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Conserved domains on  [gi|15833760|ref|NP_312533|]
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glucosyltransferase I [Escherichia coli O157:H7 str. Sakai]

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
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 7.25e-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: 7.25e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   3 VAFCLYKYFPF-GGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFELIKVPVKSHtnHGRNAEYFAWVQKHLR---- 77
Cdd:cd03801   2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLP--SLAALLRARRLLRELRpllr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  78 EHPVDKVVGFNKMPGLDVYYAADVCYAEKVAQEKGFFYHLTSRYR--HYAAFERATFEQGKPTQLLMLTDKQIADFQKHY 155
Cdd:cd03801  80 LRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALLRRADAVIAVSEALRDELRALG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 156 QTEAERFHILPPGIYPDRKYSQqpansreiFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVG 235
Cdd:cd03801 160 GIPPEKIVVIPNGVDLERFSPP--------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR-GPDVRLVIVG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 236 QDKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDAN 313
Cdd:cd03801 231 GDGPLRAELEELELGLGDRVRFlgFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15833760 314 CGEaIAEPFRQETLNEILRKALTQSSLRQAWAENARhyADTQDLYSLPEKAADII 368
Cdd:cd03801 311 GGL-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 7.25e-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: 7.25e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   3 VAFCLYKYFPF-GGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFELIKVPVKSHtnHGRNAEYFAWVQKHLR---- 77
Cdd:cd03801   2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLP--SLAALLRARRLLRELRpllr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  78 EHPVDKVVGFNKMPGLDVYYAADVCYAEKVAQEKGFFYHLTSRYR--HYAAFERATFEQGKPTQLLMLTDKQIADFQKHY 155
Cdd:cd03801  80 LRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALLRRADAVIAVSEALRDELRALG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 156 QTEAERFHILPPGIYPDRKYSQqpansreiFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVG 235
Cdd:cd03801 160 GIPPEKIVVIPNGVDLERFSPP--------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR-GPDVRLVIVG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 236 QDKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDAN 313
Cdd:cd03801 231 GDGPLRAELEELELGLGDRVRFlgFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15833760 314 CGEaIAEPFRQETLNEILRKALTQSSLRQAWAENARhyADTQDLYSLPEKAADII 368
Cdd:cd03801 311 GGL-VVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
196-350 1.19e-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: 132.78  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   196 QYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVG-QDKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAAD 272
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEK-NPNLKLVIAGdGEEEKRLKKLAEKLGLGDNVIFlgFVSDEDLPELLKIAD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833760   273 LLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEILRKALTQSSLRQAWAENARH 350
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETG-FLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
267-368 5.02e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.57  E-value: 5.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 267 LMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEILRKALTQSSLRQAWAE 346
Cdd:COG0438  17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETG-LLVPPGDPEALAEAILRLLEDPELRRRLGE 95
                        90       100
                ....*....|....*....|..
gi 15833760 347 NARHYAdtQDLYSLPEKAADII 368
Cdd:COG0438  96 AARERA--EERFSWEAIAERLL 115
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
150-351 6.24e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 54.03  E-value: 6.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  150 DFQKHYQTEAErFHILPPGIYPDrKYSQQPansREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLpDSLRHNT 229
Cdd:PRK15484 152 KFYEERLPNAD-ISIVPNGFCLE-TYQSNP---QPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKL-ATAHSNL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  230 LLYVVGQD-KPRKFEALAEKRGVR-------SNVHFFSGR--NDVSELMAAADLLLHPA-YQEAAGIVLLEAITAGLPVL 298
Cdd:PRK15484 226 KLVVVGDPtASSKGEKAAYQKKVLeaakrigDRCIMLGGQppEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVL 305
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15833760  299 TTAVCGYAHYIVDANCGEAIAEPFRQETLNEILRKALTQSSLRQAwAENARHY 351
Cdd:PRK15484 306 ASTKGGITEFVLEGITGYHLAEPMTSDSIISDINRTLADPELTQI-AEQAKDF 357
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
244-302 7.07e-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: 38.37  E-value: 7.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15833760  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 7.25e-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: 7.25e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   3 VAFCLYKYFPF-GGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFELIKVPVKSHtnHGRNAEYFAWVQKHLR---- 77
Cdd:cd03801   2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLP--SLAALLRARRLLRELRpllr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  78 EHPVDKVVGFNKMPGLDVYYAADVCYAEKVAQEKGFFYHLTSRYR--HYAAFERATFEQGKPTQLLMLTDKQIADFQKHY 155
Cdd:cd03801  80 LRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALLRRADAVIAVSEALRDELRALG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 156 QTEAERFHILPPGIYPDRKYSQqpansreiFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVG 235
Cdd:cd03801 160 GIPPEKIVVIPNGVDLERFSPP--------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR-GPDVRLVIVG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 236 QDKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDAN 313
Cdd:cd03801 231 GDGPLRAELEELELGLGDRVRFlgFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15833760 314 CGEaIAEPFRQETLNEILRKALTQSSLRQAWAENARhyADTQDLYSLPEKAADII 368
Cdd:cd03801 311 GGL-VVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
196-350 1.19e-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: 132.78  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   196 QYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVG-QDKPRKFEALAEKRGVRSNVHF--FSGRNDVSELMAAAD 272
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEK-NPNLKLVIAGdGEEEKRLKKLAEKLGLGDNVIFlgFVSDEDLPELLKIAD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833760   273 LLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEILRKALTQSSLRQAWAENARH 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 1.19e-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: 101.16  E-value: 1.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 147 QIADFQK-HYQTEAERFHILPPGIYPDRKYsqqPANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDsL 225
Cdd:cd03800 173 QEADELIsLYGADPSRINVVPPGVDLERFF---PVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE-L 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 226 RHNTLLYVVG------QDKPR-KFEALAEKRGVRSNVHFFSG--RNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLP 296
Cdd:cd03800 249 RELANLVLVGgpsddpLSMDReELAELAEELGLIDRVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTP 328
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833760 297 VLTTAVCGYAHYIVDANCGEAIaEPFRQETLNEILRKALTQSSLRQAWAENARHYAdtQDLYSLPEKAADIIT 369
Cdd:cd03800 329 VVATAVGGLQDIVRDGRTGLLV-DPHDPEALAAALRRLLDDPALWQRLSRAGLERA--RAHYTWESVADQLLT 398
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
10-349 3.25e-22

