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Conserved domains on  [gi|1717387649|gb|QDX83970|]
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glycosyltransferase [Lactiplantibacillus plantarum]

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 ...
4-204 4.22e-47

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: 157.48  E-value: 4.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVY-NERPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQNDIiKLVFNWENIGLAASLNKAIKLA 82
Cdd:cd04195     1 SVLMSVYiKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPL-KVVPLEKNRGLGKALNEGLKHC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  83 NGELIARMDADDISEPKRLELELRELKRR-SLDLVSGNIVYIDESGSvTGKKSAIPEDERLIAKLLPYGSTIIHPTVLMR 161
Cdd:cd04195    80 TYDWVARMDTDDISLPDRFEKQLDFIEKNpEIDIVGGGVLEFDSDGN-DIGKRRLPTSHDDILKFARRRSPFNHPTVMFR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1717387649 162 KSAIDQVGGYRLLPTAEDYDLWLRMIASGLKIGSINVQVLKYR 204
Cdd:cd04195   159 KSKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-204 4.22e-47

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: 157.48  E-value: 4.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVY-NERPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQNDIiKLVFNWENIGLAASLNKAIKLA 82
Cdd:cd04195     1 SVLMSVYiKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPL-KVVPLEKNRGLGKALNEGLKHC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  83 NGELIARMDADDISEPKRLELELRELKRR-SLDLVSGNIVYIDESGSvTGKKSAIPEDERLIAKLLPYGSTIIHPTVLMR 161
Cdd:cd04195    80 TYDWVARMDTDDISLPDRFEKQLDFIEKNpEIDIVGGGVLEFDSDGN-DIGKRRLPTSHDDILKFARRRSPFNHPTVMFR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1717387649 162 KSAIDQVGGYRLLPTAEDYDLWLRMIASGLKIGSINVQVLKYR 204
Cdd:cd04195   159 KSKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-211 1.34e-28

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 109.41  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   1 MEISVVMSVYNErPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLkALLQTYDQQNDIIKLVFNWENIGLAASLNKAIK 80
Cdd:COG0463     2 PLVSVVIPTYNE-EEYLEEALESLLAQTYPDFEIIVVDDGSTDGTA-EILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  81 LANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDESGSVTGKKSAIPEDERLIAKLLPYGSTIihptVLM 160
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF----RLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717387649 161 RKSAIDQVG---GYrllptAEDYDLwLRMIASGLKIGSINVqvlKYRLRDNSMT 211
Cdd:COG0463   156 RREVLEELGfdeGF-----LEDTEL-LRALRHGFRIAEVPV---RYRAGESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-167 9.46e-26

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: 100.55  E-value: 9.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVYNERPEqVRQSVEAILGQTYLPTEfIIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKLAN 83
Cdd:pfam00535   1 SVIIPTYNEEKY-LLETLESLLNQTYPNFE-IIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  84 GELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDESGSVTGKKSAIPE---DERLIAKLLPYGSTIIHPT-VL 159
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLsrlPFFLGLRLLGLNLPFLIGGfAL 158

                  ....*...
gi 1717387649 160 MRKSAIDQ 167
Cdd:pfam00535 159 YRREALEE 166
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
3-187 1.08e-07

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 52.30  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   3 ISVVMSVYNERPEQVRqSVEAILGQTYLPTEFIIVLDNpnQNDLKALLQTYDQQNDI-IKLVFNWENIGLAASLNKAIKL 81
Cdd:PRK10018    7 ISIYMPTWNRQQLAIR-AIKSVLRQDYSNWEMIIVDDC--STSWEQLQQYVTALNDPrITYIHNDINSGACAVRNQAIML 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  82 ANGELIARMDADDISEPKRLELELRELKRrsldLVSGNIVYIDE---SGSVTGKKSAIP-EDERLIAKLLPYGSTIIHPT 157
Cdd:PRK10018   84 AQGEYITGIDDDDEWTPNRLSVFLAHKQQ----LVTHAFLYANDyvcQGEVYSQPASLPlYPKSPYSRRLFYKRNIIGNQ 159
                         170       180       190
                  ....*....|....*....|....*....|
gi 1717387649 158 VLMRKSAIDQVGGYRLLPTAEDYDLWLRMI 187
Cdd:PRK10018  160 VFTWAWRFKECLFDTELKAAQDYDIFLRMV 189
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-204 4.22e-47

