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Conserved domains on  [gi|488621626|ref|WP_002558339|]
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glycosyltransferase family 4 protein [Bacteroides sp. HPS0048]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-395 3.50e-45

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


:

Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 159.63  E-value: 3.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   4 LYTFGGMPHYLNAMLNKLQAKGVDIVVITPQKGNASIGKGVKMVEsgsykrltspeKKMFYGKTAYPQLPEIIRKEQ--- 80
Cdd:cd03801   10 PPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVI-----------VPLLPSLAALLRARRLLRELRpll 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  81 ----PDILVMGWPYFLQLFfqpelRKAVKSCGTKIVIREIPFQTPPYGKIRAffeaqpmydenmrlqstgmsfYIKQWLT 156
Cdd:cd03801   79 rlrkFDVVHAHGLLAALLA-----ALLALLLGAPLVVTLHGAEPGRLLLLLA---------------------AERRLLA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 157 ARIRKYCYSKVAGTLNYSTAAYdILPSYGVEKEKIHVTYNSTDTEallrEKENVQTAPSILPPNPRRILHIGRLVKWKRV 236
Cdd:cd03801  133 RAEALLRRADAVIAVSEALRDE-LRALGGIPPEKIVVIPNGVDLE----RFSPPLRRKLGIPPDRPVLLFVGRLSPRKGV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 237 DLLIEALPKVIAQFPDTELVIVG-DGPELENLKQqaEQLNLSSYIRFAGSVYKPEvLGTYMNESAVYVLA----GMgGLS 311
Cdd:cd03801  208 DLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEE--LELGLGDRVRFLGFVPDEE-LPALYAAADVFVLPsryeGF-GLV 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 312 INDAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYL 391
Cdd:cd03801  284 VLEAMAAGLPVVATDVGGL-PEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLL 362


                 ....
gi 488621626 392 DAFK 395
Cdd:cd03801  363 DLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-395 3.50e-45

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 159.63  E-value: 3.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   4 LYTFGGMPHYLNAMLNKLQAKGVDIVVITPQKGNASIGKGVKMVEsgsykrltspeKKMFYGKTAYPQLPEIIRKEQ--- 80
Cdd:cd03801   10 PPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVI-----------VPLLPSLAALLRARRLLRELRpll 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  81 ----PDILVMGWPYFLQLFfqpelRKAVKSCGTKIVIREIPFQTPPYGKIRAffeaqpmydenmrlqstgmsfYIKQWLT 156
Cdd:cd03801   79 rlrkFDVVHAHGLLAALLA-----ALLALLLGAPLVVTLHGAEPGRLLLLLA---------------------AERRLLA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 157 ARIRKYCYSKVAGTLNYSTAAYdILPSYGVEKEKIHVTYNSTDTEallrEKENVQTAPSILPPNPRRILHIGRLVKWKRV 236
Cdd:cd03801  133 RAEALLRRADAVIAVSEALRDE-LRALGGIPPEKIVVIPNGVDLE----RFSPPLRRKLGIPPDRPVLLFVGRLSPRKGV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 237 DLLIEALPKVIAQFPDTELVIVG-DGPELENLKQqaEQLNLSSYIRFAGSVYKPEvLGTYMNESAVYVLA----GMgGLS 311
Cdd:cd03801  208 DLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEE--LELGLGDRVRFLGFVPDEE-LPALYAAADVFVLPsryeGF-GLV 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 312 INDAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYL 391
Cdd:cd03801  284 VLEAMAAGLPVVATDVGGL-PEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLL 362


                 ....
gi 488621626 392 DAFK 395
Cdd:cd03801  363 DLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 220-375 1.62e-36

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 130.47  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  220 NPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEVLgTYMNES 299
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLP-ELLKIA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488621626  300 AVYVLAGM---GGLSINDAMTYGMPVICSVCdSTERDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQR 375
Cdd:pfam00534  80 DVFVLPSRyegFGIVLLEAMACGLPVIASDV-GGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 228-399 3.60e-18

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 79.65  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 228 GRLVKWKRVDLLIEAlpkviaqfpdtelvivgdgpelenlkqqaeqlnlssyirfagsvykpevlgtYMNESAVYVL--- 304
Cdd:COG0438    2 GRLVPRKGLDLLLEA----------------------------------------------------LLAAADVFVLpsr 29

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 305 AGMGGLSINDAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINID 384
Cdd:COG0438   30 SEGFGLVLLEAMAAGLPVIATDVGGL-PEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWE 108

                        170
                 ....*....|....*
gi 488621626 385 TVSQRYLDAFKAFMR 399
Cdd:COG0438  109 AIAERLLALYEELLA 123
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
183-376 1.66e-14

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 73.98  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 183 SYGVEKEKIHVTYNSTDT-EALLREKENVQTApsilppnprRILHIGRLV--KWKRVDLLIEALPKVIAQFpdtELVIVG 259
Cdd:PRK09922 150 ARGISAQRISVIYNPVEIkTIIIPPPERDKPA---------VFLYVGRLKfeGQKNVKELFDGLSQTTGEW---QLHIIG 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 260 DGPELENLKQQAEQLNLSSYIRFAGSVYKP--EVLGTYMNESAVYVLAGMGGLSIN--DAMTYGMPVICSVCDSTERDLV 335
Cdd:PRK09922 218 DGSDFEKCKAYSRELGIEQRIIWHGWQSQPweVVQQKIKNVSALLLTSKFEGFPMTllEAMSYGIPCISSDCMSGPRDII 297

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488621626 336 TDGKNGFFFKAGDANSLAEKITTLFSspelcEKMRKESQRI 376
Cdd:PRK09922 298 KPGLNGELYTPGNIDEFVGKLNKVIS-----GEVKYQHDAI 333
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-395 3.50e-45

