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Conserved domains on  [gi|384072837|emb|CCG44327|]
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group 1 glycosyltransferase [Halobacillus halophilus DSM 2266]

Protein Classification

glycosyltransferase family 1 protein( domain architecture ID 10133579)

glycosyltransferase family 1 (GT1) protein similar to Bacillus subtilis glycosyltransferase EpsF, which may be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 6-357 6.34e-111

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: 328.09  E-value: 6.34e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMNRGGAETLIMNLYRNIDRSRVQFDFLTY--KEGVFDEEIKKLGGKVHRIPYISEVGHKQFVKGLDtfFRQH 83
Cdd:cd03812    1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATsdDKGEYDEELEELGGKIFYIPPKKKNIIKYFIKLLK--LIKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  84 FHYKIVHSHMDKMSGLVLRSAKRYGVTARIAHSHNTSSEGGFLTRLYKEYAGIFIKNNATHLYACSNLAAQWLFPKRVNE 163
Cdd:cd03812   79 EKYDIVHVHGSSSNGIILLLAAKAGVPVRIAHSHNTKDSSIKLRKIRKNVLKKLIERLSTKYLACSEDAGEWLFGEVENG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 164 -ALIIKNGIDSEKFTYSSTLRKQIRKELNLyEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKI 242
Cdd:cd03812  159 kFKVIPNGIDIEKYKFNKEKRRKRRKLLIL-EDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 243 IEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISDKISGEVDLGLgLMERLPIsSE 322
Cdd:cd03812  238 KEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN-NVEFLPL-NE 315

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 384072837 323 AQAIWVQKLLEKSSFQSQRLIS-SKKLNQSGYDIHL 357
Cdd:cd03812  316 TPSTWAEKILKLIKRKRRINKEiNKEKKELGYDDES 351
 
Name Accession Description Interval E-value
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 6-357 6.34e-111

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: 328.09  E-value: 6.34e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMNRGGAETLIMNLYRNIDRSRVQFDFLTY--KEGVFDEEIKKLGGKVHRIPYISEVGHKQFVKGLDtfFRQH 83
Cdd:cd03812    1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATsdDKGEYDEELEELGGKIFYIPPKKKNIIKYFIKLLK--LIKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  84 FHYKIVHSHMDKMSGLVLRSAKRYGVTARIAHSHNTSSEGGFLTRLYKEYAGIFIKNNATHLYACSNLAAQWLFPKRVNE 163
Cdd:cd03812   79 EKYDIVHVHGSSSNGIILLLAAKAGVPVRIAHSHNTKDSSIKLRKIRKNVLKKLIERLSTKYLACSEDAGEWLFGEVENG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 164 -ALIIKNGIDSEKFTYSSTLRKQIRKELNLyEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKI 242
Cdd:cd03812  159 kFKVIPNGIDIEKYKFNKEKRRKRRKLLIL-EDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 243 IEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISDKISGEVDLGLgLMERLPIsSE 322
Cdd:cd03812  238 KEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN-NVEFLPL-NE 315

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 384072837 323 AQAIWVQKLLEKSSFQSQRLIS-SKKLNQSGYDIHL 357
Cdd:cd03812  316 TPSTWAEKILKLIKRKRRINKEiNKEKKELGYDDES 351
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
197-295 5.59e-23

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 93.34  E-value: 5.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  197 HVIGHVGRFSL-QKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRsKIIEKIKvlRLEDKVQLLGIREDIPSLLQAIDVFL 275
Cdd:pfam13692   2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAA--GLEDRVIFTGFVEDLAELLAAADVFV 78

                          90       100
                  ....*....|....*....|
gi 384072837  276 FPSFHEGLPVTLIEAQGAGL 295
Cdd:pfam13692  79 LPSLYEGFGLKLLEAMAAGL 98
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
199-295 2.73e-12

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 67.80  E-value: 2.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 199 IGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPS 278
Cdd:PRK15490 401 IGGVFRFVGDKNPFAWIDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFS 480

                         90
                 ....*....|....*..
gi 384072837 279 FHEGLPVTLIEAQGAGL 295
Cdd:PRK15490 481 RYEGLPNVLIEAQMVGV 497
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 267-301 1.93e-05

