy 148
Cdd:PRK10018  86 GEYITGIDDDDEWTPNRLSVFLahkQQLVTHAFLYANDYVCQGEVYSQpaslplyPKSPYSRRLF-YKRNIIGNQVFTW- 163
                        170       180       190
                 ....*....|....*....|....*....|...
gi 521289070 149 vpsGSMYKRSLhdeigyFDPAVHNYWDWDFFLR 181
Cdd:PRK10018 164 ---AWRFKECL------FDTELKAAQDYDIFLR 187
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
6-192 5.80e-08

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: 52.29  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   6 VVVTHN-RVTALCELLESITKQSVapfEVIIVNDAGESVDFVERLYSDLPIRVIHLKENVKHVKARNIGVKEASG---DV 81
Cdd:cd02526    2 VVVTYNpDLSKLKELLAALAEQVD---KVVVVDNSSGNDIELRLRLNSEKIELIHLGENLGIAKALNIGIKAALEngaDY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  82 IMLCDDDDFFTPCHMERMLnALETADFVYSDAEIV---SFEEKEDKRIPtsRYLFAYSFNLDEMRKFSTYVP------SG 152
Cdd:cd02526   79 VLLFDQDSVPPPDMVEKLL-AYKILSDKNSNIGAVgprIIDRRTGENSP--GVRKSGYKLRIQKEGEEGLKEvdflitSG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 521289070 153 SMYKRSLHDEIGYFDPAVH-NYWDWDFFLRAAER-FRVKRVP 192
Cdd:cd02526  156 SLISLEALEKVGGFDEDLFiDYVDTEWCLRARSKgYKIYVVP 197
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
5-198 7.18e-08

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: 52.28  E-value: 7.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070    5 IVVVTHNRVTALCELLESITKQSVAPFEVIIVNDaGESVDFVERLYSdlpIRVIHLKENVKHV--------KARNIGVKE 76
Cdd:pfam10111   4 IPVYNGEKTHWIQERILNQTFQYDPEFELIIIND-GSTDKTLEEVSS---IKDHNLQVYYPNApdttyslaASRNRGTSH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   77 ASGDVIMLCDDDDFFTPCHMERMLNALET--------ADFVYSdaeIVSFEEKEDKRIPTSRYLFAYS-FNLDEMRKFST 147
Cdd:pfam10111  80 AIGEYISFIDGDCLWSPDKFEKQLKIATSlalqeniqAAVVLP---VTDLNDESSNFLRRGGDLTASGdVLRDLLVFYSP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 521289070  148 YV----PSGS--MYKRSLHDEIGYFDPAV--HNYWDWDFFLRAAERFRVKRVPFASVIY 198
Cdd:pfam10111 157 LAiffaPNSSnaLINRQAFIEVGGFDESFrgHGAEDFDIFLRLAARYPFVAVMPPQLLY 215
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
5-88 1.06e-07

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: 50.65  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITKQSVAPFEVIIVNDAG--ESVDFVERLYSDLPIRVIHL-KENV--KHVKARNIGVKEASG 79
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSteETKELIEEFKSQFPIPIKHVwQEDEgfRKAKIRNKAIAAAKG 80

                 ....*....
gi 521289070  80 DVIMLCDDD 88
Cdd:cd06420   81 DYLIFIDGD 89
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
18-184 1.18e-05

