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Conserved domains on  [gi|2502260919|ref|WP_281663901|]
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glycosyltransferase [Paraburkholderia fungorum]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 2-347 1.05e-91

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.


The actual alignment was detected with superfamily member cd03821:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 377  Bit Score: 281.18  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVDPRAGGPVEGVRRSGMAMQDAGHHIEVATCDAPGD----AYLAHFPFPVHAF------GPVTSRYSYSARL 71
Cdd:cd03821     1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYEslvvEENGRYIPPQDGFasipllRQGAGRTDFSPGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  72 APWLAANAKRFDAVVVHGLWQYHGLAAWKAVRKSGVPYYVYTHGMLDPWFKQaypLKHLKKWLYWPWAEYRVLRDARAVI 151
Cdd:cd03821    81 PNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQ---QKHWKKRIALHLIERRNLNNAALVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 152 FTTEEERtrARQSFWLYRAQERIVPFGTTVPPHEATPlreAFLQAVPGLRGKRIVLFLGRVHAKKGCDLLIDAFARVASR 231
Cdd:cd03821   158 FTSEQEA--DELRRFGLEPPIAVIPNGVDIPEFDPGL---RDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 232 DQSLHLVIAGPDETGWATSLRAQAQAAGVAqRISLPGMLQGELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPALIS 311
Cdd:cd03821   233 GRDWHLVIAGPDDGAYPAFLQLQSSLGLGD-RVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVIT 311

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2502260919 312 DKVNVWREIEAdGAGMVAADTVDGTEKNLVRWLELD 347
Cdd:cd03821   312 DKCGLSELVEA-GCGVVVDPNVSSLAEALAEALRDP 346
 
Name Accession Description Interval E-value
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 2-347 1.05e-91

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: 281.18  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVDPRAGGPVEGVRRSGMAMQDAGHHIEVATCDAPGD----AYLAHFPFPVHAF------GPVTSRYSYSARL 71
Cdd:cd03821     1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYEslvvEENGRYIPPQDGFasipllRQGAGRTDFSPGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  72 APWLAANAKRFDAVVVHGLWQYHGLAAWKAVRKSGVPYYVYTHGMLDPWFKQaypLKHLKKWLYWPWAEYRVLRDARAVI 151
Cdd:cd03821    81 PNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQ---QKHWKKRIALHLIERRNLNNAALVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 152 FTTEEERtrARQSFWLYRAQERIVPFGTTVPPHEATPlreAFLQAVPGLRGKRIVLFLGRVHAKKGCDLLIDAFARVASR 231
Cdd:cd03821   158 FTSEQEA--DELRRFGLEPPIAVIPNGVDIPEFDPGL---RDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 232 DQSLHLVIAGPDETGWATSLRAQAQAAGVAqRISLPGMLQGELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPALIS 311
Cdd:cd03821   233 GRDWHLVIAGPDDGAYPAFLQLQSSLGLGD-RVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVIT 311

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2502260919 312 DKVNVWREIEAdGAGMVAADTVDGTEKNLVRWLELD 347
Cdd:cd03821   312 DKCGLSELVEA-GCGVVVDPNVSSLAEALAEALRDP 346
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
203-345 2.04e-19

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 83.71  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 203 KRIVLFLGRVHAK-KGCDLLIDAFARVASRDQSLHLVIAGPdetGWATSLRAQAQAAGVaqRISLPGMLQGELKWgaFHA 281
Cdd:pfam13692   1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGD---GPEEELEELAAGLED--RVIFTGFVEDLAEL--LAA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2502260919 282 SDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWREIEADGAG-MVAADTVDGTEKNLVRWLE 345
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATD-VGGIPELVDGENGlLVPPGDPEALAEAILRLLE 137
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 278-380 5.18e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 59.62  E-value: 5.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 278 AFHASDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWREIEADGAG--MVAADTVDGTEKNLVRWLElDDTARAAMR 355
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATD-VGGLPEVIEDGETglLVPPGDPEALAEAILRLLE-DPELRRRLG 94

                          90       100
                  ....*....|....*....|....*
gi 2502260919 356 AQAARTFEARFRIETMVSALTALLE 380
Cdd:COG0438    95 EAARERAEERFSWEAIAERLLALYE 119
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
170-313 8.55e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.48  E-value: 8.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 170 AQERIVPFGTTVPP--HEATPLREAFLQAVPGlrgKRIVLFLGRVHAKKGCDLLIDAFARVASRDQSLHLVIAG------ 241
Cdd:PRK15484  161 ADISIVPNGFCLETyqSNPQPNLRQQLNISPD---ETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGdptass 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502260919 242 PDETGwATSLRAQAQAAGVAQRISLPGMLQGELKWGAFHASDVFVLPSH-QENFGVAVAEALGCGLPALISDK 313
Cdd:PRK15484  238 KGEKA-AYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTK 309
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 205-381 1.87e-03