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 43.44  E-value: 1.93e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 384072837 267 LLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISD 301
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATD 51
 
Name Accession Description Interval E-value
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 6-357 6.34e-111

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: 328.09  E-value: 6.34e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMNRGGAETLIMNLYRNIDRSRVQFDFLTY--KEGVFDEEIKKLGGKVHRIPYISEVGHKQFVKGLDtfFRQH 83
Cdd:cd03812    1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATsdDKGEYDEELEELGGKIFYIPPKKKNIIKYFIKLLK--LIKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  84 FHYKIVHSHMDKMSGLVLRSAKRYGVTARIAHSHNTSSEGGFLTRLYKEYAGIFIKNNATHLYACSNLAAQWLFPKRVNE 163
Cdd:cd03812   79 EKYDIVHVHGSSSNGIILLLAAKAGVPVRIAHSHNTKDSSIKLRKIRKNVLKKLIERLSTKYLACSEDAGEWLFGEVENG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 164 -ALIIKNGIDSEKFTYSSTLRKQIRKELNLyEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKI 242
Cdd:cd03812  159 kFKVIPNGIDIEKYKFNKEKRRKRRKLLIL-EDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 243 IEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISDKISGEVDLGLgLMERLPIsSE 322
Cdd:cd03812  238 KEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN-NVEFLPL-NE 315

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 384072837 323 AQAIWVQKLLEKSSFQSQRLIS-SKKLNQSGYDIHL 357
Cdd:cd03812  316 TPSTWAEKILKLIKRKRRINKEiNKEKKELGYDDES 351
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 6-301 2.21e-48

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: 167.49  E-value: 2.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMNRGGAETLIMNLYRNIDRSRVQFD-FLTYKEGVFDEEIKKLGGKVHRIPyisevghKQFVKGLDTFFRQHF 84
Cdd:cd03807    1 KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVvISLTGDGVLGEELLAAGVPVVCLG-------LSSGKDPGVLLRLAK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  85 HYK-----IVHSHM---DKMSGLvlrSAKRYGVTARIAHSHNTsseggfltrLYKEYAGIFIKNNATHLY-------ACS 149
Cdd:cd03807   74 LIRkrnpdVVHTWMyhaDLIGGL---AAKLAGGVKVIWSVRSS---------NIPQRLTRLVRKLCLLLSkfspatvANS 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 150 N----LAAQWLFPKRVneALIIKNGIDSEKFTYSSTLRKQIRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKK 225
Cdd:cd03807  142 SavaeFHQEQGYAKNK--IVVIYNGIDLFKLSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETH 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384072837 226 PNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISD 301
Cdd:cd03807  220 PDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATD 295
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 6-301 2.43e-46

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: 161.76  E-value: 2.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMNRGGAETLIMNLYRNIDRSRVQFDFLTY-KEGVFDEEIK---KLGGKVHRIPYISEVGHKQFVKGLDTFFR 81
Cdd:cd03811    1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLrDEGDLDKQLNgdvKLIRLLIRVLKLIKLGLLKAILKLKRILK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  82 QHfHYKIVHSHMDKMSGLVlrSAKRYGVTARIAHSHNTSSEGGFLTRLYKEYAGIFikNNATHLYACSNLAAQWL---FP 158
Cdd:cd03811   81 RA-KPDVVISFLGFATYIV--AKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKLY--KKADKIVCVSKGIKEDLirlGP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 159 KRVNEALIIKNGIDSEKFtysstlrKQIRKELNLYEDTH--VIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDG 236
Cdd:cd03811  156 SPPEKIEVIYNPIDIDRI-------RALAKEPILNEPEDgpVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDG 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384072837 237 PLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISD 301
Cdd:cd03811  229 PLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTD 293
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 6-295 1.83e-36

