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Conserved domains on  [gi|485892751|ref|WP_001484692|]
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MULTISPECIES: glycosyltransferase [Escherichia]

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 ...
4-205 3.78e-96

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 cd04195:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 201  Bit Score: 280.74  E-value: 3.78e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   4 SVLMSLYIKEKPEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLAQCE 83
Cdd:cd04195    1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  84 NDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYIEEFSETIENRLSQKiVPTTHNEIMKNIGKRNPFNHMTVVFNK 163
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 485892751 164 SEIIKVGGYEHHYLMEDYNLWLRLLKNNIQAANLPLTLVYAR 205
Cdd:cd04195  160 SKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-205 3.78e-96

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: 280.74  E-value: 3.78e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   4 SVLMSLYIKEKPEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLAQCE 83
Cdd:cd04195    1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  84 NDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYIEEFSETIENRLSQKiVPTTHNEIMKNIGKRNPFNHMTVVFNK 163
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 485892751 164 SEIIKVGGYEHHYLMEDYNLWLRLLKNNIQAANLPLTLVYAR 205
Cdd:cd04195  160 SKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 9.60e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.55  E-value: 9.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   1 MNFSVLMSLYiKEkPEYLHECLKSLYEQTKQADEIVLVYDGPiTNELDKVVNYWLNSLP-IKIIKLSKNVGLGQALNKGL 79
Cdd:COG0463    2 PLVSVVIPTY-NE-EEYLEEALESLLAQTYPDFEIIVVDDGS-TDGTAEILRELAAKDPrIRVIRLERNRGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  80 AQCENDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYIEEFSETIENRLSQKIVptthnEIMKNIGKRNPFNHMTV 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLF-----NLVRLLTNLPDSTSGFR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 485892751 160 VFNKsEIIKVGGYEHHYlMEDYNLwLRLLKNNIQAANLPLTlvYARGGDGMIYRR 214
Cdd:COG0463  154 LFRR-EVLEELGFDEGF-LEDTEL-LRALRHGFRIAEVPVR--YRAGESKLNLRD 203
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-136 2.66e-23

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: 92.84  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751    4 SVLMSLYIKEKpeYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLAQCE 83
Cdd:pfam00535   1 SVIIPTYNEEK--YLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 485892751   84 NDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYIEEFSETIENRLSQKI 136
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRI 131
PRK10073 PRK10073
putative glycosyl transferase; Provisional
4-140 7.73e-10

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 58.52  E-value: 7.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   4 SVLMSLYIKEKpeYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKlSKNVGLGQALNKGLAQCE 83
Cdd:PRK10073   9 SIIIPLYNAGK--DFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVAT 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  84 NDYVARMDTDDICHPKRFEIQIDFLNKNkNISVV---GSYIEEfsetiENRLSQKIVPTT 140
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETLMTMALED-DLDVAqcnADWCFR-----DTGETWQSIPSD 139
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-205 3.78e-96

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: 280.74  E-value: 3.78e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   4 SVLMSLYIKEKPEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLAQCE 83
Cdd:cd04195    1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  84 NDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYIEEFSETIENRLSQKiVPTTHNEIMKNIGKRNPFNHMTVVFNK 163
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 485892751 164 SEIIKVGGYEHHYLMEDYNLWLRLLKNNIQAANLPLTLVYAR 205
Cdd:cd04195  160 SKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 9.60e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.55  E-value: 9.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   1 MNFSVLMSLYiKEkPEYLHECLKSLYEQTKQADEIVLVYDGPiTNELDKVVNYWLNSLP-IKIIKLSKNVGLGQALNKGL 79
Cdd:COG0463    2 PLVSVVIPTY-NE-EEYLEEALESLLAQTYPDFEIIVVDDGS-TDGTAEILRELAAKDPrIRVIRLERNRGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  80 AQCENDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYIEEFSETIENRLSQKIVptthnEIMKNIGKRNPFNHMTV 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLF-----NLVRLLTNLPDSTSGFR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 485892751 160 VFNKsEIIKVGGYEHHYlMEDYNLwLRLLKNNIQAANLPLTlvYARGGDGMIYRR 214
Cdd:COG0463  154 LFRR-EVLEELGFDEGF-LEDTEL-LRALRHGFRIAEVPVR--YRAGESKLNLRD 203
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
3-266 1.91e-23

