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Conserved domains on  [gi|553029329|gb|AGY54746|]
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Putative glycosyltransferase ytcC [Bacteroidales bacterium CF]

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

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 ...
63-386 3.77e-48

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: 167.71  E-value: 3.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  63 FVLTNNHSFVTKLRRKIFQYSHSSFFYNYYLDFFAAEVSKKVATGNYDVLISENR--PGFVLPLRRAFNGRLFLHLH--- 137
Cdd:cd03801   37 LTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLlaALLAALLALLLGAPLVVTLHgae 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 138 -------YDNLYKGVEFAEEVVSACTGVLAVSSYIKQR-VCTLESSKNKVNVIYNGIDLEKFTDiselsVTRSQFRLKEN 209
Cdd:cd03801  117 pgrllllLAAERRLLARAEALLRRADAVIAVSEALRDElRALGGIPPEKIVVIPNGVDLERFSP-----PLRRKLGIPPD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 210 DFVIVYTGRIEPIKGIKELLEAFASIKD-FPDMKLLIVGSASvndmsknQYLEKIYKIASTLGERVIFTGFQPYKNIPAI 288
Cdd:cd03801  192 RPVLLFVGRLSPRKGVDLLLEALAKLLRrGPDVRLVIVGGDG-------PLRAELEELELGLGDRVRFLGFVPDEELPAL 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 289 LKFCNLSVIPSTCEeAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILeKDGHLTENLRKSIITIYKDKNLQQNMSK 368
Cdd:cd03801  265 YAAADVFVLPSRYE-GFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLV-VPPDDVEALADALLRLLADPELRARLGR 342
                        330
                 ....*....|....*....
gi 553029329 369 HAIEQ-SKKFSKDNYASNF 386
Cdd:cd03801  343 AARERvAERFSWERVAERL 361
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
63-386 3.77e-48

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: 167.71  E-value: 3.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  63 FVLTNNHSFVTKLRRKIFQYSHSSFFYNYYLDFFAAEVSKKVATGNYDVLISENR--PGFVLPLRRAFNGRLFLHLH--- 137
Cdd:cd03801   37 LTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLlaALLAALLALLLGAPLVVTLHgae 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 138 -------YDNLYKGVEFAEEVVSACTGVLAVSSYIKQR-VCTLESSKNKVNVIYNGIDLEKFTDiselsVTRSQFRLKEN 209
Cdd:cd03801  117 pgrllllLAAERRLLARAEALLRRADAVIAVSEALRDElRALGGIPPEKIVVIPNGVDLERFSP-----PLRRKLGIPPD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 210 DFVIVYTGRIEPIKGIKELLEAFASIKD-FPDMKLLIVGSASvndmsknQYLEKIYKIASTLGERVIFTGFQPYKNIPAI 288
Cdd:cd03801  192 RPVLLFVGRLSPRKGVDLLLEALAKLLRrGPDVRLVIVGGDG-------PLRAELEELELGLGDRVRFLGFVPDEELPAL 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 289 LKFCNLSVIPSTCEeAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILeKDGHLTENLRKSIITIYKDKNLQQNMSK 368
Cdd:cd03801  265 YAAADVFVLPSRYE-GFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLV-VPPDDVEALADALLRLLADPELRARLGR 342
                        330
                 ....*....|....*....
gi 553029329 369 HAIEQ-SKKFSKDNYASNF 386
Cdd:cd03801  343 AARERvAERFSWERVAERL 361
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
209-373 9.33e-30

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: 112.37  E-value: 9.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  209 NDFVIVYTGRIEPIKGIKELLEAFASIK-DFPDMKLLIVGSASVNDMSKNQYLEKIykiastLGERVIFTGFQPYKNIPA 287
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKeKNPNLKLVIAGDGEEEKRLKKLAEKLG------LGDNVIFLGFVSDEDLPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  288 ILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILEKDgHLTENLRKSIITIYKDKNLQQNMS 367
Cdd:pfam00534  75 LLKIADVFVLPSR-YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKP-NNAEALAEAIDKLLEDEELRERLG 152

                  ....*.
gi 553029329  368 KHAIEQ 373
Cdd:pfam00534 153 ENARKR 158
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
100-382 9.04e-24

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 101.41  E-value: 9.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 100 VSKKVATGNYDVLISENRPGFVLPLR-RAFNGRLFLHLHydNLYKGvEFAEEVVSACTGVLAVSSYIKQRVCTLEssknk 178
Cdd:PRK15484  91 IAHKFTITKDSVIVIHNSMKLYRQIReRAPQAKLVMHMH--NAFEP-ELLDKNAKIIVPSQFLKKFYEERLPNAD----- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 179 VNVIYNGIDLEKFtDISELSVTRSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASI-KDFPDMKLLIVGSASVNDMS-K 256
Cdd:PRK15484 163 ISIVPNGFCLETY-QSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLaTAHSNLKLVVVGDPTASSKGeK 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 257 NQYLEKIYKIASTLGERVIFTGFQPYKNIPAILKFCNLSVIPSTCEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNcs 336
Cdd:PRK15484 242 AAYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEG-- 319
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 553029329 337 iilEKDGHLTENLrkSIITIYKD-KNLQQNMSKHAI-EQSKKFSKDNY 382
Cdd:PRK15484 320 ---ITGYHLAEPM--TSDSIISDiNRTLADPELTQIaEQAKDFVFSKY 362
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
279-388 5.95e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 73.49  E-value: 5.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 279 FQPYKNIP----AILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILEKDGHlTENLRKSII 354
Cdd:COG0438    4 LVPRKGLDllleALLAAADVFVLPSR-SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGD-PEALAEAIL 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 553029329 355 TIYKDKNLQQNMSKHAIEQ-SKKFSKDNYASNFFA 388
Cdd:COG0438   82 RLLEDPELRRRLGEAARERaEERFSWEAIAERLLA 116
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
181-325 9.32e-09

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: 56.86  E-value: 9.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 181 VIYNGIDLEKFTDIselsvtRSQfRLKENDFVIVYTGRIEPIKGIKELLEA-FASIKDFPDMKLLIVGSASvNDMsknQY 259
Cdd:NF038011 284 VIPNGIDLPRLAPL------RAQ-RPAGIPPVVGLIGRVVPIKDIKTFIRAmRTVVRAMPEAEGWIVGPEE-EDP---AY 352
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553029329 260 LEKIYKIASTLG--ERVIFTGFQpykNIPAILKFCNLSVIpSTCEEAFPLSAIESLASGLPIIATRSG 325
Cdd:NF038011 353 AAECRSLVASLGlqDKVKFLGFQ---KIDDLLPQVGLMVL-SSISEALPLVVLEAFAAGVPVVTTDVG 416
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
63-386 3.77e-48

