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Conserved domains on  [gi|700302725|gb|AIU69544|]
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hypothetical protein TEU_03845 [Thermococcus eurythermalis]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
4-215 1.75e-34

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.


The actual alignment was detected with superfamily member cd04184:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 202  Bit Score: 123.47  E-value: 1.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   4 PNVSVLLPVANEPLKYVKLSLRSIINQTYRNLEIIVLVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGIS 83
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  84 MASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLI-------LNPKISLNNNIVTHeniqrail 156
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSepffkpdWSPDLLLSQNYIGH-------- 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725 157 rfnpfihsSILLRTQTLEQIGGYNERFETSQDYELWLRVCRR-YKCYILPKrlILYRIRT 215
Cdd:cd04184  153 --------LLVYRRSLVRQVGGFREGFEGAQDYDLVLRVSEHtDRIAHIPR--VLYHWRA 202
 
Name Accession Description Interval E-value
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
4-215 1.75e-34

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: 123.47  E-value: 1.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   4 PNVSVLLPVANEPLKYVKLSLRSIINQTYRNLEIIVLVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGIS 83
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  84 MASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLI-------LNPKISLNNNIVTHeniqrail 156
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSepffkpdWSPDLLLSQNYIGH-------- 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725 157 rfnpfihsSILLRTQTLEQIGGYNERFETSQDYELWLRVCRR-YKCYILPKrlILYRIRT 215
Cdd:cd04184  153 --------LLVYRRSLVRQVGGFREGFEGAQDYDLVLRVSEHtDRIAHIPR--VLYHWRA 202
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
3-223 1.16e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 116.34  E-value: 1.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   3 TPNVSVLLPVANEPlKYVKLSLRSIINQTYRNLEIIVLVDR-PDNkeVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVG 81
Cdd:COG0463    1 MPLVSVVIPTYNEE-EYLEEALESLLAQTYPDFEIIVVDDGsTDG--TAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  82 ISMASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGtkaYFINEEGKLILNPKISLNNNIVtheniqRAILRFNPF 161
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG---SRLIREGESDLRRLGSRLFNLV------RLLTNLPDS 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 700302725 162 IHSSILLRTQTLEQIgGYNERFetSQDYELWLRVCRRYKCYILPKRlilYRIRTHGISYSKM 223
Cdd:COG0463  149 TSGFRLFRREVLEEL-GFDEGF--LEDTELLRALRHGFRIAEVPVR---YRAGESKLNLRDL 204
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-169 3.46e-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: 90.15  E-value: 3.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725    7 SVLLPVANEPlKYVKLSLRSIINQTYRNLEIIVlVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGISMAS 86
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNFEIIV-VDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   87 GVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLILNPKISLNNNIVTHENIQRAILRFNPFIHSSI 166
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFAL 158

                  ...
gi 700302725  167 LLR 169
Cdd:pfam00535 159 YRR 161
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-114 3.09e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.81  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   3 TPNVSVLLPVANEPlKYVKLSLRSIINQTYRNLEIIvLVDRPDNKEVVEYIKAEQERDNRIRLhVNQRPLGLTKTLNVGI 82
Cdd:PRK10073   5 TPKLSIIIPLYNAG-KDFRAFMESLIAQTWTALEII-IVNDGSTDNSVEIAKHYAENYPHVRL-LHQANAGVSVARNTGL 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 700302725  83 SMASGVYIARMDADDISLPTRIERQVAFMEQN 114
Cdd:PRK10073  82 AVATGKYVAFPDADDVVYPTMYETLMTMALED 113
 
Name Accession Description Interval E-value
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
4-215 1.75e-34

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: 123.47  E-value: 1.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   4 PNVSVLLPVANEPLKYVKLSLRSIINQTYRNLEIIVLVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGIS 83
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  84 MASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLI-------LNPKISLNNNIVTHeniqrail 156
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSepffkpdWSPDLLLSQNYIGH-------- 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725 157 rfnpfihsSILLRTQTLEQIGGYNERFETSQDYELWLRVCRR-YKCYILPKrlILYRIRT 215
Cdd:cd04184  153 --------LLVYRRSLVRQVGGFREGFEGAQDYDLVLRVSEHtDRIAHIPR--VLYHWRA 202
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
7-212 4.82e-34