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: 96.27  E-value: 3.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  10 YFPFGGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFELIKVPVKShTNHGRNAEYFAWVQKHLREHPVDkVVGFN- 88
Cdd:cd03819   7 ALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLK-VPLLRALLGNVRLARLIRRERID-LIHAHs 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  89 KMPGLDVYYAADVCYAEKVaqekgFFYHLtSRYRHYAAFERATFEQgkptqllMLTDKQIA--DFQKHYQTEA-----ER 161
Cdd:cd03819  85 RAPAWLGWLASRLTGVPLV-----TTVHG-SYLATYHPKDFALAVR-------ARGDRVIAvsELVRDHLIEAlgvdpER 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 162 FHILPPGIYPDRKYSQQPANSREIFRKKNGIteqqYLLLQVGSDFTRKGVDRSIEALASLPDSLrhNTLLYVVGQDKPR- 240
Cdd:cd03819 152 IRVIPNGVDTDRFPPEAEAEERAQLGLPEGK----PVVGYVGRLSPEKGWLLLVDAAAELKDEP--DFRLLVAGDGPERd 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 241 KFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYaHYIVDANCGEAIAE 320
Cdd:cd03819 226 EIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA-REIVVHGRTGLLVP 304
                       330       340
                ....*....|....*....|....*....
gi 15833760 321 PFRQETLNEILRKALTQSSLRQAWAENAR 349
Cdd:cd03819 305 PGDAEALADAIRAAKLLPEAREKLQAAAA 333
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
146-353 5.53e-22

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: 95.91  E-value: 5.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 146 KQIADFQKHYQTEAERFHILPPGIypDRKYSQqPANSREIFRKKngiteqQYLLLQVGSDFTRKGVDRSIEALASLPDSL 225
Cdd:cd03798 159 KALAEELVALGVPRDRVDVIPNGV--DPARFQ-PEDRGLGLPLD------AFVILFVGRLIPRKGIDLLLEAFARLAKAR 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 226 RHNTLLyVVGQDKPR-KFEALAEKRGVRSNVHFFsGR---NDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTA 301
Cdd:cd03798 230 PDVVLL-IVGDGPLReALRALAEDLGLGDRVTFT-GRlphEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATD 307
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15833760 302 VCGYAHYIVDANCGEaIAEPFRQETLNEILRKALTQSSLRQAWAENARHYAD 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 ...
3-351 8.67e-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: 92.04  E-value: 8.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   3 VAFCLYKyFPFGGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFELIKVPVKSH-----TNHGRNAEYFAWVQKHLR 77
Cdd:cd03811   2 ILFVIPS-LSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLirvlkLIKLGLLKAILKLKRILK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  78 EHPVDKVVGFNkmpGLDVYYAADVCYAE--KVAQEKGFF----YHLTSRYRHYAAFERATfeqgkptQLLMLTDKQIADF 151
Cdd:cd03811  81 RAKPDVVISFL---GFATYIVAKLAAARskVIAWIHSSLsklyYLKKKLLLKLKLYKKAD-------KIVCVSKGIKEDL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 152 QKHYQTEAERFHILPPGIypDRKYSQQPANSREIFRKKNGITeqqylLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLL 231
Cdd:cd03811 151 IRLGPSPPEKIEVIYNPI--DIDRIRALAKEPILNEPEDGPV-----ILAVGRLDPQKGHDLLIEAFAKLRKK-YPDVKL 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 232 YVVGQDKPR-KFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAvCGYAHYIV 310
Cdd:cd03811 223 VILGDGPLReELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTD-CPGPREIL 301
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15833760 311 DAN-----CGEAIAEPFRQEtLNEILRKALTQsSLRQAWAENARHY 351
Cdd:cd03811 302 DDGengllVPDGDAAALAGI-LAALLQKKLDA-ALRERLAKAQEAV 345
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
12-353 2.26e-20