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: 167.71  E-value: 3.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  63 FVLTNNHSFVTKLRRKIFQYSHSSFFYNYYLDFFAAEVSKKVATGNYDVLISENR--PGFVLPLRRAFNGRLFLHLH--- 137
Cdd:cd03801   37 LTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLlaALLAALLALLLGAPLVVTLHgae 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 138 -------YDNLYKGVEFAEEVVSACTGVLAVSSYIKQR-VCTLESSKNKVNVIYNGIDLEKFTDiselsVTRSQFRLKEN 209
Cdd:cd03801  117 pgrllllLAAERRLLARAEALLRRADAVIAVSEALRDElRALGGIPPEKIVVIPNGVDLERFSP-----PLRRKLGIPPD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 210 DFVIVYTGRIEPIKGIKELLEAFASIKD-FPDMKLLIVGSASvndmsknQYLEKIYKIASTLGERVIFTGFQPYKNIPAI 288
Cdd:cd03801  192 RPVLLFVGRLSPRKGVDLLLEALAKLLRrGPDVRLVIVGGDG-------PLRAELEELELGLGDRVRFLGFVPDEELPAL 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 289 LKFCNLSVIPSTCEeAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILeKDGHLTENLRKSIITIYKDKNLQQNMSK 368
Cdd:cd03801  265 YAAADVFVLPSRYE-GFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLV-VPPDDVEALADALLRLLADPELRARLGR 342
                        330
                 ....*....|....*....
gi 553029329 369 HAIEQ-SKKFSKDNYASNF 386
Cdd:cd03801  343 AARERvAERFSWERVAERL 361
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
151-358 1.05e-40

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: 147.91  E-value: 1.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 151 VVSACTGVLAVSSYIKQRVCTLESSKNKVNVIYNGIDLEKFTDISElsvtrsQFRLKENDFVIVYTGRIEPIKGIKELLE 230
Cdd:cd03798  147 ALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDR------GLGLPLDAFVILFVGRLIPRKGIDLLLE 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 231 AFASI-KDFPDMKLLIVGsasvnDMSKNQYLEKIYKIAsTLGERVIFTGFQPYKNIPAILKFCNLSVIPSTcEEAFPLSA 309
Cdd:cd03798  221 AFARLaKARPDVVLLIVG-----DGPLREALRALAEDL-GLGDRVTFTGRLPHEQVPAYYRACDVFVLPSR-HEGFGLVL 293
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 553029329 310 IESLASGLPIIATRSGGMPEAVDSNCSIILEKDG---HLTENLRKSIITIYK 358
Cdd:cd03798  294 LEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGdadALAAALRRALAEPYL 345
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
135-378 1.23e-34

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


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 131.63  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 135 HLHYDNLYKGVEFAEEVVSA------------CTGVLAVSSYIKQrvcTLESS--KNKVNVIYNGIDLEKFTDISELSVt 200
Cdd:cd03817  116 HTMYEDYLHYIPKGKLLVKAvvrklvrrfynhTDAVIAPSEKIKD---TLREYgvKGPIEVIPNGIDLDKFEKPLNTEE- 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 201 RSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASIKDFPDMKLLIVGsasvndmsKNQYLEKIYKIASTLG--ERVIFTG 278
Cdd:cd03817  192 RRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPNIKLVIVG--------DGPEREELKELARELGlaDKVIFTG 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 279 FQPYKNIPAILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILEKDGHltENLRKSIITIYK 358
Cdd:cd03817  264 FVPREELPEYYKAADLFVFAST-TETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPND--ETLAEKLLHLRE 340
                        250       260
                 ....*....|....*....|
gi 553029329 359 DKNLQQNMSKHAIEQSKKFS 378
Cdd:cd03817  341 NLELLRKLSKNAEISAREFA 360
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
2-379 4.10e-32

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: 124.39  E-value: 4.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329   2 NIAIITTGilpvpAIKGGAVETLIDILINynEDHPEHFITIFGTYDKeferMDFSKYKRTKFVLTNNHSFVTKLRRKIfq 81
Cdd:cd03811    1 KILFVIPS-----LSGGGAERVLLNLANA--LDKRGYDVTLVLLRDE----GDLDKQLNGDVKLIRLLIRVLKLIKLG-- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  82 yshssffynyyLDFFAAEVSKKVATGNYDVLIS-ENRPGFVLPLRRAFNGRLFLHLH--YDNLYKGVEFAEEVVSA---C 155
Cdd:cd03811   68 -----------LLKAILKLKRILKRAKPDVVISfLGFATYIVAKLAAARSKVIAWIHssLSKLYYLKKKLLLKLKLykkA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 156 TGVLAVSSYIKQRVCTLE-SSKNKVNVIYNGIDLEKFTDISELSVtrsqFRLKENDFVIVYTGRIEPIKGIKELLEAFA- 233
Cdd:cd03811  137 DKIVCVSKGIKEDLIRLGpSPPEKIEVIYNPIDIDRIRALAKEPI----LNEPEDGPVILAVGRLDPQKGHDLLIEAFAk 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 234 SIKDFPDMKLLIVGsasvndmsKNQYLEKIYKIASTLG--ERVIFTGFQPykNIPAILKFCNLSVIPSTcEEAFPLSAIE 311
Cdd:cd03811  213 LRKKYPDVKLVILG--------DGPLREELEKLAKELGlaERVIFLGFQS--NPYPYLKKADLFVLSSR-YEGFPNVLLE 281
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 312 SLASGLPIIATRSGGMPEAVDSNCSIILEKDGH--LTENLRKSIITIYKDKNLQQNMSKHAIEQSKKFSK 379
Cdd:cd03811  282 AMALGTPVVSTDCPGPREILDDGENGLLVPDGDaaALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
157-370 3.02e-31

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: 122.04  E-value: 3.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 157 GVLAVSSYIKQRVCTLESSKNKVNVIYNGIDLEKFT-DISELSVTRSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASI 235
Cdd:cd03807  136 ATVANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSpDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALL 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 236 KD-FPDMKLLIVGSASVNDMSKNQYLEKiykiasTLGERVIFTGFQPykNIPAILKFCNLSVIPStCEEAFPLSAIESLA 314
Cdd:cd03807  216 VEtHPDLRLLLVGRGPERPNLERLLLEL------GLEDRVHLLGERS--DVPALLPAMDIFVLSS-RTEGFPNALLEAMA 286
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 553029329 315 SGLPIIATRSGGMPEAVDSNCSIILEKDghLTENLRKSIITIYKDKNLQQNMSKHA 370
Cdd:cd03807  287 CGLPVVATDVGGAAELVDDGTGFLVPAG--DPQALADAIRALLEDPEKRARLGRAA 340
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
132-336 1.71e-30

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: 119.77  E-value: 1.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 132 LFLHLHYDNLYKGVEFAEEVVSACTGVLAVSSYIKQRvcTLES---SKNKVNVIYNGIDLEKFTDISElSVTRSQFRLKE 208
Cdd:cd03819  104 TTVHGSYLATYHPKDFALAVRARGDRVIAVSELVRDH--LIEAlgvDPERIRVIPNGVDTDRFPPEAE-AEERAQLGLPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 209 NDFVIVYTGRIEPIKGIKELLEAFASIKDFPDMKLLIVGSASVNDMSKNQylekiykiASTLG--ERVIFTGFQpyKNIP 286
Cdd:cd03819  181 GKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLLVAGDGPERDEIRRL--------VERLGlrDRVTFTGFR--EDVP 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 553029329 287 AILKFCNLSVIPSTCEEaFPLSAIESLASGLPIIATRSGGMPEAVDSNCS 336
Cdd:cd03819  251 AALAASDVVVLPSLHEE-FGRVALEAMACGTPVVATDVGGAREIVVHGRT 299
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-370 3.40e-30