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: 122.42  E-value: 4.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   7 SVLLPV-ANEPLKYVKLSLRSIINQTYRNLEIIVLVDRPDNKEVVEYIKaEQERDNRIRLHVNQRPLGLTKTLNVGISMA 85
Cdd:cd04195    1 SVLMSVyIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLE-EFKRKLPLKVVPLEKNRGLGKALNEGLKHC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  86 SGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLILNPKISLNNnivtHENIQRAILRfNPFIHSS 165
Cdd:cd04195   80 TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRRLPTSH----DDILKFARRR-SPFNHPT 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 700302725 166 ILLRTQTLEQIGGYNErFETSQDYELWLR-VCRRYKCYILPKRLILYR 212
Cdd:cd04195  155 VMFRKSKVLAVGGYQD-LPLVEDYALWARmLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
3-223 1.16e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 116.34  E-value: 1.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   3 TPNVSVLLPVANEPlKYVKLSLRSIINQTYRNLEIIVLVDR-PDNkeVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVG 81
Cdd:COG0463    1 MPLVSVVIPTYNEE-EYLEEALESLLAQTYPDFEIIVVDDGsTDG--TAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  82 ISMASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGtkaYFINEEGKLILNPKISLNNNIVtheniqRAILRFNPF 161
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG---SRLIREGESDLRRLGSRLFNLV------RLLTNLPDS 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 700302725 162 IHSSILLRTQTLEQIgGYNERFetSQDYELWLRVCRRYKCYILPKRlilYRIRTHGISYSKM 223
Cdd:COG0463  149 TSGFRLFRREVLEEL-GFDEGF--LEDTELLRALRHGFRIAEVPVR---YRAGESKLNLRDL 204
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-262 1.44e-26

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 105.21  E-value: 1.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   2 KTPNVSVLLPVANEPlKYVKLSLRSIINQTY--RNLEIIVLVDRPDNkEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLN 79
Cdd:COG1215   27 DLPRVSVIIPAYNEE-AVIEETLRSLLAQDYpkEKLEVIVVDDGSTD-ETAEIARELAAEYPRVRVIERPENGGKAAALN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  80 VGISMASGVYIARMDADDISLPTRIERQVAFMeQNPDYGLCGTkayfineegklilnpkislnnnivtheniqrailrfn 159
Cdd:COG1215  105 AGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGASGA------------------------------------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725 160 pfihsSILLRTQTLEQIGGYNERfETSQDYELWLRVCRR-YKCYILPKRLILYRIRTHGISYSKMRTSLKYSLCARYLAI 238
Cdd:COG1215  147 -----NLAFRREALEEVGGFDED-TLGEDLDLSLRLLRAgYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKH 220
                        250       260
                 ....*....|....*....|....
gi 700302725 239 TKYGYPKWGIIYLIWPTISYIVPV 262
Cdd:COG1215  221 RPLLRPRRLLLFLLLLLLPLLLLL 244
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
8-204 9.12e-26

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: 99.12  E-value: 9.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   8 VLLPVANEPlKYVKLSLRSIINQTYRNLEIIVlVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGISMASG 87
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNFEVIV-VDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  88 VYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAyfineegklilnpkislnnnivtheniqrailrfnpfihsSIL 167
Cdd:cd00761   79 EYILFLDADDLLLPDWLERLVAELLADPEADAVGGPG----------------------------------------NLL 118
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 700302725 168 LRTQTLEQIGGYNERFETS-QDYELWLRVCRRYKCYIL 204
Cdd:cd00761  119 FRRELLEEIGGFDEALLSGeEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-169 3.46e-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: 90.15  E-value: 3.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725    7 SVLLPVANEPlKYVKLSLRSIINQTYRNLEIIVlVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGISMAS 86
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNFEIIV-VDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   87 GVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLILNPKISLNNNIVTHENIQRAILRFNPFIHSSI 166
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFAL 158

                  ...
gi 700302725  167 LLR 169
Cdd:pfam00535 159 YRR 161
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
7-221 5.19e-22