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: 91.27  E-value: 2.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  12 PFGGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFELIKVPVKSHTNHGRNAEYFAWVQKHLREHP----VDKVVGF 87
Cdd:cd03809  12 RLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPkkdkPDLLHSP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  88 NKMPGLDVYYAADVCY-----AEKVAQEKGFFYHLTSRYRHYAAFERATfeqgkptqlLMLTDKQ--IADFQKHYQTEAE 160
Cdd:cd03809  92 HNTAPLLLKGCPQVVTihdliPLRYPEFFPKRFRLYYRLLLPISLRRAD---------AIITVSEatRDDIIKFYGVPPE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 161 RFHILPPGIypDRKYSQQPANSREIFRKKngitEQQYLLLQVGSDFTRKGVDRSIEALASLPDSLR-HNtlLYVVGQ--D 237
Cdd:cd03809 163 KIVVIPLGV--DPSFFPPESAAVLIAKYL----LPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGdLK--LVIVGGkgW 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 238 KPRKFEALAEKRGVRSNVHFFSG--RNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTT------AVCGYAHYI 309
Cdd:cd03809 235 EDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASnisvlpEVAGDAALY 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15833760 310 VDANCGEAIAEPFRQETLNEILRKALTQSSLRQA----WAENARHYAD 353
Cdd:cd03809 315 FDPLDPESIADAILRLLEDPSLREELIRKGLERAkkfsWEKTAEKTLE 362
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
10-351 2.49e-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: 90.84  E-value: 2.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  10 YFPFGGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDvfELIKVPVKSHTNHGRNAEYFAWV---QKHLREHPVDKVVG 86
Cdd:cd03807   8 GLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGE--ELLAAGVPVVCLGLSSGKDPGVLlrlAKLIRKRNPDVVHT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  87 FnkMPGLDVYYAAdvcyAEKVAQEKGFFYHltsryrhyaafERATFEQGKPTQLLMLTDKQIADFQKHYQTEAER---FH 163
Cdd:cd03807  86 W--MYHADLIGGL----AAKLAGGVKVIWS-----------VRSSNIPQRLTRLVRKLCLLLSKFSPATVANSSAvaeFH 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 164 I-----------LPPGIYPDRkySQQPANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLY 232
Cdd:cd03807 149 QeqgyaknkivvIYNGIDLFK--LSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVET-HPDLRLL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 233 VVGQDKPRK-FEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVcGYAHYIVD 311
Cdd:cd03807 226 LVGRGPERPnLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDV-GGAAELVD 304
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15833760 312 ANCGeaIAEPFRQ-ETLNEILRKALTQSSLRQAWAENARHY 351
Cdd:cd03807 305 DGTG--FLVPAGDpQALADAIRALLEDPEKRARLGRAARER 343
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
140-368 9.07e-19

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: 86.65  E-value: 9.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 140 LLMLTDKQIADFQKHYQTEAERFhILPPGIYPDRKysqQPANSReifRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALA 219
Cdd:cd03821 155 LVHFTSEQEADELRRFGLEPPIA-VIPNGVDIPEF---DPGLRD---RRKHNGLEDRRIILFLGRIHPKKGLDLLIRAAR 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 220 SLPDSlRHNTLLYVVGQDKP--RKFEALAEKRGVRSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGL 295
Cdd:cd03821 228 KLAEQ-GRDWHLVIAGPDDGayPAFLQLQSSLGLGDRVTFtgPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGL 306
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833760 296 PVLTTAVCGYAHYiVDANCGeAIAEPfRQETLNEILRKALTQSSLRQAWAENARHYADTQDLYSLPEKAADII 368
Cdd:cd03821 307 PVVITDKCGLSEL-VEAGCG-VVVDP-NVSSLAEALAEALRDPADRKRLGEMARRARQVEENFSWEAVAGQLG 376
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
198-320 8.00e-18

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 79.09  E-value: 8.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   198 LLLQVGS-DFTRKGVDRSIEALASLpDSLRHNTLLYVVGQDKPRKFEALAekRGVRSNVHFFSGRNDVSELMAAADLLLH 276
Cdd:pfam13692   3 VILFVGRlHPNVKGVDYLLEAVPLL-RKRDNDVRLVIVGDGPEEELEELA--AGLEDRVIFTGFVEDLAELLAAADVFVL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15833760   277 PAYQEAAGIVLLEAITAGLPVLTTAVCGYAH-------YIVDANCGEAIAE 320
Cdd:pfam13692  80 PSLYEGFGLKLLEAMAAGLPVVATDVGGIPElvdgengLLVPPGDPEALAE 130
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
267-368 5.02e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.57  E-value: 5.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 267 LMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEILRKALTQSSLRQAWAE 346
Cdd:COG0438  17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETG-LLVPPGDPEALAEAILRLLEDPELRRRLGE 95
                        90       100
                ....*....|....*....|..
gi 15833760 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 1.01e-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: 75.90  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 200 LQVGSDFTRKGVDRSIEALASLPDSLRHNTLLYVVGQDKPRKFEALAEKRGVRSNVHFFSGRND---VSELMAAADLLLH 276
Cdd:cd01635 114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDdevLELLLAAADVFVL 193
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15833760 277 PAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGEAI 318
Cdd:cd01635 194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
156-356 9.08e-15