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: 119.75  E-value: 3.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329   2 NIAIITTGILPvpaIKGGAVETLIDILINY-NEDHPEHFITIFGTYDKEFERMDFSKYK---RTKFVLTNNHSFVTKLRR 77
Cdd:cd03794    1 KILLISQYYPP---PKGAAAARVYELAKELvRRGHEVTVLTPSPNYPLGRIFAGATETKdgiRVIRVKLGPIKKNGLIRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  78 KIfqyshssffyNYYLDFFAAEVSKKVATGNYDVLISENRPGFVLP----LRRAFNGRLFLHLH--------------YD 139
Cdd:cd03794   78 LL----------NYLSFALAALLKLLVREERPDVIIAYSPPITLGLaallLKKLRGAPFILDVRdlwpeslialgvlkKG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 140 NLYKGVEFAEEVV-SACTGVLAVSSYIKQRVCTLESSKNKVNVIYNGIDLEKFTDISelSVTRSQFRLKENDFVIVYTGR 218
Cdd:cd03794  148 SLLKLLKKLERKLyRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPP--KDELRKKLGLDDKFVVVYAGN 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 219 IEPIKGIKELLEAFASIKDFPDMKLLIVGS-ASVNDMSKNQYLEKIykiastlgERVIFTGFQPYKNIPAILKFCNLSVI 297
Cdd:cd03794  226 IGKAQGLETLLEAAERLKRRPDIRFLFVGDgDEKERLKELAKARGL--------DNVTFLGRVPKEEVPELLSAADVGLV 297
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553029329 298 P----STCEEAFPLSAIESLASGLPIIATRSGGMPEAV-DSNCSIILEkDGHLTEnLRKSIITIYKDKNLQQNMSKHA 370
Cdd:cd03794  298 PlkdnPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVeINGCGLVVE-PGDPEA-LADAILELLDDPELRRAMGENG 373
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
209-373 9.33e-30

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: 112.37  E-value: 9.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  209 NDFVIVYTGRIEPIKGIKELLEAFASIK-DFPDMKLLIVGSASVNDMSKNQYLEKIykiastLGERVIFTGFQPYKNIPA 287
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKeKNPNLKLVIAGDGEEEKRLKKLAEKLG------LGDNVIFLGFVSDEDLPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  288 ILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILEKDgHLTENLRKSIITIYKDKNLQQNMS 367
Cdd:pfam00534  75 LLKIADVFVLPSR-YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKP-NNAEALAEAIDKLLEDEELRERLG 152

                  ....*.
gi 553029329  368 KHAIEQ 373
Cdd:pfam00534 153 ENARKR 158
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
178-384 3.85e-29

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: 116.96  E-value: 3.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 178 KVNVIYNGIDLEKFTDISELSVTRSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASIKDF-PDMKLLIVG--SASVNDM 254
Cdd:cd03800  188 RINVVPPGVDLERFFPVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELrELANLVLVGgpSDDPLSM 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 255 SKNQyLEKIYKIAStLGERVIFTGFQPYKNIPAILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVdSN 334
Cdd:cd03800  268 DREE-LAELAEELG-LIDRVRFPGRVSRDDLPELYRAADVFVVPSL-YEPFGLTAIEAMACGTPVVATAVGGLQDIV-RD 343
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 553029329 335 CSIILEKDGHLTENLRKSIITIYKDKNLQQNMSKHAIEQSK-KFSKDNYAS 384
Cdd:cd03800  344 GRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARaHYTWESVAD 394
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
155-383 4.76e-27

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: 110.53  E-value: 4.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 155 CTGVLAVSSYIKQRVCT-LESSKNKVNVIYNGIDLEKFTDISELSVtrsQFRLKENDFVIVYTGRIEPIKGIKELLEAFA 233
Cdd:cd03809  139 ADAIITVSEATRDDIIKfYGVPPEKIVVIPLGVDPSFFPPESAAVL---IAKYLLPEPYFLYVGTLEPRKNHERLLKAFA 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 234 SIKD-FPDMKLLIVGSasvnDMSKNQYLEKIYKIAStLGERVIFTGFQPYKNIPAILKFCNLSVIPSTCEeAFPLSAIES 312
Cdd:cd03809  216 LLKKqGGDLKLVIVGG----KGWEDEELLDLVKKLG-LGGRVRFLGYVSDEDLPALYRGARAFVFPSLYE-GFGLPVLEA 289
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553029329 313 LASGLPIIATRSGGMPEAVDSNCSIIlekDGHLTENLRKSIITIYKDKNLQQNMSKHAIEQSKKFSKDNYA 383
Cdd:cd03809  290 MACGTPVIASNISVLPEVAGDAALYF---DPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTA 357
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
178-377 1.51e-25

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: 107.81  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 178 KVNVIYNGIDLEKFTDISElsvtrsqFRLKENDFVIVYTGRIEPIKGIKELLEAFASI-KDFPDMKLLIVGSASVNDmsk 256
Cdd:cd03813  268 KTRVIPNGIDIQRFAPARE-------ERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVrRAMPDAEGWLIGPEDEDP--- 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 257 nQYLEKIYKIASTLGER--VIFTGFQpykNIPAILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEavdsn 334
Cdd:cd03813  338 -EYAQECKRLVASLGLEnkVKFLGFQ---NIKEYYPKLGLLVLTSI-SEGQPLVILEAMASGVPVVATDVGSCRE----- 407
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 553029329 335 csIILEKDGHLT-----------ENLRKSIITIYKDKNLQQNMSKHAIEQSKKF 377
Cdd:cd03813  408 --LIYGADDALGqaglvvppadpEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
211-359 4.61e-25

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 99.12  E-value: 4.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  211 FVIVYTGRI-EPIKGIKELLEAFASIKDFP-DMKLLIVGSASvndmsknqyLEKIYKIASTLGERVIFTGFQPykNIPAI 288
Cdd:pfam13692   2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRDnDVRLVIVGDGP---------EEELEELAAGLEDRVIFTGFVE--DLAEL 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553029329  289 LKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVDsncsiilEKDGHLTEN-----LRKSIITIYKD 359
Cdd:pfam13692  71 LAAADVFVLPSL-YEGFGLKLLEAMAAGLPVVATDVGGIPELVD-------GENGLLVPPgdpeaLAEAILRLLED 138
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
100-382 9.04e-24