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 159.63  E-value: 3.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   4 LYTFGGMPHYLNAMLNKLQAKGVDIVVITPQKGNASIGKGVKMVEsgsykrltspeKKMFYGKTAYPQLPEIIRKEQ--- 80
Cdd:cd03801   10 PPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVI-----------VPLLPSLAALLRARRLLRELRpll 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  81 ----PDILVMGWPYFLQLFfqpelRKAVKSCGTKIVIREIPFQTPPYGKIRAffeaqpmydenmrlqstgmsfYIKQWLT 156
Cdd:cd03801   79 rlrkFDVVHAHGLLAALLA-----ALLALLLGAPLVVTLHGAEPGRLLLLLA---------------------AERRLLA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 157 ARIRKYCYSKVAGTLNYSTAAYdILPSYGVEKEKIHVTYNSTDTEallrEKENVQTAPSILPPNPRRILHIGRLVKWKRV 236
Cdd:cd03801  133 RAEALLRRADAVIAVSEALRDE-LRALGGIPPEKIVVIPNGVDLE----RFSPPLRRKLGIPPDRPVLLFVGRLSPRKGV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 237 DLLIEALPKVIAQFPDTELVIVG-DGPELENLKQqaEQLNLSSYIRFAGSVYKPEvLGTYMNESAVYVLA----GMgGLS 311
Cdd:cd03801  208 DLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEE--LELGLGDRVRFLGFVPDEE-LPALYAAADVFVLPsryeGF-GLV 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 312 INDAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYL 391
Cdd:cd03801  284 VLEAMAAGLPVVATDVGGL-PEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLL 362


                 ....
gi 488621626 392 DAFK 395
Cdd:cd03801  363 DLYR 366
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 1-392 4.51e-41

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 148.54  E-value: 4.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   1 MKVLYTFGGMPHYLNAMLNKLQAKGVDIVVITPQKGNAS----IGKGVKMVESGSYKRLTSPEKKMFYgkTAYPQLPEII 76
Cdd:cd03820    6 IPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPpfyeLDDNIKIKNLGDRKYSHFKLLLKYF--KKVRRLRKYL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  77 RKEQPDILV---MGWPYFLQLFFQPelrkavkscgtKIVIREIPFQtppygkirafFEAQPmydenmrlqstgmsfYIKQ 153
Cdd:cd03820   84 KNNKPDVVIsfrTSLLTFLALIGLK-----------SKLIVWEHNN----------YEAYN---------------KGLR 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 154 WLTARIRKY-CYSKVAgTLNystaAYDILPSYGVEKEKIHVTYNstdteALLREKENVQTapsilPPNPRRILHIGRLVK 232
Cdd:cd03820  128 RLLLRRLLYkRADKIV-VLT----EADKLKKYKQPNSNVVVIPN-----PLSFPSEEPST-----NLKSKRILAVGRLTY 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 233 WKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEvlgTYMNESAVYVLA----GMg 308
Cdd:cd03820  193 QKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIA---EEYANSSIFVLSsryeGF- 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 309 GLSINDAMTYGMPVICSVCDSTERDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESqRIILEEINIDTVSQ 388
Cdd:cd03820  269 PMVLLEAMAYGLPIISFDCPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNA-RKNAERFSIEKIIK 347


                 ....
gi 488621626 389 RYLD 392
Cdd:cd03820  348 QWEE 351
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 2-391 5.55e-38

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 140.42  E-value: 5.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   2 KVLY----TFGGMPHYLNaMLNKLQAKGVDIVVITPQKGNAS---IGKGVKMVESGSYKRLTSPEKKMFygktAYPQLPE 74
Cdd:cd03808    1 KILFivnvDGGFQSFRLP-LIKALVKKGYEVHVIAPDGDKLSdelKELGVKVIDIPILRRGINPLKDLK----ALFKLYK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  75 IIRKEQPDILvmgwpyflqlffqpelrkavkSCGT-KIVIreipfqtppYGKIRAFFEAQP--MYdenmrlQSTGMSFY- 150
Cdd:cd03808   76 LLKKEKPDIV---------------------HCHTpKPGI---------LGRLAARLAGVPkvIY------TVHGLGFVf 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 151 ----IKQWLTARIRKYCYSKVAGTLNYSTAAYDILPSYGVEKEKIHVTYNST--DTEALlrekenvQTAPSILPPNPRRI 224
Cdd:cd03808  120 tegkLLRLLYLLLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGSgvDLDRF-------QYSPESLPSEKVVF 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 225 LHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEvlgTYMNESAVYVL 304
Cdd:cd03808  193 LFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVP---ELLAESDVFVL 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 305 A----GMGgLSINDAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEE 380
Cdd:cd03808  270 PsyreGLP-RSLLEAMAAGRPVITTDVPGC-RELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEK 347

                        410
                 ....*....|.
gi 488621626 381 INIDTVSQRYL 391
Cdd:cd03808  348 FDEEKVVNKLL 358
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 220-375 1.62e-36

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 130.47  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  220 NPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEVLgTYMNES 299
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLP-ELLKIA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488621626  300 AVYVLAGM---GGLSINDAMTYGMPVICSVCdSTERDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQR 375
Cdd:pfam00534  80 DVFVLPSRyegFGIVLLEAMACGLPVIASDV-GGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 147-392 3.97e-34

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 130.09  E-value: 3.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 147 MSFYIKQWLTARIRKYCYSKVAGTLNYSTAAYDILPSYGVEKeKIHVTYNSTDTEALLREKENVQTAPSILPPNPRRILH 226
Cdd:cd03817  128 KGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKDTLREYGVKG-PIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEPILLY 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 227 IGRLVKWKRVDLLIEALPKVIAQfPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVyKPEVLGTYMNESAVYVLAG 306
Cdd:cd03817  207 VGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGFV-PREELPEYYKAADLFVFAS 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 307 MG---GLSINDAMTYGMPVICsVCDSTERDLVTDGKNGFFFKAGDANsLAEKITTLFSSPELCEKMRKESqRIILEEINI 383
Cdd:cd03817  285 TTetqGLVYLEAMAAGLPVVA-AKDPAASELVEDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNA-EISAREFAF 361


                 ....*....
gi 488621626 384 DTVSQRYLD 392
Cdd:cd03817  362 AKSVEKLYE 370
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 158-395 5.74e-33

