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Conserved domains on  [gi|1259166217|gb|PEO74187.1|]
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glycosyl transferase family 2 [Bacillus wiedmannii]

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]; ...
7-187 2.89e-25

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.16  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   7 PPLVSILIPTYNRPHYFKIALESALAQTYSNIEIIVGDD-STNNeTEKLIyRHYLHKHKHITYIRNASTLGQFNNALMLL 85
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDgSTDG-TAEIL-RELAAKDPRIRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  86 EQSNGEYINFLMDDDTFYNNKIEKMMFYFQQDlnkNLALITSYRTWidDNGDIIEQHPSMKKLYDEDTLLNGKDFGNRMl 165
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEG---PADLVYGSRLI--REGESDLRRLGSRLFNLVRLLTNLPDSTSGF- 152
                         170       180
                  ....*....|....*....|..
gi 1259166217 166 magqniigeptiVLFRKSLLTE 187
Cdd:COG0463   153 ------------RLFRREVLEE 162
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
7-187 2.89e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.16  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   7 PPLVSILIPTYNRPHYFKIALESALAQTYSNIEIIVGDD-STNNeTEKLIyRHYLHKHKHITYIRNASTLGQFNNALMLL 85
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDgSTDG-TAEIL-RELAAKDPRIRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  86 EQSNGEYINFLMDDDTFYNNKIEKMMFYFQQDlnkNLALITSYRTWidDNGDIIEQHPSMKKLYDEDTLLNGKDFGNRMl 165
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEG---PADLVYGSRLI--REGESDLRRLGSRLFNLVRLLTNLPDSTSGF- 152
                         170       180
                  ....*....|....*....|..
gi 1259166217 166 magqniigeptiVLFRKSLLTE 187
Cdd:COG0463   153 ------------RLFRREVLEE 162
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
11-185 1.28e-22

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: 92.07  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  11 SILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIyRHYLHKHKHITYIRNASTLGQFNNALMLLEQSNG 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIA-EEYAKKDPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  91 EYINFLMDDDTFYNNKIEKMMFYFQQDlNKNLALITSYRtwIDDNGDIIEQHPSMKKLYDEDTLLNGKDFGNRMLMAGqn 170
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEED-GADVVVGSRYV--IFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG-- 154
                         170
                  ....*....|....*
gi 1259166217 171 iigepTIVLFRKSLL 185
Cdd:pfam00535 155 -----GFALYRREAL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
12-150 1.55e-19

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: 83.71  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIYRhYLHKHKHITYIRNASTLGQFNNALMLLEQSNGE 91
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEE-YAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1259166217  92 YINFLMDDDTFYNNKIEKMMFYFQQdlNKNLALITSY------RTWIDDNGDIIEQHPSMKKLYD 150
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLA--DPEADAVGGPgnllfrRELLEEIGGFDEALLSGEEDDD 142
PRK10073 PRK10073
putative glycosyl transferase; Provisional
8-137 2.35e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.53  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   8 PLVSILIPTYNRPHYFKIALESALAQTYSNIE-IIVGDDSTNNETEklIYRHYLHKHKHITYI----------RNAStlg 76
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEiIIVNDGSTDNSVE--IAKHYAENYPHVRLLhqanagvsvaRNTG--- 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1259166217  77 qfnnalmlLEQSNGEYINFLMDDDTFYNNKIEKMMFYFQQDlnkNLALITSYRTWIDDNGD 137
Cdd:PRK10073   81 --------LAVATGKYVAFPDADDVVYPTMYETLMTMALED---DLDVAQCNADWCFRDTG 130
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
10-100 3.92e-07

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


Pssm-ID: 275233  Cd Length: 215  Bit Score: 49.99  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  10 VSILIPTYNRPHYFKIALeSALAQTYSNIEIIVGDDSTN--NETEKLIYRHYlhKHKHITYIRNASTLGQFNNALML-LE 86
Cdd:TIGR04440   2 LTIIIPTYNRPEYLKRWL-RYYSDFGCDYRIIIADSSDEkfNENNLKVFKNY--SNPNITYLHYPDLGVPFYEKLLDaLE 78
                          90
                  ....*....|....
gi 1259166217  87 QSNGEYINFLMDDD 100
Cdd:TIGR04440  79 QVETPYVVICADDD 92
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
7-187 2.89e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.16  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   7 PPLVSILIPTYNRPHYFKIALESALAQTYSNIEIIVGDD-STNNeTEKLIyRHYLHKHKHITYIRNASTLGQFNNALMLL 85
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDgSTDG-TAEIL-RELAAKDPRIRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  86 EQSNGEYINFLMDDDTFYNNKIEKMMFYFQQDlnkNLALITSYRTWidDNGDIIEQHPSMKKLYDEDTLLNGKDFGNRMl 165
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEG---PADLVYGSRLI--REGESDLRRLGSRLFNLVRLLTNLPDSTSGF- 152
                         170       180
                  ....*....|....*....|..
gi 1259166217 166 magqniigeptiVLFRKSLLTE 187
Cdd:COG0463   153 ------------RLFRREVLEE 162
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
11-185 1.28e-22