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 101.41  E-value: 9.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 100 VSKKVATGNYDVLISENRPGFVLPLR-RAFNGRLFLHLHydNLYKGvEFAEEVVSACTGVLAVSSYIKQRVCTLEssknk 178
Cdd:PRK15484  91 IAHKFTITKDSVIVIHNSMKLYRQIReRAPQAKLVMHMH--NAFEP-ELLDKNAKIIVPSQFLKKFYEERLPNAD----- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 179 VNVIYNGIDLEKFtDISELSVTRSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASI-KDFPDMKLLIVGSASVNDMS-K 256
Cdd:PRK15484 163 ISIVPNGFCLETY-QSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLaTAHSNLKLVVVGDPTASSKGeK 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 257 NQYLEKIYKIASTLGERVIFTGFQPYKNIPAILKFCNLSVIPSTCEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNcs 336
Cdd:PRK15484 242 AAYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEG-- 319
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 553029329 337 iilEKDGHLTENLrkSIITIYKD-KNLQQNMSKHAI-EQSKKFSKDNY 382
Cdd:PRK15484 320 ---ITGYHLAEPM--TSDSIISDiNRTLADPELTQIaEQAKDFVFSKY 362
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
158-382 8.22e-23

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: 98.56  E-value: 8.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 158 VLAVSSYIKQRVCTLESSKNKVNVIYNGIdlekftdISELSVTRSQFRLKENdFVIVYTGRIEPIKGIKELLEAFASIKd 237
Cdd:cd03823  147 VLAPSRFTANLHEANGLFSARISVIPNAV-------EPDLAPPPRRRPGTER-LRFGYIGRLTEEKGIDLLVEAFKRLP- 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 238 FPDMKLLIVGSASVNDMSKNQylekiykiastLGERVIFTGFQPYKNIPAILKFCNLSVIPSTCEEAFPLSAIESLASGL 317
Cdd:cd03823  218 REDIELVIAGHGPLSDERQIE-----------GGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGL 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553029329 318 PIIATRSGGMPEAvdsncsIILEKDGHL-----TENLRKSIITIYKDKNLQQNMSKHAIE-QSKKFSKDNY 382
Cdd:cd03823  287 PVIASDLGGIAEL------IQPGVNGLLfapgdAEDLAAAMRRLLTDPALLERLRAGAEPpRSTESQAEEY 351
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
176-386 3.56e-22

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: 97.05  E-value: 3.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 176 KNKVNVIYNGIDLEKFTDISELsvtRSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASIKD-FPDMKLLIVGSASvndm 254
Cdd:cd03821  173 EPPIAVIPNGVDIPEFDPGLRD---RRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEqGRDWHLVIAGPDD---- 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 255 sknQYLEKIYKIAST--LGERVIFTGFQPYKNIPAILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVD 332
Cdd:cd03821  246 ---GAYPAFLQLQSSlgLGDRVTFTGPLYGEAKWALYASADLFVLPSY-SENFGNVVAEALACGLPVVITDKCGLSELVE 321
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 553029329 333 SNCSIILEKDGhltENLRKSIITIYKDKNLQQNMSKHA---IEQSKKFSKDNYASNF 386
Cdd:cd03821  322 AGCGVVVDPNV---SSLAEALAEALRDPADRKRLGEMArraRQVEENFSWEAVAGQL 375
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
156-373 7.29e-22

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: 95.88  E-value: 7.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 156 TGVLAVSSYIKQRVCTLESSKNKVNVIYNGIDLEKFTDISELSVTRsQFRLKENDFVIVYTGRIEPIKGIKELLEAFASI 235
Cdd:cd04962  143 DRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPAGALKR-RLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARV 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 236 KDFPDMKLLIVGSASVNDMSKNQylekiykiASTLG--ERVIFTGFQPykNIPAILKFCNLSVIPSTcEEAFPLSAIESL 313
Cdd:cd04962  222 RRKIPAKLLLVGDGPERVPAEEL--------ARELGveDRVLFLGKQD--DVEELLSIADLFLLPSE-KESFGLAALEAM 290
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 314 ASGLPIIATRSGGMPEAVDSNCSIILEKDGHLtENLRKSIITIYKDKNLQQNMSKHAIEQ 373
Cdd:cd04962  291 ACGVPVVSSNAGGIPEVVKHGETGFLSDVGDV-DAMAKSALSILEDDELYNRMGRAARKR 349
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
3-381 8.68e-22

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: 95.38  E-value: 8.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329   3 IAIITTGILPVpaikGGAVETLIDiLINY--NEDHPEHFITIFGTYDKEFermdFSKYKRTKFVltnnhSFVTKLRRKIF 80
Cdd:cd03820    2 IAIVIPSISNA----GGAERVAIN-LANHlaKKGYDVTIISLDSAEKPPF----YELDDNIKIK-----NLGDRKYSHFK 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  81 QYSHssFFYNYYldffaaEVSKKVATGNYDVLISENRPGFVLPLRRAFNGRLFL--HLHYDNLYKGVEFAEEVVSACT-- 156
Cdd:cd03820   68 LLLK--YFKKVR------RLRKYLKNNKPDVVISFRTSLLTFLALIGLKSKLIVweHNNYEAYNKGLRRLLLRRLLYKra 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 157 -GVLAVSSYIKQRvcTLESSKNKVNVIYNGIDLEKFTDISELsvtrsqfrlkeNDFVIVYTGRIEPIKGIKELLEAFASI 235
Cdd:cd03820  140 dKIVVLTEADKLK--KYKQPNSNVVVIPNPLSFPSEEPSTNL-----------KSKRILAVGRLTYQKGFDLLIEAWALI 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 236 -KDFPDMKLLIVGSASVNDMSKNQYLEKIykiastLGERVIFTGFQpyKNIPAILKFCNLSVIPSTcEEAFPLSAIESLA 314
Cdd:cd03820  207 aKKHPDWKLRIYGDGPEREELEKLIDKLG------LEDRVKLLGPT--KNIAEEYANSSIFVLSSR-YEGFPMVLLEAMA 277
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553029329 315 SGLPIIATRSGGMPEAVdsncsIILEKDGHLTEN-----LRKSIITIYKDKNLQQNMSKHAIEQSKKFSKDN 381
Cdd:cd03820  278 YGLPIISFDCPTGPSEI-----IEDGENGLLVPNgdvdaLAEALLRLMEDEELRKKMGKNARKNAERFSIEK 344
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
174-370 9.82e-21

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: 92.27  E-value: 9.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 174 SSKNKVNVIYNGIDLEKFTDISElsvtrsqfRLKENDFVIVYTGRIEPIKGIKELLEAFASIKD-FPDMKLLIVGSASVN 252
Cdd:cd03808  161 KKKKTVLIPGSGVDLDRFQYSPE--------SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKkGPNVRFLLVGDGELE 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 253 DMSKnQYLEKIykiasTLGERVIFTGFQpyKNIPAILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVD 332
Cdd:cd03808  233 NPSE-ILIEKL-----GLEGRIEFLGFR--SDVPELLAESDVFVLPSY-REGLPRSLLEAMAAGRPVITTDVPGCRELVI 303
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 553029329 333 SNCSIILEKDGHLTEnLRKSIITIYKDKNLQQNMSKHA 370
Cdd:cd03808  304 DGVNGFLVPPGDVEA-LADAIEKLIEDPELRKEMGEAA 340
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
214-331 2.54e-19

