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Conserved domains on  [gi|488288167|ref|WP_002359375|]
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MULTISPECIES: cell wall glycolipid biosynthesis glucosyltransferase BgsA [Enterococcus]

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 ...
 61-317 1.28e-35

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 cd03817:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 372  Bit Score: 132.40  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  61 VRKARKLGKKVIYHAHSTEEDFRNSFIGSNQLAP-LVKKYLISLYSKADHLITPTPYSKTLLEGYGIKVPISAISNGIDL 139
Cdd:cd03817  101 LRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKaVVRKLVRRFYNHTDAVIAPSEKIKDTLREYGVKGPIEVIPNGIDL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 140 SRFYPSEEKEqkFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQL---PEYQFIWFGDTPmYSipKNIRQLVKEDH- 215
Cdd:cd03817  181 DKFEKPLNTE--ERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELkkePNIKLVIVGDGP-ER--EELKELARELGl 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 216 PENVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIPVYQ--------GWLVANENcymghsi 287
Cdd:cd03817  256 ADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASelvedgenGFLFEPND------- 328

                        250       260       270
                 ....*....|....*....|....*....|
gi 488288167 288 EEFKKYIEGLLEGKIPSTREAgyQVAEQRS 317
Cdd:cd03817  329 ETLAEKLLHLRENLELLRKLS--KNAEISA 356
 
Name Accession Description Interval E-value
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 61-317 1.28e-35

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: 132.40  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  61 VRKARKLGKKVIYHAHSTEEDFRNSFIGSNQLAP-LVKKYLISLYSKADHLITPTPYSKTLLEGYGIKVPISAISNGIDL 139
Cdd:cd03817  101 LRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKaVVRKLVRRFYNHTDAVIAPSEKIKDTLREYGVKGPIEVIPNGIDL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 140 SRFYPSEEKEqkFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQL---PEYQFIWFGDTPmYSipKNIRQLVKEDH- 215
Cdd:cd03817  181 DKFEKPLNTE--ERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELkkePNIKLVIVGDGP-ER--EELKELARELGl 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 216 PENVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIPVYQ--------GWLVANENcymghsi 287
Cdd:cd03817  256 ADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASelvedgenGFLFEPND------- 328

                        250       260       270
                 ....*....|....*....|....*....|
gi 488288167 288 EEFKKYIEGLLEGKIPSTREAgyQVAEQRS 317
Cdd:cd03817  329 ETLAEKLLHLRENLELLRKLS--KNAEISA 356
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 161-312 1.96e-16

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: 75.39  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  161 EKKVIICVGLFFERKGITDFIEVARQL----PEYQFIWFGDTPMYSIPKNIRQlvKEDHPENVIFPGYIKGDVIEGAYAA 236
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLkeknPNLKLVIAGDGEEEKRLKKLAE--KLGLGDNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  237 ANLFFFPSREETEGIVVLEALASQQQVLVRDIPVY--------QGWLVANENcymghsIEEFKKYIEGLLEGKIPSTR-- 306
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPpevvkdgeTGFLVKPNN------AEALAEAIDKLLEDEELRERlg 152


                  ....*.
gi 488288167  307 EAGYQV 312
Cdd:pfam00534 153 ENARKR 158
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 46-259 9.36e-15

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 74.75  E-value: 9.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  46 DILHINTYGVnshrMVRKARKLGKKV------IYHAHSTeedfrnSFIGSNQLAPLVKKY--LIS-LYSKADHLITPTPY 116
Cdd:PLN02871 146 DLIHASSPGI----MVFGALFYAKLLcvplvmSYHTHVP------VYIPRYTFSWLVKPMwdIIRfLHRAADLTLVTSPA 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 117 SKTLLEGYGIKVP--ISAISNGIDLSRFYP---SEEKEQKFREYfkiDEEKKVIICVGLFFERKGITDFIEVARQLPEYQ 191
Cdd:PLN02871 216 LGKELEAAGVTAAnrIRVWNKGVDSESFHPrfrSEEMRARLSGG---EPEKPLIVYVGRLGAEKNLDFLKRVMERLPGAR 292

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 192 FIWFGDTPMYSipknirQLvkEDHPE--NVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALAS 259
Cdd:PLN02871 293 LAFVGDGPYRE------EL--EKMFAgtPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMAS 354
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 223-334 3.78e-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: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 223 GYIKG--DVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIPVYQGWLVANENCYM--GHSIEEFKKYIEGLL 298
Cdd:COG0438    5 VPRKGldLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLvpPGDPEALAEAILRLL 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488288167 299 E--GKIPSTREAGYQVAEQR-SIKQIGYELKEVYETVLS 334
Cdd:COG0438   85 EdpELRRRLGEAARERAEERfSWEAIAERLLALYEELLA 123
 