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 127.11  E-value: 5.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 158 RIRKYCYSKVAGTLNYSTAAYDILPSYGVEKEKIHVTYNSTDTEallREKENvqTAPSILPPNPRRILHIGRLVKWKRVD 237
Cdd:cd03798  142 KLLRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPA---RFQPE--DRGLGLPLDAFVILFVGRLIPRKGID 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 238 LLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEVLGtYMNESAVYVLA----GMgGLSIN 313
Cdd:cd03798  217 LLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPA-YYRACDVFVLPsrheGF-GLVLL 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 314 DAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRiILEEINIDTVSQRYLDA 393
Cdd:cd03798  295 EAMACGLPVVATDVGGI-PEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARAR-VAERFSWVKAADRIAAA 372


                 ..
gi 488621626 394 FK 395
Cdd:cd03798  373 YR 374
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 17-377 4.99e-31

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 121.31  E-value: 4.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  17 MLNKLQAKGVDIVVITPQKGNASIGKGVKMVESGSYKRLTSPEKKMFyGKTAYPQLPEIIRKEQPDILV--MGWPYFLQl 94
Cdd:cd03811   21 LANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLG-LLKAILKLKRILKRAKPDVVIsfLGFATYIV- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  95 ffqpelrKAVKSCGTKIVIReipfqtppygkIRAFFEAQPmydenmrlqstgmsfyiKQWLTARIRKYCYSKVAGTL-NY 173
Cdd:cd03811   99 -------AKLAAARSKVIAW-----------IHSSLSKLY-----------------YLKKKLLLKLKLYKKADKIVcVS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 174 STAAYDILPSYGVEKEKIHVTYNSTDTEallREKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDT 253
Cdd:cd03811  144 KGIKEDLIRLGPSPPEKIEVIYNPIDID---RIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDV 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 254 ELVIVGDGPELENLKQQAEQLNLSSYIRFAGsvYKPEVLGtYMNESAVYVLA----GMgGLSINDAMTYGMPVICSVCDS 329
Cdd:cd03811  221 KLVILGDGPLREELEKLAKELGLAERVIFLG--FQSNPYP-YLKKADLFVLSsryeGF-PNVLLEAMALGTPVVSTDCPG 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488621626 330 TeRDLVTDGKNGFFFKAGDANSLAEKITTL---FSSPELCEKMRKESQRII 377
Cdd:cd03811  297 P-REILDDGENGLLVPDGDAAALAGILAALlqkKLDAALRERLAKAQEAVF 346
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
221-361 4.81e-29

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 109.91  E-value: 4.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  221 PRRILHIGRLVKW-KRVDLLIEALPKVIAQFPDTELVIVGDGPElENLKQQAEqlNLSSYIRFAGSVykpEVLGTYMNES 299
Cdd:pfam13692   1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE-EELEELAA--GLEDRVIFTGFV---EDLAELLAAA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488621626  300 AVYVLA----GMgGLSINDAMTYGMPVICSVCDSTeRDLVtDGKNGFFFKAGDANSLAEKITTLFS 361
Cdd:pfam13692  75 DVFVLPslyeGF-GLKLLEAMAAGLPVVATDVGGI-PELV-DGENGLLVPPGDPEALAEAILRLLE 137
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 185-389 1.95e-25

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 106.00  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 185 GVEKEKIHVTYNSTDTEALlrekenvqtAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPEL 264
Cdd:cd05844  162 GLPAERIHVHYIGIDPAKF---------APRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLR 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 265 ENLKQQAEQLnlsSYIRFAGSVYKPEVLgTYMNESAVYVLA----------GMgGLSINDAMTYGMPVICSVCDSTErDL 334
Cdd:cd05844  233 PALQALAAAL---GRVRFLGALPHAEVQ-DWMRRAEIFCLPsvtaasgdseGL-GIVLLEAAACGVPVVSSRHGGIP-EA 306

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488621626 335 VTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQR 389
Cdd:cd05844  307 ILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAK 361
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 206-373 6.07e-25

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 103.92  E-value: 6.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 206 EKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGS 285
Cdd:cd04949  145 YVDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGY 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 286 VYKPEVLgtyMNESAVYVLAGMG---GLSINDAMTYGMPVICSVCDSTERDLVTDGKNGFFFKAGDANSLAEKITTLFSS 362
Cdd:cd04949  225 HSNLDQE---YQDAYLSLLTSQMegfGLTLMEAIGHGLPVVSYDVKYGPSELIEDGENGYLIEKNNIDALADKIIELLND 301

                        170
                 ....*....|.
gi 488621626 363 PELCEKMRKES 373
Cdd:cd04949  302 PEKLQQFSEES 312
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 180-369 1.14e-24

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 103.59  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 180 ILPSYGVEKEKIHVTYNSTDTEALLREKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQfPDTELVIVG 259
Cdd:cd03819  141 LIEALGVDPERIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVAG 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 260 DGPELENLKQQAEQLNLSSYIRFAGsvYKPEVLgTYMNESAVYVLAGMG---GLSINDAMTYGMPVIcSVCDSTERDLVT 336
Cdd:cd03819  220 DGPERDEIRRLVERLGLRDRVTFTG--FREDVP-AALAASDVVVLPSLHeefGRVALEAMACGTPVV-ATDVGGAREIVV 295

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488621626 337 DGKNGFFFKAGDANSLAEKITTLFSSPELCEKM 369
Cdd:cd03819  296 HGRTGLLVPPGDAEALADAIRAAKLLPEAREKL 328
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 8-391 1.55e-24