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: 92.07  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  11 SILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIyRHYLHKHKHITYIRNASTLGQFNNALMLLEQSNG 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIA-EEYAKKDPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  91 EYINFLMDDDTFYNNKIEKMMFYFQQDlNKNLALITSYRtwIDDNGDIIEQHPSMKKLYDEDTLLNGKDFGNRMLMAGqn 170
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEED-GADVVVGSRYV--IFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG-- 154
                         170
                  ....*....|....*
gi 1259166217 171 iigepTIVLFRKSLL 185
Cdd:pfam00535 155 -----GFALYRREAL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
12-150 1.55e-19

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: 83.71  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIYRhYLHKHKHITYIRNASTLGQFNNALMLLEQSNGE 91
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEE-YAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1259166217  92 YINFLMDDDTFYNNKIEKMMFYFQQdlNKNLALITSY------RTWIDDNGDIIEQHPSMKKLYD 150
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLA--DPEADAVGGPgnllfrRELLEEIGGFDEALLSGEEDDD 142
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
11-228 2.34e-19

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: 84.13  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  11 SILIPTYNRPHYFKIALESALAQTYSNIEIIVGD-DSTNNeTEKLIyRHYLHKhkhITYIRNASTLGQ---FNNALMLle 86
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDgGSTDG-TVDII-KKYEDK---ITYWISEPDKGIydaMNKGIAL-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  87 qSNGEYINFLMDDDTFYNNKIEKMMFYFQqdLNKNLALITSYRTWIDDNGDIIEQHPSMKKlydedtllngkdfgNRMLM 166
Cdd:cd06433    74 -ATGDIIGFLNSDDTLLPGALLAVVAAFA--EHPEVDVVYGDVLLVDENGRVIGRRRPPPF--------------LDKFL 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1259166217 167 AGQNIIGEPTIvLFRKSLLtEPFGTLNgRKYGCSVDMASWISLLSKGDAM-YITEPLSSFRLH 228
Cdd:cd06433   137 LYGMPICHQAT-FFRRSLF-EKYGGFD-ESYRIAADYDLLLRLLLAGKIFkYLPEVLAAFRLG 196
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-233 1.88e-18

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: 81.91  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  11 SILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIyRHYLHKHKHITYI-RNASTLGQFNNALMLLEQSN 89
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEII-KEYIDKDPFIIILiRNGKNLGVARNFESLLQAAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  90 GEYInFLMD-DDTFYNNKIEKMMFYFQQDLNKnlALITSYRTWIDDNGDIIeqHPSMKKLYDedtLLNGKDFGNRMLmag 168
Cdd:cd04196    80 GDYV-FFCDqDDIWLPDKLERLLKAFLKDDKP--LLVYSDLELVDENGNPI--GESFFEYQK---IKPGTSFNNLLF--- 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217 169 QNIIGEPTIVlFRKSLLT--EPFGTlngrkYGCSV-DMasWISLL--SKGDAMYITEPLSSFRLHTGQQV 233
Cdd:cd04196   149 QNVVTGCTMA-FNRELLElaLPFPD-----ADVIMhDW--WLALLasAFGKVVFLDEPLILYRQHGNNVV 210
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-180 2.04e-18

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 81.58  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   8 PLVSILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIYRhylHKHKHITYIRNASTLG---QFNNAlml 84
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAA---LAFPRVRVIRNPENLGfaaARNLG--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  85 LEQSNGEYInFLMDDDTFYN-NKIEKMmfyfqqdLNKNLALITsyRTWIDDNGDIIEQHPsmkkLYDEDTllngkDFGNR 163
Cdd:COG1216    77 LRAAGGDYL-LFLDDDTVVEpDWLERL-------LAAACLLIR--REVFEEVGGFDERFF----LYGEDV-----DLCLR 137
                         170
                  ....*....|....*..
gi 1259166217 164 MLMAGQNIIGEPTIVLF 180
Cdd:COG1216   138 LRKAGYRIVYVPDAVVY 154
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
5-178 6.80e-18