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: 96.73  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   3 FSVLMSLYiKEkPEYLHECLKSLYEQT--KQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLA 80
Cdd:COG1215   31 VSVIIPAY-NE-EAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  81 QCENDYVARMDTDDICHPKRFEIQIDFLnKNKNISVVGSyieefsetienrlsqkivptthneimknigkrnpfnhmTVV 160
Cdd:COG1215  109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGASGA--------------------------------------NLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751 161 FNKSEIIKVGGYEHHYLMEDYNLWLRLLKNNIQAANLPLTLVYARGGDGMI-YRRSGLRYIKSEYKLYKLKQRLGYQNYI 239
Cdd:COG1215  150 FRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRaLFRQRRRWARGGLQLLLKHRPLLRPRRL 229
                        250       260
                 ....*....|....*....|....*..
gi 485892751 240 ISSLVFFLrsVPRVFPPYILKAIYRFL 266
Cdd:COG1215  230 LLFLLLLL--LPLLLLLLLLALLALLL 254
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-136 2.66e-23

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: 92.84  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751    4 SVLMSLYIKEKpeYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLAQCE 83
Cdd:pfam00535   1 SVIIPTYNEEK--YLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 485892751   84 NDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYIEEFSETIENRLSQKI 136
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRI 131
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
15-119 6.07e-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: 81.01  E-value: 6.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  15 PEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLAQCENDYVARMDTDD 94
Cdd:cd00761    9 EPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDADD 88
                         90       100
                 ....*....|....*....|....*
gi 485892751  95 ICHPKRFEIQIDFLNKNKNISVVGS 119
Cdd:cd00761   89 LLLPDWLERLVAELLADPEADAVGG 113
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-98 2.48e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 72.33  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   1 MNFSVLMSLYikEKPEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNslPIKIIKLSKNVGLGQALNKGLA 80
Cdd:COG1216    3 PKVSVVIPTY--NRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFP--RVRVIRNPENLGFAAARNLGLR 78
                         90
                 ....*....|....*...
gi 485892751  81 QCENDYVARMDTDDICHP 98
Cdd:COG1216   79 AAGGDYLLFLDDDTVVEP 96
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-205 8.91e-13

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: 65.30  E-value: 8.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   3 FSVLMSLYiKEKPEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVN-YWLNSLPIKIIKLSKNVGLGQALNKGLAQ 81
Cdd:cd04184    3 ISIVMPVY-NTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKkYAAQDPRIKVVFREENGGISAATNSALEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  82 CENDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVgsYieefseTIENRLSqkivptthneimkNIGKR-NPF------ 154
Cdd:cd04184   82 ATGEFVALLDHDDELAPHALYEVVKALNEHPDADLI--Y------SDEDKID-------------EGGKRsEPFfkpdws 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485892751 155 ----------NHMtVVFNKSEIIKVGGYEHHY-LMEDYNLWLRLLKNNIQAANLPLTLVYAR 205
Cdd:cd04184  141 pdlllsqnyiGHL-LVYRRSLVRQVGGFREGFeGAQDYDLVLRVSEHTDRIAHIPRVLYHWR 201
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
16-207 1.56e-12

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: 64.87  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  16 EYLHECLKSLYEQTKQADEIVLVyDGpitNELDKVVNyWLNSLPIKIIKLS--KNVGLGQALNKGLAQCENDYVARMDTD 93
Cdd:cd06433   11 ETLEETIDSVLSQTYPNIEYIVI-DG---GSTDGTVD-IIKKYEDKITYWIsePDKGIYDAMNKGIALATGDIIGFLNSD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  94 DICHPKRFEIQIDFLNKNKNISVVGSYIEEFSEtiENRLSQKIVPTTHNeiMKNIGKRNPFNHMTVVFNKSEIIKVGGY- 172
Cdd:cd06433   86 DTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDE--NGRVIGRRRPPPFL--DKFLLYGMPICHQATFFRRSLFEKYGGFd 161
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 485892751 173 -EHHYLMeDYNLWLRLLKNNIQAANLPLTLVYARGG 207
Cdd:cd06433  162 eSYRIAA-DYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
14-121 5.86e-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: 62.19  E-value: 5.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  14 KPEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNslpIKIIKLSKNVGLGQALNKGLAQCENDYVARMDTD 93
Cdd:cd04186    8 SLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE---VRLIRNGENLGFGAGNNQGIREAKGDYVLLLNPD 84
                         90       100
                 ....*....|....*....|....*...
gi 485892751  94 DICHPKRFEIQIDFLNKNKNISVVGSYI 121
Cdd:cd04186   85 TVVEPGALLELLDAAEQDPDVGIVGPKV 112
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
4-164 1.13e-11