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: 74.64  E-value: 9.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 156 QTEAERFHILPPGIypDRKySQQPANSREIFRKKNGITEQqYLLLQVGsdftR----KGVDRSIEALASLPDSLRHnTLL 231
Cdd:cd03814 162 GHGFERVRLWPRGV--DTE-LFHPSRRDAALRRRLGPPGR-PLLLYVG----RlapeKNLEALLDADLPLAASPPV-RLV 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 232 yVVGqDKPRKfEALAEKRgvrSNVHF--FSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYI 309
Cdd:cd03814 233 -VVG-DGPAR-AELEARG---PDVIFtgFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIV 306
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15833760 310 VDANCGeAIAEPFRQETLNEILRKALTQSSLRQAWAENARHYADTQD 356
Cdd:cd03814 307 RPGGTG-ALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYS 352
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
163-349 1.36e-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: 74.29  E-value: 1.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 163 HILPPGIYPDRkysQQPANSREIfRKKNGITEQQYLLLQVGSDFT--RKGVDRSIEALASLPDslRHNTLLYVVGQDKPR 240
Cdd:cd03825 164 VVIPNGIDTEI---FAPVDKAKA-RKRLGIPQDKKVILFGAESVTkpRKGFDELIEALKLLAT--KDDLLLVVFGKNDPQ 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 241 KFEAlaekrgvRSNVHFFSGRNDVSELM---AAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeA 317
Cdd:cd03825 238 IVIL-------PFDIISLGYIDDDEQLVdiySAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTG-Y 309
                       170       180       190
                ....*....|....*....|....*....|..
gi 15833760 318 IAEPFRQETLNEILRKALTQSSLRQAWAENAR 349
Cdd:cd03825 310 LVPPGDVQALAEAIEWLLANPKERESLGERAR 341
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
161-364 2.28e-14

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: 73.47  E-value: 2.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 161 RFHILPPGIypDRKYSQQPANSREifRKKNGITEQQYLLLQVGsdftR----KGVDRSIEALASLPDslRHNTLLYVVGQ 236
Cdd:cd03817 170 PIEVIPNGI--DLDKFEKPLNTEE--RRKLGLPPDEPILLYVG----RlakeKNIDFLLRAFAELKK--EPNIKLVIVGD 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 237 --DKPrKFEALAEKRGVRSNVHFFsG---RNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVD 311
Cdd:cd03817 240 gpERE-ELKELARELGLADKVIFT-GfvpREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVED 317
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15833760 312 ANCGEAI---AEPFRQETLNEILRKALTQSSLRQAwAENARHYADTQDLYSLPEKA 364
Cdd:cd03817 318 GENGFLFepnDETLAEKLLHLRENLELLRKLSKNA-EISAREFAFAKSVEKLYEEV 372
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 15833760 160 ERFHILPPGIYPDR-KYSQQPANSReifrKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDsLRHNTLLYVVGQ-D 237
Cdd:cd03812 158 GKFKVIPNGIDIEKyKFNKEKRRKR----RKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKK-KNPNVKLVLVGEgE 232
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833760 238 KPRKFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLT 299
Cdd:cd03812 233 LKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLL 294
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
208-352 1.60e-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: 71.09  E-value: 1.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 208 RKGVDRSIEALASLpdSLRH-NTLLYVVGQDKPRKF-EALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGI 285
Cdd:cd03808 201 DKGIDELIEAAKIL--KKKGpNVRFLLVGDGELENPsEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPR 278
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833760 286 VLLEAITAGLPVLTTAVCGyahyivdanCGEAI--------AEPFRQETLNEILRKALTQSSLRQAWAENARHYA 352
Cdd:cd03808 279 SLLEAMAAGRPVITTDVPG---------CRELVidgvngflVPPGDVEALADAIEKLIEDPELRKEMGEAARKRV 344
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
173-343 5.02e-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: 66.61  E-value: 5.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 173 RKYSQQPAnsrEIFRKKNGITEQQYLLLQVgSDFTR-KGVDRSIEALASLPDSLRHNTLLYVVGQDKPRKFEaLAEKRGV 251
Cdd:cd04962 176 DVFKRKPA---GALKRRLLAPPDEKVVIHV-SNFRPvKRIDDVVRVFARVRRKIPAKLLLVGDGPERVPAEE-LARELGV 250
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 252 RSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCG--------EAIAEPFR 323
Cdd:cd04962 251 EDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGflsdvgdvDAMAKSAL 330
                       170       180
                ....*....|....*....|
gi 15833760 324 QETLNEILRKALTQSSLRQA 343
Cdd:cd04962 331 SILEDDELYNRMGRAARKRA 350
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
3-352 1.86e-11