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 103.96  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   8 GGMPHYLNAMLNKLQAKGVDIVVITPQKGNASIGKGVKMVEsgsykrlTSPEKKMFYGKTAYPQLPEIIRKeqpdiLVMG 87
Cdd:cd03794   14 GAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATE-------TKDGIRVIRVKLGPIKKNGLIRR-----LLNY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  88 WPYFLQLFFQpeLRKAVKSCGTKIVIREIPFQTPPYGKIRAFFEAqPMYDENM-----RLQSTGMSFY-IKQWLTARIRK 161
Cdd:cd03794   82 LSFALAALLK--LLVREERPDVIIAYSPPITLGLAALLLKKLRGA-PFILDVRdlwpeSLIALGVLKKgSLLKLLKKLER 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 162 YCYSKVAGTLNYSTAAYDILPSYGVEKEKIHVTYNSTDTEALLREKENVQTAPSILPpNPRRILHIGRLVKWKRVDLLIE 241
Cdd:cd03794  159 KLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLGLD-DKFVVVYAGNIGKAQGLETLLE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 242 ALpKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIrFAGSVYKPEVLgTYMNES----------AVYVLAGMGGLS 311
Cdd:cd03794  238 AA-ERLKRRPDIRFLFVGDGDEKERLKELAKARGLDNVT-FLGRVPKEEVP-ELLSAAdvglvplkdnPANRGSSPSKLF 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 312 inDAMTYGMPVICSVcDSTERDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYL 391
Cdd:cd03794  315 --EYMAAGKPILASD-DGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 185-383 3.60e-23

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 99.45  E-value: 3.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 185 GVEKEKIHVTYNSTDTEALlrekenvQTAPSILPPN-PRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPE 263
Cdd:cd03799  144 GCDEKKIIVHRSGIDCNKF-------RFKPRYLPLDgKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDL 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 264 LENLKQQAEQLNLSSYIRFAGSVYKPEVLgTYMNESAVYVL-------AGMGGL--SINDAMTYGMPVIcsvcdSTER-- 332
Cdd:cd03799  217 KEQLQQLIQELNIGDCVKLLGWKPQEEII-EILDEADIFIApsvtaadGDQDGPpnTLKEAMAMGLPVI-----STEHgg 290

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488621626 333 --DLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINI 383
Cdd:cd03799  291 ipELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDI 343
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 151-395 7.58e-23

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 98.54  E-value: 7.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 151 IKQWLTARIRKYC--YSKV-AGTLNYSTAAYDILPSYGVEKEKIHVTYNSTDTEALL--REKENVQTAPSILPPNPRRIL 225
Cdd:cd03807  115 IPQRLTRLVRKLCllLSKFsPATVANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSpdDASRARARRRLGLAEDRRVIG 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 226 HIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGsvYKPEVlGTYMNESAVYVLA 305
Cdd:cd03807  195 IVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLG--ERSDV-PALLPAMDIFVLS 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 306 ----GMgGLSINDAMTYGMPVICS-VCDSteRDLVtDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEE 380
Cdd:cd03807  272 srteGF-PNALLEAMACGLPVVATdVGGA--AELV-DDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANE 347

                        250
                 ....*....|....*
gi 488621626 381 INIDTVSQRYLDAFK 395
Cdd:cd03807  348 FSIDAMVRRYETLYY 362
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 149-392 2.64e-22

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 97.05  E-value: 2.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 149 FYIKQWLTARIRKYCYSKVAGTLNYSTA--------AYDILPSYGVEKEKIHVTYNSTDTEALLREKENVQTAPSILPPn 220
Cdd:cd03809  114 LRYPEFFPKRFRLYYRLLLPISLRRADAiitvseatRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPE- 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 221 pRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVG-DGPELENLKQQAEQLNLSSYIRFAGSVYKPEVLGTYmNES 299
Cdd:cd03809  193 -PYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGgKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALY-RGA 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 300 AVYVLAGMG---GLSINDAMTYGMPVICS-------VCdsterdlvtdGKNGFFFKAGDANSLAEKITTLFSSPELCEKM 369
Cdd:cd03809  271 RAFVFPSLYegfGLPVLEAMACGTPVIASnisvlpeVA----------GDAALYFDPLDPESIADAILRLLEDPSLREEL 340

                        250       260
                 ....*....|....*....|...
gi 488621626 370 RkESQRIILEEINIDTVSQRYLD 392
Cdd:cd03809  341 I-RKGLERAKKFSWEKTAEKTLE 362
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 178-384 2.22e-20

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 91.57  E-value: 2.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 178 YDILPsYGVEKEKihvtYNSTDTEALLREKENvqtapsilpPNPRRILHIGRLVKWKRVDLLIEAlpkviAQFPDTELVI 257
Cdd:cd03795  162 VRVIP-LGIDKNV----YNIPRVDFENIKREK---------KGKKIFLFIGRLVYYKGLDYLIEA-----AQYLNYPIVI 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 258 VGDGPELENLKQQAEqLNLSSYIRFAGSVYKPEVLgTYMNESAVYVL-----AGMGGLSINDAMTYGMPVICSVCDSTER 332
Cdd:cd03795  223 GGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEEKV-IYLHLCDVFVFpsvlrSEAFGIVLLEAMMCGKPVISTNIGTGVP 300

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488621626 333 DLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINID 384
Cdd:cd03795  301 YVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAE 352
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 185-396 1.41e-19

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 89.31  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 185 GVEKEKIHVTYNSTDTEALLREKENVQTAPSilppnprRILHIGRLVKWKRVDLLIEALPKviAQFPDTELVIVGDGPEL 264
Cdd:cd03823  162 GLFSARISVIPNAVEPDLAPPPRRRPGTERL-------RFGYIGRLTEEKGIDLLVEAFKR--LPREDIELVIAGHGPLS 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 265 enlkqQAEQLNLSSYIRFAGSvYKPEVLGTYMNESAVYVLAGM----GGLSINDAMTYGMPVICSvcDS---TErdLVTD 337
Cdd:cd03823  233 -----DERQIEGGRRIAFLGR-VPTDDIKDFYEKIDVLVVPSIwpepFGLVVREAIAAGLPVIAS--DLggiAE--LIQP 302

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488621626 338 GKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKesqrIILEEINIDTVSQRYLDAFKA 396
Cdd:cd03823  303 GVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRA----GAEPPRSTESQAEEYLKLYRD 357
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 184-392 1.87e-19