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 40.09  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 205 IVLFLGRVHAKKGCDLLIDAFARVASR----DQSLHLVIAGP-----------DETGWATSLRAQAQaagvaqRISLPGM 269
Cdd:TIGR03088 196 VVGTVGRLQAVKDQPTLVRAFALLVRQlpegAERLRLVIVGDgpargaceqmvRAAGLAHLVWLPGE------RDDVPAL 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 270 LQgelkwgafhASDVFVLPSHQENFGVAVAEALGCGLPALISDKVNVWREIEADGAG-MVAADTVDGTEKNLVRWLElDD 348
Cdd:TIGR03088 270 MQ---------ALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGaLVPPGDAVALARALQPYVS-DP 339

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2502260919 349 TARAAMRAQAARTFEARFRIETMVSALTALLET 381
Cdd:TIGR03088 340 AARRAHGAAGRARAEQQFSINAMVAAYAGLYDQ 372
 
Name Accession Description Interval E-value
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 2-347 1.05e-91

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: 281.18  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVDPRAGGPVEGVRRSGMAMQDAGHHIEVATCDAPGD----AYLAHFPFPVHAF------GPVTSRYSYSARL 71
Cdd:cd03821     1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYEslvvEENGRYIPPQDGFasipllRQGAGRTDFSPGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  72 APWLAANAKRFDAVVVHGLWQYHGLAAWKAVRKSGVPYYVYTHGMLDPWFKQaypLKHLKKWLYWPWAEYRVLRDARAVI 151
Cdd:cd03821    81 PNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQ---QKHWKKRIALHLIERRNLNNAALVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 152 FTTEEERtrARQSFWLYRAQERIVPFGTTVPPHEATPlreAFLQAVPGLRGKRIVLFLGRVHAKKGCDLLIDAFARVASR 231
Cdd:cd03821   158 FTSEQEA--DELRRFGLEPPIAVIPNGVDIPEFDPGL---RDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 232 DQSLHLVIAGPDETGWATSLRAQAQAAGVAqRISLPGMLQGELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPALIS 311
Cdd:cd03821   233 GRDWHLVIAGPDDGAYPAFLQLQSSLGLGD-RVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVIT 311

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2502260919 312 DKVNVWREIEAdGAGMVAADTVDGTEKNLVRWLELD 347
Cdd:cd03821   312 DKCGLSELVEA-GCGVVVDPNVSSLAEALAEALRDP 346
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-380 3.55e-40

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: 146.53  E-value: 3.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVDPRAGGPVEGVRRSGMAMQDAGHHIEVATCDAPGDAYLAHFPFPVHAFGPVTSRYSYSARLAP--WLAANA 79
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRelRPLLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  80 KRFDAVVVHGLwqYHGLAAWKAVRKSGVPYYVYTHGMLDPWFKQAYPLKhlKKWLYwpwAEYRVLRDARAVIFTTEEERT 159
Cdd:cd03801    81 RKFDVVHAHGL--LAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAE--RRLLA---RAEALLRRADAVIAVSEALRD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 160 RARQSFWLYRAQERIVPFGTTVppheaTPLREAFLQAVPGLRGKRIVLFLGRVHAKKGCDLLIDAFARVASRDQSLHLVI 239
Cdd:cd03801   154 ELRALGGIPPEKIVVIPNGVDL-----ERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 240 AGPDETgWATSLRAQAQAAGVaqRISLPGMLQGELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWRE 319
Cdd:cd03801   229 VGGDGP-LRAELEELELGLGD--RVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATD-VGGLPE 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502260919 320 IEADGAG--MVAADTVDGTEKNLVRWLElDDTARAAMRAQAARTFEARFRIETMVSALTALLE 380
Cdd:cd03801   305 VVEDGEGglVVPPDDVEALADALLRLLA-DPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 12-312 2.68e-23

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: 100.15  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  12 PRAGGPVEGV--RRSGMAMQDAGHHIEVATCDAPG-------DAYLAHFPFPVHAFGPVTSRY-------SYSARLAP-W 74
Cdd:cd03798     9 PNANSPGRGIfvRRQVRALSRRGVDVEVLAPAPWGpaaarllRKLLGEAVPPRDGRRLLPLKPrlrllapLRAPSLAKlL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  75 LAANAKRFDAVVVHGLWQYhGLAAWKAVRKSGVPYYVYTHG------MLDPWFKQAYplkhlkKWlywpwaeyrVLRDAR 148
Cdd:cd03798    89 KRRRRGPPDLIHAHFAYPA-GFAAALLARLYGVPYVVTEHGsdinvfPPRSLLRKLL------RW---------ALRRAA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 149 AVIFTTEEERTRArQSFWLYRAQERIVPFGttVPPHeatplREAFLQAVPGLR-GKRIVLFLGRVHAKKGCDLLIDAFAR 227
Cdd:cd03798   153 RVIAVSKALAEEL-VALGVPRDRVDVIPNG--VDPA-----RFQPEDRGLGLPlDAFVILFVGRLIPRKGIDLLLEAFAR 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 228 VASRDQSLHLVIAGPDETGWAtsLRAQAQAAGVAQRISLPG-MLQGELKwGAFHASDVFVLPSHQENFGVAVAEALGCGL 306
Cdd:cd03798   225 LAKARPDVVLLIVGDGPLREA--LRALAEDLGLGDRVTFTGrLPHEQVP-AYYRACDVFVLPSRHEGFGLVLLEAMACGL 301