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: 64.57  E-value: 1.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   3 VAFCLYKYFPFGGLQRDFMRIAQTVAARGHHVRVYTqSWEGECPDVFEL-----IKVPVKSHTNHGRNAEYFAWVQ---- 73
Cdd:cd03820   2 IAIVIPSISNAGGAERVAINLANHLAKKGYDVTIIS-LDSAEKPPFYELddnikIKNLGDRKYSHFKLLLKYFKKVrrlr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  74 KHLREHPVDKVVGFNKMPGLDVYYAADVCyaEKVAQE-------KGFFYHLTSRYRHYAAFERatfeqgkptqLLMLTDk 146
Cdd:cd03820  81 KYLKNNKPDVVISFRTSLLTFLALIGLKS--KLIVWEhnnyeayNKGLRRLLLRRLLYKRADK----------IVVLTE- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 147 qiADFQKHYQTEAERFHILPPgIYPDRKYSQQPANSREIFrkkngiteqqyllLQVGSDFTRKGVDRSIEALASLPDslR 226
Cdd:cd03820 148 --ADKLKKYKQPNSNVVVIPN-PLSFPSEEPSTNLKSKRI-------------LAVGRLTYQKGFDLLIEAWALIAK--K 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 227 H---NTLLYVVGQDKPrKFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVC 303
Cdd:cd03820 210 HpdwKLRIYGDGPERE-ELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCP 288
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15833760 304 ---------GYAHYIVDANCGEAIAEPFRQETLNEILRKALTQSSLrqawaENARHYA 352
Cdd:cd03820 289 tgpseiiedGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNAR-----KNAERFS 341
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
7-349 3.53e-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: 3.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   7 LYKYFP--FGGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFELIKVPVKSHTNHGRNAEYFAW-VQKHLRE----- 78
Cdd:cd03795   5 VFKFYYpdIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPsYIKRFKKlakey 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  79 ------HP---VDKVVGFNKMPG-LDVYYAADVcyaekVAQEK-GFFYH-LTSRYRHYAAFERATFEQgkptqlLMLTDK 146
Cdd:cd03795  85 diihyhFPnplADLLLFFSGAKKpVVVHWHSDI-----VKQKKlLKLYKpLMTRFLRRADRIIATSPN------YVETSP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 147 QIADFQKhyqteaeRFHILPPGIYPDRKYSqqPANSREIFRKKNGITeqqYLLLQVGSDFTRKGVDRSIEALAslpdslR 226
Cdd:cd03795 154 TLREFKN-------KVRVIPLGIDKNVYNI--PRVDFENIKREKKGK---KIFLFIGRLVYYKGLDYLIEAAQ------Y 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 227 HNTLLYVVGqDKPRK--FEALAEKrGVRSNVHFFSGRNDVSE--LMAAADLLLHPAY--QEAAGIVLLEAITAGLPVLTT 300
Cdd:cd03795 216 LNYPIVIGG-EGPLKpdLEAQIEL-NLLDNVKFLGRVDDEEKviYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVIST 293
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15833760 301 AVCGYAHYIVdaNCGEA--IAEPFRQETLNEILRKALTQSSLRQAWAENAR 349
Cdd:cd03795 294 NIGTGVPYVN--NNGETglVVPPKDPDALAEAIDKLLSDEELRESYGENAK 342
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
165-331 1.15e-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: 62.46  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 165 LPPGIYPDR-KYSQqpaNSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRHNTLLYVVGQDKPR-KF 242
Cdd:cd04951 159 VYNGIDLNKfKKDI---NVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILS-KNDFKLLIAGDGPLRnEL 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 243 EALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGEAIAEPF 322
Cdd:cd04951 235 ERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQ 314
                       170
                ....*....|
gi 15833760 323 R-QETLNEIL 331
Cdd:cd04951 315 LlAEKIKEIF 324
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
1-368 5.13e-10

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: 60.43  E-value: 5.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760   1 MIVAFCLYKYFPFGGLQRDFMRIAQTVAARGHHVRVYTQSWEG----------ECPDVFELIKVPVKSHTNHG---RNAE 67
Cdd:cd03794   1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYplgrifagatETKDGIRVIRVKLGPIKKNGlirRLLN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  68 YFAWVQKHLRehpvdKVVGFNKMPGLDVYYAAD------VCYAEKVAQEKgFFYHLT----------------SRYRHYA 125
Cdd:cd03794  81 YLSFALAALL-----KLLVREERPDVIIAYSPPitlglaALLLKKLRGAP-FILDVRdlwpeslialgvlkkgSLLKLLK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 126 AFERATFEQGKptqLLMLTDKQIADFQKHYQTEAERFHILPPGIYPDRkysqqPANSREIFRKKNGITEQQYLLLQVGS- 204
Cdd:cd03794 155 KLERKLYRLAD---AIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEE-----FKPPPKDELRKKLGLDDKFVVVYAGNi 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 205 DFTRkGVDRSIEALASLPDSLRHNTLLYVVGQDKPRkFEALAEKRGvRSNVHFFSG--RNDVSELMAAADLLLHP----- 277
Cdd:cd03794 227 GKAQ-GLETLLEAAERLKRRPDIRFLFVGDGDEKER-LKELAKARG-LDNVTFLGRvpKEEVPELLSAADVGLVPlkdnp 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 278 AYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNEILRKALTQSSLRQAWAENARHYADTQdl 357
Cdd:cd03794 304 ANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCG-LVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEK-- 380
                       410
                ....*....|.
gi 15833760 358 YSLpEKAADII 368
Cdd:cd03794 381 FSR-EKLADRL 390
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
159-320 1.71e-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: 58.62  E-value: 1.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 159 AERFHILPPGIYPDRKYSQQPAnsreifrkkngitEQQYLLLQVGSDFTRKGVDRSIEALASLPDslRHNTLLYVVGQDK 238
Cdd:cd05844 165 AERIHVHYIGIDPAKFAPRDPA-------------ERAPTILFVGRLVEKKGCDVLIEAFRRLAA--RHPTARLVIAGDG 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 239 P--RKFEALAEKRGvrsNVHFFS--GRNDVSELMAAADLLLHPAY------QEAAGIVLLEAITAGLPVLTTAVCGYAHY 308
Cdd:cd05844 230 PlrPALQALAAALG---RVRFLGalPHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEA 306
                       170
                ....*....|..
gi 15833760 309 IVDANCGEAIAE 320
Cdd:cd05844 307 ILDGETGFLVPE 318
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
148-354 4.37e-09