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 89.22  E-value: 1.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 184 YGVEKEKIHVTYNSTDTEaLLR--EKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVG-- 259
Cdd:cd03800  182 YGADPSRINVVPPGVDLE-RFFpvDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGgp 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 260 -DGPEL---ENLKQQAEQLNLSSYIRFAGSVyKPEVLGTYMNESAVYV---LAGMGGLSINDAMTYGMPVICSvCDSTER 332
Cdd:cd03800  261 sDDPLSmdrEELAELAEELGLIDRVRFPGRV-SRDDLPELYRAADVFVvpsLYEPFGLTAIEAMACGTPVVAT-AVGGLQ 338

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 333 DLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYLD 392
Cdd:cd03800  339 DIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT 398
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 8-372 6.25e-19

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 87.35  E-value: 6.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   8 GGMPHYLNAMLNKLQAKGVDIVVITPQKGNASIGKGVKMVESGSYKRLTSPEKKMFYGktAYPQLPEIIRKEQPDILVMG 87
Cdd:cd03814   14 NGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFPLPFYPEYRLALP--LPRRVRRLIKEFQPDIIHIA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626  88 WPYFLQLffqpelrKAVKSCgtkiVIREIPFQTppygkirAFFEAQPMYdenmrLQSTGMSFYIKqWLTARIRKYcYSKV 167
Cdd:cd03814   92 TPGPLGL-------AALRAA----RRLGLPVVT-------SYHTDFPEY-----LSYYTLGPLSW-LAWAYLRWF-HNPF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 168 AGTLNYSTAAYDILPSYGVEKekIHVTYNSTDTEALLREKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKvI 247
Cdd:cd03814  147 DTTLVPSPSIARELEGHGFER--VRLWPRGVDTELFHPSRRDAALRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLP-L 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 248 AQFPDTELVIVGDGPELENLkqQAEQLNlssyIRFAGSVyKPEVLGTYMNESAVYVLAGMG---GLSINDAMTYGMPVIC 324
Cdd:cd03814  224 AASPPVRLVVVGDGPARAEL--EARGPD----VIFTGFL-TGEELARAYASADVFVFPSRTetfGLVVLEAMASGLPVVA 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 488621626 325 SvcDST-ERDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKE 372
Cdd:cd03814  297 A--DAGgPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAAR 343
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 188-397 6.85e-19

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 87.41  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 188 KEKIHVTYNSTDTEALLREKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTeLVIVGDGPELENL 267
Cdd:cd04962  163 DKDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPAK-LLLVGDGPERVPA 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 268 KQQAEQLNLSSYIRFAGSVykPEVLGTYMNESAVYVLAGMG--GLSINDAMTYGMPVICSVCDSTErDLVTDGKNGFFFK 345
Cdd:cd04962  242 EELARELGVEDRVLFLGKQ--DDVEELLSIADLFLLPSEKEsfGLAALEAMACGVPVVSSNAGGIP-EVVKHGETGFLSD 318

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488621626 346 AGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYLDAFKAF 397
Cdd:cd04962  319 VGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 228-399 3.60e-18

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 79.65  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 228 GRLVKWKRVDLLIEAlpkviaqfpdtelvivgdgpelenlkqqaeqlnlssyirfagsvykpevlgtYMNESAVYVL--- 304
Cdd:COG0438    2 GRLVPRKGLDLLLEA----------------------------------------------------LLAAADVFVLpsr 29

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 305 AGMGGLSINDAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINID 384
Cdd:COG0438   30 SEGFGLVLLEAMAAGLPVIATDVGGL-PEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWE 108

                        170
                 ....*....|....*
gi 488621626 385 TVSQRYLDAFKAFMR 399
Cdd:COG0438  109 AIAERLLALYEELLA 123
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 152-392 4.51e-18

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 85.11  E-value: 4.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 152 KQWLTARIRKYCYSKVAGTLNYSTAAYDILPSYGVEkEKIHVTYNSTDTEALLREKENVQTAPsiLPPNPRRILHIGRLV 231
Cdd:cd03821  138 KRIALHLIERRNLNNAALVHFTSEQEADELRRFGLE-PPIAVIPNGVDIPEFDPGLRDRRKHN--GLEDRRIILFLGRIH 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 232 KWKRVDLLIEALPKVIAQFPDTELVIVG-DGPELENLKQQAEQLNLSSYIRFAGSVYkPEVLGTYMNESAVYVLAGM--- 307
Cdd:cd03821  215 PKKGLDLLIRAARKLAEQGRDWHLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTGPLY-GEAKWALYASADLFVLPSYsen 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 308 GGLSINDAMTYGMPVI----CSVCDSTERD--LVTDgkngfffkaGDANSLAEKITTLFSSPELCEKMRKESQRIILEEI 381
Cdd:cd03821  294 FGNVVAEALACGLPVVitdkCGLSELVEAGcgVVVD---------PNVSSLAEALAEALRDPADRKRLGEMARRARQVEE 364

                        250
                 ....*....|...
gi 488621626 382 N--IDTVSQRYLD 392
Cdd:cd03821  365 NfsWEAVAGQLGE 377
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 225-344 2.06e-16

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 77.83  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 225 LHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEVLGTYMNESAVYVL 304
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488621626 305 A----GMgGLSINDAMTYGMPVICSVCDSTeRDLVTDGKNGFFF 344
Cdd:cd01635  194 PsrseGF-GLVLLEAMAAGKPVIATDVGGI-PEFVVDGENGLLV 235
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
183-376 1.66e-14

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 73.98  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 183 SYGVEKEKIHVTYNSTDT-EALLREKENVQTApsilppnprRILHIGRLV--KWKRVDLLIEALPKVIAQFpdtELVIVG 259
Cdd:PRK09922 150 ARGISAQRISVIYNPVEIkTIIIPPPERDKPA---------VFLYVGRLKfeGQKNVKELFDGLSQTTGEW---QLHIIG 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 260 DGPELENLKQQAEQLNLSSYIRFAGSVYKP--EVLGTYMNESAVYVLAGMGGLSIN--DAMTYGMPVICSVCDSTERDLV 335
Cdd:PRK09922 218 DGSDFEKCKAYSRELGIEQRIIWHGWQSQPweVVQQKIKNVSALLLTSKFEGFPMTllEAMSYGIPCISSDCMSGPRDII 297