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: 90.68  E-value: 5.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   7 SVLLPVANePLKYVKLSLRSIINQTYRNLEIIVlVD--RPDNkeVVEYIKAEQ--------ERDNrirlhvnqrplGLTK 76
Cdd:cd06433    1 SIITPTYN-QAETLEETIDSVLSQTYPNIEYIV-IDggSTDG--TVDIIKKYEdkitywisEPDK-----------GIYD 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  77 TLNVGISMASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLILNPKISLNNNivtheniqRAIL 156
Cdd:cd06433   66 AMNKGIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLD--------KFLL 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 700302725 157 RFNPFIHSSILLRTQTLEQIGGYNERFETSQDYELWLRVCRRYKC-YILPKRLILYriRTHGISYS 221
Cdd:cd06433  138 YGMPICHQATFFRRSLFEKYGGFDESYRIAADYDLLLRLLLAGKIfKYLPEVLAAF--RLGGVSST 201
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-217 7.02e-19

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 82.68  E-value: 7.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   7 SVLLPVANePLKYVKLSLRSIINQTYRNLEIIVLVDRP-DNkeVVEYIKA-EQERDNRIRLHVNQRPLGLTKTLNVGISM 84
Cdd:cd04196    1 AVLMATYN-GEKYLREQLDSILAQTYKNDELIISDDGStDG--TVEIIKEyIDKDPFIIILIRNGKNLGVARNFESLLQA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  85 ASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEEGKLILnPKISLNNNIVTHENIQRAILRfNPFIHS 164
Cdd:cd04196   78 ADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIG-ESFFEYQKIKPGTSFNNLLFQ-NVVTGC 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 700302725 165 SILLRTQTLEQIGGYNERFETSQDYELWLRVCRRYKCYILPKRLILYRIrtHG 217
Cdd:cd04196  156 TMAFNRELLELALPFPDADVIMHDWWLALLASAFGKVVFLDEPLILYRQ--HG 206
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
6-214 3.79e-18

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 81.12  E-value: 3.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   6 VSVLLPVANEPlKYVKLSLRSIINQTY--RNLEIIVlVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLgLTKTLNVGIS 83
Cdd:cd02525    2 VSIIIPVRNEE-KYIEELLESLLNQSYpkDLIEIIV-VDGGSTDGTREIVQEYAAKDPRIRLIDNPKRI-QSAGLNIGIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  84 MASGVYIARMDADDISLPTRIERQVAFMEQnPDYGLCGTKAYFINE---EGKLILNPKISLNNNIVTHENIQRAIlRFNP 160
Cdd:cd02525   79 NSRGDIIIRVDAHAVYPKDYILELVEALKR-TGADNVGGPMETIGEskfQKAIAVAQSSPLGSGGSAYRGGAVKI-GYVD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 700302725 161 FIHsSILLRTQTLEQIGGYNERFETSQDYELWLRVCRR-YKCYILPKRLILYRIR 214
Cdd:cd02525  157 TVH-HGAYRREVFEKVGGFDESLVRNEDAELNYRLRKAgYKIWLSPDIRVYYYPR 210
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
3-252 4.33e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.64  E-value: 4.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   3 TPNVSVLLPVANEPlKYVKLSLRSIINQTYRNLEIIVlVDRPDNKEVVEYIKAEQerDNRIRLHVNQRPLGLTKTLNVGI 82
Cdd:COG1216    2 RPKVSVVIPTYNRP-ELLRRCLESLLAQTYPPFEVIV-VDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  83 SMASGVYIARMDADDISLPTRIERQVAFmeqnpdyglcgtkayfineegklilnpkislnnnivtheniqrailrfnpfi 162
Cdd:COG1216   78 RAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725 163 hSSILLRTQTLEQIGGYNERFE-TSQDYELWLRVCRR-YKCYILPKRLILYRIRTHGISYSKMRtslkYSLCARYLAITK 240
Cdd:COG1216  106 -ACLLIRREVFEEVGGFDERFFlYGEDVDLCLRLRKAgYRIVYVPDAVVYHLGGASSGPLLRAY----YLGRNRLLFLRK 180
                        250
                 ....*....|..
gi 700302725 241 YGYPKWGIIYLI 252
Cdd:COG1216  181 HGPRPLLRLALL 192
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
8-181 8.53e-15