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: 86.30  E-value: 2.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 214 VYTGRIEPIKGIKELLEAFASIK-DFPDMKLLIVGSAsvndmsKNQYLEKIYKIASTLGERVIFTGFQPYK-NIPAILKF 291
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKaRLPDLVLVLVGGG------GEREEEEALAAALGLLERVVIIGGLVDDeVLELLLAA 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 553029329 292 CNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAV 331
Cdd:cd01635  188 ADVFVLPSR-SEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
160-378 3.06e-19

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: 88.27  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 160 AVSSYIKQRVctleSSKNKVNVIYNGIDLEKFT-DISELSVTRSQFRLKENDFVIVYTGRIEPIKGIKELLEAFAS-IKD 237
Cdd:cd04951  141 ALDEFIAKKA----FSKNKSVPVYNGIDLNKFKkDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISElILS 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 238 FPDMKLLIVGSASVndmsKNQYLEKIYKIasTLGERVIFTGFqpYKNIPAILKFCNLSVIPSTCEeAFPLSAIESLASGL 317
Cdd:cd04951  217 KNDFKLLIAGDGPL----RNELERLICNL--NLVDRVILLGQ--ISNISEYYNAADLFVLSSEWE-GFGLVVAEAMACER 287
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553029329 318 PIIATRSGGMPEAV-DSNCSIILEKDGHLTENLRKSIITIYKDKNLQQNMSKHAIeqsKKFS 378
Cdd:cd04951  288 PVVATDAGGVAEVVgDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIA---KNFS 346
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
2-334 4.70e-19

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 87.34  E-value: 4.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329   2 NIAIITTGILPVPAIKGGAVE----TLIDILINYNedhpeHFITIFGTYDkefermdfSKYKRTkfvltnNHSFVTKLRR 77
Cdd:cd03802    1 RIAQVSPPRGPVPPGKYGGTElvvsALTEGLVRRG-----HEVTLFAPGD--------SHTSAP------LVAVIPRALR 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  78 kifqySHSSFFYNYYLDFFAAEVsKKVATGNYDVLisENRPGFVLPLRRAFNGRLFLHLHYDNL--YKGVEFAEEvvsAC 155
Cdd:cd03802   62 -----LDPIPQESKLAELLEALE-VQLRASDFDVI--HNHSYDWLPPFAPLIGTPFVTTLHGPSipPSLAIYAAE---PP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 156 TGVLAVSSyiKQRVCTLESskNKVNVIYNGIDLEKFTdiselsvtrsqFRLKENDFVIvYTGRIEPIKGIKELLEAFASI 235
Cdd:cd03802  131 VNYVSISD--AQRAATPPI--DYLTVVHNGLDPADYR-----------FQPDPEDYLA-FLGRIAPEKGLEDAIRVARRA 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 236 KdfpdMKLLIVGSASVNDMSKnqylekiYKIASTLGERVIFTGFQPYKNIPAILKFCNLSVIPSTCEEAFPLSAIESLAS 315
Cdd:cd03802  195 G----LPLKIAGKVRDEDYFY-------YLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMAC 263
                        330
                 ....*....|....*....
gi 553029329 316 GLPIIATRSGGMPEAVDSN 334
Cdd:cd03802  264 GTPVIAYRRGGLPEVIQHG 282
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
157-331 4.37e-17

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: 81.73  E-value: 4.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 157 GVLAVSSYIKQRVCTLESSKNKVNVIYNGIDLEKFTDISELSVTRsqfrlkendfVIVYTGRIEPIKGIKELLEAFASIK 236
Cdd:cd05844  146 LFVAVSGFIRDRLLARGLPAERIHVHYIGIDPAKFAPRDPAERAP----------TILFVGRLVEKKGCDVLIEAFRRLA 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 237 D-FPDMKLLIVGSASVNDMSKNQylekiykiASTLGeRVIFTGFQPYKNIPAILK----FCNLSVIPSTCE-EAFPLSAI 310
Cdd:cd05844  216 ArHPTARLVIAGDGPLRPALQAL--------AAALG-RVRFLGALPHAEVQDWMRraeiFCLPSVTAASGDsEGLGIVLL 286
                        170       180
                 ....*....|....*....|.
gi 553029329 311 ESLASGLPIIATRSGGMPEAV 331
Cdd:cd05844  287 EAAACGVPVVSSRHGGIPEAI 307
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
213-382 1.45e-16

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: 80.04  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 213 IVYTGRIEPIKGIKELLEAFA-SIKDFPDMKLLIVGSASVNDMSKNqyLEKIYKiastLGERVIFTGFQpyKNIPAILKF 291
Cdd:cd04949  163 IITISRLAPEKQLDHLIEAVAkAVKKVPEITLDIYGYGEEREKLKK--LIEELH----LEDNVFLKGYH--SNLDQEYQD 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 292 CNLSVIPSTcEEAFPLSAIESLASGLPIIATRSG-GMPEAVDSNcsiileKDGHLTEN-----LRKSIITIYKDKNLQQN 365
Cdd:cd04949  235 AYLSLLTSQ-MEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDG------ENGYLIEKnnidaLADKIIELLNDPEKLQQ 307
                        170
                 ....*....|....*..
gi 553029329 366 MSKHAIEQSKKFSKDNY 382
Cdd:cd04949  308 FSEESYKIAEKYSTENV 324
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
156-320 2.76e-16

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: 79.26  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 156 TGVLAVSsYIKQRVCTLESSKNKVNVIYNGIDLEKFTDISELSVTRSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASI 235
Cdd:cd03812  138 TKYLACS-EDAGEWLFGEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEEL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 236 KD-FPDMKLLIVGsasvndmsKNQYLEKIYKIASTLG--ERVIFTGFQpyKNIPAILKFCNLSVIPSTCeEAFPLSAIES 312
Cdd:cd03812  217 KKkNPNVKLVLVG--------EGELKEKIKEKVKELGleDKVIFLGFR--NDVSEILSAMDVFLFPSLY-EGLPLVAVEA 285

                 ....*...
gi 553029329 313 LASGLPII 320
Cdd:cd03812  286 QASGLPCL 293
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
279-388 5.95e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 73.49  E-value: 5.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 279 FQPYKNIP----AILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILEKDGHlTENLRKSII 354
Cdd:COG0438    4 LVPRKGLDllleALLAAADVFVLPSR-SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGD-PEALAEAIL 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 553029329 355 TIYKDKNLQQNMSKHAIEQ-SKKFSKDNYASNFFA 388
Cdd:COG0438   82 RLLEDPELRRRLGEAARERaEERFSWEAIAERLLA 116
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
158-387 1.08e-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: 74.68  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 158 VLAVSSYIKQRV-CTLESSKNKVNVIYNGIDLEKFTDIsELSVTRSQFRLKENDFVIVY--TGRIEPIKGIKELLEAFAS 234
Cdd:cd03825  141 IVAPSRWLADMVrRSPLLKGLPVVVIPNGIDTEIFAPV-DKAKARKRLGIPQDKKVILFgaESVTKPRKGFDELIEALKL 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 235 IKDFPDMKLLIVGSASVNDMSknqylekiykiastLGERVIFTGFQPYKNIPA-ILKFCNLSVIPSTcEEAFPLSAIESL 313
Cdd:cd03825  220 LATKDDLLLVVFGKNDPQIVI--------------LPFDIISLGYIDDDEQLVdIYSAADLFVHPSL-ADNLPNTLLEAM 284
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553029329 314 ASGLPIIATRSGGMPEAVDSNCSIILEKDGHlTENLRKSIITIYKDKNLQQNMSKHAIE-QSKKFSKDNYASNFF 387
Cdd:cd03825  285 ACGTPVVAFDTGGSPEIVQHGVTGYLVPPGD-VQALAEAIEWLLANPKERESLGERARAlAENHFDQRVQAQRYL 358
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
159-342 1.38e-12