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488621626 336 TDGKNGFFFKAGDANSLAEKITTLFSspelcEKMRKESQRI 376
Cdd:PRK09922 298 KPGLNGELYTPGNIDEFVGKLNKVIS-----GEVKYQHDAI 333
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 225-356 2.63e-13

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 70.39  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 225 LHIGRLVKWKRVDLLIEA---LPKviaqfpdtELVIVGDGPELENLKQQAeqlnlSSYIRFAGsvYKP-EVLGTYMNESA 300
Cdd:cd03804  203 LTASRLVPYKRIDLAVEAfneLPK--------RLVVIGDGPDLDRLRAMA-----SPNVEFLG--YQPdEVLKELLSKAR 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488621626 301 VYVLAGMG--GLSINDAMTYGMPVICSVCDSTeRDLVTDGKNGFFFKAGDANSLAEKI 356
Cdd:cd03804  268 AFVFAAEEdfGIVPVEAQACGTPVIAFGKGGA-LETVRPGPTGILFGEQTVESLKAAV 324
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 185-375 8.26e-13

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 69.74  E-value: 8.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 185 GVEKEKIHVTYNSTDTEALLREKEnvqtapsilpPNPRRILHIGRLVKWKRVDllieALPKVIAQFPDTELVIVGDGPEL 264
Cdd:PLN02871 237 GVDSESFHPRFRSEEMRARLSGGE----------PEKPLIVYVGRLGAEKNLD----FLKRVMERLPGARLAFVGDGPYR 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 265 ENLKQQAEQLNLSsyirFAGSVYKPEVLGTYmnESA-VYVLAGMG---GLSINDAMTYGMPVICSVCDSTErDLVTD--- 337
Cdd:PLN02871 303 EELEKMFAGTPTV----FTGMLQGDELSQAY--ASGdVFVMPSESetlGFVVLEAMASGVPVVAARAGGIP-DIIPPdqe 375

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488621626 338 GKNGFFFKAGDANSLAEKITTLFSSPELCEKM----RKESQR 375
Cdd:PLN02871 376 GKTGFLYTPGDVDDCVEKLETLLADPELRERMgaaaREEVEK 417
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 217-395 9.90e-13

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 68.95  E-value: 9.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 217 LPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVG-DGPEL------ENLKQQAEQLNLSSYIRFAGSVYKP 289
Cdd:cd03822  183 LPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGeLHPSLaryegeRYRKAAIEELGLQDHVDFHNNFLPE 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 290 EVLGTYMNESAVYVL-------AGMGGLSIndAMTYGMPVICSVCDStERDLVTDGkNGFFFKAGDANSLAEKITTLFSS 362
Cdd:cd03822  263 EEVPRYISAADVVVLpylnteqSSSGTLSY--AIACGKPVISTPLRH-AEELLADG-RGVLVPFDDPSAIAEAILRLLED 338

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488621626 363 PELCEKMRKESQRiILEEINIDTVSQRYLDAFK 395
Cdd:cd03822  339 DERRQAIAERAYA-YARAMTWESIADRYLRLFN 370
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 185-286 4.10e-12

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 67.26  E-value: 4.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 185 GVEKEKIHVTYNSTDTEALlrekenvQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPEL 264
Cdd:cd03796  164 SLDPRIVSVIPNAVDSSDF-------TPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKR 236

                         90       100
                 ....*....|....*....|..
gi 488621626 265 ENLKQQAEQLNLSSYIRFAGSV 286
Cdd:cd03796  237 IELEEMREKYQLQDRVELLGAV 258
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 183-395 6.08e-12

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 66.59  E-value: 6.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 183 SYGVEKEKIHVTYNSTDTE-------ALLREKENV-QTAPSILppnprrILHIGRLVKWKRVDLLIEALpKVIAQFPDTE 254
Cdd:cd03825  155 SPLLKGLPVVVIPNGIDTEifapvdkAKARKRLGIpQDKKVIL------FGAESVTKPRKGFDELIEAL-KLLATKDDLL 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 255 LVIVGDGPElenlkqqaEQLNLSSYIRFAGSVYKPEVLGTYMNESAVYVLAGMG---GLSINDAMTYGMPVICSVCDSTe 331
Cdd:cd03825  228 LVVFGKNDP--------QIVILPFDIISLGYIDDDEQLVDIYSAADLFVHPSLAdnlPNTLLEAMACGTPVVAFDTGGS- 298

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488621626 332 RDLVTDGKNGFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYLDAFK 395
Cdd:cd03825  299 PEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYK 362
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 158-386 2.46e-11

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 64.39  E-value: 2.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 158 RIRKYCYSKV----AGTLNYSTAAYDILPSY-GVEKEKIHVTYNSTDTEALLRE---KENVQTAPSILPpNPRRILHIGR 229
Cdd:cd04951  118 RIRMFIYRLTdflcDITTNVSREALDEFIAKkAFSKNKSVPVYNGIDLNKFKKDinvRLKIRNKLNLKN-DEFVILNVGR 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 230 LVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKpevLGTYMNESAVYVLAGMG- 308
Cdd:cd04951  197 LTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQISN---ISEYYNAADLFVLSSEWe 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 309 --GLSINDAMTYGMPVICSvcDSTERDLVTDGKNgFFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTV 386
Cdd:cd04951  274 gfGLVVAEAMACERPVVAT--DAGGVAEVVGDHN-YVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTI 350
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 186-376 9.33e-10

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 59.61  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 186 VEKEKIHVTYNSTDTEALL--REKENVQTAPSILPpNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGDGPE 263
Cdd:cd03812  155 VENGKFKVIPNGIDIEKYKfnKEKRRKRRKLLILE-DKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGEL 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 264 LENLKQQAEQLNLSSYIRFAGSVYKPEvlgTYMNESAVYVLA----GMGGLSInDAMTYGMPVICSvcDSTERDLVTdGK 339
Cdd:cd03812  234 KEKIKEKVKELGLEDKVIFLGFRNDVS---EILSAMDVFLFPslyeGLPLVAV-EAQASGLPCLLS--DTITKECDI-TN 306