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: 135.74  E-value: 1.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVV--VNMNRGGAETLIMNLYRNIDRSRVQFDFLTYKEGVFDEEIKKLGGKVHRIPYISEVGHKQFVKGLDTFFRQH 83
Cdd:cd03801    1 KILLLSpeLPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  84 FHYKIVHSHMDKMSGLVLRSAKRYGVtARIAHSHNTSSEGGFLTRLYKE---YAGIFIKNNATHLYACSNLAAQWL---F 157
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLALLLGA-PLVVTLHGAEPGRLLLLLAAERrllARAEALLRRADAVIAVSEALRDELralG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 158 PKRVNEALIIKNGIDSEKFtysstlRKQIRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIG-DG 236
Cdd:cd03801  160 GIPPEKIVVIPNGVDLERF------SPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDG 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384072837 237 PLRSKIIEKIkvLRLEDKVQLLGIR--EDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGL 295
Cdd:cd03801  234 PLRAELEELE--LGLGDRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGL 292
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 6-301 6.29e-34

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: 128.87  E-value: 6.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMnrGGAETLIMNLYRNIDRSRVQFDFLTYKEGVFDEEIKKLGGKVHRIPyISEVG--HKQFVKGLdTFFRQH 83
Cdd:cd03808    1 KILFIVNVD--GGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIP-ILRRGinPLKDLKAL-FKLYKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  84 FH---YKIVHSHMDKmSGLVLR-SAKRYGVTARIAHSHNTSSEGG-------FLTRLYKeyagiFIKNNATHLYACS--- 149
Cdd:cd03808   77 LKkekPDIVHCHTPK-PGILGRlAARLAGVPKVIYTVHGLGFVFTegkllrlLYLLLEK-----LALLFTDKVIFVNedd 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 150 -NLAAQWLFPKRVNEALIIKNGIDSEKFTYSSTlrkqirkelNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNS 228
Cdd:cd03808  151 rDLAIKKGIIKKKKTVLIPGSGVDLDRFQYSPE---------SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNV 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384072837 229 RLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISD 301
Cdd:cd03808  222 RFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTD 294
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 6-295 1.00e-27

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: 111.77  E-value: 1.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMNRGGAETLIMNLYRNIDR--SRVQFDFLT----YKEGVFDEEIKKLG-GKVHRIPYISEVGHKQFVKgldt 78
Cdd:cd04951    1 KILYVITGLGLGGAEKQTVLLADQMFIrgHDVNIVYLTgeveVKPLNNNIIIYNLGmDKNPRSLLKALLKLKKIIS---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  79 ffrqHFHYKIVHSHMDKMSGLVLRSAKRYGVTARIAHSHNTSSEGGFLTRLYKEYAGIFIKNNATHLYACSNLAAQWLFP 158
Cdd:cd04951   77 ----AFKPDVVHSHMFHANIFARFLRMLYPIPLLICTAHNKNEGGRIRMFIYRLTDFLCDITTNVSREALDEFIAKKAFS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 159 KrvNEALIIKNGIDSEKFTYSSTLRKQIRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPL 238
Cdd:cd04951  153 K--NKSVPVYNGIDLNKFKKDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPL 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384072837 239 RSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGL 295
Cdd:cd04951  231 RNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACER 287
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 17-294 2.83e-27

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: 110.14  E-value: 2.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  17 GGAETLIMNLYRNIDRSRVQFDFLTYK-EGVFDEEIKKLGGKVHRIPYISEVGHKQFVKGLdtffRQHFHYKIVHSHMDK 95
Cdd:cd03819   11 GGAETYILDLARALAERGHRVLVVTAGgPLLPRLRQIGIGLPGLKVPLLRALLGNVRLARL----IRRERIDLIHAHSRA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  96 MSGLVLRSAKRYGVtARIAHSHNTSSEGGFLTRLYKeyagiFIKNNATHLYACSNLAAQWLF------PKRVNealIIKN 169
Cdd:cd03819   87 PAWLGWLASRLTGV-PLVTTVHGSYLATYHPKDFAL-----AVRARGDRVIAVSELVRDHLIealgvdPERIR---VIPN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 170 GIDSEKFTYSSTLRKqiRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEySRKKPNSRLLLIGDGPLRSKIIEKIKVL 249
Cdd:cd03819  158 GVDTDRFPPEAEAEE--RAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAE-LKDEPDFRLLVAGDGPERDEIRRLVERL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 384072837 250 RLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAG 294
Cdd:cd03819  235 GLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACG 279
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 49-295 2.34e-24