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: 70.72  E-value: 8.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   8 VLLPVANEPlKYVKLSLRSIINQTYRNLEIIVLVDRPDNKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGISMASG 87
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAKG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  88 VYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFINEegklilnpkislNNNIVTH------ENIQRAILRFNPF 161
Cdd:cd06423   80 DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNG------------SENLLTRlqaieyLSIFRLGRRAQSA 147
                        170       180
                 ....*....|....*....|....*..
gi 700302725 162 IHSSILL-------RTQTLEQIGGYNE 181
Cdd:cd06423  148 LGGVLVLsgafgafRREALREVGGWDE 174
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
4-209 2.47e-14

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: 70.29  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   4 PNVSVLLPVANEPLKYVKLSLRSIINQTYRN--LEIIVLVDRPDnKEVVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVG 81
Cdd:cd06421    1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHdkLRVYVLDDGRR-PELRALAAELGVEYGYRYLTRPDNRHAKAGNLNNA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  82 ISMASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYFIN-EEGKLILNPkiSLNNNIVTHENIQRAILRFNP 160
Cdd:cd06421   80 LAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNpDPFDWLADG--APNEQELFYGVIQPGRDRWGA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 700302725 161 --FIHSSILLRTQTLEQIGGYNErFETSQDYELWLRVCRR-YKCYILPKRLI 209
Cdd:cd06421  158 afCCGSGAVVRREALDEIGGFPT-DSVTEDLATSLRLHAKgWRSVYVPEPLA 208
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-209 2.71e-14

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: 70.09  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725    4 PNVSVLLPVANEPLKYVKLsLRSIINQTYRNLEIIVLVDrPDNKEVVEYIKAEQER--DNRIRLHVNQRPLGLTKT---L 78
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRV-LEAILAQPYPPVEVVVVVN-PSDAETLDVAEEIAARfpDVRLRVIRNARLLGPTGKsrgL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   79 NVGISMASGVYIARMDADDISLPTRIERQVAFMEQnPDYGLCGTKAYFINeeGKLILNPkisLNNNIVTHENIQRAILRF 158
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTPVFSLN--RSTMLSA---LGALEFALRHLRMMSLRL 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 700302725  159 N---PFIHSSI-LLRTQTLEQIGGYNERFETSQDYELWLRVCRR-YKCYILPKRLI 209
Cdd:pfam13641 154 AlgvLPLSGAGsAIRREVLKELGLFDPFFLLGDDKSLGRRLRRHgWRVAYAPDAAV 209
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
12-210 6.09e-12

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: 62.58  E-value: 6.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  12 VANEPLKYVKLSLRSIINQTYRNLEIIVlVDRPDNKEVVEYIKAEQErdnRIRLHVNQRPLGLTKTLNVGISMASGVYIA 91
Cdd:cd04186    4 VNYNSLEYLKACLDSLLAQTYPDFEVIV-VDNASTDGSVELLRELFP---EVRLIRNGENLGFGAGNNQGIREAKGDYVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  92 RMDADDISLPTRIERQVAFMEQNPDYGLCGtkayfineegklilnPKISlnnnivtheniqrailrfnpfiHSSILLRTQ 171
Cdd:cd04186   80 LLNPDTVVEPGALLELLDAAEQDPDVGIVG---------------PKVS----------------------GAFLLVRRE 122
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 700302725 172 TLEQIGGYNERFET-SQDYELWLRV-CRRYKCYILPKRLIL 210
Cdd:cd04186  123 VFEEVGGFDEDFFLyYEDVDLCLRArLAGYRVLYVPQAVIY 163
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
7-214 1.72e-10

