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Conserved domains on  [gi|446556883|ref|WP_000634229|]
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MULTISPECIES: glycosyltransferase family 4 protein [Enterobacteriaceae]

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 ...
 3-368 6.13e-49

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: 168.87  E-value: 6.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   3 VAFCLYKYFPF-GGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIFELIkVPVKSHTNHGRNAEYFAWVQK---HLRE 78
Cdd:cd03801    2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDG-VIVPLLPSLAALLRARRLLRElrpLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  79 HPVDRVVGFNKMPGLDVYYAADVCYAEKVAQEKGFFYRLTSRYR--HYAAFERATFEQGKPTQLLMLTDKQIADFQKHYQ 156
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALLRRADAVIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 157 TEAERFHILPPGIYPDRKYSQqpansreiFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVGQ 236
Cdd:cd03801  161 IPPEKIVVIPNGVDLERFSPP--------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR-GPDVRLVIVGG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 237 DKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANC 314
Cdd:cd03801  232 DGPLRAELEELELGLGDRVRFlgFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEG 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446556883 315 GEaIAEPFRQETLNEFLRKALTQSSLRQAWAENARhyADTQDLYSLPEKAADII 368
Cdd:cd03801  312 GL-VVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-368 6.13e-49

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: 168.87  E-value: 6.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   3 VAFCLYKYFPF-GGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIFELIkVPVKSHTNHGRNAEYFAWVQK---HLRE 78
Cdd:cd03801    2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDG-VIVPLLPSLAALLRARRLLRElrpLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  79 HPVDRVVGFNKMPGLDVYYAADVCYAEKVAQEKGFFYRLTSRYR--HYAAFERATFEQGKPTQLLMLTDKQIADFQKHYQ 156
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALLRRADAVIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 157 TEAERFHILPPGIYPDRKYSQqpansreiFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVGQ 236
Cdd:cd03801  161 IPPEKIVVIPNGVDLERFSPP--------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR-GPDVRLVIVGG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 237 DKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANC 314
Cdd:cd03801  232 DGPLRAELEELELGLGDRVRFlgFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEG 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446556883 315 GEaIAEPFRQETLNEFLRKALTQSSLRQAWAENARhyADTQDLYSLPEKAADII 368
Cdd:cd03801  312 GL-VVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 196-350 3.12e-37

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: 132.01  E-value: 3.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  196 QYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVG-QDKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAAD 272
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEK-NPNLKLVIAGdGEEEKRLKKLAEKLGLGDNVIFlgFVSDEDLPELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446556883  273 LLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEFLRKALTQSSLRQAWAENARH 350
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETG-FLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 267-368 1.36e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 75.41  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 267 LMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEFLRKALTQSSLRQAWAE 346
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETG-LLVPPGDPEALAEAILRLLEDPELRRRLGE 95

                         90       100
                 ....*....|....*....|..
gi 446556883 347 NARHYAdtQDLYSLPEKAADII 368
Cdd:COG0438   96 AARERA--EERFSWEAIAERLL 115
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
150-351 6.59e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 54.03  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 150 DFQKHYQTEAErFHILPPGIYPDrKYSQQPansREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLpDSLRHNT 229
Cdd:PRK15484 152 KFYEERLPNAD-ISIVPNGFCLE-TYQSNP---QPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKL-ATAHSNL 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 230 LLYVVGQD-KPRKFEALAEKRGVR-------SNVHFFSGR--NDVSELMAAADLLLHPA-YQEAAGIVLLEAITAGLPVL 298
Cdd:PRK15484 226 KLVVVGDPtASSKGEKAAYQKKVLeaakrigDRCIMLGGQppEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVL 305

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446556883 299 TTAVCGYAHYIVDANCGEAIAEPFRQETLNEFLRKALTQSSLRQAwAENARHY 351
Cdd:PRK15484 306 ASTKGGITEFVLEGITGYHLAEPMTSDSIISDINRTLADPELTQI-AEQAKDF 357
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 244-302 7.92e-03

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 37.99  E-value: 7.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446556883 244 ALAEKRGVRSNVHFFSGRNdVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAV 302
Cdd:NF038011 358 SLVASLGLQDKVKFLGFQK-IDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDV 415
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-368 6.13e-49

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: 168.87  E-value: 6.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   3 VAFCLYKYFPF-GGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIFELIkVPVKSHTNHGRNAEYFAWVQK---HLRE 78
Cdd:cd03801    2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDG-VIVPLLPSLAALLRARRLLRElrpLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  79 HPVDRVVGFNKMPGLDVYYAADVCYAEKVAQEKGFFYRLTSRYR--HYAAFERATFEQGKPTQLLMLTDKQIADFQKHYQ 156
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALLRRADAVIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 157 TEAERFHILPPGIYPDRKYSQqpansreiFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVGQ 236
Cdd:cd03801  161 IPPEKIVVIPNGVDLERFSPP--------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR-GPDVRLVIVGG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 237 DKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANC 314
Cdd:cd03801  232 DGPLRAELEELELGLGDRVRFlgFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEG 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446556883 315 GEaIAEPFRQETLNEFLRKALTQSSLRQAWAENARhyADTQDLYSLPEKAADII 368
Cdd:cd03801  312 GL-VVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 196-350 3.12e-37