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: 82.10  E-value: 6.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   5 KNPPLVSILIPTYNRPHYFKIALESALAQTY--SNIEIIVGDDSTNNETEKLIyRHYLHKHKHITYIRNASTLGQfNNAL 82
Cdd:COG1215    26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIA-RELAAEYPRVRVIERPENGGK-AAAL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  83 -MLLEQSNGEYInFLMDDDTFYN-NKIEKMMFYFQQDlnkNLALITSY----RTWIDDNGdiieqhpsmkkLYDEDTLLN 156
Cdd:COG1215   104 nAGLKAARGDIV-VFLDADTVLDpDWLRRLVAAFADP---GVGASGANlafrREALEEVG-----------GFDEDTLGE 168
                         170       180
                  ....*....|....*....|..
gi 1259166217 157 GKDFGNRMLMAGQNIIGEPTIV 178
Cdd:COG1215   169 DLDLSLRLLRAGYRIVYVPDAV 190
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
8-187 1.94e-16

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: 76.09  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   8 PLVSILIPTYNRPH-YFKIALESALAQTYSNIEIIVGDDSTNNETEKLIYRHYLHKHKHITYIRNASTLGQFNNALMLLE 86
Cdd:cd04184     1 PLISIVMPVYNTPEkYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  87 QSNGEYINFLMDDDTfynnkIEKMMFYF-QQDLNKN--LALITSYRTWIDDNGDIIEqhPSMKKLYDEDTLLngkdfgnr 163
Cdd:cd04184    81 LATGEFVALLDHDDE-----LAPHALYEvVKALNEHpdADLIYSDEDKIDEGGKRSE--PFFKPDWSPDLLL-------- 145
                         170       180
                  ....*....|....*....|....
gi 1259166217 164 mlmaGQNIIGEptIVLFRKSLLTE 187
Cdd:cd04184   146 ----SQNYIGH--LLVYRRSLVRQ 163
PRK10073 PRK10073
putative glycosyl transferase; Provisional
8-137 2.35e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.53  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   8 PLVSILIPTYNRPHYFKIALESALAQTYSNIE-IIVGDDSTNNETEklIYRHYLHKHKHITYI----------RNAStlg 76
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEiIIVNDGSTDNSVE--IAKHYAENYPHVRLLhqanagvsvaRNTG--- 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1259166217  77 qfnnalmlLEQSNGEYINFLMDDDTFYNNKIEKMMFYFQQDlnkNLALITSYRTWIDDNGD 137
Cdd:PRK10073   81 --------LAVATGKYVAFPDADDVVYPTMYETLMTMALED---DLDVAQCNADWCFRDTG 130
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
8-173 1.47e-10

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 60.78  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   8 PLVSILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIYRHYLHKHKhITYIRNASTLGQF---NNALMl 84
Cdd:PRK10018    5 PLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSWEQLQQYVTALNDPR-ITYIHNDINSGACavrNQAIM- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  85 leQSNGEYINFLMDDDTFYNNKIEKMMFYFQQdlnknlaLITSYRTWIDD---NGDIIEQhPSMKKLYDedtllngKDFG 161
Cdd:PRK10018   83 --LAQGEYITGIDDDDEWTPNRLSVFLAHKQQ-------LVTHAFLYANDyvcQGEVYSQ-PASLPLYP-------KSPY 145
                         170
                  ....*....|..
gi 1259166217 162 NRMLMAGQNIIG 173
Cdd:PRK10018  146 SRRLFYKRNIIG 157
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
12-119 1.50e-10

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 58.72  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIYRHYlhkhKHITYIRNASTLGqF---NNALMllEQS 88
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELF----PEVRLIRNGENLG-FgagNNQGI--REA 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1259166217  89 NGEYINFLMDDDTFYNNKIEKMMFYFQQDLN 119
Cdd:cd04186    74 KGDYVLLLNPDTVVEPGALLELLDAAEQDPD 104
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
13-133 1.51e-09