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: 59.98  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725    7 SVLLPVAN-EPLKYVKLSLRSIINQTYRNLEIIVLVD--RPDNKEVVEYIKAEQERDNRIrlHVNQRPLGLTKTLNVGIS 83
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERILNQTFQYDPEFELIIINDgsTDKTLEEVSSIKDHNLQVYYP--NAPDTTYSLAASRNRGTS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   84 MASGVYIARMDADDISLPTRIERQVAF-----MEQNPDYGLCGTKAYFINEEgklilNPKISLNNNIVTHENIQRAILRF 158
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFEKQLKIatslaLQENIQAAVVLPVTDLNDES-----SNFLRRGGDLTASGDVLRDLLVF 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 700302725  159 -NPFIH------SSILLRTQTLEQIGGYNERFET--SQDYELWLRVCRRYKCYILPKRLILYRIR 214
Cdd:pfam10111 154 ySPLAIffapnsSNALINRQAFIEVGGFDESFRGhgAEDFDIFLRLAARYPFVAVMPPQLLYRLS 218
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
6-123 1.42e-07

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: 51.10  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   6 VSVLLPVANEPLKYVKLSLRSIINQTyrNLEIIVLVDrpDNKEVVEYIKAEQERDNRIRLHVNQRPlGLTKTLNVGISMA 85
Cdd:cd06434    2 VTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTD--GDDEPYLSILSQTVKYGGIFVITVPHP-GKRRALAEGIRHV 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 700302725  86 SGVYIARMDaDDISLPTR-IERQVAFMEqNPDYGLCGTK 123
Cdd:cd06434   77 TTDIVVLLD-SDTVWPPNaLPEMLKPFE-DPKVGGVGTN 113
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-126 1.44e-07

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 51.14  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   8 VLLPVANEPLKYVKLsLRSIINQTY--RNLEIIVLVDRP--DNKEVVEYIKAEQERdNRIRLHVNQRPL-GLTKTLNVGI 82
Cdd:cd04192    1 VVIAARNEAENLPRL-LQSLSALDYpkEKFEVILVDDHStdGTVQILEFAAAKPNF-QLKILNNSRVSIsGKKNALTTAI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 700302725  83 SMASGVYIARMDADDISLPTRIERQVAFMEQNPDYGLCGTKAYF 126
Cdd:cd04192   79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYF 122
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-114 3.09e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.81  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   3 TPNVSVLLPVANEPlKYVKLSLRSIINQTYRNLEIIvLVDRPDNKEVVEYIKAEQERDNRIRLhVNQRPLGLTKTLNVGI 82
Cdd:PRK10073   5 TPKLSIIIPLYNAG-KDFRAFMESLIAQTWTALEII-IVNDGSTDNSVEIAKHYAENYPHVRL-LHQANAGVSVARNTGL 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 700302725  83 SMASGVYIARMDADDISLPTRIERQVAFMEQN 114
Cdd:PRK10073  82 AVATGKYVAFPDADDVVYPTMYETLMTMALED 113
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
8-115 5.03e-06

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: 46.30  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   8 VLLPVAN-EPlkYVKLSLRSIINQTYRN-LEIIVLVDRPDNK--EVVEYIKAEQERDNRIRL---HVNQRPLGLTKTLNV 80
Cdd:cd06913    1 IILPVHNgEQ--WLDECLESVLQQDFEGtLELSVFNDASTDKsaEIIEKWRKKLEDSGVIVLvgsHNSPSPKGVGYAKNQ 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 700302725  81 GISMASGVYIARMDADDISLPTRIERQVAFMEQNP 115
Cdd:cd06913   79 AIAQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHP 113
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-199 1.02e-05