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: 132.01  E-value: 3.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  196 QYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVG-QDKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAAD 272
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEK-NPNLKLVIAGdGEEEKRLKKLAEKLGLGDNVIFlgFVSDEDLPELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446556883  273 LLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEFLRKALTQSSLRQAWAENARH 350
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETG-FLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 147-369 2.36e-23

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: 100.01  E-value: 2.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 147 QIADFQK-HYQTEAERFHILPPGIYPDRKYsqqPANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDsL 225
Cdd:cd03800  173 QEADELIsLYGADPSRINVVPPGVDLERFF---PVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE-L 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 226 RHNTLLYVVG------QDKPR-KFEALAEKRGVRSNVHFFSG--RNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLP 296
Cdd:cd03800  249 RELANLVLVGgpsddpLSMDReELAELAEELGLIDRVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTP 328

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446556883 297 VLTTAVCGYAHYIVDANCGEAIaEPFRQETLNEFLRKALTQSSLRQAWAENARHYAdtQDLYSLPEKAADIIT 369
Cdd:cd03800  329 VVATAVGGLQDIVRDGRTGLLV-DPHDPEALAAALRRLLDDPALWQRLSRAGLERA--RAHYTWESVADQLLT 398
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 12-353 6.35e-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: 95.51  E-value: 6.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  12 PFGGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIFELIKVPVKSHTNHGRNAEYFAWVQKHLREHP----VDRVVGF 87
Cdd:cd03809   12 RLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPkkdkPDLLHSP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  88 NKMPGLDVYYAADVCY-----AEKVAQEKGFFYRLTSRYRHYAAFERATfeqgkptqlLMLTDKQ--IADFQKHYQTEAE 160
Cdd:cd03809   92 HNTAPLLLKGCPQVVTihdliPLRYPEFFPKRFRLYYRLLLPISLRRAD---------AIITVSEatRDDIIKFYGVPPE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 161 RFHILPPGIypDRKYSQQPANSREIFRKKngitEQQYLLLQVGSDFTRKGVDRSIEALASLPDSLR-HNtlLYVVGQ--D 237
Cdd:cd03809  163 KIVVIPLGV--DPSFFPPESAAVLIAKYL----LPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGdLK--LVIVGGkgW 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 238 KPRKFEALAEKRGVRSNVHFFSG--RNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTT------AVCGYAHYI 309
Cdd:cd03809  235 EDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASnisvlpEVAGDAALY 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 446556883 310 VDANCGEAIAEPFRQETLNEFLRKALTQSSLRQA----WAENARHYAD 353
Cdd:cd03809  315 FDPLDPESIADAILRLLEDPSLREELIRKGLERAkkfsWEKTAEKTLE 362
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 10-351 1.88e-21

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: 93.96  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  10 YFPFGGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIFELIKVPVKShTNHGRNAEYFAWVQKHLREHPVDrVVGFN- 88
Cdd:cd03819    7 ALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLK-VPLLRALLGNVRLARLIRRERID-LIHAHs 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  89 KMPGLDVYYAADVCYAEKVAQEKGFfYRLTSRYRHYAAFERAtfeqgkptqllmLTDKQIA--DFQKHYQTEA-----ER 161
Cdd:cd03819   85 RAPAWLGWLASRLTGVPLVTTVHGS-YLATYHPKDFALAVRA------------RGDRVIAvsELVRDHLIEAlgvdpER 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 162 FHILPPGIYPDRKYSQQPANSREIFRKKNGIteqqYLLLQVGSDFTRKGVDRSIEALASLPDSLrhNTLLYVVGQDKPR- 240
Cdd:cd03819  152 IRVIPNGVDTDRFPPEAEAEERAQLGLPEGK----PVVGYVGRLSPEKGWLLLVDAAAELKDEP--DFRLLVAGDGPERd 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 241 KFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAH--------YIVDA 312
Cdd:cd03819  226 EIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREivvhgrtgLLVPP 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446556883 313 NCGEAIAEPFRQETLNEFLRKAL-TQSSLRQAWAENARHY 351
Cdd:cd03819  306 GDAEALADAIRAAKLLPEAREKLqAAAALTEAVRELLLRV 345
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 146-353 2.86e-21

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: 93.98  E-value: 2.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 146 KQIADFQKHYQTEAERFHILPPGIypDRKYSQqPANSREIFRKKngiteqQYLLLQVGSDFTRKGVDRSIEALASLPDSL 225
Cdd:cd03798  159 KALAEELVALGVPRDRVDVIPNGV--DPARFQ-PEDRGLGLPLD------AFVILFVGRLIPRKGIDLLLEAFARLAKAR 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 226 RHNTLLyVVGQDKPR-KFEALAEKRGVRSNVHFFsGR---NDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTA 301
Cdd:cd03798  230 PDVVLL-IVGDGPLReALRALAEDLGLGDRVTFT-GRlphEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATD 307

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446556883 302 VCGYAHYIVDANCGEaIAEPFRQETLNEFLRKALTQSSLRQAWAENARHYAD 353
Cdd:cd03798  308 VGGIPEVVGDPETGL-LVPPGDADALAAALRRALAEPYLRELGEAARARVAE 358
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 3-359 4.27e-21