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: 102.74  E-value: 2.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  49 EEIKKLGGKVHRI--------PYISEVGHKQFVKGLDTFFRQHFHYKIVHSHMDKMsglvlrsaKRYGvtARIAHSHNTS 120
Cdd:cd03817   25 RALEKRGHEVYVItpsdpgaeDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRI--------KELG--PDIIHTHTPF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 121 SEGGFLTRL---------------YKEYAGIFIK-----------------NNATHLYACSNLAAQWL------FPKRVn 162
Cdd:cd03817   95 SLGKLGLRIarklkipivhtyhtmYEDYLHYIPKgkllvkavvrklvrrfyNHTDAVIAPSEKIKDTLreygvkGPIEV- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 163 ealiIKNGIDSEKFtySSTLRKQIRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEySRKKPNSRLLLIGDGPLRSKI 242
Cdd:cd03817  174 ----IPNGIDLDKF--EKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAE-LKKEPNIKLVIVGDGPEREEL 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384072837 243 IEKIKVLRLEDKVQLLGI--REDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGL 295
Cdd:cd03817  247 KELARELGLADKVIFTGFvpREELPEYYKAADLFVFASTTETQGLVYLEAMAAGL 301
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
197-295 5.59e-23

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 93.34  E-value: 5.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  197 HVIGHVGRFSL-QKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRsKIIEKIKvlRLEDKVQLLGIREDIPSLLQAIDVFL 275
Cdd:pfam13692   2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAA--GLEDRVIFTGFVEDLAELLAAADVFV 78

                          90       100
                  ....*....|....*....|
gi 384072837  276 FPSFHEGLPVTLIEAQGAGL 295
Cdd:pfam13692  79 LPSLYEGFGLKLLEAMAAGL 98
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 198-301 1.96e-21

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: 89.64  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  198 VIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGI--REDIPSLLQAIDVFL 275
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFvsDEDLPELLKIADVFV 83

                          90       100
                  ....*....|....*....|....*.
gi 384072837  276 FPSFHEGLPVTLIEAQGAGLHCFISD 301
Cdd:pfam00534  84 LPSRYEGFGIVLLEAMACGLPVIASD 109
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 13-295 1.60e-20

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: 91.67  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  13 NMNRGGAETLIMNLYRNIDRSRVQFDFLTYKEGVFDEEIKKLGGKVHRIPYISEVGHKQFVKGLDT-------------F 79
Cdd:cd03798   10 NANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLlaplrapslakllK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  80 FRQHFHYKIVHSHMDKMSGLVLRSAKR-----YGVTARiahshnTSSEGGFLTRLYKEYAGIFIKNNATHLYACSN---- 150
Cdd:cd03798   90 RRRRGPPDLIHAHFAYPAGFAAALLARlygvpYVVTEH------GSDINVFPPRSLLRKLLRWALRRAARVIAVSKalae 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 151 -LAAQWLFPKRVNealIIKNGIDSEKFtysstlrKQIRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSR 229
Cdd:cd03798  164 eLVALGVPRDRVD---VIPNGVDPARF-------QPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVV 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384072837 230 LLLIGDGPLRSKIIEKIKVLRLEDKVQLLGI--REDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGL 295
Cdd:cd03798  234 LLIVGDGPLREALRALAEDLGLGDRVTFTGRlpHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGL 301
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 140-301 3.96e-19

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


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 87.79  E-value: 3.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 140 NNATHLYACSNLAAQW---LFPKRvNEALIIKNGIDSEKFtySSTLRKQIRKELNLYEDTHVIGHVGRFSLQKNHMFLIE 216
Cdd:cd04962  140 NKSDRVTAVSSSLRQEtyeLFDVD-KDIEVIHNFIDEDVF--KRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVR 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 217 VFAEYSRKKPnSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLH 296
Cdd:cd04962  217 VFARVRRKIP-AKLLLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVP 295


                 ....*
gi 384072837 297 CFISD 301
Cdd:cd04962  296 VVSSN 300
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 202-305 1.23e-18

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: 86.14  E-value: 1.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 202 VGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPSFHE 281
Cdd:cd03820  187 VGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYE 266

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 384072837 282 GLPVTLIEAQGAGLHC-----------FISDKISG 305
Cdd:cd03820  267 GFPMVLLEAMAYGLPIisfdcptgpseIIEDGENG 301
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 124-295 1.35e-17

