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Conserved domains on  [gi|2187933679|ref|WP_236762278|]
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MULTISPECIES: polysaccharide biosynthesis endo-1,4-beta-xylanase UppH [Agrobacterium]

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]; ...
 1-221 2.84e-42

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.84  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   1 MVSVSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFS--DPRVKLLaRPQGRQGVSAVRNFGLS 78
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAakDPRIRVI-RLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  79 QARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeridengtKIGRRNLIRRREKPDGFILQSLLGGNFIVNGG 158
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR--------LIREGESDLRRLGSRLFNLVRLLTNLPDSTSG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2187933679 159 IMLVRTRIFQDFgGFDEtlRYAEDWyGWCRLAAAG-RFVYLPgchvLDYRVHRTSVMMNRLLTF 221
Cdd:COG0463   152 FRLFRREVLEEL-GFDE--GFLEDT-ELLRALRHGfRIAEVP----VRYRAGESKLNLRDLLRL 207
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-221 2.84e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.84  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   1 MVSVSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFS--DPRVKLLaRPQGRQGVSAVRNFGLS 78
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAakDPRIRVI-RLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  79 QARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeridengtKIGRRNLIRRREKPDGFILQSLLGGNFIVNGG 158
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR--------LIREGESDLRRLGSRLFNLVRLLTNLPDSTSG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2187933679 159 IMLVRTRIFQDFgGFDEtlRYAEDWyGWCRLAAAG-RFVYLPgchvLDYRVHRTSVMMNRLLTF 221
Cdd:COG0463   152 FRLFRREVLEEL-GFDE--GFLEDT-ELLRALRHGfRIAEVP----VRYRAGESKLNLRDLLRL 207
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 5-209 3.00e-40

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: 139.22  E-value: 3.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFSDPRVKLLARPQGrqGVSAVRNFGLSQARGEW 84
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDK--GIYDAMNKGIALATGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  85 TMFLDADDRLKPGAITALCAGISG-PDVVAVYGDYERIDENGTKIGRRnlirrreKPDGFILQSLLGGNFIVNGGiMLVR 163
Cdd:cd06433    79 IGFLNSDDTLLPGALLAVVAAFAEhPEVDVVYGDVLLVDENGRVIGRR-------RPPPFLDKFLLYGMPICHQA-TFFR 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2187933679 164 TRIFQDFGGFDETLRYAEDWYGWCRLAAAGR-FVYLPGCHVlDYRVH 209
Cdd:cd06433   151 RSLFEKYGGFDESYRIAADYDLLLRLLLAGKiFKYLPEVLA-AFRLG 196
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-169 1.15e-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: 118.27  E-value: 1.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFS--DPRVKLLARPQgRQGVSAVRNFGLSQARG 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAkkDPRVRVIRLPE-NRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  83 EWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYERIDENGTKIGRRNLIRRREKPDGFILQSLLGGNFIVNGGIMLV 162
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159


                  ....*..
gi 2187933679 163 RTRIFQD 169
Cdd:pfam00535 160 RREALEE 166
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 4-218 9.36e-22

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 91.03  E-value: 9.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESvLLQGETIREVLVVDDGSTDATAQKVEGFSDprvKLLARPQGRqgvsAVR-NFGLSQARG 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRGDAEVIVVDGGSTDGTVEIARSLGA---KVIHSPKGR----ARQmNAGAALAKG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  83 EWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeRIDENG--TKIGRRnLIRRRekpdgfilqSLLGGnfIVNG--G 158
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEAIRRALAKPGYVAGAFDL-RFDGPGllLRLIEW-GVNLR---------SRLTG--IPYGdqG 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2187933679 159 ImLVRTRIFQDFGGFdETLRYAEDWYGWCRLAAAGRFVYLPGCHVLDYR------VHRTSVMMNRL 218
Cdd:TIGR04283 140 L-FVRRSLFEQIGGF-PDIPLMEDIELSRRLRRLGRLAILPAPVVTSARrwekngILRTILLNWRL 203
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-97 1.49e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 87.02  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFSD--PRVKLLArpQGRQGVSAVRNFGLSQAR 81
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAEnyPHVRLLH--QANAGVSVARNTGLAVAT 85