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 62.65  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   4 SVLMSLYIKEKpeYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYW-LNSLPIKIIKLSKNVGLGQALNKGLAQC 82
Cdd:cd04196    1 AVLMATYNGEK--YLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIdKDPFIIILIRNGKNLGVARNFESLLQAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  83 ENDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGS---YIEEFSETIENRLSQkIVPTTHNEIMKNIGKRNPFNHMTV 159
Cdd:cd04196   79 DGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSdleLVDENGNPIGESFFE-YQKIKPGTSFNNLLFQNVVTGCTM 157

                 ....*
gi 485892751 160 VFNKS 164
Cdd:cd04196  158 AFNRE 162
PRK10073 PRK10073
putative glycosyl transferase; Provisional
4-140 7.73e-10

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 58.52  E-value: 7.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   4 SVLMSLYIKEKpeYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYWLNSLPIKIIKlSKNVGLGQALNKGLAQCE 83
Cdd:PRK10073   9 SIIIPLYNAGK--DFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVAT 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  84 NDYVARMDTDDICHPKRFEIQIDFLNKNkNISVV---GSYIEEfsetiENRLSQKIVPTT 140
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETLMTMALED-DLDVAqcnADWCFR-----DTGETWQSIPSD 139
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
14-193 9.54e-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: 53.74  E-value: 9.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  14 KPEYLHECLKSLYEQTKQADEIVLVYDGPiTNELDKVVNYWLNSLPIKIIKL-SKNVG--LGQALNKGLAQCENDYVARM 90
Cdd:cd06420    8 RPEALELVLKSVLNQSILPFEVIIADDGS-TEETKELIEEFKSQFPIPIKHVwQEDEGfrKAKIRNKAIAAAKGDYLIFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  91 DTDDICHPKrFeIQIDFLNKNKNISVVGSYIEefsetienrLSQKivptthneimkniGKRNPFNHMTVVFNKSEIIKVG 170
Cdd:cd06420   87 DGDCIPHPD-F-IADHIELAEPGVFLSGSRVL---------LNEK-------------LTERGIRGCNMSFWKKDLLAVN 142
                        170       180
                 ....*....|....*....|....*.
gi 485892751 171 GY---EHHYLMEDYNLWLRLLKNNIQ 193
Cdd:cd06420  143 GFdeeFTGWGGEDSELVARLLNSGIK 168
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
18-180 8.40e-08

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: 51.07  E-value: 8.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  18 LHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYW-LNSLPIKIIKLSKNVGLGQALNKGLAQCENDYVARMDTDDIC 96
Cdd:cd06423   12 IERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAaLYIRRVLVVRDKENGGKAGALNAGLRHAKGDIVVVLDADTIL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  97 HP---KRfeIQIDFLNKNKNISVVG---------SYIEEFSeTIENRLSQKIvptthneimkNIGKRNPFNHMTVV---- 160
Cdd:cd06423   92 EPdalKR--LVVPFFADPKVGAVQGrvrvrngseNLLTRLQ-AIEYLSIFRL----------GRRAQSALGGVLVLsgaf 158
                        170       180
                 ....*....|....*....|..
gi 485892751 161 --FNKSEIIKVGGYEHHYLMED 180
Cdd:cd06423  159 gaFRREALREVGGWDEDTLTED 180
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
14-118 1.78e-07

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 50.75  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  14 KPEyLHECLKSLYEQTKQADEIVLVYDGPitnELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKG---LAQCENDYVARM 90
Cdd:cd02526    7 NPD-LSKLKELLAALAEQVDKVVVVDNSS---GNDIELRLRLNSEKIELIHLGENLGIAKALNIGikaALENGADYVLLF 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 485892751  91 DTDDICHP---KRFEIQIDFLNKNKNISVVG 118
Cdd:cd02526   83 DQDSVPPPdmvEKLLAYKILSDKNSNIGAVG 113
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
17-104 1.13e-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: 48.22  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  17 YLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYW---LNSLPIKIIKLSKN----VGLGQALNKGLAQCENDYVAR 89
Cdd:cd06913   11 WLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWrkkLEDSGVIVLVGSHNspspKGVGYAKNQAIAQSSGRYLCF 90
                         90
                 ....*....|....*
gi 485892751  90 MDTDDICHPKRFEIQ 104
Cdd:cd06913   91 LDSDDVMMPQRIRLQ 105
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-203 5.52e-06