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: 80.91  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 124 GFLTRLYKEYAGIFIKNNATHLYACSNLAAQWLfpkRVNEALIIKNGI-------DSEKFTYSSTLRKQIRKELNLYEDt 196
Cdd:cd01635   37 ALLLLALRRILKKLLELKPDVVHAHSPHAAALA---ALLAARLLGIPIvvtvhgpDSLESTRSELLALARLLVSLPLAD- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 197 HVigHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLG---IREDIPSLLQAIDV 273
Cdd:cd01635  113 KV--SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGglvDDEVLELLLAAADV 190

                        170       180
                 ....*....|....*....|..
gi 384072837 274 FLFPSFHEGLPVTLIEAQGAGL 295
Cdd:cd01635  191 FVLPSRSEGFGLVLLEAMAAGK 212
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 6-326 7.21e-17

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: 81.26  E-value: 7.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHVVVNMN--RGGAETLIMNLYRNIDRSRVQFDFLTY---KEGVFDEEIKKLGGKV---HRIP-YISEVGHKQFVKGL 76
Cdd:cd03821    1 KILHVTPSISpkAGGPVKVVLRLAAALAALGHEVTIVSTgdgYESLVVEENGRYIPPQdgfASIPlLRQGAGRTDFSPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  77 DTFFRQHFH-YKIVHSH--MDKMSGLVLRSAKR----YGVTARIAHSHNTSSEGGFLTRLYKEYAGIFIKNNATHLYACS 149
Cdd:cd03821   81 PNWLRRNLReYDVVHIHgvWTYTSLAACKLARRrgipYVVSPHGMLDPWALQQKHWKKRIALHLIERRNLNNAALVHFTS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 150 NLAAQWLFPKRVNEA-LIIKNGIDSEKFtySSTLRKqiRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNS 228
Cdd:cd03821  161 EQEADELRRFGLEPPiAVIPNGVDIPEF--DPGLRD--RRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDW 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 229 RLLLIG-DGPLRSKIIEKIKVLRLEDKVQLLGI--REDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISDK--I 303
Cdd:cd03821  237 HLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTGPlyGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKcgL 316

                        330       340
                 ....*....|....*....|...
gi 384072837 304 SGEVDLGLGLMERLPISSEAQAI 326
Cdd:cd03821  317 SELVEAGCGVVVDPNVSSLAEAL 339
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 71-295 2.86e-15

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: 76.51  E-value: 2.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  71 QFVKGLDTFFRQHF-HYKIVHSHMdKMSGLV-LRSAKRYGVT-ARIAHShntsseggfLTRLYKEYAGI----------- 136
Cdd:cd03800   86 EFADGLLRFIAREGgRYDLIHSHY-WDSGLVgALLARRLGVPlVHTFHS---------LGRVKYRHLGAqdtyhpslrit 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 137 ---FIKNNATHLYA-CSNLAA-QW----LFPKRVNealIIKNGIDSEKFtYSSTLRKQIRKELNLYEDTHVIGHVGRFSL 207
Cdd:cd03800  156 aeeQILEAADRVIAsTPQEADeLIslygADPSRIN---VVPPGVDLERF-FPVDRAEARRARLLLPPDKPVVLALGRLDP 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 208 QKNHMFLIEVFAEYSRKKPNSRLLLIG--DGPLRSK----IIEKIKVLRLEDKVQLLG--IREDIPSLLQAIDVFLFPSF 279
Cdd:cd03800  232 RKGIDTLVRAFAQLPELRELANLVLVGgpSDDPLSMdreeLAELAEELGLIDRVRFPGrvSRDDLPELYRAADVFVVPSL 311

                        250
                 ....*....|....*.
gi 384072837 280 HEGLPVTLIEAQGAGL 295
Cdd:cd03800  312 YEPFGLTAIEAMACGT 327
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 156-301 1.08e-13

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: 71.63  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 156 LFPKRVNEALIIKNGIDSEKFTYSSTLRKQIRKELnlyeDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIG- 234
Cdd:cd03809  156 FYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLL----PEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGg 231