                  ....*.
gi 2502260919 307 PALISD 312
Cdd:cd03798   302 PVVATD 307
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
203-345 2.04e-19

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 83.71  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 203 KRIVLFLGRVHAK-KGCDLLIDAFARVASRDQSLHLVIAGPdetGWATSLRAQAQAAGVaqRISLPGMLQGELKWgaFHA 281
Cdd:pfam13692   1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGD---GPEEELEELAAGLED--RVIFTGFVEDLAEL--LAA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2502260919 282 SDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWREIEADGAG-MVAADTVDGTEKNLVRWLE 345
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATD-VGGIPELVDGENGlLVPPGDPEALAEAILRLLE 137
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 202-348 2.80e-19

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: 84.25  E-value: 2.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 202 GKRIVLFLGRVHAKKGCDLLIDAFARVASRDQSLHLVIAGpdETGWATSLRAQAQAAGVAQRISLPGMLQGELKWGAFHA 281
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG--DGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2502260919 282 SDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWREIEADG-AGMVAADTVDGTEKNLVRWLELDD 348
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASD-VGGPPEVVKDGeTGFLVKPNNAEALAEAIDKLLEDE 145
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 81-312 3.70e-19

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: 88.04  E-value: 3.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  81 RFDAVVVH----GLwqYHGLAAWKAvrksGVPYYVYT-HGMldPWFKqaypLKHLKKWLYWPWAEYRVLRDARAVIFTTE 155
Cdd:cd03808    81 KPDIVHCHtpkpGI--LGRLAARLA----GVPKVIYTvHGL--GFVF----TEGKLLRLLYLLLEKLALLFTDKVIFVNE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 156 EERTRARQSFwLYRAQERIVPFGTTVPPHEATPLREAFLQAVPglrgkrIVLFLGRVHAKKGCDLLIDAFARVASRDQSL 235
Cdd:cd03808   149 DDRDLAIKKG-IIKKKKTVLIPGSGVDLDRFQYSPESLPSEKV------VFLFVARLLKDKGIDELIEAAKILKKKGPNV 221

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2502260919 236 HLVIAGPDETGWATSLRAQAQAAGVaqRISLPGMLQGELKWgaFHASDVFVLPSHQENFGVAVAEALGCGLPALISD 312
Cdd:cd03808   222 RFLLVGDGELENPSEILIEKLGLEG--RIEFLGFRSDVPEL--LAESDVFVLPSYREGLPRSLLEAMAAGRPVITTD 294
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 12-345 1.11e-18

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: 86.95  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  12 PRAGGPVEGVRRSGMAMQDAGHHIEVATCDAPGD----------AYLAHFPFPVHAFGPVTSRYSYSARLAPWlaanakR 81
Cdd:cd03817    11 PQVNGVATSVRNLARALEKRGHEVYVITPSDPGAedeeevvryrSFSIPIRKYHRQHIPFPFKKAVIDRIKEL------G 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  82 FDavVVHglwqYH-----GLAAWKAVRKSGVP--------YYVYTHGMLDPWFKQAYPLKHLKKWLYwpwaeyrvlRDAR 148
Cdd:cd03817    85 PD--IIH----THtpfslGKLGLRIARKLKIPivhtyhtmYEDYLHYIPKGKLLVKAVVRKLVRRFY---------NHTD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 149 AVIFTTEEERTRARQSfwLYRAQERIVPFGTTVPPHEAtPLREAFLQAVPGLRGKRIVLFLGRVHAKKGCDLLIDAFARV 228
Cdd:cd03817   150 AVIAPSEKIKDTLREY--GVKGPIEVIPNGIDLDKFEK-PLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAEL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 229 ASRDQS-LHLVIAGPDETgwatSLRAQAQAAGVAQRISLPGMLQGELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLP 307
Cdd:cd03817   227 KKEPNIkLVIVGDGPERE----ELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLP 302

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2502260919 308 ALISDKVNVwREIEADG-AGMvaadTVDGTEKNLVRWLE 345
Cdd:cd03817   303 VVAAKDPAA-SELVEDGeNGF----LFEPNDETLAEKLL 336
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 200-328 1.86e-18

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: 83.99  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 200 LRGKRIVLFLGRVHAKKGCDLLIDAFARVASRDQSLHLVIAGPDETGWAtSLRAQAQAAGVAQRISLPGMLQGELKWGAF 279
Cdd:cd01635   107 SLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREE-EEALAAALGLLERVVIIGGLVDDEVLELLL 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2502260919 280 HASDVFVLPSHQENFGVAVAEALGCGLPALISDKVNVWREIEADGAGMV 328
Cdd:cd01635   186 AAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 14-324 9.58e-18