                          90
                  ....*....|....*.
gi 2187933679  82 GEWTMFLDADDRLKPG 97
Cdd:PRK10073   86 GKYVAFPDADDVVYPT 101
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
5-94 7.47e-09

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 55.96  E-value: 7.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGERYIVEAIESVLLQGET--IR-EVLVVDDGSTDATAQKVEGFS---DPRVKLLARPQGRQGVSAVRNFGLS 78
Cdd:NF038302    4 TVAIPTYNGANRLPEVLERLRSQIGTesLSwEIIVVDNNSTDNTAQVVQEYQknwPSPYPLRYCFEPQQGAAFARQRAIQ 83

                          90
                  ....*....|....*.
gi 2187933679  79 QARGEWTMFLDaDDRL 94
Cdd:NF038302   84 EAKGELIGFLD-DDNL 98
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-221 2.84e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.84  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   1 MVSVSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFS--DPRVKLLaRPQGRQGVSAVRNFGLS 78
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAakDPRIRVI-RLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  79 QARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeridengtKIGRRNLIRRREKPDGFILQSLLGGNFIVNGG 158
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR--------LIREGESDLRRLGSRLFNLVRLLTNLPDSTSG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2187933679 159 IMLVRTRIFQDFgGFDEtlRYAEDWyGWCRLAAAG-RFVYLPgchvLDYRVHRTSVMMNRLLTF 221
Cdd:COG0463   152 FRLFRREVLEEL-GFDE--GFLEDT-ELLRALRHGfRIAEVP----VRYRAGESKLNLRDLLRL 207
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 5-209 3.00e-40

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: 139.22  E-value: 3.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFSDPRVKLLARPQGrqGVSAVRNFGLSQARGEW 84
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDK--GIYDAMNKGIALATGDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  85 TMFLDADDRLKPGAITALCAGISG-PDVVAVYGDYERIDENGTKIGRRnlirrreKPDGFILQSLLGGNFIVNGGiMLVR 163
Cdd:cd06433    79 IGFLNSDDTLLPGALLAVVAAFAEhPEVDVVYGDVLLVDENGRVIGRR-------RPPPFLDKFLLYGMPICHQA-TFFR 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2187933679 164 TRIFQDFGGFDETLRYAEDWYGWCRLAAAGR-FVYLPGCHVlDYRVH 209
Cdd:cd06433   151 RSLFEKYGGFDESYRIAADYDLLLRLLLAGKiFKYLPEVLA-AFRLG 196
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-198 7.29e-33

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 118.76  E-value: 7.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFS--DPRVKLLaRPQGRQGVSAVRNFGLSQARGE 83
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAkkDPRVIRV-INEENQGLAAARNAGLKAARGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  84 WTMFLDADDRLKPGAITALCAG-ISGPDVVAVYGDyeridengtkigrrnlirrrekpdgfilqsllggnfivngGIMLV 162
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAElLADPEADAVGGP----------------------------------------GNLLF 119

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2187933679 163 RTRIFQDFGGFDETLR-YAEDWYGWCRLAAAGRFVYL 198
Cdd:cd00761   120 RRELLEEIGGFDEALLsGEEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-169 1.15e-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: 118.27  E-value: 1.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFS--DPRVKLLARPQgRQGVSAVRNFGLSQARG 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAkkDPRVRVIRLPE-NRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  83 EWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYERIDENGTKIGRRNLIRRREKPDGFILQSLLGGNFIVNGGIMLV 162
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159


                  ....*..
gi 2187933679 163 RTRIFQD 169
Cdd:pfam00535 160 RREALEE 166
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-209 1.18e-32