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384072837 235 DGPLRSKIIEKIKVLRLEDKVQLLGI--REDIPSLLQAIDVFLFPSFHE--GLPVtlIEAQGAGLHCFISD 301
Cdd:cd03809  232 KGWEDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEgfGLPV--LEAMACGTPVIASN 300
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 80-328 1.63e-13

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: 70.94  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  80 FRQHFHYKIVHSHMDKMsGLVLRSAKRYGVtarIAHSHNTSSEGGFLTRLYKEYAgifiKNNATHLYACSN--LAAQWLF 157
Cdd:cd03799   65 LNKKGAYDIIHCQFGPL-GALGALLRRLKV---LKGKLVTSFRGYDISMYVILEG----NKVYPQLFAQGDlfLPNCELF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 158 PKRV-----NEALII--KNGIDSEKFTYsstlrkqirKELNLYEDTHV-IGHVGRFSLQKNHMFLIEVFAEYSRKKPNSR 229
Cdd:cd03799  137 KHRLialgcDEKKIIvhRSGIDCNKFRF---------KPRYLPLDGKIrILTVGRLTEKKGLEYAIEAVAKLAQKYPNIE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 230 LLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIR--EDIPSLLQAIDVFLFPSF------HEGLPVTLIEAQGAGL------ 295
Cdd:cd03799  208 YQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKpqEEIIEILDEADIFIAPSVtaadgdQDGPPNTLKEAMAMGLpviste 287

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 384072837 296 HC----FISDKISG----EVDLGlGLMERLPISSEAQAIWV 328
Cdd:cd03799  288 HGgipeLVEDGVSGflvpERDAE-AIAEKLTYLIEHPAIWP 327
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
199-295 2.73e-12

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 67.80  E-value: 2.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 199 IGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPS 278
Cdd:PRK15490 401 IGGVFRFVGDKNPFAWIDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFS 480

                         90
                 ....*....|....*..
gi 384072837 279 FHEGLPVTLIEAQGAGL 295
Cdd:PRK15490 481 RYEGLPNVLIEAQMVGV 497
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 129-295 4.10e-12

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 67.37  E-value: 4.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 129 LYKEYA---GIFIKNN---ATHLYAcsnlaaQWL-FPKRvnEALIIKNGIDSEKFTYSSTLRK---QIRKELNlyEDTHV 198
Cdd:PRK15179 450 IYSELLkmrGVALSSNsqfAAHRYA------DWLgVDER--RIPVVYNGLAPLKSVQDDACTAmmaQFDARTS--DARFT 519

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 199 IGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQAIDVFLFPS 278
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLS 599

                        170
                 ....*....|....*..
gi 384072837 279 FHEGLPVTLIEAQGAGL 295
Cdd:PRK15179 600 RFEGLPNVLIEAQFSGV 616
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 170-295 5.20e-12

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: 66.55  E-value: 5.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 170 GIDSEKFtySSTLRKQ-IRKELnLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPnSRLLLIGDGPLRskiiekiKV 248
Cdd:cd03814  174 GVDTELF--HPSRRDAaLRRRL-GPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPP-VRLVVVGDGPAR-------AE 242

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384072837 249 LRLED-KVQLLGIR--EDIPSLLQAIDVFLFPSFHE--GLpVTLiEAQGAGL 295
Cdd:cd03814  243 LEARGpDVIFTGFLtgEELARAYASADVFVFPSRTEtfGL-VVL-EAMASGL 292
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 177-295 2.08e-11

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: 64.24  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 177 TYSSTLRKqirKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQ 256
Cdd:cd04949  144 GYVDQLDT---AESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVF 220

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 384072837 257 LLGIREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGL 295
Cdd:cd04949  221 LKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGL 259
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 6-295 5.41e-11