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: 84.21  E-value: 9.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  14 AGGPVEGVRRSGMAMQDAGHHIEV---ATCDAPGD-------AYLAHFPFpvhafGPVtsRYSYSARLAPWL---AANAK 80
Cdd:cd03800    20 TGGQNVYVLELARALAELGYQVDIftrRISPADPEvveiapgARVIRVPA-----GPP--EYLPKEELWPYLeefADGLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  81 RFDAV------VVHGLWQYHGLAAWKAVRKSGVPYYVYTHGMldpwfkQAYPLKHL-KKWLYWPW----AEYRVLRDARA 149
Cdd:cd03800    93 RFIAReggrydLIHSHYWDSGLVGALLARRLGVPLVHTFHSL------GRVKYRHLgAQDTYHPSlritAEEQILEAADR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 150 VIFTTEEERTRARQSFWLYRAQERIVPFGTT----VPPHEATPLREAFLQAvpglRGKRIVLFLGRVHAKKGCDLLIDAF 225
Cdd:cd03800   167 VIASTPQEADELISLYGADPSRINVVPPGVDlerfFPVDRAEARRARLLLP----PDKPVVLALGRLDPRKGIDTLVRAF 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 226 ARVASRDQSLHLVIAGPDETGWATSLRAQAQAAGVAQRISlpgmlqGELKWGAFH----------ASDVFVLPSHQENFG 295
Cdd:cd03800   243 AQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLI------DRVRFPGRVsrddlpelyrAADVFVVPSLYEPFG 316

                         330       340
                  ....*....|....*....|....*....
gi 2502260919 296 VAVAEALGCGLPALISDkVNVWREIEADG 324
Cdd:cd03800   317 LTAIEAMACGTPVVATA-VGGLQDIVRDG 344
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 32-345 1.86e-16

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: 80.10  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  32 GHHIEVATCDAPGDAYLAHFPFPVHAFGPVTSRYSYSARLAPWLAANAKRFDAVVVhgLWQYHGLAAwkaVRKSGVPYYV 111
Cdd:cd03809    32 PDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDL--LHSPHNTAP---LLLKGCPQVV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 112 YTHGMLDPWFKQAYPLKHlkkWLYWPWAEYRVLRDARAVIFTTEEERTRARQsfWLYRAQERIVPFGTTVPPHEATPLRE 191
Cdd:cd03809   107 TIHDLIPLRYPEFFPKRF---RLYYRLLLPISLRRADAIITVSEATRDDIIK--FYGVPPEKIVVIPLGVDPSFFPPESA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 192 AFLQAVPGLRgKRIVLFLGRVHAKKGCDLLIDAFARVASRDQSLHLVIAGPDETGWAtSLRAQAQAAGVAQRISLPGMLQ 271
Cdd:cd03809   182 AVLIAKYLLP-EPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDE-ELLDLVKKLGLGGRVRFLGYVS 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2502260919 272 GELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWREIEADGAGMVAADTVDGTEKNLVRWLE 345
Cdd:cd03809   260 DEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASN-ISVLPEVAGDAALYFDPLDPESIADAILRLLE 332
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 2-312 4.97e-16

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: 78.55  E-value: 4.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVdprAGGPVEGVRRSGM-AMQDAGHHIEVATCDAPGDAYLAHFPFPVHAFGPVTSRYSYSARL---APWLAA 77
Cdd:cd03811     1 KILFVIPSL---SGGGAERVLLNLAnALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLlkaILKLKR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  78 NAKR--FDAVVVHGlwqYHGLAAWKAVRKSGVPYYVYTHGMLDPWFKqayplkhLKKWLYWpwaEYRVLRDARAVIFTTE 155
Cdd:cd03811    78 ILKRakPDVVISFL---GFATYIVAKLAAARSKVIAWIHSSLSKLYY-------LKKKLLL---KLKLYKKADKIVCVSK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 156 EERTRARQSFWLYRAQERIVPFGTTVPPHEATPLREAFLQavpgLRGKRIVLFLGRVHAKKGCDLLIDAFARVASRDQSL 235
Cdd:cd03811   145 GIKEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILNE----PEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDV 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502260919 236 HLVIAG--PDETgwatSLRAQAQAAGVAQRISLPGMLQGELKWgaFHASDVFVLPSHQENFGVAVAEALGCGLPALISD 312
Cdd:cd03811   221 KLVILGdgPLRE----ELEKLAKELGLAERVIFLGFQSNPYPY--LKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTD 293
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 2-328 2.92e-15