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 46.50  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751    4 SVLMSLYIKEKPEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYW-LNSLPIKIIKLSKNVGLGQALNKGLAQC 82
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKdHNLQVYYPNAPDTTYSLAASRNRGTSHA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   83 ENDYVARMDTDDICHPKRFE-----IQIDFLNKNKNISVVGS---YIEEFSE--------TIENRLSQKIVpTTHNEIMK 146
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEkqlkiATSLALQENIQAAVVLPvtdLNDESSNflrrggdlTASGDVLRDLL-VFYSPLAI 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  147 NIGKrnpfNHMTVVFNKSEIIKVGGYEHHYL---MEDYNLWLRLLKNNIQAANLPLTLVY 203
Cdd:pfam10111 160 FFAP----NSSNALINRQAFIEVGGFDESFRghgAEDFDIFLRLAARYPFVAVMPPQLLY 215
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
4-218 1.07e-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: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751   4 SVLMSLYIKEKpeYLHECLKSLYEQT--KQADEIVLVyDGPITNELDKVVNYWLNSLPIkiIKLSKNVGLGQ--ALNKGL 79
Cdd:cd02525    3 SIIIPVRNEEK--YIEELLESLLNQSypKDLIEIIVV-DGGSTDGTREIVQEYAAKDPR--IRLIDNPKRIQsaGLNIGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  80 AQCENDYVARMDTDDICHPKRFEIQIDFLNKNKNISVVGSYieefsETIENRLSQKIVPTTHNEIMKNIGK--RNPFNHM 157
Cdd:cd02525   78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPM-----ETIGESKFQKAIAVAQSSPLGSGGSayRGGAVKI 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485892751 158 TVV-------FNKSEIIKVGGY-EHHYLMEDYNLWLRLLKNNIQAANLPLTLVYArggdgmiYRRSGLR 218
Cdd:cd02525  153 GYVdtvhhgaYRREVFEKVGGFdESLVRNEDAELNYRLRKAGYKIWLSPDIRVYY-------YPRSTLK 214
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
20-93 1.13e-05

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: 44.87  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  20 ECLKSLYEQTKQA------DEIVLVYDGPITNELDKVVNYWLNSLPIKIIKLSKNVGLGQALNKGLAQCENDYVARMDTD 93
Cdd:cd04179   10 ENIPELVERLLAVleegydYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTMDAD 89
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
15-119 3.80e-04

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 40.63  E-value: 3.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  15 PEYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNYW-LNSLPIKIIKLSKNVGLGQALNKGLAQCENDYVARMDTD 93
Cdd:cd04188   13 PPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLArKNPALIRVLTLPKNRGKGGAVRAGMLAARGDYILFADAD 92
                         90       100       110
                 ....*....|....*....|....*....|
gi 485892751  94 ---DICHPKRFEIQIdflnKNKNISVV-GS 119
Cdd:cd04188   93 latPFEELEKLEEAL----KTSGYDIAiGS 118
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
16-93 1.49e-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: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485892751  16 EYLHECLKSLYEQTKQADEIVLVYDGPITNELDKVVNyWLNSLP-IKIIKLSKNVGLGQALNKGLAQCENDYVARMDTD 93
Cdd:cd04187   13 PELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRE-LAARDPrVKVIRLSRNFGQQAALLAGLDHARGDAVITMDAD 90
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
49-186 2.76e-03

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: 38.06  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  49 KVVNYWLNSLPIKIIKLSKNVGL-GQALNKGLAQCENDYVARMDTDDIcHPKRFEIQIDFLNKNKNISVVGSYIEeFSET 127
Cdd:cd06437   52 IVEEYAAQGVNIKHVRRADRTGYkAGALAEGMKVAKGEYVAIFDADFV-PPPDFLQKTPPYFADPKLGFVQTRWG-HINA 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485892751 128 IENRLS--QKIVPTTHNEIMKNIGKRN----PFNHMTVVFNKSEIIKVGGYEHHYLMEDYNLWLR 186
Cdd:cd06437  130 NYSLLTrvQAMSLDYHFTIEQVARSSTglffNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYR 194
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
17-119 5.76e-03

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 36.84  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485892751  17 YLHECLKSLYEQTKQADEIVLV----YDGpiTNEldkvvnyWLNSL----PIKIIKLSKNVGLGQALNKGLA---QCEND 85
Cdd:cd04185   11 LLKECLDALLAQTRPPDHIIVIdnasTDG--TAE-------WLTSLgdldNIVYLRLPENLGGAGGFYEGVRrayELGYD 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 485892751  86 YVARMDTDDICHPKRFEIQIDFLNKNKNISVVGS 119
Cdd:cd04185   82 WIWLMDDDAIPDPDALEKLLAYADKDNPQFLAPL 115
 
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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