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: 119.66  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGF--SDPRVKLLARPQGRQGVsaVRNF--GLSQA 80
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYidKDPFIIILIRNGKNLGV--ARNFesLLQAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  81 RGEWTMFLDADDRLKPGAITALCAGISGPDV-VAVYGDYERIDENGTKIGRRNLIRRREKPdGFILQSLLGGNFiVNGGI 159
Cdd:cd04196    79 DGDYVFFCDQDDIWLPDKLERLLKAFLKDDKpLLVYSDLELVDENGNPIGESFFEYQKIKP-GTSFNNLLFQNV-VTGCT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2187933679 160 MLVRTRIFQDFGGFDETLRYAEDWYGWCRLAAAGRFVYLPGCHVLdYRVH 209
Cdd:cd04196   157 MAFNRELLELALPFPDADVIMHDWWLALLASAFGKVVFLDEPLIL-YRQH 205
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-212 9.96e-31

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 114.32  E-value: 9.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   1 MVSVSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFSDPRVKLLARPqGRQGVSAVRNFGLSQA 80
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNP-ENLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  81 RGEWTMFLDADDRLKPGAITALcagisgpdvvavygdyeridengtkigrrnlirrrekpdgfilqsllggnfiVNGGIM 160
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERL----------------------------------------------------LAAACL 108

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2187933679 161 LVRTRIFQDFGGFDETLR-YAEDW-YGWcRLAAAG-RFVYLPGCHVldYRVHRTS 212
Cdd:COG1216   109 LIRREVFEEVGGFDERFFlYGEDVdLCL-RLRKAGyRIVYVPDAVV--YHLGGAS 160
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-217 2.18e-30

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: 116.38  E-value: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   3 SVSIVIPVRNGERYIVEAIESVLLQ--GETIREVLVVDDGSTDATAQKVEGF--SDPRVKLLARPQgRQGVSAVRNFGLS 78
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQdyPKEKLEVIVVDDGSTDETAEIARELaaEYPRVRVIERPE-NGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  79 QARGEWTMFLDADDRLKPGAITALCAGISGPDVVAvygdyeridengtkigrrnlirrrekpdgfilqsllggnfivNGG 158
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGA------------------------------------------SGA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679 159 IMLVRTRIFQDFGGFDETLrYAEDWYGWCRLAAAG-RFVYLPGCHVLDYRVHRTSVMMNR 217
Cdd:COG1215   147 NLAFRREALEEVGGFDEDT-LGEDLDLSLRLLRAGyRIVYVPDAVVYEEAPETLRALFRQ 205
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-170 8.37e-27

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: 105.36  E-value: 8.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   3 SVSIVIPVRNGERYIVEAIESVLLQ---GETIrEVLVVDDGSTDATAQKVEGFSDPRVKLLARPQgRQGVSAVRNFGLSQ 79
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALdypRDRL-EIIVVSDGSTDGTAEIAREYADKGVKLLRFPE-RRGKAAALNRALAL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  80 ARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYERIDENGTKIGRR------NLIRRREkpdgfilqSLLGGNF 153
Cdd:cd06439   108 ATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGSGSGEGlywkyeNWLKRAE--------SRLGSTV 179

                         170
                  ....*....|....*..
gi 2187933679 154 IVNGGIMLVRTRIFQDF 170
Cdd:cd06439   180 GANGAIYAIRRELFRPL 196
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 6-182 1.23e-26

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: 103.08  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGF--SDPRVKLLARPQGRQGVSAVRNFGLSQARGE 83
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELaaLYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  84 WTMFLDADDRLKPGAITAL-CAGISGPDVVAVYGDYERIDENGTKIGRR-NLIRRREKPDGFILQSLLGGNFIVNGGIML 161
Cdd:cd06423    81 IVVVLDADTILEPDALKRLvVPFFADPKVGAVQGRVRVRNGSENLLTRLqAIEYLSIFRLGRRAQSALGGVLVLSGAFGA 160

                         170       180
                  ....*....|....*....|..
gi 2187933679 162 VRTRIFQDFGGFDE-TLryAED 182
Cdd:cd06423   161 FRREALREVGGWDEdTL--TED 180
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 3-208 2.09e-24