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: 76.59  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVDPraGGPVEGVRRSGMAMQDAGHHIEVATCDAPGD--AYLAHFPFPVHAFGpvtSRYSYSARLAPWLAANA 79
Cdd:cd03807     1 KVAHVITGLNV--GGAETMLLRLLEHMDKSRFEHVVISLTGDGVlgEELLAAGVPVVCLG---LSSGKDPGVLLRLAKLI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  80 KRFDAVVVHGlWQYH-----GLAAWKAvrksGVPYYVYT-HGMLDPwfkqayplKHLKKWLYW--PWAEYRVlrdaRAVI 151
Cdd:cd03807    76 RKRNPDVVHT-WMYHadligGLAAKLA----GGVKVIWSvRSSNIP--------QRLTRLVRKlcLLLSKFS----PATV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 152 FTTEEERTRArQSFWLYRAQERIVPFGTTVP---PHEATPLREAFLQAVPglRGKRIVLFLGRVHAKKGCDLLIDAFARV 228
Cdd:cd03807   139 ANSSAVAEFH-QEQGYAKNKIVVIYNGIDLFklsPDDASRARARRRLGLA--EDRRVIGIVGRLHPVKDHSDLLRAAALL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 229 ASRDQSLHLVIAGpDETGWATSLRAQAQAAGVA------QRISLPGMLqgelkwgafHASDVFVLPSHQENFGVAVAEAL 302
Cdd:cd03807   216 VETHPDLRLLLVG-RGPERPNLERLLLELGLEDrvhllgERSDVPALL---------PAMDIFVLSSRTEGFPNALLEAM 285

                         330       340
                  ....*....|....*....|....*.
gi 2502260919 303 GCGLPALISDKVNVwREIEADGAGMV 328
Cdd:cd03807   286 ACGLPVVATDVGGA-AELVDDGTGFL 310
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 2-315 5.93e-15

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: 75.39  E-value: 5.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVDPRAGGPVEGVRRSGMAMQDAGHHIEVATC--DAPGDAYL--AHFPFPVHAFGPVTS-RYSYSArlAPWLA 76
Cdd:cd03795     1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCFskEKETPEKEenGIRIHRVKSFLNVAStPFSPSY--IKRFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  77 ANAKRFDAVVVHGLWQYHGLA-AWKAVRKsgvPYYVYTHGMLdpwFKQAYPLKhlkkwLYWPWaEYRVLRDARAVIFTTe 155
Cdd:cd03795    79 KLAKEYDIIHYHFPNPLADLLlFFSGAKK---PVVVHWHSDI---VKQKKLLK-----LYKPL-MTRFLRRADRIIATS- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 156 eeRTRARQSFWL--YRAQERIVPFG--TTVPPHEATPLREAFLQAVpglrGKRIVLFLGRVHAKKGCDLLIDafarvASR 231
Cdd:cd03795   146 --PNYVETSPTLreFKNKVRVIPLGidKNVYNIPRVDFENIKREKK----GKKIFLFIGRLVYYKGLDYLIE-----AAQ 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 232 DQSLHLVIAGpdeTGWATSLRAQAQAAGVAQRISLPGMLQGELKWGAFHASDVFVLPSH--QENFGVAVAEALGCGLPaL 309
Cdd:cd03795   215 YLNYPIVIGG---EGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKP-V 290


                  ....*.
gi 2502260919 310 ISDKVN 315
Cdd:cd03795   291 ISTNIG 296
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 13-312 9.92e-15

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: 74.70  E-value: 9.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  13 RAGGPVEGVRRSGMAMQDAGHHIEVATCDAPGDAYLAHFPFPVHAFGPVTSRYSYSARLapwLAANAKRFDAVVVHglwq 92
Cdd:cd03819     9 EIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPLLRALLGNVR---LARLIRRERIDLIH---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  93 YH----GLAAWKAVRKSGVPYyVYThgmldpwfkqayplKHLKKWLYWPWAEYRVLRDARA--VIFTTEEERTRARQSfw 166
Cdd:cd03819    82 AHsrapAWLGWLASRLTGVPL-VTT--------------VHGSYLATYHPKDFALAVRARGdrVIAVSELVRDHLIEA-- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 167 LYRAQERIVPFGTTVPPHEATPLREAFLQAVPGL-RGKRIVLFLGRVHAKKGCDLLIDAFARVAsRDQSLHLVIAGPDET 245
Cdd:cd03819   145 LGVDPERIRVIPNGVDTDRFPPEAEAEERAQLGLpEGKPVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLLVAGDGPE 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2502260919 246 gwATSLRAQAQAAGVAQRISLPGMLqgELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPALISD 312
Cdd:cd03819   224 --RDEIRRLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATD 286
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 12-348 1.64e-13