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: 57.39  E-value: 4.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 148 IADFQKHYQTEAERFHILPPGIyPDRKYSQQPAnsreifRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDSlRH 227
Cdd:cd03822 146 RFLLVRIKLIPAVNIEVIPHGV-PEVPQDPTTA------LKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAE-FP 217
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 228 NTLLYVVGQDKP--------RKFEALAEKRGVRSNVHF---FSGRNDVSELMAAADLLLHPaYQE---AAGIVLLEAITA 293
Cdd:cd03822 218 DVRLVIAGELHPslaryegeRYRKAAIEELGLQDHVDFhnnFLPEEEVPRYISAADVVVLP-YLNteqSSSGTLSYAIAC 296
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833760 294 GLPVLTTAVcGYAHYIVDANCGeAIAEPFRQETLNEILRKALTQSSLRQAWAENARHYADT 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 5.69e-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: 53.84  E-value: 5.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 143 LTDKQIADFQKHYQtEAERFHILPPGIYPDRKYSQQpansrEIFRKKNGIteqqyllLQVGSDFTRKGVDRSIEALASLP 222
Cdd:cd04949 120 STEQQKQDLSERFN-KYPPIFTIPVGYVDQLDTAES-----NHERKSNKI-------ITISRLAPEKQLDHLIEAVAKAV 186
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833760 223 DSLrHNTLLYVVGQDKPR-KFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLT 299
Cdd:cd04949 187 KKV-PEITLDIYGYGEEReKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVS 263
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
150-351 6.24e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 54.03  E-value: 6.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  150 DFQKHYQTEAErFHILPPGIYPDrKYSQQPansREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLpDSLRHNT 229
Cdd:PRK15484 152 KFYEERLPNAD-ISIVPNGFCLE-TYQSNP---QPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKL-ATAHSNL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  230 LLYVVGQD-KPRKFEALAEKRGVR-------SNVHFFSGR--NDVSELMAAADLLLHPA-YQEAAGIVLLEAITAGLPVL 298
Cdd:PRK15484 226 KLVVVGDPtASSKGEKAAYQKKVLeaakrigDRCIMLGGQppEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVL 305
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15833760  299 TTAVCGYAHYIVDANCGEAIAEPFRQETLNEILRKALTQSSLRQAwAENARHY 351
Cdd:PRK15484 306 ASTKGGITEFVLEGITGYHLAEPMTSDSIISDINRTLADPELTQI-AEQAKDF 357
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
216-369 6.51e-08

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: 53.86  E-value: 6.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 216 EALASLPDSLRHNTLLYVVGQDKPRKfEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLhpayQEAAGIVLLEAITAGL 295
Cdd:cd17507 214 ETVEALLDSLRAGQVLVVCGKNKKLY-EKLSGLEEDYINVRVLGYVDDMNELMAASDLVI----TKPGGLTISEALARGL 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 296 P-VLTTAVCGY----AHYIVDANCGEAIaepFRQETLNEILRKALTQSSL----RQAWAENARHYAdtqdlyslPEKAAD 366
Cdd:cd17507 289 PvIIYDPIPGQeeenADFLENNGAGIIA---RDPEELLEIVARLIDPPSLlrmmSEAAKELKPPAA--------AKVIAD 357

                ...
gi 15833760 367 IIT 369
Cdd:cd17507 358 ILS 360
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
161-353 9.34e-07

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: 50.41  E-value: 9.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 161 RFHILPPGIYPDRKYSQQPANSREIFRkkngiteqqylLLQVGSDFTRKGVDRSIEALASLPdslRHNTLLYVVG--QDK 238
Cdd:cd03823 167 RISVIPNAVEPDLAPPPRRRPGTERLR-----------FGYIGRLTEEKGIDLLVEAFKRLP---REDIELVIAGhgPLS 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 239 PRKFEALAEKRGVRSNVHFfsgrNDVSELMAAADLLLHPA-YQEAAGIVLLEAITAGLPVLTTAVCGYAH--------YI 309
Cdd:cd03823 233 DERQIEGGRRIAFLGRVPT----DDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAGLPVIASDLGGIAEliqpgvngLL 308
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15833760 310 VDANCGEAIA-EPFRQETLNEILRKALTQSSLRQAWAENARHYAD 353
Cdd:cd03823 309 FAPGDAEDLAaAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLK 353
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
152-360 2.35e-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: 49.26  E-value: 2.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 152 QKHYQTEAERFHILPPGIYPDRkYsqqpANSREIFRKKNGITeqqylLLQVGSDFTRKGVDRSIEALaSLPDSLRHNTLL 231
Cdd:cd03813 259 QIRLGADPDKTRVIPNGIDIQR-F----APAREERPEKEPPV-----VGLVGRVVPIKDVKTFIRAF-KLVRRAMPDAEG 327
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 232 YVVG-QDKPRKFEA----LAEKRGVRSNVHFfSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAV--CG 304
Cdd:cd03813 328 WLIGpEDEDPEYAQeckrLVASLGLENKVKF-LGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVgsCR 406
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833760 305 YAHYIVDANCGEA-----IAEPfrqETLNEILRKALTQSSLRQAWAENARhyADTQDLYSL 360
Cdd:cd03813 407 ELIYGADDALGQAglvvpPADP---EALAEALIKLLRDPELRQAFGEAGR--KRVEKYYTL 462
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
179-352 5.62e-06