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: 56.87  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  13 LIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIYRhyLHKHKHITYIRNASTLGQ---FNNALMLLEQSN 89
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTS--LGDLDNIVYLRLPENLGGaggFYEGVRRAYELG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1259166217  90 GEYInFLMDDDTFYN-NKIEKMMFYFQQDlnkNLALITSYRTWID 133
Cdd:cd04185    80 YDWI-WLMDDDAIPDpDALEKLLAYADKD---NPQFLAPLVLDPD 120
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
12-117 2.16e-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: 55.70  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALAQTYSNIEIIVGDD-STNNETEKLIYRHYLHKHKHITYIR--NASTLGQFNNAlmlLEQS 88
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDgSTDDTLEILEELAALYIRRVLVVRDkeNGGKAGALNAG---LRHA 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1259166217  89 NGEYInFLMDDDT-FYNNKIEKMMFYFQQD 117
Cdd:cd06423    78 KGDIV-VVLDADTiLEPDALKRLVVPFFAD 106
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
12-96 9.19e-09

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: 54.12  E-value: 9.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALAQTYSNIEIIVGDDSTNNETEKLIyRHYLHKH----KHI---------TYIRNastlgqf 78
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELI-EEFKSQFpipiKHVwqedegfrkAKIRN------- 72
                          90
                  ....*....|....*...
gi 1259166217  79 nnalMLLEQSNGEYINFL 96
Cdd:cd06420    73 ----KAIAAAKGDYLIFI 86
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
10-100 3.92e-07

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


Pssm-ID: 275233  Cd Length: 215  Bit Score: 49.99  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  10 VSILIPTYNRPHYFKIALeSALAQTYSNIEIIVGDDSTN--NETEKLIYRHYlhKHKHITYIRNASTLGQFNNALML-LE 86
Cdd:TIGR04440   2 LTIIIPTYNRPEYLKRWL-RYYSDFGCDYRIIIADSSDEkfNENNLKVFKNY--SNPNITYLHYPDLGVPFYEKLLDaLE 78
                          90
                  ....*....|....
gi 1259166217  87 QSNGEYINFLMDDD 100
Cdd:TIGR04440  79 QVETPYVVICADDD 92
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
9-110 1.35e-05

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: 45.69  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   9 LVSILIPTYNRPHYFKIALESALAQTYS--NIEIIVGDD-STNNETEklIYRHYLHKHKHITYI----RNASTlgqfnnA 81
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGgSTDGTRE--IVQEYAAKDPRIRLIdnpkRIQSA------G 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1259166217  82 LML-LEQSNGEYINFlMDDDTFY-NNKIEKM 110
Cdd:cd02525    73 LNIgIRNSRGDIIIR-VDAHAVYpKDYILEL 102
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
7-101 2.12e-05

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: 45.05  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   7 PPLVSILIPTYNRPHYFKIALESALAQTYSNIEIIVG----DDSTNNETEKLIYRhylHKHKHITYIRNASTLGQFNNAL 82
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVvnpsDAETLDVAEEIAAR---FPDVRLRVIRNARLLGPTGKSR 77
                          90       100
                  ....*....|....*....|..
gi 1259166217  83 MLLE---QSNGEYInFLMDDDT 101
Cdd:pfam13641  78 GLNHgfrAVKSDLV-VLHDDDS 98
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
12-129 2.25e-05

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: 44.97  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALAQTY--SNIEIIVGDDSTNNETEKLIYRHYLHKHKHITYIRN--ASTLGQFNNALMLLEQ 87
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNsrVSISGKKNALTTAIKA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1259166217  88 SNGEYInFLMDDDTFYN-NKIEKMMFYFQQDLNKNLALITSYR 129
Cdd:cd04192    81 AKGDWI-VTTDADCVVPsNWLLTFVAFIQKEQIGLVAGPVIYF 122
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
5-101 9.99e-05

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: 42.95  E-value: 9.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   5 KNPPLVSILIPTYNRPHYFKIALESALAQTYSN--IEIIVGDD-STNNETEklIYRHYLHK--HKHITYIRnastLGQfN 79
Cdd:cd06439    26 AYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDgSTDGTAE--IAREYADKgvKLLRFPER----RGK-A 98
                          90       100
                  ....*....|....*....|....*...
gi 1259166217  80 NAL-MLLEQSNGEYINF-----LMDDDT 101
Cdd:cd06439    99 AALnRALALATGEIVVFtdanaLLDPDA 126
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
8-93 1.13e-04

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


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 42.68  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   8 PLVSILIPTYNRPHYFKIALESALAQTY--SNIEIIVGDDSTNNETEKLIYR--HYLHKHKHITYIRNASTLGQFNNALM 83
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYpkDRLEIQVLDDSTDETVRLAREIveEYAAQGVNIKHVRRADRTGYKAGALA 80
                          90
                  ....*....|.
gi 1259166217  84 L-LEQSNGEYI 93
Cdd:cd06437    81 EgMKVAKGEYV 91
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
8-234 1.43e-04