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: 71.17  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  12 PRAGGPVEGVRRSGMAMQDAGHHIEVATCDAPGDAYLAHFP-FPVHAFG-PVTSRYSYSARLAPWLAANAKRFDAVVVH- 88
Cdd:cd03814    11 PQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRvVSVPSFPlPFYPEYRLALPLPRRVRRLIKEFQPDIIHi 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  89 GLWQYHGLAAWKAVRKSGVPYYVYTHGMLDpwfkqAYPLKHLKKWLYWP-WAEYRVL-RDARAVIFTTEEERTRARQsfw 166
Cdd:cd03814    91 ATPGPLGLAALRAARRLGLPVVTSYHTDFP-----EYLSYYTLGPLSWLaWAYLRWFhNPFDTTLVPSPSIARELEG--- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 167 lyRAQERIVPFGTTV------PPHEATPLREAFLQAvpglrGKRIVLFLGRVHAKKGCDLLIDAFARVASRDqSLHLVIA 240
Cdd:cd03814   163 --HGFERVRLWPRGVdtelfhPSRRDAALRRRLGPP-----GRPLLLYVGRLAPEKNLEALLDADLPLAASP-PVRLVVV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 241 G--PDetgwATSLRAQAQAagvaqrISLPGMLQGELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPALISDKVNVwR 318
Cdd:cd03814   235 GdgPA----RAELEARGPD------VIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGP-R 303

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2502260919 319 EIEADG-AGMVAADTVDGTEKNLVRWLELDD 348
Cdd:cd03814   304 DIVRPGgTGALVEPGDAAAFAAALRALLEDP 334
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 2-312 2.26e-13

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: 70.82  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919   2 KILHLLASVDPRAGGPVEGVRRSGM-AMQDAGHHIEVATCD----------APGDAYLAHF----PFPVHAFGPVTSRYs 66
Cdd:cd03823     1 KILLVNSLYPPQRVGGAEISVHDLAeALVAEGHEVAVLTAGvgppgqatvaRSVVRYRRAPdetlPLALKRRGYELFET- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  67 YSARLAPWLAANAKRF--DAVVVHGLwQYHGLAAWKAVRKSGVPYYVYTHgmlDPWFKqaYPLKHLKKWlywpwaeyrvl 144
Cdd:cd03823    80 YNPGLRRLLARLLEDFrpDVVHTHNL-SGLGASLLDAARDLGIPVVHTLH---DYWLL--CPRQFLFKK----------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 145 rDARAVIFTTEEERTRARQsfWLYRAQERIV-PFGTTVPPheatPLREAFLQAVPGLRgkriVLFLGRVHAKKGCDLLID 223
Cdd:cd03823   143 -GGDAVLAPSRFTANLHEA--NGLFSARISViPNAVEPDL----APPPRRRPGTERLR----FGYIGRLTEEKGIDLLVE 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 224 AFARVASRDqsLHLVIAGpdeTGWATSLRaqaqAAGVAQRISLPGML-QGELKWgAFHASDVFVLPSH-QENFGVAVAEA 301
Cdd:cd03823   212 AFKRLPRED--IELVIAG---HGPLSDER----QIEGGRRIAFLGRVpTDDIKD-FYEKIDVLVVPSIwPEPFGLVVREA 281

                         330
                  ....*....|.
gi 2502260919 302 LGCGLPALISD 312
Cdd:cd03823   282 IAAGLPVIASD 292
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 30-312 2.54e-13

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: 70.73  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  30 DAGHHIEVATCDAPGDAYlaHFPFP------------VHAFGPVTSRYSYSARLAPWLAANakRFDAVVVHGlwqyHGLA 97
Cdd:cd03820    28 KKGYDVTIISLDSAEKPP--FYELDdnikiknlgdrkYSHFKLLLKYFKKVRRLRKYLKNN--KPDVVISFR----TSLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  98 AWKAVRKSGVPYYVYTHgmldpwfkqaYPLKHLKKWLYWPWAEYRVLRDARAVIFTTEEERTRarqSFWLYRAQERIVPF 177
Cdd:cd03820   100 TFLALIGLKSKLIVWEH----------NNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLK---KYKQPNSNVVVIPN 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 178 GTTVPPHEATPLREAflqavpglrgkRIVLFLGRVHAKKGCDLLIDAFARVASR--DQSLHLVIAGPDEtgwaTSLRAQA 255
Cdd:cd03820   167 PLSFPSEEPSTNLKS-----------KRILAVGRLTYQKGFDLLIEAWALIAKKhpDWKLRIYGDGPER----EELEKLI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2502260919 256 QAAGVAQRISLPGMLQG-ELKWgafHASDVFVLPSHQENFGVAVAEALGCGLPALISD 312
Cdd:cd03820   232 DKLGLEDRVKLLGPTKNiAEEY---ANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFD 286
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 66-329 3.52e-12