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 45.75  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   4 PNVSVLLPVANEPLKYVKlSLRSIINQTYRNLEIIVLVDRPDNKEVVEYIkAEQERDNRIRLHVNQRPLGLTKTLNVGIS 83
Cdd:PRK10018   5 PLISIYMPTWNRQQLAIR-AIKSVLRQDYSNWEMIIVDDCSTSWEQLQQY-VTALNDPRITYIHNDINSGACAVRNQAIM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  84 MASGVYIARMDADDISLPTRIERQVAFMEQ--------NPDYgLCGTKAYfiNEEGKLILNPKISLNNNIVTHENIqrai 155
Cdd:PRK10018  83 LAQGEYITGIDDDDEWTPNRLSVFLAHKQQlvthaflyANDY-VCQGEVY--SQPASLPLYPKSPYSRRLFYKRNI---- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 700302725 156 lrfnpfIHSSILLRTQTLEQIgGYNERFETSQDYELWLRVCRRY 199
Cdd:PRK10018 156 ------IGNQVFTWAWRFKEC-LFDTELKAAQDYDIFLRMVVEY 192
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
8-131 1.21e-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: 41.79  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   8 VLLPVANEPlKYVKLSLRSIINQTYRNLEIIVLVD--RPDNKEVVEyikaEQERDNRIRL-HVNQRPLG--LTKTLNVGI 82
Cdd:cd06420    1 LIITTYNRP-EALELVLKSVLNQSILPFEVIIADDgsTEETKELIE----EFKSQFPIPIkHVWQEDEGfrKAKIRNKAI 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 700302725  83 SMASGVYIARMDADDISLPTRIERQVAFMEqnPDYGLCGTKAYfINEEG 131
Cdd:cd06420   76 AAAKGDYLIFIDGDCIPHPDFIADHIELAE--PGVFLSGSRVL-LNEKL 121
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
4-194 1.55e-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: 41.91  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   4 PNVSVLLPVANEplKYV-KLSLRSIINQTY-RN-LEIIVLVDRPDN--KEVVEYIKAEQERDNRIR-LHVNQRPLGLTKT 77
Cdd:cd06437    1 PMVTVQLPVFNE--KYVvERLIEAACALDYpKDrLEIQVLDDSTDEtvRLAREIVEEYAAQGVNIKhVRRADRTGYKAGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725  78 LNVGISMASGVYIARMDADDISLPTRIERqVAFMEQNPDYGLCGTKAYFINEEGKLILNPK-ISLNNNI-VTHENIQRAI 155
Cdd:cd06437   79 LAEGMKVAKGEYVAIFDADFVPPPDFLQK-TPPYFADPKLGFVQTRWGHINANYSLLTRVQaMSLDYHFtIEQVARSSTG 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 700302725 156 LRFNpFIHSSILLRTQTLEQIGGYNERfETSQDYELWLR 194
Cdd:cd06437  158 LFFN-FNGTAGVWRKECIEDAGGWNHD-TLTEDLDLSYR 194
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
2-96 2.90e-04

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 41.22  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   2 KTPNVSVLLPVANEPLK---YVKLSLRSIinQTYRNLEIIVLVD-RPDN-KEVVEYIKAEQErDNRIRLHVNQRPLGLTK 76
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNialIVYLIFKAL--QDVKDFEIIVVDDgSPDGtQDVVKQLQKVYG-EDRILLRPRPGKLGLGT 83
                         90       100
                 ....*....|....*....|
gi 700302725  77 TLNVGISMASGVYIARMDAD 96
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDAD 103
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
24-96 1.60e-03

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: 38.61  E-value: 1.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700302725  24 LRSIINQTYRNLEIIVLVDR-PDNKevVEYIKAEQERDNRIRLHVNQRPLGLTKTLNVGISMASGVYIARMDAD 96
Cdd:cd04187   19 LKAVLESLGYDYEIIFVDDGsTDRT--LEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDAVITMDAD 90
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
89-209 1.97e-03

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: 38.47  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   89 YIARMDADDISLPTRIERQVAFMEQnPDYGLCGTKAYFINEEGKLILNPKISLNNNIVTHENIQRAILRFNPFIHSSILL 168
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 700302725  169 RTQTLEQIGGYNERFeTSQDYELWLRVCRR-YKCYILPKRLI 209
Cdd:pfam13632  80 RRSALQEVGGWDDGS-VSEDFDFGLRLQRAgYRVRFAPYSAV 120
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
7-95 2.36e-03

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: 38.72  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302725   7 SVLLPVANEPLKYVKLSLRSIINQTYRNL--EIIvLVD----RPDNKEVVEYIKaeQERDNRIRLHVNQRPLGLTKTLNV 80
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELlkEII-LVDdfsdKPELKLLLEEYY--KKYLPKVKVLRLKKREGLIRARIA 77
                         90
                 ....*....|....*
gi 700302725  81 GISMASGVYIARMDA 95
Cdd:cd02510   78 GARAATGDVLVFLDS 92
 
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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