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


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 68.25  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 159 LAVSSYIKQRVCTLESSKNKVNVIYNGIDLEKFTdiselsvtrsqFRL----KENDFVIVYTGRIEPIKGIKELLEAFAS 234
Cdd:cd03799  130 LPNCELFKHRLIALGCDEKKIIVHRSGIDCNKFR-----------FKPrylpLDGKIRILTVGRLTEKKGLEYAIEAVAK 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 235 IKDF-PDMKLLIVGSASVNDMSKnQYLEKIYkiastLGERVIFTGFQPYKNIPAILKFCNLSVIPSTC-----EEAFPLS 308
Cdd:cd03799  199 LAQKyPNIEYQIIGDGDLKEQLQ-QLIQELN-----IGDCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgdQDGPPNT 272
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 553029329 309 AIESLASGLPIIATRSGGMPEAVDSNCSIIL--EKD 342
Cdd:cd03799  273 LKEAMAMGLPVISTEHGGIPELVEDGVSGFLvpERD 308
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
171-370 2.22e-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: 64.60  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 171 TLESSKNKVNVIYNGIDlekftdISELSVTRSQFRLKENDFV----IVYTGRIEPIKGIKELLEAfASIKDFPdmkLLIV 246
Cdd:cd03795  154 TLREFKNKVRVIPLGID------KNVYNIPRVDFENIKREKKgkkiFLFIGRLVYYKGLDYLIEA-AQYLNYP---IVIG 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 247 GSASVNDmsknqYLEKiyKIASTLGERVIFTGFQPYKNIPAILKFCNLSVIPS-TCEEAFPLSAIESLASGLPIIATR-- 323
Cdd:cd03795  224 GEGPLKP-----DLEA--QIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSvLRSEAFGIVLLEAMMCGKPVISTNig 296
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 553029329 324 SGGMPEAVDSNCSIILE-KDghlTENLRKSIITIYKDKNLQQNMSKHA 370
Cdd:cd03795  297 TGVPYVNNNGETGLVVPpKD---PDALAEAIDKLLSDEELRESYGENA 341
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
185-332 4.45e-11

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: 63.85  E-value: 4.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 185 GIDLEKFtdiselsvtRSQFR--------LKENDFVIVYTGRIEPIKGIKELLEAFASIKDFPDMKLLIVGsasvnDMSK 256
Cdd:cd03814  174 GVDTELF---------HPSRRdaalrrrlGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVRLVVVG-----DGPA 239
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553029329 257 NQYLEKIYKiastlgeRVIFTGFQPYKNIPAILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVD 332
Cdd:cd03814  240 RAELEARGP-------DVIFTGFLTGEELARAYASADVFVFPSR-TETFGLVVLEAMASGLPVVAADAGGPRDIVR 307
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
176-388 1.90e-10

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 62.00  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 176 KNKVNVIYNGIDLEKFT-----DISELSVTRsqfrLKENDFVIVYTGR-IEPIKGIKELLEAFASI-KDFPDMKLLIVGS 248
Cdd:cd03818  178 RDRISVIHDGVDTDRLApdpaaRLRLLNGTE----LKAGDPVITYVARnLEPYRGFHVFMRALPRIqARRPDARVVVVGG 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 249 ASVNDMSKNQYLE--KIYKIASTLG--ERVIFTGFQPYKNIPAILKFCNLSVIPsTCEEAFPLSAIESLASGLPIIATRS 324
Cdd:cd03818  254 DGVSYGSPPPDGGswKQKMLAELGVdlERVHFVGKVPYDQYVRLLQLSDAHVYL-TYPFVLSWSLLEAMACGCPVIGSDT 332
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 325 GGMPEAVDSNcsiileKDGHL-----TENLRKSIITIYKDKNLQQNMSKHAIEQ-SKKFSKDNYASNFFA 388
Cdd:cd03818  333 APVREVIRDG------RNGLLvdffdPDALAAAVLELLEDPDRAAALRRAARRTvERSDSLDVCLARYLA 396
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
158-386 6.01e-10

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: 60.38  E-value: 6.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 158 VLAVSSYIKQRVCTL---ESSknkvnVIYNGIDLEKFTDISElsvtrsqfrlKENDFVIVytGRIEPIKGIKELLEAFAS 234
Cdd:cd03804  161 FIANSQFVARRIKKFygrEST-----VIYPPVDTDAFAPAAD----------KEDYYLTA--SRLVPYKRIDLAVEAFNE 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 235 IkdfpDMKLLIVGSAsvndmsknQYLEKIYKIAStlgERVIFTGFQPYKNIPAILKFCNLSVIPStcEEAFPLSAIESLA 314
Cdd:cd03804  224 L----PKRLVVIGDG--------PDLDRLRAMAS---PNVEFLGYQPDEVLKELLSKARAFVFAA--EEDFGIVPVEAQA 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553029329 315 SGLPIIATRSGGMPEAVDSNCSIILEKDGhlTENLRKSIITIYKDKnlQQNMSKHAIEQS-KKFSKDNYASNF 386
Cdd:cd03804  287 CGTPVIAFGKGGALETVRPGPTGILFGEQ--TVESLKAAVEEFEQN--FDRFKPQAIRANaERFSRARFRQEI 355
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
38-388 5.14e-09