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: 98.84  E-value: 2.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   3 SVSIVIPVRNGERYIVEAIESVLLQ--GETIREVLVVDDGSTDATAQKVEGF--SDPRVKLLARPQGRQgvSAVRNFGLS 78
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQsyPKDLIEIIVVDGGSTDGTREIVQEYaaKDPRIRLIDNPKRIQ--SAGLNIGIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  79 QARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYERIDENGTKIGrrnlirrrekpDGFILQSLLG-GNFIVNG 157
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKA-----------IAVAQSSPLGsGGSAYRG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2187933679 158 GIM-----------LVRTRIFQDFGGFDETLRYAEDWYGWCRLAAAGRFVYLPGCHVLDYRV 208
Cdd:cd02525   148 GAVkigyvdtvhhgAYRREVFEKVGGFDESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYP 209
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 4-183 2.76e-24

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: 97.27  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNG-ERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVE---GFSDPRVKLLARPqGRQGVSAVRNFGLSQ 79
Cdd:cd04184     3 ISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLkkyAAQDPRIKVVFRE-ENGGISAATNSALEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  80 ARGEWTMFLDADDRLKPGAITALCAGISG-PDVVAVYGDYERIDENGTkigrrnlirRRE---KPDgFILQSLLGGNFIV 155
Cdd:cd04184    82 ATGEFVALLDHDDELAPHALYEVVKALNEhPDADLIYSDEDKIDEGGK---------RSEpffKPD-WSPDLLLSQNYIG 151

                         170       180
                  ....*....|....*....|....*...
gi 2187933679 156 NGGImlVRTRIFQDFGGFDETLRYAEDW 183
Cdd:cd04184   152 HLLV--YRRSLVRQVGGFREGFEGAQDY 177
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 4-200 9.65e-23

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: 93.79  E-value: 9.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFsdpRVKLLARPQGRqgvSAVRNFGLSQARGE 83
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSA---GVVVISSPKGR---ARQMNAGAAAARGD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  84 WTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeRIDEngtkigrrnlirrrekpDGFILQSLLGGNFI-VNG-GI-- 159
Cdd:cd02522    75 WLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRL-RFDD-----------------PGPRLRLLELGANLrSRLfGLpy 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2187933679 160 ----MLVRTRIFQDFGGFDETLrYAEDWYGWCRLAAAGRFVYLPG 200
Cdd:cd02522   137 gdqgLFIRRELFEELGGFPELP-LMEDVELVRRLRRRGRPALLPS 180
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-209 2.99e-22

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: 93.88  E-value: 2.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGER--YIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFSDPR--VKLLARPQGRQGVSAVRNFGLSQA 80
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNlqVYYPNAPDTTYSLAASRNRGTSHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  81 RGEWTMFLDADD---------RLKPGAITALCAGISGPDVVAVYgDYERIDENGTKIGRRNLIRRREKPDGFILQSLLGG 151
Cdd:pfam10111  81 IGEYISFIDGDClwspdkfekQLKIATSLALQENIQAAVVLPVT-DLNDESSNFLRRGGDLTASGDVLRDLLVFYSPLAI 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679 152 NFIVNGGIMLVRTRIFQDFGGFDETLRY--AEDWYGWCRLAAAGRFVYLPGCHVLdYRVH 209
Cdd:pfam10111 160 FFAPNSSNALINRQAFIEVGGFDESFRGhgAEDFDIFLRLAARYPFVAVMPPQLL-YRLS 218
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 4-218 9.36e-22

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 91.03  E-value: 9.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESvLLQGETIREVLVVDDGSTDATAQKVEGFSDprvKLLARPQGRqgvsAVR-NFGLSQARG 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRGDAEVIVVDGGSTDGTVEIARSLGA---KVIHSPKGR----ARQmNAGAALAKG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  83 EWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeRIDENG--TKIGRRnLIRRRekpdgfilqSLLGGnfIVNG--G 158
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEAIRRALAKPGYVAGAFDL-RFDGPGllLRLIEW-GVNLR---------SRLTG--IPYGdqG 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2187933679 159 ImLVRTRIFQDFGGFdETLRYAEDWYGWCRLAAAGRFVYLPGCHVLDYR------VHRTSVMMNRL 218
Cdd:TIGR04283 140 L-FVRRSLFEQIGGF-PDIPLMEDIELSRRLRRLGRLAILPAPVVTSARrwekngILRTILLNWRL 203
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-204 4.49e-21