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


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 63.06  E-value: 5.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   6 RVLHV--VVNMNRGGAETLIMNLYRNIDRSRVQFDFLTYKEGVFDEEIKKLGGKVHRIPYISEVGHKQF-VKGLDTFFRQ 82
Cdd:cd03795    1 KVLHVfkFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFsPSYIKRFKKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  83 HFHYKIVHSH-----MDKMSGLVLRSAKRygvtarIAHSHNTSSEGGFLTRLYKEYAGIFIKNNATHLYACSNLAA--QW 155
Cdd:cd03795   81 AKEYDIIHYHfpnplADLLLFFSGAKKPV------VVHWHSDIVKQKKLLKLYKPLMTRFLRRADRIIATSPNYVEtsPT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 156 LFPKRvNEALIIKNGIDSEKFTYSSTLRKQIRKElnlYEDTHVIGHVGRFSLQKNHMFLIEvfaeySRKKPNSRLLLIGD 235
Cdd:cd03795  155 LREFK-NKVRVIPLGIDKNVYNIPRVDFENIKRE---KKGKKIFLFIGRLVYYKGLDYLIE-----AAQYLNYPIVIGGE 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384072837 236 GPLRSKIIEKIKVLRLeDKVQLLGI--REDIPSLLQAIDVFLFPSF--HEGLPVTLIEAQGAGL 295
Cdd:cd03795  226 GPLKPDLEAQIELNLL-DNVKFLGRvdDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGK 288
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 166-301 1.33e-10

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: 62.35  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 166 IIKNGIDSEKFtysstlrKQIRKELNlYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIG---DGPL-RSK 241
Cdd:cd03813  271 VIPNGIDIQRF-------APAREERP-EKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGpedEDPEyAQE 342

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 242 IIEKIKVLRLEDKVQLLGiREDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISD 301
Cdd:cd03813  343 CKRLVASLGLENKVKFLG-FQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATD 401
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 152-295 1.56e-10

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 62.42  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 152 AAQWLFPKRVneaLIIKNGIDSEKFT---YSSTLRKQIRkelNLYEDTHVIGHVGRFSLQKNHMFLIEVFAeysrKKPNS 228
Cdd:PLN02871 222 AAGVTAANRI---RVWNKGVDSESFHprfRSEEMRARLS---GGEPEKPLIVYVGRLGAEKNLDFLKRVME----RLPGA 291

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384072837 229 RLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGirEDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGL 295
Cdd:PLN02871 292 RLAFVGDGPYREELEKMFAGTPTVFTGMLQG--DELSQAYASGDVFVMPSESETLGFVVLEAMASGV 356
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 194-294 2.05e-09

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


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 58.62  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 194 EDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLrleDKVQLLGI--REDIPSLLQAI 271
Cdd:cd05844  187 ERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL---GRVRFLGAlpHAEVQDWMRRA 263

                         90       100
                 ....*....|....*....|....*....
gi 384072837 272 DVFLFPSF------HEGLPVTLIEAQGAG 294
Cdd:cd05844  264 EIFCLPSVtaasgdSEGLGIVLLEAAACG 292
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 88-295 3.44e-09

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: 57.72  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837  88 IVHSH-MDKMSGLVLRSAKRYG----VTAR----IAHSHNTSSEGG--------FLTRLYkEYAGifiknnathlyacsn 150
Cdd:cd03823   99 VVHTHnLSGLGASLLDAARDLGipvvHTLHdywlLCPRQFLFKKGGdavlapsrFTANLH-EANG--------------- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 151 laaqwLFPKRVneaLIIKNGIDSEKftysstlrkqIRKELNLYEDTH-VIGHVGRFSLQKNHMFLIEVFAEYSRkkPNSR 229
Cdd:cd03823  163 -----LFSARI---SVIPNAVEPDL----------APPPRRRPGTERlRFGYIGRLTEEKGIDLLVEAFKRLPR--EDIE 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384072837 230 LLLIGDGPLrskiiEKIKVLRLEDKVQLLGI--REDIPSLLQAIDVFLFPS-FHEGLPVTLIEAQGAGL 295
Cdd:cd03823  223 LVIAGHGPL-----SDERQIEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAGL 286
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 158-307 3.84e-09

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: 57.63  E-value: 3.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 158 PKRVNealIIKNGIDSEKFTYSSTLRKQirkelnlyeDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDGP 237
Cdd:cd03796  167 PRIVS---VIPNAVDSSDFTPDPSKPDP---------NKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGP 234

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384072837 238 LRSKIIEKIKVLRLEDKVQLLGI--REDIPSLLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCfISDKISG--EV 307
Cdd:cd03796  235 KRIELEEMREKYQLQDRVELLGAvpHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLV-VSTRVGGipEV 307
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
166-302 5.82e-09