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


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 57.47  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329  38 HFITIFGTYDKEFErmdFSKYKRTKFVLTnnhSFVTK-----LRRKIFQYSHSSFFYNYYLDFFAAEVSKKVATGNYDVL 112
Cdd:cd04946   76 VFYKEIWIKDKPRS---GSFLLLYYFLIA---SFLSKhrvlaLLQFVSIFGQGTVVYSYWLNHTALGLGLLKDEYYRDVV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 113 IS---------ENRPGFVLPLRRAFngrlflhlhydnlykgvefaeevvsactgvlavSSYIKQRVCTLESSKNKVNVIY 183
Cdd:cd04946  150 ISrahrydlyeDQYGSYYLPLREYL---------------------------------VSYLDAVFLISKEGKDYLQKCY 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 184 NGIDLEKFtdISELSVTRSQFRLK---ENDFVIVYTGRIEPIKGIKELLEAFASIKDFPDMKLL----IVGSAsvndmsk 256
Cdd:cd04946  197 PAYKEKIF--VSRLGVSDKEQYSKvkkEGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSICIswthIGGGP------- 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 257 nqYLEKIYKIASTLGE--RVIFTGFQPYKNIPAILK------FCNLSVipstcEEAFPLSAIESLASGLPIIATRSGGMP 328
Cdd:cd04946  268 --LKERLEKLAENKLEnvKVNFTGEVSNKEVKQLYKendvdvFVNVSE-----SEGIPVSIMEAISFGIPVIATNVGGTR 340
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553029329 329 EAV-DSNCSIILEKDGhLTENLRKSIITIYKDKNLQQNMSKHAIEQSKK--FSKDNYasNFFA 388
Cdd:cd04946  341 EIVeNETNGLLLDKDP-TPNEIVSSIMKFYLDGGDYKTMKISARECWEErfNAEVNY--SKFA 400
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
134-391 6.12e-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: 6.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 134 LHLHYDNLYKGVEFAEEVVSACTGV--LAVSSYIKqrvctlesSKNKVNVIYNGIDLEKFTDiselSVTRSQFRLKENDF 211
Cdd:cd03822  121 GKQALKVLFRIATLSERVVVMAPISrfLLVRIKLI--------PAVNIEVIPHGVPEVPQDP----TTALKRLLLPEGKK 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 212 VIVYTGRIEPIKGIKELLEAFASIKD-FPDMKLLIVGSASVNdMSKNQYLEKIYKIASTLG--ERVIF-TGFQPYKNIPA 287
Cdd:cd03822  189 VILTFGFIGPGKGLEILLEALPELKAeFPDVRLVIAGELHPS-LARYEGERYRKAAIEELGlqDHVDFhNNFLPEEEVPR 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 288 ILKFCNLSVIPST-CEEAFPLSAIESLASGLPIIATRSGGMPEAVDSNCSIILEKDGhlTENLRKSIITIYKDKNLQQNM 366
Cdd:cd03822  268 YISAADVVVLPYLnTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRGVLVPFDD--PSAIAEAILRLLEDDERRQAI 345
                        250       260
                 ....*....|....*....|....*
gi 553029329 367 SKHAIEQSKKFSKDNYASNFFASIK 391
Cdd:cd03822  346 AERAYAYARAMTWESIADRYLRLFN 370
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
181-325 9.32e-09

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: 56.86  E-value: 9.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 181 VIYNGIDLEKFTDIselsvtRSQfRLKENDFVIVYTGRIEPIKGIKELLEA-FASIKDFPDMKLLIVGSASvNDMsknQY 259
Cdd:NF038011 284 VIPNGIDLPRLAPL------RAQ-RPAGIPPVVGLIGRVVPIKDIKTFIRAmRTVVRAMPEAEGWIVGPEE-EDP---AY 352
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553029329 260 LEKIYKIASTLG--ERVIFTGFQpykNIPAILKFCNLSVIpSTCEEAFPLSAIESLASGLPIIATRSG 325
Cdd:NF038011 353 AAECRSLVASLGlqDKVKFLGFQ---KIDDLLPQVGLMVL-SSISEALPLVVLEAFAAGVPVVTTDVG 416
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
175-386 4.19e-08

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


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 54.52  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 175 SKNKVNVIYNGIDLEKFTDISELSVTRSQfRLKENDFVIVYTGRIEPIKGIKELLEAFASIKD----FPDMKLLIVGSAS 250
Cdd:cd03805  177 AKNPPEVLYPCVDTDSFDSTSEDPDPGDL-IAKSNKKFFLSINRFERKKNIALAIEAFAKLKQklpeFENVRLVIAGGYD 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 251 vNDMSKN-QYLEKIYKIASTL---GERVIFtgfqpYKNIPAILKFcnlSVIPSTC-------EEAFPLSAIESLASGLPI 319
Cdd:cd03805  256 -PRVAENvEYLEELQRLAEELlnvEDQVLF-----LRSISDSQKE---QLLSSALallytpsNEHFGIVPLEAMYAGKPV 326
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553029329 320 IATRSGGMPEAVDSNCS-IILEKDghlTENLRKSIITIYKDKNLQQNMSKHAIEQ-SKKFSKDNYASNF 386
Cdd:cd03805  327 IACNSGGPLETVVEGVTgFLCEPT---PEAFAEAMLKLANDPDLADRMGAAGRKRvKEKFSREAFAERL 392
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
159-391 5.03e-08

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 54.33  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 159 LAVSSYIKQRVCTLESSKNKVNVIYNGIdlekftDISELSVTRSQfrlKENDFVIVYTGRI--EPIKGIKELLEAFASIK 236
Cdd:PRK09922 138 LAISSGIKEQMMARGISAQRISVIYNPV------EIKTIIIPPPE---RDKPAVFLYVGRLkfEGQKNVKELFDGLSQTT 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 237 DfpDMKLLIVGSASvnDMSKNQYLEKIYKIAstlgERVIFTGFQ--PYKNIPAILKFCNLSVIPSTCeEAFPLSAIESLA 314
Cdd:PRK09922 209 G--EWQLHIIGDGS--DFEKCKAYSRELGIE----QRIIWHGWQsqPWEVVQQKIKNVSALLLTSKF-EGFPMTLLEAMS 279
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553029329 315 SGLPIIATRSGGMPE-AVDSNCSIILEKDGHLTENLRKSIITIYKDKNLQQNMSKHAIEqskKFskdnYASNFFASIK 391
Cdd:PRK09922 280 YGIPCISSDCMSGPRdIIKPGLNGELYTPGNIDEFVGKLNKVISGEVKYQHDAIPNSIE---RF----YEVLYFKNLN 350
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
175-329 2.11e-07

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: 52.63  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 175 SKNKVNVIYNGIDLEKFTDiselsvtrSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASI-KDFPDMKLLIVGSASVND 253
Cdd:cd03796  166 DPRIVSVIPNAVDSSDFTP--------DPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRIcKKHPNVRFIIGGDGPKRI 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 254 MSKnQYLEKIYkiastLGERVIFTGFQPYKNIPAILK----FCNLSVIpstceEAFPLSAIESLASGLPIIATRSGGMPE 329
Cdd:cd03796  238 ELE-EMREKYQ-----LQDRVELLGAVPHEEVRDVLVqghiFLNTSLT-----EAFCIAIVEAASCGLLVVSTRVGGIPE 306
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
184-322 1.49e-06

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 49.97  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 184 NGIDLEKFTDISELSVT--RSQFRLKENDFVIVYTGRIEPIKGIKELLEAFASIKDFPDMKLLIVGSASvndmsknqYLE 261
Cdd:PRK10307 201 NWSEVARFQPVADADVDalRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRDRPDLIFVICGQGG--------GKA 272
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553029329 262 KIYKIASTLG-ERVIFTGFQPYKNIPAILKFCNLSVIPSTCEEA---FP--LSAIesLASGLPIIAT 322
Cdd:PRK10307 273 RLEKMAQCRGlPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAAdlvLPskLTNM--LASGRNVVAT 337
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
212-370 1.54e-06