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: 87.61  E-value: 4.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFSdPRVKLLaRPQGRQGVSAVRNFGLSQARGEWT 85
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELF-PEVRLI-RNGENLGFGAGNNQGIREAKGDYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  86 MFLDADDRLKPGAITALcagisgpdvvavygdYERIDENGtKIGrrnlirrrekpdgfILQSLLGGNFivnggiMLVRTR 165
Cdd:cd04186    79 LLLNPDTVVEPGALLEL---------------LDAAEQDP-DVG--------------IVGPKVSGAF------LLVRRE 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2187933679 166 IFQDFGGFDETLR-YAEDwYGWC-RLAAAG-RFVYLPGCHVL 204
Cdd:cd04186   123 VFEEVGGFDEDFFlYYED-VDLClRARLAGyRVLYVPQAVIY 163
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-97 1.49e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 87.02  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGFSD--PRVKLLArpQGRQGVSAVRNFGLSQAR 81
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAEnyPHVRLLH--QANAGVSVARNTGLAVAT 85

                          90
                  ....*....|....*.
gi 2187933679  82 GEWTMFLDADDRLKPG 97
Cdd:PRK10073   86 GKYVAFPDADDVVYPT 101
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-143 4.40e-19

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: 83.88  E-value: 4.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESVLLQgetIREVLVVDDGSTDATAQKVEGFSdprVKLLARPQGrqGVSAVRNFGLSQARGE 83
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKWA---VDEIIVVDSGSTDRTVEIAKEYG---AKVYQRWWD--GFGAQRNFALELATND 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  84 WTMFLDADDRLKPGAITALCAGISGPdvvavygdyeriDENGTKIGRRNLIRRREKPDGF 143
Cdd:cd02511    74 WVLSLDADERLTPELADEILALLATD------------DYDGYYVPRRNFFLGRWIRHGG 121
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-207 9.39e-17

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: 77.41  E-value: 9.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATA----QKVEGFSDPRVKLL--ARPQGRQGVSAVRNFGL 77
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLdvaeEIAARFPDVRLRVIrnARLLGPTGKSRGLNHGF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  78 SQARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYERidENGTKIGRRNLIRRREKPDGFILQSLLGGNF-IVN 156
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFS--LNRSTMLSALGALEFALRHLRMMSLRLALGVlPLS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2187933679 157 GGIMLVRTRIFQDFGGFDETLRYAEDWYGWCRLAAAG-RFVYLPGCHVLDYR 207
Cdd:pfam13641 162 GAGSAIRREVLKELGLFDPFFLLGDDKSLGRRLRRHGwRVAYAPDAAVRTVF 213
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 6-189 1.15e-16

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: 76.46  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVL--LQGETIREVLVVDDGSTDATAQKVE--GFSDPRVKLLARPQGR-QGvSAVRNfGLSQA 80
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLavLEEGYDYEIIVVDDGSTDGTAEIARelAARVPRVRVIRLSRNFgKG-AAVRA-GFKAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  81 RGEWTMFLDADDRLKPGAITALCAGI--SGPDVvaVYGD-YERIDENGTKIGRRNLIRrrekpdGF--ILQSLLGGNFI- 154
Cdd:cd04179    79 RGDIVVTMDADLQHPPEDIPKLLEKLleGGADV--VIGSrFVRGGGAGMPLLRRLGSR------LFnfLIRLLLGVRISd 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2187933679 155 VNGGIMLVRTRIFQDFGGFDETLRYAEDWYGWCRL 189
Cdd:cd04179   151 TQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 6-91 2.10e-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: 72.90  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYI---VEAIESVLLQGETIREVLVVDDGSTDATAQKVEGF--SDPRVKL--LARPQGRQgvSAVRNfGLS 78
Cdd:cd04187     1 IVVPVYNEEENLpelYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELaaRDPRVKVirLSRNFGQQ--AALLA-GLD 77