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 48.05  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  179 PANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPDslrHNTLLYVV---GQDKPRkFEALAEKRGVRsNV 255
Cdd:PRK10307 212 ADADVDALRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRD---RPDLIFVIcgqGGGKAR-LEKMAQCRGLP-NV 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  256 HFFS--GRNDVSELMAAADLLLHPAYQEAAGIVL---LEAITA-GLPVLTTAVCGYAHYIVDANCGeAIAEPFRQETLNE 329
Cdd:PRK10307 287 HFLPlqPYDRLPALLKMADCHLLPQKAGAADLVLpskLTNMLAsGRNVVATAEPGTELGQLVEGIG-VCVEPESVEALVA 365
                        170       180
                 ....*....|....*....|...
gi 15833760  330 ILRKALTQSSLRQAWAENARHYA 352
Cdd:PRK10307 366 AIAALARQALLRPKLGTVAREYA 388
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
14-172 9.84e-06

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 45.60  E-value: 9.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760    14 GGLQRDFMRIAQTVAARGHHVRVYTQSWEG----ECPDVFELIKVPVKSHTNHGRNAEYFAWVQKHLREHPVDKVVGFNK 89
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGplaeEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760    90 MPGLDVYYAADVCYAEKV--------AQEKGFFYHLTSRYRHYAAFERATFEQGKptQLLMLTDKQIADFQKHYQTEAER 161
Cdd:pfam13439  81 FPLGLAALAARLRLGIPLvvtyhglfPDYKRLGARLSPLRRLLRRLERRLLRRAD--RVIAVSEAVADELRRLYGVPPEK 158
                         170
                  ....*....|.
gi 15833760   162 FHILPPGIYPD 172
Cdd:pfam13439 159 IRVIPNGVDLE 169
SpsG COG3980
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ...
215-349 1.13e-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: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 215 IEALASLPDSLRhntLLYVVGQDKP--RKFEALAEKRGVrsNVHFFSGRNDVSELMAAADLLLhpayqEAAGIVLLEAIT 292
Cdd:COG3980 190 LRALLQLDPDLK---ITVVVGPGYPhlDELRALAAERPL--NIELHRNVKDMAELMAQADLAI-----SAAGTTTYELAA 259
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833760 293 AGLPVLTTAVC----GYAHYIVDANCGEAI--AEPFRQETLNEILRKALTQSSLRQAWAENAR 349
Cdd:COG3980 260 LGLPTIVVAVAdnqrAIAEALEENGAAINLglGEELTDEELANALDELLLDPERRARMSRKAR 322
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
140-350 4.35e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 42.01  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  140 LLMLTDKQIA-DFQKHYQTEAERFHILPPGIYPDR---KYsqqpaNSREIFRKKNGITEQQYLLLQVGsdftRKGVDRSI 215
Cdd:PLN02871 208 LTLVTSPALGkELEAAGVTAANRIRVWNKGVDSESfhpRF-----RSEEMRARLSGGEPEKPLIVYVG----RLGAEKNL 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  216 EALASLPDSLRhNTLLYVVGqDKPRKFEAlaEKRGVRSNVHF---FSGrNDVSELMAAADLLLHPAYQEAAGIVLLEAIT 292
Cdd:PLN02871 279 DFLKRVMERLP-GARLAFVG-DGPYREEL--EKMFAGTPTVFtgmLQG-DELSQAYASGDVFVMPSESETLGFVVLEAMA 353
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  293 AGLPVLTTAVCGYAHYIVDANCGEA--IAEPFRQETLNEILRKALTQSSLRQAWAENARH 350
Cdd:PLN02871 354 SGVPVVAARAGGIPDIIPPDQEGKTgfLYTPGDVDDCVEKLETLLADPELRERMGAAARE 413
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
14-93 5.60e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 40.08  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760    14 GGLQRDFMRIAQTVAARGHHVRVYTQSWEGECPDVFE----LIKVPVKSHTNHGRNAEYFAWVQKHLREHPVDKVVGFNK 89
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGdgvrVHRLPVPPRPSPLADLAALRRLRRLLRAERPDVVHAHSP 80