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: 49.63  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 212 VIVYTGRIEPIKGIKELLEAFASIKD-FPDMKLLIVGSASVNDMSKNQYLEKIYKIASTLGERVIFTGFQPYKNIPAILK 290
Cdd:cd03792  199 YILQVARFDPSKDPLGVIDAYKLFKRrAEEPQLVICGHGAVDDPEGSVVYEEVMEYAGDDHDIHVLRLPPSDQEINALQR 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 291 FCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGMPEAVdsncsiileKDGHLT------ENLRKSIITIYKDKNLQQ 364
Cdd:cd03792  279 AATVVLQLST-REGFGLTVSEALWKGKPVIATPAGGIPLQV---------IDGETGflvnsvEGAAVRILRLLTDPELRR 348

                 ....*.
gi 553029329 365 NMSKHA 370
Cdd:cd03792  349 KMGLAA 354
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
174-378 2.03e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 49.71  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 174 SSKNKVNVIYNGIDLEKFTDISELSVTRSqfRL---KENDFVIVYTGRI---EPIKGIKELLEAFasikdfPDMKLLIVG 247
Cdd:PLN02871 226 TAANRIRVWNKGVDSESFHPRFRSEEMRA--RLsggEPEKPLIVYVGRLgaeKNLDFLKRVMERL------PGARLAFVG 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 248 sasvnDMSKNQYLEKIYKiastlGERVIFTGFQPYKNIPAILKFCNLSVIPSTcEEAFPLSAIESLASGLPIIATRSGGM 327
Cdd:PLN02871 298 -----DGPYREELEKMFA-----GTPTVFTGMLQGDELSQAYASGDVFVMPSE-SETLGFVVLEAMASGVPVVAARAGGI 366
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 553029329 328 PEAV---DSNCSIILEKDGHLTENLRKsIITIYKDKNLQQNMSKHAIEQSKKFS 378
Cdd:PLN02871 367 PDIIppdQEGKTGFLYTPGDVDDCVEK-LETLLADPELRERMGAAAREEVEKWD 419
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
138-386 1.64e-05

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 46.95  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 138 YDNLYKGVEFAEEVVSACTGVLAVSSYIKQrvctLESSKNKVNVIYNGI-DLEKFTDISElSVTRSQFRLKEND--FVIV 214
Cdd:PRK15179 447 YDIIYSELLKMRGVALSSNSQFAAHRYADW----LGVDERRIPVVYNGLaPLKSVQDDAC-TAMMAQFDARTSDarFTVG 521
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 215 YTGRIEPIKGIKELLEAFAS-IKDFPDMKLLIVGSASVndmsknqyLEKIYKIASTL--GERVIFTGFQpyKNIPAILKF 291
Cdd:PRK15179 522 TVMRVDDNKRPFLWVEAAQRfAASHPKVRFIMVGGGPL--------LESVREFAQRLgmGERILFTGLS--RRVGYWLTQ 591
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 292 CNLSVIPSTCEeAFPLSAIESLASGLPIIATRSGGMPEAVDSNCS-IILEKDGHLTENLRKSIITIYKDKNLQQNMSKHA 370
Cdd:PRK15179 592 FNAFLLLSRFE-GLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTgLTLPADTVTAPDVAEALARIHDMCAADPGIARKA 670
                        250
                 ....*....|....*..
gi 553029329 371 IEQ-SKKFSKDNYASNF 386
Cdd:PRK15179 671 ADWaSARFSLNQMIAST 687
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
174-385 5.50e-05

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 44.91  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 174 SSKNKVNVIYNGIDLEKFTDISELSVTR-------SQFRLKENDFVIvytgriepIKGIKELLEAFASIKDfPDMKLLIV 246
Cdd:cd03806  209 KRNIKPSIVYPPCDTEELTKLPIDEKTRenqilsiAQFRPEKNHPLQ--------LRAFAELLKRLPESIR-SNPKLVLI 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 247 GSA-SVNDMS---KNQYLEKIYKIAstlgERVIFtgfqpYKNIPailkFCNLSVIPSTCE--------EAFPLSAIESLA 314
Cdd:cd03806  280 GSCrNEEDKErveALKLLAKELILE----DSVEF-----VVDAP----YEELKELLSTASiglhtmwnEHFGIGVVEYMA 346
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553029329 315 SGLPIIATRSGGmPEavdsnCSIILEKDGHLT-------ENLRKSIITIYKDKNLQQNMSKHAIEQS-KKFSKDNYASN 385
Cdd:cd03806  347 AGLIPLAHASAG-PL-----LDIVVPWDGGPTgflastpEEYAEAIEKILTLSEEERLQRREAARSSaERFSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
153-390 1.61e-04

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 43.57  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 153 SACTGVLAVSSYIKQRVCTLESSKNKVNVIYNGIDLEkftDISELSVTRSqfrlkENDFVIVYTGRIEPIKGIKELLEAF 232
Cdd:PLN02949 219 RCAHLAMVNSSWTKSHIEALWRIPERIKRVYPPCDTS---GLQALPLERS-----EDPPYIISVAQFRPEKAHALQLEAF 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 233 ASIK-----DFPDMKLLIVGSAsvNDMSKNQYLEKIYKIASTLGervIFTGFQPYKNIP--AILKFCNLSV--IPSTCEE 303
Cdd:PLN02949 291 ALALekldaDVPRPKLQFVGSC--RNKEDEERLQKLKDRAKELG---LDGDVEFHKNVSyrDLVRLLGGAVagLHSMIDE 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329 304 AFPLSAIESLASGLPIIATRSGGmpEAVDsncsIILEKDGHLTENLRKSIITiYKDKNLQ---------QNMSKHAIEQS 374
Cdd:PLN02949 366 HFGISVVEYMAAGAVPIAHNSAG--PKMD----IVLDEDGQQTGFLATTVEE-YADAILEvlrmreterLEIAAAARKRA 438
                        250
                 ....*....|....*.
gi 553029329 375 KKFSKDNYASNFFASI 390
Cdd:PLN02949 439 NRFSEQRFNEDFKDAI 454
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
18-189 2.51e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 41.36  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329   18 GGaVETLIDILINY--NEDHPEHFITIFGTYDKEFERMDFSKYKRTKFVLTNNH----SFVTKLRRKIFQY------SHS 85
Cdd:pfam13439   1 GG-VERYVLELARAlaRRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLlrslAFLRRLRRLLRRErpdvvhAHS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553029329   86 SFFYNYYLDFFAAEVSKKVATGNYDVLISENRPGFVLPLRRAFNGRLFLHLHydnlykgvefaeevvSACTGVLAVSSYI 165
Cdd:pfam13439  80 PFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRLL---------------RRADRVIAVSEAV 144
                         170       180
                  ....*....|....*....|....*
gi 553029329  166 KQRVCT-LESSKNKVNVIYNGIDLE 189
Cdd:pfam13439 145 ADELRRlYGVPPEKIRVIPNGVDLE 169
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
274-332 5.05e-03

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 38.89  E-value: 5.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553029329 274 VIFTGFQPYKNIPAILKFCNLSVIP-----STCEeAFPLSAIESLASGLPIIATRsggMPEAVD 332
Cdd:cd04950  255 IHWLGPKPYKELPAYLAGFDVALLPfalneYTRF-ISPLKLFEYLAAGKPVVATS---IPSVVR 314
 
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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