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: 157.48  E-value: 4.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVY-NERPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQNDIiKLVFNWENIGLAASLNKAIKLA 82
Cdd:cd04195     1 SVLMSVYiKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPL-KVVPLEKNRGLGKALNEGLKHC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  83 NGELIARMDADDISEPKRLELELRELKRR-SLDLVSGNIVYIDESGSvTGKKSAIPEDERLIAKLLPYGSTIIHPTVLMR 161
Cdd:cd04195    80 TYDWVARMDTDDISLPDRFEKQLDFIEKNpEIDIVGGGVLEFDSDGN-DIGKRRLPTSHDDILKFARRRSPFNHPTVMFR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1717387649 162 KSAIDQVGGYRLLPTAEDYDLWLRMIASGLKIGSINVQVLKYR 204
Cdd:cd04195   159 KSKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-211 1.34e-28

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 109.41  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   1 MEISVVMSVYNErPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLkALLQTYDQQNDIIKLVFNWENIGLAASLNKAIK 80
Cdd:COG0463     2 PLVSVVIPTYNE-EEYLEEALESLLAQTYPDFEIIVVDDGSTDGTA-EILRELAAKDPRIRVIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  81 LANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDESGSVTGKKSAIPEDERLIAKLLPYGSTIihptVLM 160
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF----RLF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717387649 161 RKSAIDQVG---GYrllptAEDYDLwLRMIASGLKIGSINVqvlKYRLRDNSMT 211
Cdd:COG0463   156 RREVLEELGfdeGF-----LEDTEL-LRALRHGFRIAEVPV---RYRAGESKLN 200
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
3-208 3.82e-28

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: 110.60  E-value: 3.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   3 ISVVMSVYNErPEQVRQSVEAILGQTYLPTEF-IIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKL 81
Cdd:COG1215    31 VSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLeVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  82 ANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYidesgsvtgkksaipederliakllpygstiihptvlmR 161
Cdd:COG1215   110 ARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANLAF--------------------------------------R 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1717387649 162 KSAIDQVGGYRLLPTAEDYDLWLRMIASGLKIGSINVQVLKYRLRDN 208
Cdd:COG1215   152 REALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPET 198
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-206 3.84e-27

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: 105.36  E-value: 3.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   3 ISVVMSVYNERPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKLA 82
Cdd:cd04184     3 ISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALELA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  83 NGELIARMDADDISEPKRLELELRELKRRS-LDLVSGNIVYIDESG---SVTGKKSAIPEderliakLLPYGSTIIHPTV 158
Cdd:cd04184    83 TGEFVALLDHDDELAPHALYEVVKALNEHPdADLIYSDEDKIDEGGkrsEPFFKPDWSPD-------LLLSQNYIGHLLV 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1717387649 159 LmRKSAIDQVGGYRL-LPTAEDYDLWLRMIASGLKIGSINvQVLkYRLR 206
Cdd:cd04184   156 Y-RRSLVRQVGGFREgFEGAQDYDLVLRVSEHTDRIAHIP-RVL-YHWR 201
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-167 9.46e-26

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: 100.55  E-value: 9.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVYNERPEqVRQSVEAILGQTYLPTEfIIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKLAN 83
Cdd:pfam00535   1 SVIIPTYNEEKY-LLETLESLLNQTYPNFE-IIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  84 GELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDESGSVTGKKSAIPE---DERLIAKLLPYGSTIIHPT-VL 159
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLsrlPFFLGLRLLGLNLPFLIGGfAL 158

                  ....*...
gi 1717387649 160 MRKSAIDQ 167
Cdd:pfam00535 159 YRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-193 1.93e-24

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 96.81  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNERPEqVRQSVEAILGQTYLPTEFIIVlDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKLANG 84
Cdd:cd00761     1 VIIPAYNEEPY-LERCLESLLAQTYPNFEVIVV-DDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  85 ELIARMDADDISEPKRLE-LELRELKRRSLDLVSGNIVYidesgsvtgkksaipederliakllpygstiihptvLMRKS 163
Cdd:cd00761    79 EYILFLDADDLLLPDWLErLVAELLADPEADAVGGPGNL------------------------------------LFRRE 122
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1717387649 164 AIDQVGGY--RLLPTAEDYDLWLRMIASGLKI 193
Cdd:cd00761   123 LLEEIGGFdeALLSGEEDDDFLLRLLRGGKVA 154
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
4-212 1.53e-23