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: 67.37  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  66 SYSARLAPWLAANAKRFDAVVVHGLWQYHGLAAWKAVRKSGVPYYVYTHgmlDPWFKQAYPLKHLKKWL---YWPWAEYR 142
Cdd:cd03794    83 SFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVR---DLWPESLIALGVLKKGSllkLLKKLERK 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 143 VLRDARAVIFTTEEERTRARQsfwLYRAQERI--VPFGttVPPHEATPLREAFLQAVPGLRGKRIVLFLGrVHAKK-GCD 219
Cdd:cd03794   160 LYRLADAIIVLSPGLKEYLLR---KGVPKEKIivIPNW--ADLEEFKPPPKDELRKKLGLDDKFVVVYAG-NIGKAqGLE 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 220 LLIDAFARVASRDQsLHLVIAGP-DETGWatsLRAQAQAAGVAQRISLPGMLQGELKwGAFHASDVFVLPSHQENFGVAV 298
Cdd:cd03794   234 TLLEAAERLKRRPD-IRFLFVGDgDEKER---LKELAKARGLDNVTFLGRVPKEEVP-ELLSAADVGLVPLKDNPANRGS 308

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2502260919 299 A-----EALGCGLPALISDKVNVWREIEADGAGMVA 329
Cdd:cd03794   309 SpsklfEYMAAGKPILASDDGGSDLAVEINGCGLVV 344
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
15-178 6.08e-12

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 63.19  E-value: 6.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  15 GGPVEGVRRSGMAMQDAGHHIEVATCDAPGDAY-LAHFPFPVHAFG-PVTSRYSYSARLAPWLAANAKRFDAVVVHGLWQ 92
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPeLVGDGVRVHRLPvPPRPSPLADLAALRRLRRLLRAERPDVVHAHSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  93 YHGLAAWKAVRKSGVPYYVYTHGMLDPwfkqayPLKHLKKWLYWpWAEYRVLRDARAVIFTTEEERTRARQSFwLYRAQE 172
Cdd:pfam13579  81 TAGLAARLARRRRGVPLVVTVHGLALD------YGSGWKRRLAR-ALERRLLRRADAVVVVSEAEAELLRALG-VPAARV 152


                  ....*.
gi 2502260919 173 RIVPFG 178
Cdd:pfam13579 153 VVVPNG 158
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
27-176 3.30e-11

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 61.39  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  27 AMQDAGHHIEVATCDAPGDAY--LAHFPFPVHAFGPVTSRYSYSARLAPWLAANAKRFDAVVVHG-LWQYHGLAAWKAVR 103
Cdd:pfam13439  13 ALARRGHEVTVVTPGGPGPLAeeVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAhSPFPLGLAALAARL 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502260919 104 KSGVPYYVYTHGMLDPWFKQAYPLKHLKKWLYWpwAEYRVLRDARAVIFTTEEERTRARQSFWLYRAQERIVP 176
Cdd:pfam13439  93 RLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRR--LERRLLRRADRVIAVSEAVADELRRLYGVPPEKIRVIP 163
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 278-380 5.18e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 59.62  E-value: 5.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 278 AFHASDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWREIEADGAG--MVAADTVDGTEKNLVRWLElDDTARAAMR 355
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATD-VGGLPEVIEDGETglLVPPGDPEALAEAILRLLE-DPELRRRLG 94

                          90       100
                  ....*....|....*....|....*
gi 2502260919 356 AQAARTFEARFRIETMVSALTALLE 380
Cdd:COG0438    95 EAARERAEERFSWEAIAERLLALYE 119
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 160-309 2.53e-08

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: 55.42  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 160 RARQSFWLYRAQERIVPFG--TTVP-PHEATPLREAFLqaVPGlrGKRIVLFLGRVHAK--KGCDLLIDAFaRVASRDQS 234
Cdd:cd03825   151 MVRRSPLLKGLPVVVIPNGidTEIFaPVDKAKARKRLG--IPQ--DKKVILFGAESVTKprKGFDELIEAL-KLLATKDD 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2502260919 235 LHLVIAGPDEtgwatslraQAQAAGVAQRISLPGMLQGELKWGAFHASDVFVLPSHQENFGVAVAEALGCGLPAL 309
Cdd:cd03825   226 LLLVVFGKND---------PQIVILPFDIISLGYIDDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVV 291
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 85-330 6.13e-08

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: 54.00  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  85 VVVHGLWQYHGLAAWKAVRKSGVPYYVYTHGMlDPWFKQAYpLKHLKKWLYWPWAEYRVLRdARAVIFTTEEERTRARqs 164
Cdd:cd05844    83 ALVHAHFGRDGVYALPLARALGVPLVVTFHGF-DITTSRAW-LAASPGWPSQFQRHRRALQ-RPAALFVAVSGFIRDR-- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 165 fwlyrAQERIVPFG-TTVPPHEATPLReaFLQAVPGLRGKRIvLFLGRVHAKKGCDLLIDAFARVASRDQSLHLVIAGPd 243
Cdd:cd05844   158 -----LLARGLPAErIHVHYIGIDPAK--FAPRDPAERAPTI-LFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGD- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 244 etgwATSLRAQAQAAGVAQRISLPGMLQGELKWGAFHASDVFVLPS------HQENFGVAVAEALGCGLPALISDKVNVW 317
Cdd:cd05844   229 ----GPLRPALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIP 304

                         250
                  ....*....|...
gi 2502260919 318 REIEADGAGMVAA 330
Cdd:cd05844   305 EAILDGETGFLVP 317
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 78-328 1.05e-07