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: 45.32  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  18 ELLESITKQSvaPFEVIIVNDaGESVDFVERL---YSDLPIRVIhlkeNVKHVKARN---IGVKEASGDVIMLCDDDDFF 91
Cdd:cd06434   18 ECLRSILRQK--PLEIIVVTD-GDDEPYLSILsqtVKYGGIFVI----TVPHPGKRRalaEGIRHVTTDIVVLLDSDTVW 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  92 TPCHMERMLNALEtadfvysDAEI--VSfeekEDKRI--PTSRYLFAYSFNLDEMRKF----------STYVPSG--SMY 155
Cdd:cd06434   91 PPNALPEMLKPFE-------DPKVggVG----TNQRIlrPRDSKWSFLAAEYLERRNEeiraamsydgGVPCLSGrtAAY 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 521289070 156 KRS-LHDEIgyFDPAVHNYWDWDFFLRAAE 184
Cdd:cd06434  160 RTEiLKDFL--FLEEFTNETFMGRRLNAGD 187
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
3-83 3.05e-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: 44.10  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNRVTALCELLESITKQSVAPFEVIIVnDAGeSVDFVERLYSDLPIRVIHLKenvkhvKAR----NIGVKEAS 78
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVV-DGG-STDGTVAIARSAGVVVISSP------KGRarqmNAGAAAAR 72

                 ....*
gi 521289070  79 GDVIM 83
Cdd:cd02522   73 GDWLL 77
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-88 5.34e-05

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: 42.85  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITK---QSVAPFEVIIVNDAG--ESVDFVERLYSDLP-IRVIHLKENVKHVKARNIGVKEAS 78
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAvleSLGYDYEIIFVDDGStdRTLEILRELAARDPrVKVIRLSRNFGQQAALLAGLDHAR 80
                         90
                 ....*....|
gi 521289070  79 GDVIMLCDDD 88
Cdd:cd04187   81 GDAVITMDAD 90
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
13-107 6.04e-05

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: 42.94  E-value: 6.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070  13 VTALCELLESITKQSvapFEVIIVNDAG--ESVDFVERLYSDLP--IRVIHLKENVKHVKARNIGVKEASGDVIMLCDDD 88
Cdd:cd04188   16 LEEAVEYLEERPSFS---YEIIVVDDGSkdGTAEVARKLARKNPalIRVLTLPKNRGKGGAVRAGMLAARGDYILFADAD 92
                         90
                 ....*....|....*....
gi 521289070  89 DFFTPCHMERMLNALETAD 107
Cdd:cd04188   93 LATPFEELEKLEEALKTSG 111
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
4-97 3.46e-04

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


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 41.42  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   4 SIVVVTHNRvtALCELLESIT---KQSVAPF--EVIIVNDAGESVDFVERLYSD----LP-IRVIHLKENVKHVKARNIG 73
Cdd:cd02510    1 SVIIIFHNE--ALSTLLRTVHsviNRTPPELlkEIILVDDFSDKPELKLLLEEYykkyLPkVKVLRLKKREGLIRARIAG 78
                         90       100
                 ....*....|....*....|....
gi 521289070  74 VKEASGDVImlcddddFFTPCHME 97
Cdd:cd02510   79 ARAATGDVL-------VFLDSHCE 95
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-88 3.94e-04

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 40.73  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   5 IVVVTHNRVTALCELLESITKQSVAP--FEVIIVNDAGE--SVDFVERLYSDLPIRVIHLKENVKHVK----ARNIGVKE 76
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTdgTVQILEFAAAKPNFQLKILNNSRVSISgkknALTTAIKA 80
                         90
                 ....*....|..
gi 521289070  77 ASGDVIMLCDDD 88
Cdd:cd04192   81 AKGDWIVTTDAD 92
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
3-105 7.16e-04

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 39.50  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289070   3 ISIVVVTHNRVTALCELLESITKQSVAPFEVII-VNDAG-ESVDFVERL---YSDLPIRVIHLKENVKH-VKARNI--GV 74
Cdd:cd02520    3 VSILKPLCGVDPNLYENLESFFQQDYPKYEILFcVQDEDdPAIPVVRKLiakYPNVDARLLIGGEKVGInPKVNNLikGY 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 521289070  75 KEASGDVIMLCDDDDFFTPCHMERMLNALET 105
Cdd:cd02520   83 EEARYDILVISDSDISVPPDYLRRMVAPLMD 113
 
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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