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: 93.19  E-value: 4.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   3 VAFCLYKyFPFGGLQRDFMRIAQTVAARGHHV--------RVYAQSWEGECPDIFELIKVPVKshtNHGRNAEYFAWVQK 74
Cdd:cd03811    2 ILFVIPS-LSGGGAERVLLNLANALDKRGYDVtlvllrdeGDLDKQLNGDVKLIRLLIRVLKL---IKLGLLKAILKLKR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  75 HLREHPVDRVVGFNkmpGLDVYYAADVCYAE--KVAQEKGFF----YRLTSRYRHYAAFERATfeqgkptQLLMLTDKQI 148
Cdd:cd03811   78 ILKRAKPDVVISFL---GFATYIVAKLAAARskVIAWIHSSLsklyYLKKKLLLKLKLYKKAD-------KIVCVSKGIK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 149 ADFQKHYQTEAERFHILPPGIypDRKYSQQPANSREIFRKKNGITeqqylLLQVGSDFTRKGVDRSIEALASLPDSlRHN 228
Cdd:cd03811  148 EDLIRLGPSPPEKIEVIYNPI--DIDRIRALAKEPILNEPEDGPV-----ILAVGRLDPQKGHDLLIEAFAKLRKK-YPD 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 229 TLLYVVGQDKPR-KFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAvCGYAH 307
Cdd:cd03811  220 VKLVILGDGPLReELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTD-CPGPR 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446556883 308 YIVDANcGEAIAEPFRQETLNEFLRKALTQSSLRQawaENARHYADTQDLYS 359
Cdd:cd03811  299 EILDDG-ENGLLVPDGDAAALAGILAALLQKKLDA---ALRERLAKAQEAVF 346
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 10-351 1.66e-20

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: 91.61  E-value: 1.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  10 YFPFGGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDifELIKVPVKSHTNHGRNAEYFAWV---QKHLREHPVDRVVG 86
Cdd:cd03807    8 GLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGE--ELLAAGVPVVCLGLSSGKDPGVLlrlAKLIRKRNPDVVHT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  87 FnkMPGLDVY--YAADVCYAEKV---AQEKGFFYRLTsryRHYAAFERATFeqgKPTQLLMLTDKQIADFQKHYQTEAER 161
Cdd:cd03807   86 W--MYHADLIggLAAKLAGGVKViwsVRSSNIPQRLT---RLVRKLCLLLS---KFSPATVANSSAVAEFHQEQGYAKNK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 162 FHILPPGIYPDRkySQQPANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVGQDKPRK 241
Cdd:cd03807  158 IVVIYNGIDLFK--LSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVET-HPDLRLLLVGRGPERP 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 242 -FEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVcGYAHYIVDANCGeaIAE 320
Cdd:cd03807  235 nLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDV-GGAAELVDDGTG--FLV 311

                        330       340       350
                 ....*....|....*....|....*....|..
gi 446556883 321 PFRQ-ETLNEFLRKALTQSSLRQAWAENARHY 351
Cdd:cd03807  312 PAGDpQALADAIRALLEDPEKRARLGRAARER 343
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 140-368 4.62e-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: 84.73  E-value: 4.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 140 LLMLTDKQIADFQKHYQTEAERFhILPPGIYPDRKysqQPANSReifRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALA 219
Cdd:cd03821  155 LVHFTSEQEADELRRFGLEPPIA-VIPNGVDIPEF---DPGLRD---RRKHNGLEDRRIILFLGRIHPKKGLDLLIRAAR 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 220 SLPDSlRHNTLLYVVGQDKP--RKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGL 295
Cdd:cd03821  228 KLAEQ-GRDWHLVIAGPDDGayPAFLQLQSSLGLGDRVTFtgPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGL 306

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446556883 296 PVLTTAVCGYAHYiVDANCGeAIAEPfRQETLNEFLRKALTQSSLRQAWAENARHYADTQDLYSLPEKAADII 368
Cdd:cd03821  307 PVVITDKCGLSEL-VEAGCG-VVVDP-NVSSLAEALAEALRDPADRKRLGEMARRARQVEENFSWEAVAGQLG 376
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
198-320 8.93e-18

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 79.09  E-value: 8.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  198 LLLQVGS-DFTRKGVDRSIEALASLpDSLRHNTLLYVVGQDKPRKFEALAekRGVRSNVHFFSGRNDVSELMAAADLLLH 276
Cdd:pfam13692   3 VILFVGRlHPNVKGVDYLLEAVPLL-RKRDNDVRLVIVGDGPEEELEELA--AGLEDRVIFTGFVEDLAELLAAADVFVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446556883  277 PAYQEAAGIVLLEAITAGLPVLTTAVCGYAH-------YIVDANCGEAIAE 320
Cdd:pfam13692  80 PSLYEGFGLKLLEAMAAGLPVVATDVGGIPElvdgengLLVPPGDPEALAE 130
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 267-368 1.36e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 75.41  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 267 LMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEFLRKALTQSSLRQAWAE 346
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETG-LLVPPGDPEALAEAILRLLEDPELRRRLGE 95

                         90       100
                 ....*....|....*....|..
gi 446556883 347 NARHYAdtQDLYSLPEKAADII 368
Cdd:COG0438   96 AARERA--EERFSWEAIAERLL 115
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 200-318 1.09e-15

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: 75.52  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 200 LQVGSDFTRKGVDRSIEALASLPDSLRHNTLLYVVGQDKPRKFEALAEKRGVRSNVHFFSGRND---VSELMAAADLLLH 276
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDdevLELLLAAADVFVL 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446556883 277 PAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGEAI 318
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 161-367 3.83e-15