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: 53.54  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919  78 NAKRFDAVVVHglWQY------HGLAAWKAVRKSGVPYYVYTHgmldpwfkQAYPLKHLkkwlyWPWAEYRVLRDARA-- 149
Cdd:cd03822    72 NFKKPDVVHIQ--HEFgifggkYGLYALGLLLHLRIPVITTLH--------TVLDLSDP-----GKQALKVLFRIATLse 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 150 -VIFTTEEERTRARQSFWLYRAQERIVPFGTTVPPHEATPLREAFLqavpGLRGKRIVLFLGRVHAKKGCDLLIDAFARV 228
Cdd:cd03822   137 rVVVMAPISRFLLVRIKLIPAVNIEVIPHGVPEVPQDPTTALKRLL----LPEGKKVILTFGFIGPGKGLEILLEALPEL 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 229 ASRDQSLHLVIAGpdetGWATSLRAQAQAAGVAQRISLPGmLQGELKWGA-----------FHASDVFVLPSHQENFGV- 296
Cdd:cd03822   213 KAEFPDVRLVIAG----ELHPSLARYEGERYRKAAIEELG-LQDHVDFHNnflpeeevpryISAADVVVLPYLNTEQSSs 287

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2502260919 297 -AVAEALGCGLPAlISDKVNVWREIEADGAGMV 328
Cdd:cd03822   288 gTLSYAIACGKPV-ISTPLRHAEELLADGRGVL 319
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 281-314 2.60e-06

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: 49.21  E-value: 2.60e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2502260919 281 ASDVFVLPSHQENFGVAVAEALGCGLPALISDKV 314
Cdd:cd03812   265 AMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTI 298
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
170-313 8.55e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.48  E-value: 8.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 170 AQERIVPFGTTVPP--HEATPLREAFLQAVPGlrgKRIVLFLGRVHAKKGCDLLIDAFARVASRDQSLHLVIAG------ 241
Cdd:PRK15484  161 ADISIVPNGFCLETyqSNPQPNLRQQLNISPD---ETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGdptass 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502260919 242 PDETGwATSLRAQAQAAGVAQRISLPGMLQGELKWGAFHASDVFVLPSH-QENFGVAVAEALGCGLPALISDK 313
Cdd:PRK15484  238 KGEKA-AYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTK 309
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 279-312 2.92e-05

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: 45.90  E-value: 2.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2502260919 279 FHASDVFVLPSHQENFGVAVAEALGCGLPALISD 312
Cdd:cd04951   260 YNAADLFVLSSEWEGFGLVVAEAMACERPVVATD 293
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 199-307 4.26e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.47  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 199 GLRGKRIVLFLGRVHAKKGCDLLIDAFARVAsrDQSLHLVIAGPDetgwatslRAQAQAAGVAQRISLPGMLQGELKWGA 278
Cdd:PLN02871  259 GEPEKPLIVYVGRLGAEKNLDFLKRVMERLP--GARLAFVGDGPY--------REELEKMFAGTPTVFTGMLQGDELSQA 328

                          90       100
                  ....*....|....*....|....*....
gi 2502260919 279 FHASDVFVLPSHQENFGVAVAEALGCGLP 307
Cdd:PLN02871  329 YASGDVFVMPSESETLGFVVLEAMASGVP 357
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 281-373 5.14e-05

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: 45.04  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 281 ASDVFVLPSHQENFGVAVAEALGCGLPALISDkVNVWREIEADGAG--MVAADTVDGTEKNLVRWLElDDTARAAMRAQA 358
Cdd:cd04962   269 IADLFLLPSEKESFGLAALEAMACGVPVVSSN-AGGIPEVVKHGETgfLSDVGDVDAMAKSALSILE-DDELYNRMGRAA 346

                          90
                  ....*....|....*
gi 2502260919 359 ARTFEARFRIETMVS 373
Cdd:cd04962   347 RKRAAERFDPERIVP 361
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 205-381 1.87e-03

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 40.09  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 205 IVLFLGRVHAKKGCDLLIDAFARVASR----DQSLHLVIAGP-----------DETGWATSLRAQAQaagvaqRISLPGM 269
Cdd:TIGR03088 196 VVGTVGRLQAVKDQPTLVRAFALLVRQlpegAERLRLVIVGDgpargaceqmvRAAGLAHLVWLPGE------RDDVPAL 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502260919 270 LQgelkwgafhASDVFVLPSHQENFGVAVAEALGCGLPALISDKVNVWREIEADGAG-MVAADTVDGTEKNLVRWLElDD 348
Cdd:TIGR03088 270 MQ---------ALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGaLVPPGDAVALARALQPYVS-DP 339

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2502260919 349 TARAAMRAQAARTFEARFRIETMVSALTALLET 381
Cdd:TIGR03088 340 AARRAHGAAGRARAEQQFSINAMVAAYAGLYDQ 372
 
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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