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: 95.69  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVYNeRPEQVRQSVEAILGQTYLPTEFIIV--------LDnpnqndlkaLLQTYdqQNDIIKLVFNWENiGLAASL 75
Cdd:cd06433     1 SIITPTYN-QAETLEETIDSVLSQTYPNIEYIVIdggstdgtVD---------IIKKY--EDKITYWISEPDK-GIYDAM 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  76 NKAIKLANGELIARMDADDISEPKRLELELRELKRR-SLDLVSGNIVYIDESGSVTGKKSAIPEDERLIAkllpYGSTII 154
Cdd:cd06433    68 NKGIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHpEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLL----YGMPIC 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1717387649 155 HPTVLMRKSAIDQVGGYRL-LPTAEDYDLWLRMIASGLKIGSINVQVLKYRLRDNSMTS 212
Cdd:cd06433   144 HQATFFRRSLFEKYGGFDEsYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-249 5.81e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.59  E-value: 5.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   1 MEISVVMSVYNeRPEQVRQSVEAILGQTYLPTEFIIVlDNPNQNDLKALLQTYDQQNdiIKLVFNWENIGLAASLNKAIK 80
Cdd:COG1216     3 PKVSVVIPTYN-RPELLRRCLESLLAQTYPPFEVIVV-DNGSTDGTAELLAALAFPR--VRVIRNPENLGFAAARNLGLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  81 LANGELIARMDADDISEPKRLelelrelkrrsldlvsgnivyidesgsvtgkksaipedERLIAkllpygstiiHPTVLM 160
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDWL--------------------------------------ERLLA----------AACLLI 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649 161 RKSAIDQVGGY--RLLPTAEDYDLWLRMIASGLKIGSINVQVLKYRLRDNSMTSNAWKTYVVSR-YIQKLYAQRVHTGDD 237
Cdd:COG1216   111 RREVFEEVGGFdeRFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYLGRNRlLFLRKHGPRPLLRLA 190
                         250
                  ....*....|..
gi 1717387649 238 AFKSDDPDLFAK 249
Cdd:COG1216   191 LLRGLRLRLRGR 202
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
3-208 2.00e-20

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: 88.44  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   3 ISVVMSVYNErpEQ-VRQSVEAILGQTYLPTEF-IIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIgLAASLNKAIK 80
Cdd:cd02525     2 VSIIIPVRNE--EKyIEELLESLLNQSYPKDLIeIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRI-QSAGLNIGIR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  81 LANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDEsgSVTGKKSAIPEDERL--IAKLLPYGSTIIH--P 156
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGE--SKFQKAIAVAQSSPLgsGGSAYRGGAVKIGyvD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1717387649 157 TV---LMRKSAIDQVGGY-RLLPTAEDYDLWLRMIASGLKIGSINVQVLKYRLRDN 208
Cdd:cd02525   157 TVhhgAYRREVFEKVGGFdESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRST 212
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
4-204 2.65e-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: 84.60  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVYN-ER--PEQVrqsvEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIK 80
Cdd:cd04196     1 AVLMATYNgEKylREQL----DSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNFESLLQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  81 LANGELIARMDADDISEPKRLELELR-ELKRRSLDLVSGNIVYIDESGSVTGKK-------SAIPEDERLIAKLLPYGST 152
Cdd:cd04196    77 AADGDYVFFCDQDDIWLPDKLERLLKaFLKDDKPLLVYSDLELVDENGNPIGESffeyqkiKPGTSFNNLLFQNVVTGCT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1717387649 153 IihptvLMRKSAIDqvggyRLLPTAEDY----DLWLRMIASGL-KIGSINVQVLKYR 204
Cdd:cd04196   157 M-----AFNRELLE-----LALPFPDADvimhDWWLALLASAFgKVVFLDEPLILYR 203
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-179 9.27e-17

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: 76.50  E-value: 9.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNErPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKLANG 84
Cdd:cd06423     1 IIVPAYNE-EAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  85 ELIARMDADDISEP---KRLELELRELKRrsLDLVSGNIVYIDESGSVTGKKSAIpEDERLIAKLLPYGSTIIHPTVLM- 160
Cdd:cd06423    80 DIVVVLDADTILEPdalKRLVVPFFADPK--VGAVQGRVRVRNGSENLLTRLQAI-EYLSIFRLGRRAQSALGGVLVLSg 156
                         170       180
                  ....*....|....*....|....
gi 1717387649 161 -----RKSAIDQVGGYRLLPTAED 179
Cdd:cd06423   157 afgafRREALREVGGWDEDTLTED 180
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-193 4.09e-11