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: 75.78  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 161 RFHILPPGIypDRKYSQQPANSREifRKKNGITEQQYLLLQVGsdftR----KGVDRSIEALASLPDslRHNTLLYVVGQ 236
Cdd:cd03817  170 PIEVIPNGI--DLDKFEKPLNTEE--RRKLGLPPDEPILLYVG----RlakeKNIDFLLRAFAELKK--EPNIKLVIVGD 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 237 --DKPrKFEALAEKRGVRSNVHFFsG---RNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVD 311
Cdd:cd03817  240 gpERE-ELKELARELGLADKVIFT-GfvpREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVED 317

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446556883 312 ANCGEAIAEpfRQETLNEFLRKALTQSSLRQAWAENARHYADTqdlYSLPEKAADI 367
Cdd:cd03817  318 GENGFLFEP--NDETLAEKLLHLRENLELLRKLSKNAEISARE---FAFAKSVEKL 368
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 163-349 2.20e-14

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: 73.52  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 163 HILPPGIYPDRkysQQPANSREIfRKKNGITEQQYLLLQVGSDFT--RKGVDRSIEALASLPDslRHNTLLYVVGQDKPR 240
Cdd:cd03825  164 VVIPNGIDTEI---FAPVDKAKA-RKRLGIPQDKKVILFGAESVTkpRKGFDELIEALKLLAT--KDDLLLVVFGKNDPQ 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 241 KFEAlaekrgvRSNVHFFSGRNDVSELM---AAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeA 317
Cdd:cd03825  238 IVIL-------PFDIISLGYIDDDEQLVdiySAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTG-Y 309

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446556883 318 IAEPFRQETLNEFLRKALTQSSLRQAWAENAR 349
Cdd:cd03825  310 LVPPGDVQALAEAIEWLLANPKERESLGERAR 341
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 156-356 2.25e-14

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: 73.48  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 156 QTEAERFHILPPGIypDRKySQQPANSREIFRKKNGITEQqYLLLQVGSDFTRKGVDRSIEALASLPDSLRHnTLLyVVG 235
Cdd:cd03814  162 GHGFERVRLWPRGV--DTE-LFHPSRRDAALRRRLGPPGR-PLLLYVGRLAPEKNLEALLDADLPLAASPPV-RLV-VVG 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 236 qDKPRKfEALAEKRgvrSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDAN 313
Cdd:cd03814  236 -DGPAR-AELEARG---PDVIFtgFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGG 310

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446556883 314 CGeAIAEPFRQETLNEFLRKALTQSSLRQAWAENARHYADTQD 356
Cdd:cd03814  311 TG-ALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYS 352
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 160-299 7.14e-14

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: 71.94  E-value: 7.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 160 ERFHILPPGIYPDR-KYSQQPANSReifrKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDsLRHNTLLYVVGQ-D 237
Cdd:cd03812  158 GKFKVIPNGIDIEKyKFNKEKRRKR----RKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKK-KNPNVKLVLVGEgE 232

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446556883 238 KPRKFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLT 299
Cdd:cd03812  233 LKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLL 294
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 208-352 6.43e-13

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: 69.16  E-value: 6.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 208 RKGVDRSIEALASLpdSLRH-NTLLYVVGQDKPRKF-EALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGI 285
Cdd:cd03808  201 DKGIDELIEAAKIL--KKKGpNVRFLLVGDGELENPsEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPR 278

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446556883 286 VLLEAITAGLPVLTTAVCGyahyivdanCGEAI--------AEPFRQETLNEFLRKALTQSSLRQAWAENARHYA 352
Cdd:cd03808  279 SLLEAMAAGRPVITTDVPG---------CRELVidgvngflVPPGDVEALADAIEKLIEDPELRKEMGEAARKRV 344
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 3-352 4.39e-12

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: 66.49  E-value: 4.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   3 VAFCLYKYFPFGGLQRDFMRIAQTVAARGHHVRVYAqSWEGECPDIFEL-----IKVPVKSHTNHGRNAEYFAWVQ---- 73
Cdd:cd03820    2 IAIVIPSISNAGGAERVAINLANHLAKKGYDVTIIS-LDSAEKPPFYELddnikIKNLGDRKYSHFKLLLKYFKKVrrlr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  74 KHLREHPVDRVVGFNKMPGLDVYYAADVCyaEKVAQE-------KGFFYRLTSRYRHYAAFERatfeqgkptqLLMLTDk 146
Cdd:cd03820   81 KYLKNNKPDVVISFRTSLLTFLALIGLKS--KLIVWEhnnyeayNKGLRRLLLRRLLYKRADK----------IVVLTE- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 147 qiADFQKHYQTEAERFHILPPgIYPDRKYSQQPANSREIFrkkngiteqqyllLQVGSDFTRKGVDRSIEALASLPDslR 226
Cdd:cd03820  148 --ADKLKKYKQPNSNVVVIPN-PLSFPSEEPSTNLKSKRI-------------LAVGRLTYQKGFDLLIEAWALIAK--K 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 227 H---NTLLYVVGQDKPrKFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVC 303
Cdd:cd03820  210 HpdwKLRIYGDGPERE-ELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCP 288