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


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 42.56  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217   8 PLVSILIPTYNRPH-YFKIALESALAQTY--SNIEIIVGDDSTNNETEKL-------IYRHYLHKHKHITYirNAstlGQ 77
Cdd:cd06421     1 PTVDVFIPTYNEPLeIVRKTLRAALAIDYphDKLRVYVLDDGRRPELRALaaelgveYGYRYLTRPDNRHA--KA---GN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  78 FNNAlmlLEQSNGEYI-----------NFLmdddtfynnkiEKMMFYFqqDLNKNLALI-TSYRTWIDDNGDIIEQHPSM 145
Cdd:cd06421    76 LNNA---LAHTTGDFVaildadhvptpDFL-----------RRTLGYF--LDDPKVALVqTPQFFYNPDPFDWLADGAPN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217 146 KKLYDEDTLLNGKDFGNRMLMAGQNiigeptiVLFRKSLLTEpfgtLNGRKYGC-SVDMASWISLLSKG-DAMYITEPLS 223
Cdd:cd06421   140 EQELFYGVIQPGRDRWGAAFCCGSG-------AVVRREALDE----IGGFPTDSvTEDLATSLRLHAKGwRSVYVPEPLA 208
                         250
                  ....*....|....*..
gi 1259166217 224 ------SFRLHTGQQVR 234
Cdd:cd06421   209 aglapeTLAAYIKQRLR 225
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
12-108 6.73e-04

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: 40.13  E-value: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALAQTYSN-IEIIVGDDSTNNETEKLIYRHylhkHKHITYIRNASTLGQFNNAL-------- 82
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKW----RKKLEDSGVIVLVGSHNSPSpkgvgyak 76
                          90       100
                  ....*....|....*....|....*..
gi 1259166217  83 -MLLEQSNGEYINFLMDDDTFYNNKIE 108
Cdd:cd06913    77 nQAIAQSSGRYLCFLDSDDVMMPQRIR 103
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
10-114 1.99e-03

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: 38.77  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  10 VSILIPTYNR-PHYFKIALESALAQTYSNIeIIVGDDSTNNETEKLIyRHYLHKHKHITYIRNASTLGQFNNALMLLEqs 88
Cdd:cd06434     2 VTVIIPVYDEdPDVFRECLRSILRQKPLEI-IVVTDGDDEPYLSILS-QTVKYGGIFVITVPHPGKRRALAEGIRHVT-- 77
                          90       100
                  ....*....|....*....|....*..
gi 1259166217  89 nGEYINFLmDDDTF-YNNKIEKMMFYF 114
Cdd:cd06434    78 -TDIVVLL-DSDTVwPPNALPEMLKPF 102
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
12-100 4.75e-03

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: 37.55  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  12 ILIPTYNRPHYFKIALESALA--QTYSNIEIIVGDDSTNNETEKLIyRHYLHKHKHITYIRNASTLGQFnNALML-LEQS 88
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIA-RELAARVPRVRVIRLSRNFGKG-AAVRAgFKAA 78
                          90
                  ....*....|..
gi 1259166217  89 NGEYInFLMDDD 100
Cdd:cd04179    79 RGDIV-VTMDAD 89
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
11-226 9.36e-03

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: 36.52  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  11 SILIPTYNR--PHYFKIALESALAQTYSNIEII-VGDDSTNNETEKLIYRhYLHKH--KHITYIRNaSTLGQfnnALML- 84
Cdd:cd04195     1 SVLMSVYIKekPEFLREALESILKQTLPPDEVVlVKDGPVTQSLNEVLEE-FKRKLplKVVPLEKN-RGLGK---ALNEg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259166217  85 LEQSNGEYInFLMD-DDTFYNNKIEKMMFYFQQDLNknlalitsyrtwIDDNGDIIEQhpsmkklYDEDtllnGKDFGNR 163
Cdd:cd04195    76 LKHCTYDWV-ARMDtDDISLPDRFEKQLDFIEKNPE------------IDIVGGGVLE-------FDSD----GNDIGKR 131
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1259166217 164 MLMAGQNIIGEPTI---------VLFRKSLLTEPFGTLNGRKYGcsvDMASWISLLSKGDAMY-ITEPLSSFR 226
Cdd:cd04195   132 RLPTSHDDILKFARrrspfnhptVMFRKSKVLAVGGYQDLPLVE---DYALWARMLANGARFAnLPEILVKAR 201
 
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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