                          90
                  ....*....|...
gi 2187933679  79 QARGEWTMFLDAD 91
Cdd:cd04187    78 HARGDAVITMDAD 90
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 5-207 1.60e-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: 65.03  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGER--YIVEAIESVLLQGETIREVLVVDDGS-TDATAQKVEGFS-DPRVKLLARPQGRqGVSAVRNFGLSQA 80
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKrKLPLKVVPLEKNR-GLGKALNEGLKHC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  81 RGEWTMFLDADDRLKPGAI-TALCAGISGPDVVAVYGDYERIDENGTKIGRRNL------IR---RREKPdgfilqsllg 150
Cdd:cd04195    80 TYDWVARMDTDDISLPDRFeKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRRLptshddILkfaRRRSP---------- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2187933679 151 gnfiVNGGIMLVRTRIFQDFGGFdETLRYAEDWYGWCRLAAAG-RFVYLPGChVLDYR 207
Cdd:cd04195   150 ----FNHPTVMFRKSKVLAVGGY-QDLPLVEDYALWARMLANGaRFANLPEI-LVKAR 201
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 6-96 2.19e-12

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: 65.17  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQG-ETIREVLVVDDGSTDATAQKVEGF----SDPRVKLLAR----PQGRqGVSAVRNFG 76
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDfEGTLELSVFNDASTDKSAEIIEKWrkklEDSGVIVLVGshnsPSPK-GVGYAKNQA 79

                          90       100
                  ....*....|....*....|
gi 2187933679  77 LSQARGEWTMFLDADDRLKP 96
Cdd:cd06913    80 IAQSSGRYLCFLDSDDVMMP 99
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 6-111 3.18e-11

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 61.25  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQGETIReVLVVDDGSTDATAQKVEGF-SDPRVKLLAR--PQGRQGVSAVRNFGLSQ--- 79
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNKPNFL-VLVIDDASDDDTAGIVRLAiTDSRVHLLRRhlPNARTGKGDALNAAYDQirq 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2187933679  80 --------ARGEWTMFLDADDRLKPGAITALCAGISGPDV 111
Cdd:cd06436    80 ilieegadPERVIIAVIDADGRLDPNALEAVAPYFSDPRV 119
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-180 3.60e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 61.92  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQGETIR--EVLVVDDGSTDATAQKVE---GFSDPRVKLLARPQGR-QGVSAVRNFGLSQ 79
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKEkfEVILVDDHSTDGTVQILEfaaAKPNFQLKILNNSRVSiSGKKNALTTAIKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  80 ARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYERIDENGtkigrrnLIRRREKPDGFILQSL------LGGNF 153
Cdd:cd04192    81 AKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKS-------LLAKFQRLDWLSLLGLiagsfgLGKPF 153

                         170       180
                  ....*....|....*....|....*..
gi 2187933679 154 IVNGGIMLVRTRIFQDFGGFDETLRYA 180
Cdd:cd04192   154 MCNGANMAYRKEAFFEVGGFEGNDHIA 180
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 6-116 2.60e-10

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: 59.12  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVL--LQGETIR--EVLVVDDGSTDATAQKVEGFSDPR---VKLLARPQGRQGVSAVRNfGLS 78
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVeyLEERPSFsyEIIVVDDGSKDGTAEVARKLARKNpalIRVLTLPKNRGKGGAVRA-GML 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2187933679  79 QARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYG 116
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIG 117
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 76-221 4.56e-10

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 57.68  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  76 GLSQARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeridengTKIGRRNLIRRREK----PDGFILQSLLGG 151
Cdd:pfam13506  25 GLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTSPP-------VGSDPKGLAAALEAaffnTLAGVLQAALSG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2187933679 152 NFIVNGGIMLVRTRIFQDFGGFDETLRY-AEDWYGWCRLAAAGRFVYL---PGCHVLDYRVHRTSVMMNRLLTF 221
Cdd:pfam13506  98 IGFAVGMSMAFRRADLERIGGFEALADYlAEDYALGKLLRAAGLKVVLsprPILQTSGPRRTSFRAFMARQLRW 171
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-104 7.25e-10

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 58.47  E-value: 7.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGST--DATAQKVEGFSDPRVKLLaRPQGRQGVSAVRNFGLSQAR 81
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTswEQLQQYVTALNDPRITYI-HNDINSGACAVRNQAIMLAQ 85