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446556883 304 ---------GYAHYIVDANCGEAIAEPFRQETLNEFLRKALTQSSLrqawaENARHYA 352
Cdd:cd03820  289 tgpseiiedGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNAR-----KNAERFS 341
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 173-343 7.16e-12

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: 65.84  E-value: 7.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 173 RKYSQQPAnsrEIFRKKNGITEQQYLLLQVgSDFTR-KGVDRSIEALASLPDSLRHNTLLYVVGQDKPRKFEaLAEKRGV 251
Cdd:cd04962  176 DVFKRKPA---GALKRRLLAPPDEKVVIHV-SNFRPvKRIDDVVRVFARVRRKIPAKLLLVGDGPERVPAEE-LARELGV 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 252 RSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCG--------EAIAEPFR 323
Cdd:cd04962  251 EDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGflsdvgdvDAMAKSAL 330

                        170       180
                 ....*....|....*....|
gi 446556883 324 QETLNEFLRKALTQSSLRQA 343
Cdd:cd04962  331 SILEDDELYNRMGRAARKRA 350
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 7-349 3.17e-11

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: 63.83  E-value: 3.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   7 LYKYFP--FGGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIFELIKVPVKSHTNHGRNAEYFAW-VQKHLRE----- 78
Cdd:cd03795    5 VFKFYYpdIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPsYIKRFKKlakey 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  79 ------HP---VDRVVGFNKMPG-LDVYYAADVcyaekVAQEKgfFYRLtsryrhYAAFERATFEQGK---PTQLLML-T 144
Cdd:cd03795   85 diihyhFPnplADLLLFFSGAKKpVVVHWHSDI-----VKQKK--LLKL------YKPLMTRFLRRADriiATSPNYVeT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 145 DKQIADFQKhyqteaeRFHILPPGIYPDRKYSqqPANSREIFRKKNGITeqqYLLLQVGSDFTRKGVDRSIEALAslpds 224
Cdd:cd03795  152 SPTLREFKN-------KVRVIPLGIDKNVYNI--PRVDFENIKREKKGK---KIFLFIGRLVYYKGLDYLIEAAQ----- 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 225 lRHNTLLYVVGqDKPRK--FEALAEKrGVRSNVHFFSGRNDVSE--LMAAADLLLHPAY--QEAAGIVLLEAITAGLPVL 298
Cdd:cd03795  215 -YLNYPIVIGG-EGPLKpdLEAQIEL-NLLDNVKFLGRVDDEEKviYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVI 291

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446556883 299 TTAVCGYAHYIVdaNCGEA--IAEPFRQETLNEFLRKALTQSSLRQAWAENAR 349
Cdd:cd03795  292 STNIGTGVPYVN--NNGETglVVPPKDPDALAEAIDKLLSDEELRESYGENAK 342
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 165-331 1.38e-10

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: 62.08  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 165 LPPGIYPDR-KYSQqpaNSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVGQDKPR-KF 242
Cdd:cd04951  159 VYNGIDLNKfKKDI---NVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILS-KNDFKLLIAGDGPLRnEL 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 243 EALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGEAIAEPF 322
Cdd:cd04951  235 ERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQ 314

                        170
                 ....*....|
gi 446556883 323 R-QETLNEFL 331
Cdd:cd04951  315 LlAEKIKEIF 324
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 159-352 2.55e-09

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: 58.23  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 159 AERFHILPPGIYPDRKYSQQPAnsreifrkkngitEQQYLLLQVGSDFTRKGVDRSIEALASLPDslRHNTLLYVVGQDK 238
Cdd:cd05844  165 AERIHVHYIGIDPAKFAPRDPA-------------ERAPTILFVGRLVEKKGCDVLIEAFRRLAA--RHPTARLVIAGDG 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 239 P--RKFEALAEKRGvrsNVHFFS--GRNDVSELMAAADLLLHPAY------QEAAGIVLLEAITAGLPVLTTAVCGYAHY 308
Cdd:cd05844  230 PlrPALQALAAALG---RVRFLGalPHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEA 306

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446556883 309 IVDANCGEAIAEPfRQETLNEFLRKALTQSSLRQAWAENARHYA 352
Cdd:cd05844  307 ILDGETGFLVPEG-DVDALADALQALLADRALADRMGGAARAFV 349
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 1-368 3.01e-09

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: 58.12  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   1 MIVAFCLYKYFPFGGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIF----------ELIKVPVKSHTNHG---RNAE 67
Cdd:cd03794    1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFagatetkdgiRVIRVKLGPIKKNGlirRLLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883  68 YFAWVQKHLRehpvdRVVGFNKMPGLDVYYAAD------VCYAEKVAQEKGFFY---------------RLTSRYRHYAA 126
Cdd:cd03794   81 YLSFALAALL-----KLLVREERPDVIIAYSPPitlglaALLLKKLRGAPFILDvrdlwpeslialgvlKKGSLLKLLKK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 127 FERATFEQGKptqLLMLTDKQIADFQKHYQTEAERFHILPPGIYPDRkysqqPANSREIFRKKNGITEQQYLLLQVGS-D 205
Cdd:cd03794  156 LERKLYRLAD---AIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEE-----FKPPPKDELRKKLGLDDKFVVVYAGNiG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 206 FTRkGVDRSIEALASLPDSLRHNTLLYVVGQDKPRkFEALAEKRGvRSNVHFFSG--RNDVSELMAAADLLLHP-----A 278
Cdd:cd03794  228 KAQ-GLETLLEAAERLKRRPDIRFLFVGDGDEKER-LKELAKARG-LDNVTFLGRvpKEEVPELLSAADVGLVPlkdnpA 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 279 YQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEFLRKALTQSSLRQAWAENARHYADTQdlY 358
Cdd:cd03794  305 NRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCG-LVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEK--F 381