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 62.21  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   3 ISVVMSVYNErpEQV-RQSVEAILGQTYlPT---EFIIVLDNPNQNDLkALLQTYDQQNdiIKLVFNWENIGLAASLNKA 78
Cdd:cd06439    31 VTIIIPAYNE--EAViEAKLENLLALDY-PRdrlEIIVVSDGSTDGTA-EIAREYADKG--VKLLRFPERRGKAAALNRA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  79 IKLANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDESGSVTGKK------SAIPEDERLIakllpyGST 152
Cdd:cd06439   105 LALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGSGSGEGlywkyeNWLKRAESRL------GST 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1717387649 153 IIH--PTVLMRKSAidqvggYRLLPT---AEDYDLWLRMIASGLKI 193
Cdd:cd06439   179 VGAngAIYAIRREL------FRPLPAdtiNDDFVLPLRIARQGYRV 218
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-193 1.80e-10

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 58.72  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNeRPEQVRQSVEAILGQTYLPTEFIIVlDNPNQNDLKALLQTYDQQndiIKLVFNWENIGLAASLNKAIKLANG 84
Cdd:cd04186     1 IIIVNYN-SLEYLKACLDSLLAQTYPDFEVIVV-DNASTDGSVELLRELFPE---VRLIRNGENLGFGAGNNQGIREAKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  85 ELIARMDADDISEPKRLELELRELKRRsldlvsgnivyiDESGSVTGKKSAipederliAKLlpygstiihptvLMRKSA 164
Cdd:cd04186    76 DYVLLLNPDTVVEPGALLELLDAAEQD------------PDVGIVGPKVSG--------AFL------------LVRREV 123
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1717387649 165 IDQVGGY--RLLPTAEDYDLWLRMIASGLKI 193
Cdd:cd04186   124 FEEVGGFdeDFFLYYEDVDLCLRARLAGYRV 154
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
5-128 2.24e-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: 56.05  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNeRPEQVRQSVEAILGQTYLPTEfIIVLDNPNQNDLKALLQTYdQQNDIIKLVFNW-ENIG--LAASLNKAIKL 81
Cdd:cd06420     1 LIITTYN-RPEALELVLKSVLNQSILPFE-VIIADDGSTEETKELIEEF-KSQFPIPIKHVWqEDEGfrKAKIRNKAIAA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1717387649  82 ANGELIARMDADDISEPKRLELELRELKRRSldLVSGNIVYIDESGS 128
Cdd:cd06420    78 AKGDYLIFIDGDCIPHPDFIADHIELAEPGV--FLSGSRVLLNEKLT 122
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
3-193 1.57e-08

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: 54.30  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   3 ISVVMSVYNErPEQVRQSVEAILGQTYLPTEfIIVLDNPNQ----NDLKALLQTYdqQNDIIKLVFNWENIGL---AASL 75
Cdd:pfam13641   4 VSVVVPAFNE-DSVLGRVLEAILAQPYPPVE-VVVVVNPSDaetlDVAEEIAARF--PDVRLRVIRNARLLGPtgkSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  76 NKAIKLANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNiVYIDESGSVTgkkSAIPEDE-----------RLIA 144
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTP-VFSLNRSTML---SALGALEfalrhlrmmslRLAL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1717387649 145 KLLPYGSTiihpTVLMRKSAIDQVGGY-RLLPTAEDYDLWLRMIASGLKI 193
Cdd:pfam13641 156 GVLPLSGA----GSAIRREVLKELGLFdPFFLLGDDKSLGRRLRRHGWRV 201
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
10-190 4.86e-08

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 52.79  E-value: 4.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  10 YNERPEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQ-NDIIKLVFNWENIGL-AASLNKAIKLANG--E 85
Cdd:cd06435     7 YEEPPEMVKETLDSLAALDYPNFEVIVIDNNTKDEALWKPVEAHCAQlGERFRFFHVEPLPGAkAGALNYALERTAPdaE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  86 LIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDESGSVTgkKSAIPEDERLIAKL-LP----YGSTIIHPTV-L 159
Cdd:cd06435    87 IIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLF--KRMCYAEYKGFFDIgMVsrneRNAIIQHGTMcL 164
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1717387649 160 MRKSAIDQVGGYRLLPTAEDYDLWLRMIASG 190
Cdd:cd06435   165 IRRSALDDVGGWDEWCITEDSELGLRMHEAG 195
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
3-187 1.08e-07