                  ....
gi 15833760    90 MPGL 93
Cdd:pfam13579  81 TAGL 84
PRK13609 PRK13609
diacylglycerol glucosyltransferase; Provisional
168-298 1.11e-03

diacylglycerol glucosyltransferase; Provisional


Pssm-ID: 237445 [Multi-domain]  Cd Length: 380  Bit Score: 40.86  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  168 GIyPDRKYSQQPANSREIFRKKNGITEQQYLLLQVGSDFTRKGVDRSIEALASLPdslrHNTLLYVVGQDKPRKFEALAE 247
Cdd:PRK13609 176 GI-PIRSSFELKINPDIIYNKYQLCPNKKILLIMAGAHGVLGNVKELCQSLMSVP----DLQVVVVCGKNEALKQSLEDL 250
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15833760  248 KRGVRSNVHFFSGRNDVSELMAAADLLLhpayQEAAGIVLLEAITAGLPVL 298
Cdd:PRK13609 251 QETNPDALKVFGYVENIDELFRVTSCMI----TKPGGITLSEAAALGVPVI 297
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
160-351 1.86e-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: 40.00  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 160 ERFHILPPGIYP----DRKYSqqPANSREIFRKKNGITEQQYLLLQVgSDFTR-KGVDRSIEALASLPDSLRHNTLLYVV 234
Cdd:cd03792 159 PPKFYIPPSIDPlsgkNKDLS--PADIRYYLEKPFVIDPERPYILQV-ARFDPsKDPLGVIDAYKLFKRRAEEPQLVICG 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 235 G--QDKP---RKFEALAEKRGVRSNVHFFS-GRND--VSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYA 306
Cdd:cd03792 236 HgaVDDPegsVVYEEVMEYAGDDHDIHVLRlPPSDqeINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIP 315
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15833760 307 HYIVDANCGEAIAEPfrQETLNEILRKaLTQSSLRQAWAENARHY 351
Cdd:cd03792 316 LQVIDGETGFLVNSV--EGAAVRILRL-LTDPELRRKMGLAAREH 357
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
208-304 2.30e-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: 39.53  E-value: 2.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 208 RKGVDRSIEALASLpdSLRHNTLLYVVGQDKPRK--FEALAEKRGVRSNVHFFsGR---NDVSELMAAADLLLHPAYQEA 282
Cdd:cd03796 205 RKGIDLLVGIIPRI--CKKHPNVRFIIGGDGPKRieLEEMREKYQLQDRVELL-GAvphEEVRDVLVQGHIFLNTSLTEA 281
                        90       100
                ....*....|....*....|..
gi 15833760 283 AGIVLLEAITAGLPVLTTAVCG 304
Cdd:cd03796 282 FCIAIVEAASCGLLVVSTRVGG 303
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
215-352 2.65e-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: 39.51  E-value: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 215 IEALASLPDslRHNTLLYVVGqdkPRKFEALAEK-RGVRSNVHFFSGRNDVSELMAAADLLLHPayqeaAG-IVLLEAIT 292
Cdd:cd03785 201 PKALPKLLE--RGIQVIHQTG---KGDYDEVKKLyEDLGINVKVFPFIDDMAAAYAAADLVISR-----AGaSTIAELTA 270
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833760 293 AGLPVL----TTAVCGY----AHYIVDANCGEAIAEP-FRQETLNEILRKALTQSSLRQAWAENARHYA 352
Cdd:cd03785 271 AGKPAIlipyPYAADDHqeanARALEKAGAAIVIDQEeLTPEVLAEAILDLLNDPERLKKMAEAAKKLA 339
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
161-369 4.16e-03

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 39.25  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  161 RFHILPPGIyPDRKYSQQPANSREI--FRKKNGITEQQylllqVGSDFTRKGVDRS---IEALASLPDSLRHNTLLYVVG 235
Cdd:PRK15179 483 RIPVVYNGL-APLKSVQDDACTAMMaqFDARTSDARFT-----VGTVMRVDDNKRPflwVEAAQRFAASHPKVRFIMVGG 556
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760  236 QDKPRKFEALAEKRGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCG 315
Cdd:PRK15179 557 GPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTG 636
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15833760  316 EAI-AEPFRQETLNEILRKALTQSSLRQAWAENARHYAdtQDLYSLPEKAADIIT 369
Cdd:PRK15179 637 LTLpADTVTAPDVAEALARIHDMCAADPGIARKAADWA--SARFSLNQMIASTVR 689
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
209-298 4.54e-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: 38.81  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 209 KGVDRSIEALASLPDSLrhntllyVVGQDKP--RKFEALAekrgvRSNVHF--FSGRNDVSELMAAADLLLHPAyQEAAG 284
Cdd:cd03804 212 KRIDLAVEAFNELPKRL-------VVIGDGPdlDRLRAMA-----SPNVEFlgYQPDEVLKELLSKARAFVFAA-EEDFG 278
                        90
                ....*....|....
gi 15833760 285 IVLLEAITAGLPVL 298
Cdd:cd03804 279 IVPVEAQACGTPVI 292
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
209-315 4.93e-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: 4.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833760 209 KGVDRSIEALASLpdSLRHNTLLY----VVGQDKPRKFEALAEKRGVRSNVHF--FSGRNDVSEL--MAAADLLLHPAYQ 280
Cdd:cd04946 237 KRIDLIIETLNSL--CVAHPSICIswthIGGGPLKERLEKLAENKLENVKVNFtgEVSNKEVKQLykENDVDVFVNVSES 314
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15833760 281 EAAGIVLLEAITAGLPVLTTAVCGYAHYIVDANCG 315
Cdd:cd04946 315 EGIPVSIMEAISFGIPVIATNVGGTREIVENETNG 349
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
244-302 7.07e-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: 38.37  E-value: 7.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15833760  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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