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 57.11  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 166 IIKNGIDSEkfTYSSTLRKQIRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIGDgPLRSKIIEK 245
Cdd:PRK15484 165 IVPNGFCLE--TYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGD-PTASSKGEK 241

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384072837 246 I----KVL----RLEDKVQLLGIR--EDIPSLLQAIDVFLFPS-FHEGLPVTLIEAQGAGLHCFISDK 302
Cdd:PRK15484 242 AayqkKVLeaakRIGDRCIMLGGQppEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTK 309
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
17-174 9.57e-09

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 54.08  E-value: 9.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   17 GGAETLIMNLYRNIDRSRVQFDFLTYKEGVFDEEIKKLGGKVHRIPYISEVGHKQFVKGLDTFFR--QHFHYKIVHSHMD 94
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRllRRERPDVVHAHSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837   95 KMSGLVLRSAKRYGVTARIAHSHNTSSEGGFLTRLYKEYAGIFIK------NNATHLYACSNLAAQWL---FPKRVNEAL 165
Cdd:pfam13439  81 FPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRlerrllRRADRVIAVSEAVADELrrlYGVPPEKIR 160


                  ....*....
gi 384072837  166 IIKNGIDSE 174
Cdd:pfam13439 161 VIPNGVDLE 169
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 166-295 7.53e-08

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: 53.89  E-value: 7.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 166 IIKNGIDSEKFTYSStlRKQIRKELNLyEDTHVIGHVGRFSLQKNHMFLIEVfAEYSRKKPNSRLLLIGDGPLRSKIIEK 245
Cdd:cd03794  190 VIPNWADLEEFKPPP--KDELRKKLGL-DDKFVVVYAGNIGKAQGLETLLEA-AERLKRRPDIRFLFVGDGDEKERLKEL 265

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384072837 246 IKvLRLEDKVQLLG--IREDIPSLLQAIDVFLFP-----SFHEGLPVTLIEAQGAGL 295
Cdd:cd03794  266 AK-ARGLDNVTFLGrvPKEEVPELLSAADVGLVPlkdnpANRGSSPSKLFEYMAAGK 321
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 166-295 2.28e-07

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: 52.33  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 166 IIKNGIDSEKFTYSStlRKQIRKELNLYEDTHVI--GHVGRFSLQKNHMFLIEVFAEYSrKKPNSRLLLIGDGPLRSKII 243
Cdd:cd03825  165 VIPNGIDTEIFAPVD--KAKARKRLGIPQDKKVIlfGAESVTKPRKGFDELIEALKLLA-TKDDLLLVVFGKNDPQIVIL 241

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 384072837 244 --EKIKVLRLEDKVQLLgiredipSLLQAIDVFLFPSFHEGLPVTLIEAQGAGL 295
Cdd:cd03825  242 pfDIISLGYIDDDEQLV-------DIYSAADLFVHPSLADNLPNTLLEAMACGT 288
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
201-309 1.57e-05

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 46.24  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 201 HVGR--FSLQKNhmfLIEVFAEYSRKKPNSRLLLIGDGPLRSKIIEKIKVLRLEDKVQLLGIREDIPSLLQA----IDVF 274
Cdd:PRK09922 185 YVGRlkFEGQKN---VKELFDGLSQTTGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVQQkiknVSAL 261

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 384072837 275 LFPSFHEGLPVTLIEAQGAGLHCFISDKISGEVDL 309
Cdd:PRK09922 262 LLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDI 296
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 267-301 1.93e-05

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 43.44  E-value: 1.93e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 384072837 267 LLQAIDVFLFPSFHEGLPVTLIEAQGAGLHCFISD 301
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATD 51
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 186-277 6.10e-04

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: 41.60  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384072837 186 IRKELNLYEDTHVIGHVGRFSLQKNHMFLIEVFAEYSRKKPNSRLLLIG---DGPLRSKIIEK----IKVLRLEDKVQLL 258
Cdd:cd03822  177 ALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelhPSLARYEGERYrkaaIEELGLQDHVDFH 256

                         90       100
                 ....*....|....*....|..
gi 384072837 259 --GIR-EDIPSLLQAIDVFLFP 277
Cdd:cd03822  257 nnFLPeEEVPRYISAADVVVLP 278
 
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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