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 52.30  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   3 ISVVMSVYNERPEQVRqSVEAILGQTYLPTEFIIVLDNpnQNDLKALLQTYDQQNDI-IKLVFNWENIGLAASLNKAIKL 81
Cdd:PRK10018    7 ISIYMPTWNRQQLAIR-AIKSVLRQDYSNWEMIIVDDC--STSWEQLQQYVTALNDPrITYIHNDINSGACAVRNQAIML 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  82 ANGELIARMDADDISEPKRLELELRELKRrsldLVSGNIVYIDE---SGSVTGKKSAIP-EDERLIAKLLPYGSTIIHPT 157
Cdd:PRK10018   84 AQGEYITGIDDDDEWTPNRLSVFLAHKQQ----LVTHAFLYANDyvcQGEVYSQPASLPlYPKSPYSRRLFYKRNIIGNQ 159
                         170       180       190
                  ....*....|....*....|....*....|
gi 1717387649 158 VLMRKSAIDQVGGYRLLPTAEDYDLWLRMI 187
Cdd:PRK10018  160 VFTWAWRFKECLFDTELKAAQDYDIFLRMV 189
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
5-211 4.96e-07

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: 49.76  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNERPeQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYD---QQNDIIKLVFNWEN---IGLAASLNKA 78
Cdd:cd06913     1 IILPVHNGEQ-WLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRkklEDSGVIVLVGSHNSpspKGVGYAKNQA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  79 IKLANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDESGSV--TGKKSAIPEDERLIAKLLPYGSTIIHP 156
Cdd:cd06913    80 IAQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTEryTRWINTLTREQLLTQVYTSHGPTVIMP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1717387649 157 TVLMRKSAIDQVGGY----RLLPtaEDYDLWLRMIASGLKIGSINVQVLKYRLRDNSMT 211
Cdd:cd06913   160 TWFCSREWFSHVGPFdeggKGVP--EDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATT 216
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
10-205 9.59e-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: 49.20  E-value: 9.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  10 YNERPEQVRQSVEAILGQTylptEFIIVLDNPNQNDLKALLQTYDQQNDIIKLvfnWENIGLAASLNKAIKLA---NGEL 86
Cdd:cd02526     6 YNPDLSKLKELLAALAEQV----DKVVVVDNSSGNDIELRLRLNSEKIELIHL---GENLGIAKALNIGIKAAlenGADY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  87 IARMDADDISEP---KRLELELREL-KRRSLDLVSGNIVYIDESgsvtGKKSAIPEDERLIAKLLPYGSTIIHPTVLM-- 160
Cdd:cd02526    79 VLLFDQDSVPPPdmvEKLLAYKILSdKNSNIGAVGPRIIDRRTG----ENSPGVRKSGYKLRIQKEGEEGLKEVDFLIts 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717387649 161 ----RKSAIDQVGGYR--LLPTAEDYDLWLRMIASGLKIGSINVQVLKYRL 205
Cdd:cd02526   155 gsliSLEALEKVGGFDedLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHEL 205
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
5-119 9.64e-07

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: 48.34  E-value: 9.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNERpEQVRQSVEAIL--GQTYLPTEFIIVlDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKLA 82
Cdd:cd04179     1 VVIPAYNEE-ENIPELVERLLavLEEGYDYEIIVV-DDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1717387649  83 NGELIARMDADDISEPKRLELELRELKRRSLDLVSGN 119
Cdd:cd04179    79 RGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGS 115
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
5-190 2.14e-06

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: 47.95  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNERPEQVRQSVEAILGQTYLPTEF-IIVLDNPNQNDLKALLQtydqqndiiKLVFNWENIGL---------AAS 74
Cdd:cd06421     5 VFIPTYNEPLEIVRKTLRAALAIDYPHDKLrVYVLDDGRRPELRALAA---------ELGVEYGYRYLtrpdnrhakAGN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  75 LNKAIKLANGELIARMDADDISEPKRLELELRELKR-RSLDLVSGNIVYIDesgsvtgkksaiPEDERLIAKLLPYGSTI 153
Cdd:cd06421    76 LNNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDdPKVALVQTPQFFYN------------PDPFDWLADGAPNEQEL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717387649 154 IHPTV-----------------LMRKSAIDQVGGYRLLPTAEDYDLWLRMIASG 190
Cdd:cd06421   144 FYGVIqpgrdrwgaafccgsgaVVRREALDEIGGFPTDSVTEDLATSLRLHAKG 197
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-118 5.18e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 47.00  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   1 MEISVVMSVYNERPEQvrqsveAILgqTYL-------PTEF-IIVLDN--PN--QNDLKALLQTYDqqNDIIKLVFNWEN 68
Cdd:PLN02726    9 MKYSIIVPTYNERLNI------ALI--VYLifkalqdVKDFeIIVVDDgsPDgtQDVVKQLQKVYG--EDRILLRPRPGK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1717387649  69 IGLAASLNKAIKLANGELIARMDADDISEPKRLELELRELKRRSLDLVSG 118
Cdd:PLN02726   79 LGLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTG 128
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
10-218 9.75e-06