                        410
                 ....*....|
gi 446556883 359 SLpEKAADII 368
Cdd:cd03794  382 SR-EKLADRL 390
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 148-354 2.80e-08

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: 55.08  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 148 IADFQKHYQTEAERFHILPPGIyPDRKYSQQPAnsreifRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRH 227
Cdd:cd03822  146 RFLLVRIKLIPAVNIEVIPHGV-PEVPQDPTTA------LKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAE-FP 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 228 NTLLYVVGQDKP--------RKFEALAEKRGVRSNVHF---FSGRNDVSELMAAADLLLHPaYQE---AAGIVLLEAITA 293
Cdd:cd03822  218 DVRLVIAGELHPslaryegeRYRKAAIEELGLQDHVDFhnnFLPEEEVPRYISAADVVVLP-YLNteqSSSGTLSYAIAC 296

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446556883 294 GLPVLTTAVcGYAHYIVDANCGeAIAEPFRQETLNEFLRKALTQSSLRQAWAENARHYADT 354
Cdd:cd03822  297 GKPVISTPL-RHAEELLADGRG-VLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARA 355
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 143-299 4.63e-08

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: 54.23  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 143 LTDKQIADFQKHYQtEAERFHILPPGIYPDRKYSQQpansrEIFRKKNGIteqqyllLQVGSDFTRKGVDRSIEALASLP 222
Cdd:cd04949  120 STEQQKQDLSERFN-KYPPIFTIPVGYVDQLDTAES-----NHERKSNKI-------ITISRLAPEKQLDHLIEAVAKAV 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446556883 223 DSLRHNTL-LYvvGQDKPR-KFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLT 299
Cdd:cd04949  187 KKVPEITLdIY--GYGEEReKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVS 263
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
150-351 6.59e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 54.03  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 150 DFQKHYQTEAErFHILPPGIYPDrKYSQQPansREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLpDSLRHNT 229
Cdd:PRK15484 152 KFYEERLPNAD-ISIVPNGFCLE-TYQSNP---QPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKL-ATAHSNL 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 230 LLYVVGQD-KPRKFEALAEKRGVR-------SNVHFFSGR--NDVSELMAAADLLLHPA-YQEAAGIVLLEAITAGLPVL 298
Cdd:PRK15484 226 KLVVVGDPtASSKGEKAAYQKKVLeaakrigDRCIMLGGQppEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVL 305

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446556883 299 TTAVCGYAHYIVDANCGEAIAEPFRQETLNEFLRKALTQSSLRQAwAENARHY 351
Cdd:PRK15484 306 ASTKGGITEFVLEGITGYHLAEPMTSDSIISDINRTLADPELTQI-AEQAKDF 357
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
 216-369 5.23e-07

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). 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: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 51.16  E-value: 5.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 216 EALASLPDSLRHNTLLYVVGQDKPRKfEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLhpayQEAAGIVLLEAITAGL 295
Cdd:cd17507  214 ETVEALLDSLRAGQVLVVCGKNKKLY-EKLSGLEEDYINVRVLGYVDDMNELMAASDLVI----TKPGGLTISEALARGL 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 296 P-VLTTAVCGY----AHYIVDANCGEAIaepFRQETLNEFLRKALTQSSL----RQAWAENARHYAdtqdlyslPEKAAD 366
Cdd:cd17507  289 PvIIYDPIPGQeeenADFLENNGAGIIA---RDPEELLEIVARLIDPPSLlrmmSEAAKELKPPAA--------AKVIAD 357


                 ...
gi 446556883 367 IIT 369
Cdd:cd17507  358 ILS 360
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 152-360 3.08e-06

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: 48.87  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 152 QKHYQTEAERFHILPPGIYPDRkYsqqpANSREIFRKKNGITeqqylLLQVGSDFTRKGVDRSIEALaSLPDSLRHNTLL 231
Cdd:cd03813  259 QIRLGADPDKTRVIPNGIDIQR-F----APAREERPEKEPPV-----VGLVGRVVPIKDVKTFIRAF-KLVRRAMPDAEG 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 232 YVVG-QDKPRKFEA----LAEKRGVRSNVHFfSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAV--CG 304
Cdd:cd03813  328 WLIGpEDEDPEYAQeckrLVASLGLENKVKF-LGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVgsCR 406

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446556883 305 YAHYIVDANCGEA-----IAEPfrqETLNEFLRKALTQSSLRQAWAENARhyADTQDLYSL 360
Cdd:cd03813  407 ELIYGADDALGQAglvvpPADP---EALAEALIKLLRDPELRQAFGEAGR--KRVEKYYTL 462
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
14-172 3.41e-06