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488621626 340 NGFFFKAGDANSL-AEKITTLFSspelcEKMRKESQRI 376
Cdd:cd03812  307 NVEFLPLNETPSTwAEKILKLIK-----RKRRINKEIN 339
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 223-384 5.50e-09

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 57.47  E-value: 5.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 223 RILHIGRLVKWKRVDLLIEALPKVIAQFPDT--ELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEVLGTYMNESA 300
Cdd:cd04946  226 RLVSCSSIVPVKRIDLIIETLNSLCVAHPSIciSWTHIGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLYKENDV 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 301 ---VYVLAGMG-GLSINDAMTYGMPVIcSVCDSTERDLVTDGKNGFFFKAGDANS-LAEKITTLFSSPELCEKMRKESQR 375
Cdd:cd04946  306 dvfVNVSESEGiPVSIMEAISFGIPVI-ATNVGGTREIVENETNGLLLDKDPTPNeIVSSIMKFYLDGGDYKTMKISARE 384


                 ....*....
gi 488621626 376 IILEEINID 384
Cdd:cd04946  385 CWEERFNAE 393
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 216-392 2.12e-08

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 55.83  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 216 ILPPNPRRILHIGR-LVKWKRVDLLIEALPKVIAQFPDTELVIVGDG--------PELENLKQQA-EQLNLS-SYIRFAG 284
Cdd:cd03818  208 ELKAGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDARVVVVGGDgvsygsppPDGGSWKQKMlAELGVDlERVHFVG 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 285 SV-YkpEVLGTYMNESAVYVLAGMGGL---SINDAMTYGMPVICSvcdSTE--RDLVTDGKNGFFFKAGDANSLAEKITT 358
Cdd:cd03818  288 KVpY--DQYVRLLQLSDAHVYLTYPFVlswSLLEAMACGCPVIGS---DTApvREVIRDGRNGLLVDFFDPDALAAAVLE 362

                        170       180       190
                 ....*....|....*....|....*....|....
gi 488621626 359 LFSSPELCEKMRKESQRIILEEINIDTVSQRYLD 392
Cdd:cd03818  363 LLEDPDRAAALRRAARRTVERSDSLDVCLARYLA 396
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 142-395 6.78e-08

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 54.26  E-value: 6.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 142 LQST-GMSFYIKQWLT--ARIRKYCY--SKVAGTLNYSTAAYDILpsYGVEKEKIHVTYNSTDTEA---LLREKENvqta 213
Cdd:cd03813  217 LQSTwIMGYIKKLWIRffERLGKLAYqqADKIISLYEGNRRRQIR--LGADPDKTRVIPNGIDIQRfapAREERPE---- 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 214 psilpPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVG---DGPE-LENLKQQAEQLNLSSYIRFAGSVYKP 289
Cdd:cd03813  291 -----KEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGpedEDPEyAQECKRLVASLGLENKVKFLGFQNIK 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 290 EVLGtymnESAVYVLA----GMgGLSINDAMTYGMPVICSVCDSTeRDLVTDGKNGfFFKAG------DANSLAEKITTL 359
Cdd:cd03813  366 EYYP----KLGLLVLTsiseGQ-PLVILEAMASGVPVVATDVGSC-RELIYGADDA-LGQAGlvvppaDPEALAEALIKL 438

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 488621626 360 FSSPELCEKMRKESQRIILEEINIDTVSQRYLDAFK 395
Cdd:cd03813  439 LRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
8-201 6.41e-07

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 49.07  E-value: 6.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626    8 GGMPHYLNAMLNKLQAKGVDIVVITPQKGNASIGKGVKMVESGSYKRLTSPEKKMFYgkTAYPQLPEIIRKEQPDIL-VM 86
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSL--AFLRRLRRLLRRERPDVVhAH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626   87 GWPYFLqlffqPELRKAVKSCGTKIVIReipFQTPPYGKIRAFFEAQPmydenmrlqstgmsfyiKQWLTARIRKYCYSK 166
Cdd:pfam13439  79 SPFPLG-----LAALAARLRLGIPLVVT---YHGLFPDYKRLGARLSP-----------------LRRLLRRLERRLLRR 133

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 488621626  167 VAGTLNYSTAAYDIL-PSYGVEKEKIHVTYNSTDTE 201
Cdd:pfam13439 134 ADRVIAVSEAVADELrRLYGVPPEKIRVIPNGVDLE 169
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
217-371 1.35e-06

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 50.09  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 217 LPPNPRRIL--HIGRLVKWKRVDLLIEALPKVIAQfpDTELVIVGDG-PELEN-LKQQAEQL--NLSSYIRFagsvykpe 290
Cdd:COG0297  289 LPVDPDAPLigMVSRLTEQKGLDLLLEALDELLEE--DVQLVVLGSGdPEYEEaFRELAARYpgRVAVYIGY-------- 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 291 vlgtymNES---AVYvlAG-----MG------GLS--IndAMTYG-MPVICSV---CDS-TERDLVTDGKNGFFFKAGDA 349
Cdd:COG0297  359 ------DEAlahRIY--AGadfflMPsrfepcGLNqmY--ALRYGtVPIVRRTgglADTvIDYNEATGEGTGFVFDEYTA 428

                        170       180
                 ....*....|....*....|....*
gi 488621626 350 NSLAEKI---TTLFSSPELCEKMRK 371
Cdd:COG0297  429 EALLAAIrraLALYRDPEAWRKLQR 453
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 217-371 3.81e-06