                          90       100
                  ....*....|....*....|...
gi 2187933679  82 GEWTMFLDADDRLKPGAITALCA 104
Cdd:PRK10018   86 GEYITGIDDDDEWTPNRLSVFLA 108
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 6-91 2.60e-09

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: 56.39  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNgER----YIVEAIESVLLQGETirEVLVVDDGSTDATAQKVEGFS--DPRVKLLARPQGRQGVSAVRNfGLSQ 79
Cdd:cd06442     1 IIIPTYN-ERenipELIERLDAALKGIDY--EIIVVDDNSPDGTAEIVRELAkeYPRVRLIVRPGKRGLGSAYIE-GFKA 76

                          90
                  ....*....|..
gi 2187933679  80 ARGEWTMFLDAD 91
Cdd:cd06442    77 ARGDVIVVMDAD 88
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
5-94 7.47e-09

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 55.96  E-value: 7.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGERYIVEAIESVLLQGET--IR-EVLVVDDGSTDATAQKVEGFS---DPRVKLLARPQGRQGVSAVRNFGLS 78
Cdd:NF038302    4 TVAIPTYNGANRLPEVLERLRSQIGTesLSwEIIVVDNNSTDNTAQVVQEYQknwPSPYPLRYCFEPQQGAAFARQRAIQ 83

                          90
                  ....*....|....*.
gi 2187933679  79 QARGEWTMFLDaDDRL 94
Cdd:NF038302   84 EAKGELIGFLD-DDNL 98
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 3-185 1.19e-08

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: 54.57  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   3 SVSIVIPV-RNGERYIVEAIESVLLQGEtiREVLVVDDGSTDATAQKVEG-FSDPRVKLLARPQ-GRQGVSAVrnfGLSQ 79
Cdd:cd06434     1 DVTVIIPVyDEDPDVFRECLRSILRQKP--LEIIVVTDGDDEPYLSILSQtVKYGGIFVITVPHpGKRRALAE---GIRH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  80 ARGEWTMFLDADDRLKPGAITALCAGISGPDVVAVYGDyERIDENGTKI----GRRNLIRRREkpDGFILQSLLGGNFIV 155
Cdd:cd06434    76 VTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTN-QRILRPRDSKwsflAAEYLERRNE--EIRAAMSYDGGVPCL 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 2187933679 156 NGGIMLVRTRIFQDfggFDETLRYAEDWYG 185
Cdd:cd06434   153 SGRTAAYRTEILKD---FLFLEEFTNETFM 179
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-113 1.20e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 51.62  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   1 MVSVSIVIPVRNgERYIVEAIesVLLQGETIR-----EVLVVDDGSTDATAQKVEG----FSDPRVKLLARPqGRQGVSA 71
Cdd:PLN02726    8 AMKYSIIVPTYN-ERLNIALI--VYLIFKALQdvkdfEIIVVDDGSPDGTQDVVKQlqkvYGEDRILLRPRP-GKLGLGT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2187933679  72 VRNFGLSQARGEWTMFLDADDRLKPGAITALCAGI--SGPDVVA 113
Cdd:PLN02726   84 AYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQreTGADIVT 127
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 3-120 1.47e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 48.76  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   3 SVSIVIPVRNGERYIVEAIESV--LLQGETIREVLVVDDGSTDATAQKVEGFSdPRVklLARPQGRQGVSAVRNFG---- 76
Cdd:PRK13915   32 TVSVVLPALNEEETVGKVVDSIrpLLMEPLVDELIVIDSGSTDATAERAAAAG-ARV--VSREEILPELPPRPGKGealw 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2187933679  77 --LSQARGEWTMFLDAD-----DRLKPGAITALcagISGPDVVAVYGDYER 120
Cdd:PRK13915  109 rsLAATTGDIVVFVDADlinfdPMFVPGLLGPL---LTDPGVHLVKAFYRR 156
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 2-91 3.92e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 47.84  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   2 VSVSIVIPVRNGERYIVEAIESVL--------LQGETIREVLVVDDGSTDATAQKVEGFS--------DPRVKLLARPQG 65
Cdd:PTZ00260   70 VDLSIVIPAYNEEDRLPKMLKETIkylesrsrKDPKFKYEIIIVNDGSKDKTLKVAKDFWrqninpniDIRLLSLLRNKG 149