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 46.76  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   14 GGLQRDFMRIAQTVAARGHHVRVYAQSWEG----ECPDIFELIKVPVKSHTNHGRNAEYFAWVQKHLREHPVDRVVGFNK 89
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGplaeEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   90 MPGLDVYYAADVCYAEKV--------AQEKGFFYRLTSRYRHYAAFERATFEQGKptQLLMLTDKQIADFQKHYQTEAER 161
Cdd:pfam13439  81 FPLGLAALAARLRLGIPLvvtyhglfPDYKRLGARLSPLRRLLRRLERRLLRRAD--RVIAVSEAVADELRRLYGVPPEK 158

                         170
                  ....*....|.
gi 446556883  162 FHILPPGIYPD 172
Cdd:pfam13439 159 IRVIPNGVDLE 169
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 161-353 4.61e-06

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: 48.09  E-value: 4.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 161 RFHILPPGIYPDRKYSQQPANSREIFRkkngiteqqylLLQVGSDFTRKGVDRSIEALASLPdslRHNTLLYVVG--QDK 238
Cdd:cd03823  167 RISVIPNAVEPDLAPPPRRRPGTERLR-----------FGYIGRLTEEKGIDLLVEAFKRLP---REDIELVIAGhgPLS 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 239 PRKFEALAEKRGVRSNVHFfsgrNDVSELMAAADLLLHPA-YQEAAGIVLLEAITAGLPVLTTAVCGYAH--------YI 309
Cdd:cd03823  233 DERQIEGGRRIAFLGRVPT----DDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAGLPVIASDLGGIAEliqpgvngLL 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446556883 310 VDANCGEAIA-EPFRQETLNEFLRKALTQSSLRQAWAENARHYAD 353
Cdd:cd03823  309 FAPGDAEDLAaAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLK 353
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
179-352 8.60e-06

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 47.28  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 179 PANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDslrHNTLLYVV---GQDKPRkFEALAEKRGVRsNV 255
Cdd:PRK10307 212 ADADVDALRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRD---RPDLIFVIcgqGGGKAR-LEKMAQCRGLP-NV 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 256 HFFS--GRNDVSELMAAADLLLHPAYQEAAGIVL---LEAITA-GLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNE 329
Cdd:PRK10307 287 HFLPlqPYDRLPALLKMADCHLLPQKAGAADLVLpskLTNMLAsGRNVVATAEPGTELGQLVEGIG-VCVEPESVEALVA 365

                        170       180
                 ....*....|....*....|...
gi 446556883 330 FLRKALTQSSLRQAWAENARHYA 352
Cdd:PRK10307 366 AIAALARQALLRPKLGTVAREYA 388
SpsG COG3980
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ...
 215-349 1.22e-04

Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443179 [Multi-domain]  Cd Length: 342  Bit Score: 43.76  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 215 IEALASLPDSLRhntLLYVVGQDKP--RKFEALAEKRGVrsNVHFFSGRNDVSELMAAADLLLhpayqEAAGIVLLEAIT 292
Cdd:COG3980  190 LRALLQLDPDLK---ITVVVGPGYPhlDELRALAAERPL--NIELHRNVKDMAELMAQADLAI-----SAAGTTTYELAA 259

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446556883 293 AGLPVLTTAVC----GYAHYIVDANCGEAI--AEPFRQETLNEFLRKALTQSSLRQAWAENAR 349
Cdd:COG3980  260 LGLPTIVVAVAdnqrAIAEALEENGAAINLglGEELTDEELANALDELLLDPERRARMSRKAR 322
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 140-350 5.66e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 41.62  E-value: 5.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 140 LLMLTDKQIA-DFQKHYQTEAERFHILPPGIYPDR---KYsqqpaNSREIFRKKNGITEQQYLLLQVGsdftRKGVDRSI 215
Cdd:PLN02871 208 LTLVTSPALGkELEAAGVTAANRIRVWNKGVDSESfhpRF-----RSEEMRARLSGGEPEKPLIVYVG----RLGAEKNL 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 216 EALASLPDSLRhNTLLYVVGqDKPRKFEAlaEKRGVRSNVHF---FSGrNDVSELMAAADLLLHPAYQEAAGIVLLEAIT 292
Cdd:PLN02871 279 DFLKRVMERLP-GARLAFVG-DGPYREEL--EKMFAGTPTVFtgmLQG-DELSQAYASGDVFVMPSESETLGFVVLEAMA 353

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 293 AGLPVLTTAVCGYAHYIVDANCGEA--IAEPFRQETLNEFLRKALTQSSLRQAWAENARH 350
Cdd:PLN02871 354 SGVPVVAARAGGIPDIIPPDQEGKTgfLYTPGDVDDCVEKLETLLADPELRERMGAAARE 413
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
14-93 5.87e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 40.08  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883   14 GGLQRDFMRIAQTVAARGHHVRVYAQSWEGECPDIFE----LIKVPVKSHTNHGRNAEYFAWVQKHLREHPVDRVVGFNK 89
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGdgvrVHRLPVPPRPSPLADLAALRRLRRLLRAERPDVVHAHSP 80


                  ....
gi 446556883   90 MPGL 93
Cdd:pfam13579  81 TAGL 84
PRK13609 PRK13609
diacylglycerol glucosyltransferase; Provisional
 168-298 9.59e-04

diacylglycerol glucosyltransferase; Provisional


Pssm-ID: 237445 [Multi-domain]  Cd Length: 380  Bit Score: 40.86  E-value: 9.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 168 GIyPDRKYSQQPANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPdslrHNTLLYVVGQDKPRKFEALAE 247
Cdd:PRK13609 176 GI-PIRSSFELKINPDIIYNKYQLCPNKKILLIMAGAHGVLGNVKELCQSLMSVP----DLQVVVVCGKNEALKQSLEDL 250