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 48.71  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 217 LPPNPRRIL--HIGRLVKWKRVDLLIEALPKVIAQfpDTELVIVGDG-PELEN-LKQQAEQL--NLSSYIRFAgsvykpE 290
Cdd:cd03791  288 LPVDPDAPLfgFVGRLTEQKGVDLILDALPELLEE--GGQLVVLGSGdPEYEQaFRELAERYpgKVAVVIGFD------E 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 291 VLGTYMNESAVYVLagM------GGLS--IndAMTYGMPVICS--------VcdsTERDLVTDGKNGFFFKAGDANSLAE 354
Cdd:cd03791  360 ALAHRIYAGADFFL--MpsrfepCGLVqmY--AMRYGTLPIVRrtggladtV---FDYDPETGEGTGFVFEDYDAEALLA 432

                        170       180
                 ....*....|....*....|
gi 488621626 355 KIT---TLFSSPELCEKMRK 371
Cdd:cd03791  433 ALRralALYRNPELWRKLQK 452
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 185-389 3.97e-05

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 45.27  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 185 GVEKEKIHVTYNSTDTEALLREKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQ---FPDTELVIVG-- 259
Cdd:cd03805  175 SLAKNPPEVLYPCVDTDSFDSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKlpeFENVRLVIAGgy 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 260 DGPELEN------LKQQAEQL-NLSSYIRFAGSVykPEVLGTYMNESAVYVLA-------GMGGLsinDAMTYGMPVIcs 325
Cdd:cd03805  255 DPRVAENveyleeLQRLAEELlNVEDQVLFLRSI--SDSQKEQLLSSALALLYtpsnehfGIVPL---EAMYAGKPVI-- 327

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488621626 326 VCDS---TERdlVTDGKNGfFFKAGDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQR 389
Cdd:cd03805  328 ACNSggpLET--VVEGVTG-FLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAER 391
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 167-375 2.45e-04

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 43.10  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 167 VAGTLNYSTAAYDILPSYGVEKEKIHVTYNSTDTEALLREKENVQTAPSILPPNPRRILHIG---RLVKWKRVDLLIEAL 243
Cdd:PRK15179 460 VALSSNSQFAAHRYADWLGVDERRIPVVYNGLAPLKSVQDDACTAMMAQFDARTSDARFTVGtvmRVDDNKRPFLWVEAA 539

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 244 PKVIAQFPDTELVIVGDGPELENLKQQAEQLNLSSYIRFAGSVYKPEVLGTYMNesAVYVLAGMGGLS--INDAMTYGMP 321
Cdd:PRK15179 540 QRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFN--AFLLLSRFEGLPnvLIEAQFSGVP 617

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 322 VICSVCDSTErDLVTDGKNGFFFKAGD------ANSLAEKITTLFSSPELCEKMRKESQR 375
Cdd:PRK15179 618 VVTTLAGGAG-EAVQEGVTGLTLPADTvtapdvAEALARIHDMCAADPGIARKAADWASA 676
PRK14099 PRK14099
glycogen synthase GlgA;
134-369 7.01e-04

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 41.63  E-value: 7.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 134 PMYDENMRLQSTGMSfyikqwLTARIRKYCySKVAGTLN-YSTAAYDilPSygvEKEKIHVTYNSTDTEALLREKENVQT 212
Cdd:PRK14099 218 PTYALEIQGPEAGMG------LDGLLRQRA-DRLSGILNgIDTAVWN--PA---TDELIAATYDVETLAARAANKAALQA 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 213 APSiLPPNPRRILH--IGRLVKWKRVDLLIEALPKVIAQfpDTELVIVGDG-PELENLKQQAEQlnlssyiRFAGSVykP 289
Cdd:PRK14099 286 RFG-LDPDPDALLLgvISRLSWQKGLDLLLEALPTLLGE--GAQLALLGSGdAELEARFRAAAQ-------AYPGQI--G 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 290 EVLGtYMNESAVYVLAGMG-----------GLSINDAMTYG-MPVIC-------SVCDSTERDLVTDGKNGFFFKAGDAN 350
Cdd:PRK14099 354 VVIG-YDEALAHLIQAGADallvpsrfepcGLTQLCALRYGaVPVVArvggladTVVDANEMAIATGVATGVQFSPVTAD 432

                        250       260
                 ....*....|....*....|..
gi 488621626 351 SLA---EKITTLFSSPELCEKM 369
Cdd:PRK14099 433 ALAaalRKTAALFADPVAWRRL 454
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
191-390 7.02e-04

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 41.31  E-value: 7.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 191 IHVTYNSTDTEALLREKENVQTAPSILPPNPRRILHIGRLVKWKRVDLLIEALPKVIAQFPDTELVIVGD---------G 261
Cdd:PRK15484 163 ISIVPNGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDptasskgekA 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488621626 262 PELENLKQQAEQlnLSSYIRFAGSVyKPEVLGTYMNESAVYVLAG-------MGGLsinDAMTYGMPVICSVCDSTErDL 334
Cdd:PRK15484 243 AYQKKVLEAAKR--IGDRCIMLGGQ-PPEKMHNYYPLADLVVVPSqveeafcMVAV---EAMAAGKPVLASTKGGIT-EF 315

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488621626 335 VTDGKNGFFFKAG-DANSLAEKITTLFSSPELCEkMRKESQRIILEEINIDTVSQRY 390
Cdd:PRK15484 316 VLEGITGYHLAEPmTSDSIISDINRTLADPELTQ-IAEQAKDFVFSKYSWEGVTQRF 371
glgA PRK00654
glycogen synthase GlgA;
227-275 2.23e-03

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 40.10  E-value: 2.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488621626 227 IGRLVKWKRVDLLIEALPKVIAQfpDTELVIVGDG-PELEN-LKQQAEQLN 275
Cdd:PRK00654 288 VSRLTEQKGLDLVLEALPELLEQ--GGQLVLLGTGdPELEEaFRALAARYP 336
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
323-392 2.78e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 36.81  E-value: 2.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488621626  323 ICSVCDSTE--RDLVTDGKNGFFFKagDANSLAEKITTLFSSPELCEKMRKESQRIILEEINIDTVSQRYLD 392
Cdd:pfam13524  24 APLLTDRTPglEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAEQLLD 93
 
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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