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: 45.70  E-value: 9.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  10 YNeRPEQVRQSVEAILGQTYLPTEFIIVlDNPNQNDLKALLQTYDQQnDIIKLVFNWENIGLAASLNKAIKLA---NGEL 86
Cdd:cd04185     6 YN-RLDLLKECLDALLAQTRPPDHIIVI-DNASTDGTAEWLTSLGDL-DNIVYLRLPENLGGAGGFYEGVRRAyelGYDW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  87 IARMDADDISEPKRLELELRELKRRSLDLVSGNIVYIDesGSVTGkksaipederliakllpygstiihptVLMRKSAID 166
Cdd:cd04185    83 IWLMDDDAIPDPDALEKLLAYADKDNPQFLAPLVLDPD--GSFVG--------------------------VLISRRVVE 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717387649 167 QVGgyrlLPTAE------DYDLWLRMIASGLKIGSINVQVLKYR--LRDNSMTSN---AWKTY 218
Cdd:cd04185   135 KIG----LPDKEffiwgdDTEYTLRASKAGPGIYVPDAVVVHKTaiNKGSSAVVNidpPWKLY 193
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
2-120 5.28e-05

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 43.78  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   2 EISVVMSVYNERPEQVRQSVEAILGQTylPTEFIIVLDNPNQNDLKALLQTYdQQNDIIKLVFNWENIGLAASLnkAIKL 81
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSILSQTV-KYGGIFVITVPHPGKRRALAE--GIRH 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1717387649  82 ANGELIARMDADDISEPKRLELELRELKRRSLDLVSGNI 120
Cdd:cd06434    76 VTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTNQ 114
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
4-92 1.01e-04

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


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 43.35  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   4 SVVMSVYNERPEQVRQSVEAILGQT--YLPTEFIIVLDNPNQNDLKALLQTYDQ-QNDIIKLVFNWENIGLAASLNKAIK 80
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTppELLKEIILVDDFSDKPELKLLLEEYYKkYLPKVKVLRLKKREGLIRARIAGAR 80
                          90
                  ....*....|..
gi 1717387649  81 LANGELIARMDA 92
Cdd:cd02510    81 AATGDVLVFLDS 92
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
5-118 3.74e-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: 41.01  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   5 VVMSVYNE--R-PEQVRQSVEAILGQTYLPTEFIIVLDNPNQNDLKALLQTYDQQNDIIKLVFNWENIGLAASLNKAIKL 81
Cdd:cd04188     1 VVIPAYNEekRlPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGKGGAVRAGMLA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1717387649  82 ANGELIARMDAD---DISEPKRLElelRELKRRSLDLVSG 118
Cdd:cd04188    81 ARGDYILFADADlatPFEELEKLE---EALKTSGYDIAIG 117
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
90-194 4.66e-04

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: 40.40  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649  90 MDADDISEPKRLELELRELKRRSLDLVSGNIVYiDESGSVTGKKSAIPEDERlIAKLLPYGSTIIHPTVLM------RKS 163
Cdd:pfam13632   5 LDADTVLPPDCLLGIANEMASPEVAIIQGPILP-MNVGNYLEELAALFFADD-HGKSIPVRMALGRVLPFVgsgaflRRS 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717387649 164 AIDQVGGYRLLPTAEDYDLWLRMIASGLKIG 194
Cdd:pfam13632  83 ALQEVGGWDDGSVSEDFDFGLRLQRAGYRVR 113
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-93 5.22e-03

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 38.18  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717387649   2 EISVVMSVYNER---PEQVRQSVEAI--LGQTYlptEFIIVLDNPNQNDLKALLQTYDQ-QNDIIKLVFNwENIGLAASL 75
Cdd:PRK10714    7 KVSVVIPVYNEQeslPELIRRTTAACesLGKEY---EILLIDDGSSDNSAEMLVEAAQApDSHIVAILLN-RNYGQHSAI 82
                          90
                  ....*....|....*...
gi 1717387649  76 NKAIKLANGELIARMDAD 93
Cdd:PRK10714   83 MAGFSHVTGDLIITLDAD 100
 
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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