                          90       100
                  ....*....|....*....|....*.
gi 2187933679  66 RQGvsAVRnFGLSQARGEWTMFLDAD 91
Cdd:PTZ00260  150 KGG--AVR-IGMLASRGKYILMVDAD 172
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 84-200 5.14e-06

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 46.17  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  84 WTMFLDADDRLKPGAITALCAGISGPDVVAVYGDYeRIDENGTKIGRRNLIRRREKPDGFILQ-SLLGGNFIVNGGIMLV 162
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPEVAIIQGPI-LPMNVGNYLEELAALFFADDHGKSIPVrMALGRVLPFVGSGAFL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2187933679 163 RTRIFQDFGGFDETLrYAEDWYGWCRLAAAG-RFVYLPG 200
Cdd:pfam13632  80 RRSALQEVGGWDDGS-VSEDFDFGLRLQRAGyRVRFAPY 117
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 5-90 5.94e-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: 46.81  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   5 SIVIPVRNGER-YIVEAIESVLLQG--ETIREVLVVDDGSTDATAqKVEGFSD-----PRVKLLaRPQGRQGVSAVRNFG 76
Cdd:cd02510     1 SVIIIFHNEALsTLLRTVHSVINRTppELLKEIILVDDFSDKPEL-KLLLEEYykkylPKVKVL-RLKKREGLIRARIAG 78

                          90
                  ....*....|....
gi 2187933679  77 LSQARGEWTMFLDA 90
Cdd:cd02510    79 ARAATGDVLVFLDS 92
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 4-112 4.64e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 44.34  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   4 VSIVIPVRNGERYIVEAIESVLLQGETIR---EVLVVDDGSTDATAQK-VEGFSDPRVK----LLARPQGRQgvSAVRNf 75
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAACESLGkeyEILLIDDGSSDNSAEMlVEAAQAPDSHivaiLLNRNYGQH--SAIMA- 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2187933679  76 GLSQARGEWTMFLDADDRLKPGAITALCAGIS-GPDVV 112
Cdd:PRK10714   85 GFSHVTGDLIITLDADLQNPPEEIPRLVAKADeGYDVV 122
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 6-171 1.54e-04

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 41.82  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQ--GETIREVLVVDDGSTDATAQKVEGFSdprVKLLAR--PQGRqGVSAVRNFGLSQAR 81
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQdyPRELYRIFVVADNCTDDTAQVARAAG---ATVLERhdPERR-GKGYALDFGFRHLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679  82 GEWTMF-----LDADDRLKPGAITALCAGI-SGPDVVAVYGDYERIDEN------GTKIGRRNLIRRREKpdgfilqSLL 149
Cdd:cd06438    77 NLADDPdavvvFDADNLVDPNALEELNARFaAGARVVQAYYNSKNPDDSwitrlyAFAFLVFNRLRPLGR-------SNL 149

                         170       180
                  ....*....|....*....|..
gi 2187933679 150 GGNFIVNGGIMLVRTRIFQDFG 171
Cdd:cd06438   150 GLSCQLGGTGMCFPWAVLRQAP 171
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 6-91 1.96e-04

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: 41.41  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933679   6 IVIPVRNGERYIVEAIESVLLQGETIREVLVVDDGSTDATAQKVEGF-SDPRVKLLARPQGRQG--VSAVRNFGLSQARG 82
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFkSQFPIPIKHVWQEDEGfrKAKIRNKAIAAAKG 80


                  ....*....
gi 2187933679  83 EWTMFLDAD 91
Cdd:cd06420    81 DYLIFIDGD 89
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 31-91 2.41e-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: 36.84  E-value: 2.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2187933679  31 IREVLVVDDGSTDATAQKVEGfsDPRVKL----LARPQGRQGVsAVRNFGLSQ-ARGEWTMFLDAD 91
Cdd:pfam13704  19 FDHIYVYDNGSDDGTAEILAR--LPDVSIlrsdLSYKDARFQV-DWRNALLARyAEADWVLVVDAD 81
 
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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