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446556883 248 KRGVRSNVHFFSGRNDVSELMAAADLLLhpayQEAAGIVLLEAITAGLPVL 298
Cdd:PRK13609 251 QETNPDALKVFGYVENIDELFRVTSCMI----TKPGGITLSEAAALGVPVI 297
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 160-351 1.09e-03

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 40.77  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 160 ERFHILPPGIYP----DRKYSqqPANSREIFRKKNGITEQQYLLLQVgSDFTR-KGVDRSIEALASLPDSLRHNTLLYVV 234
Cdd:cd03792  159 PPKFYIPPSIDPlsgkNKDLS--PADIRYYLEKPFVIDPERPYILQV-ARFDPsKDPLGVIDAYKLFKRRAEEPQLVICG 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 235 G--QDKP---RKFEALAEKRGVRSNVHFFS-GRND--VSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYA 306
Cdd:cd03792  236 HgaVDDPegsVVYEEVMEYAGDDHDIHVLRlPPSDqeINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIP 315

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446556883 307 HYIVDANCGEAIAEPfrqETLNEFLRKALTQSSLRQAWAENARHY 351
Cdd:cd03792  316 LQVIDGETGFLVNSV---EGAAVRILRLLTDPELRRKMGLAAREH 357
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 208-304 2.28e-03

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: 39.91  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 208 RKGVDRSIEALASLpdSLRHNTLLYVVGQDKPRK--FEALAEKRGVRSNVHFFsGR---NDVSELMAAADLLLHPAYQEA 282
Cdd:cd03796  205 RKGIDLLVGIIPRI--CKKHPNVRFIIGGDGPKRieLEEMREKYQLQDRVELL-GAvphEEVRDVLVQGHIFLNTSLTEA 281

                         90       100
                 ....*....|....*....|..
gi 446556883 283 AGIVLLEAITAGLPVLTTAVCG 304
Cdd:cd03796  282 FCIAIVEAASCGLLVVSTRVGG 303
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 209-315 4.84e-03

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: 38.60  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 209 KGVDRSIEALASLpdSLRHNTLLY----VVGQDKPRKFEALAEKRGVRSNVHF--FSGRNDVSEL--MAAADLLLHPAYQ 280
Cdd:cd04946  237 KRIDLIIETLNSL--CVAHPSICIswthIGGGPLKERLEKLAENKLENVKVNFtgEVSNKEVKQLykENDVDVFVNVSES 314

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446556883 281 EAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCG 315
Cdd:cd04946  315 EGIPVSIMEAISFGIPVIATNVGGTREIVENETNG 349
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
211-353 5.20e-03

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 38.30  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 211 VDRSIEALASLPDslrhnTLLYVVGQDKPRKFEALAEkrgvrsNVHFFsGRNDVSELMAAADLLLHPAyqeAAGIVLlEA 290
Cdd:COG1819  138 LRAVLEALADLGV-----RVVVTTGGLDPAELGPLPD------NVRVV-DYVPQDALLPRADAVVHHG---GAGTTA-EA 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446556883 291 ITAGLPVLTTAVCG----YAHYIVDANCGEAI-AEPFRQETLNEFLRKALTQSSLRqawaENARHYAD 353
Cdd:COG1819  202 LRAGVPQVVVPFGGdqplNAARVERLGAGLALpPRRLTAEALRAALRRLLADPSYR----ERAARLAA 265
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 209-298 5.32e-03

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: 38.42  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 209 KGVDRSIEALASLPDSLrhntllyVVGQDKP--RKFEALAekrgvRSNVHF--FSGRNDVSELMAAADLLLHPAyQEAAG 284
Cdd:cd03804  212 KRIDLAVEAFNELPKRL-------VVIGDGPdlDRLRAMA-----SPNVEFlgYQPDEVLKELLSKARAFVFAA-EEDFG 278

                         90
                 ....*....|....
gi 446556883 285 IVLLEAITAGLPVL 298
Cdd:cd03804  279 IVPVEAQACGTPVI 292
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 215-352 6.83e-03

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 37.97  E-value: 6.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556883 215 IEALASLPDslRHNTLLYVVGqdkPRKFEALAEK-RGVRSNVHFFSGRNDVSELMAAADLLLHPayqeaAG-IVLLEAIT 292
Cdd:cd03785  201 PKALPKLLE--RGIQVIHQTG---KGDYDEVKKLyEDLGINVKVFPFIDDMAAAYAAADLVISR-----AGaSTIAELTA 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446556883 293 AGLPVL----TTAVCGY----AHYIVDANCGEAIAEP-FRQETLNEFLRKALTQSSLRQAWAENARHYA 352
Cdd:cd03785  271 AGKPAIlipyPYAADDHqeanARALEKAGAAIVIDQEeLTPEVLAEAILDLLNDPERLKKMAEAAKKLA 339
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 244-302 7.92e-03

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 37.99  E-value: 7.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446556883 244 ALAEKRGVRSNVHFFSGRNdVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAV 302
Cdd:NF038011 358 SLVASLGLQDKVKFLGFQK-IDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDV 415
 
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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