Name Accession Description Interval E-value
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 61-317 1.28e-35

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: 132.40  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  61 VRKARKLGKKVIYHAHSTEEDFRNSFIGSNQLAP-LVKKYLISLYSKADHLITPTPYSKTLLEGYGIKVPISAISNGIDL 139
Cdd:cd03817  101 LRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKaVVRKLVRRFYNHTDAVIAPSEKIKDTLREYGVKGPIEVIPNGIDL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 140 SRFYPSEEKEqkFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQL---PEYQFIWFGDTPmYSipKNIRQLVKEDH- 215
Cdd:cd03817  181 DKFEKPLNTE--ERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELkkePNIKLVIVGDGP-ER--EELKELARELGl 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 216 PENVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIPVYQ--------GWLVANENcymghsi 287
Cdd:cd03817  256 ADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASelvedgenGFLFEPND------- 328

                        250       260       270
                 ....*....|....*....|....*....|
gi 488288167 288 EEFKKYIEGLLEGKIPSTREAgyQVAEQRS 317
Cdd:cd03817  329 ETLAEKLLHLRENLELLRKLS--KNAEISA 356
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 7-330 2.17e-30

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: 118.41  E-value: 2.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167   7 FEGEKILAKSGIGRALDHQKRALSEVGIEYTLdadcSDYDILHINTYGVnSHRMVRKARKLGKKVIYHAHSTEEDFRNSF 86
Cdd:cd03801   49 LEDGVIVPLLPSLAALLRARRLLRELRPLLRL----RKFDVVHAHGLLA-ALLAALLALLLGAPLVVTLHGAEPGRLLLL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  87 igSNQLAPLVKKYLIsLYSKADHLITPTPYSKTLLEGYGIKVP--ISAISNGIDLSRFYPseekeqKFREYFKIDEEKKV 164
Cdd:cd03801  124 --LAAERRLLARAEA-LLRRADAVIAVSEALRDELRALGGIPPekIVVIPNGVDLERFSP------PLRRKLGIPPDRPV 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 165 IICVGLFFERKGITDFIEVARQL----PEYQFIWFGDTPmySIPKNIRQLVKEDHpENVIFPGYIKGDVIEGAYAAANLF 240
Cdd:cd03801  195 LLFVGRLSPRKGVDLLLEALAKLlrrgPDVRLVIVGGDG--PLRAELEELELGLG-DRVRFLGFVPDEELPALYAAADVF 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 241 FFPSREETEGIVVLEALASQQQVLVRDIPVYQGWLVANENCYM--GHSIEEFKKYIEGLLEGkiPSTR----EAGYQVAE 314
Cdd:cd03801  272 VLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVvpPDDVEALADALLRLLAD--PELRarlgRAARERVA 349

                        330
                 ....*....|....*..
gi 488288167 315 QR-SIKQIGYELKEVYE 330
Cdd:cd03801  350 ERfSWERVAERLLDLYR 366
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 46-267 2.37e-26

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: 107.38  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  46 DILHINTYGVNSHRMVRKARKLGKKVI--YHahsteEDFrNSFIGSNQLAPLVK---KYLISLYSKADHLITPTPYSKTL 120
Cdd:cd03814   86 DIIHIATPGPLGLAALRAARRLGLPVVtsYH-----TDF-PEYLSYYTLGPLSWlawAYLRWFHNPFDTTLVPSPSIARE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 121 LEGYGIKvPISAISNGIDLSRFYPSEeKEQKFREYFKiDEEKKVIICVGLFFERKGITDFIEVARQLPE---YQFIWFGD 197
Cdd:cd03814  160 LEGHGFE-RVRLWPRGVDTELFHPSR-RDAALRRRLG-PPGRPLLLYVGRLAPEKNLEALLDADLPLAAsppVRLVVVGD 236

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 198 TPmysipknIRQLVKEDHPeNVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRD 267
Cdd:cd03814  237 GP-------ARAELEARGP-DVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAAD 298
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 45-269 8.76e-22

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: 94.31  E-value: 8.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  45 YDILHINTYGvnSHRMVRKARKL--GKKVIYHAHSTEEDFRnsfigsnqLAPLVKKY--LISLYSKAdhLITPTPYSKTL 120
Cdd:cd03807   80 PDVVHTWMYH--ADLIGGLAAKLagGVKVIWSVRSSNIPQR--------LTRLVRKLclLLSKFSPA--TVANSSAVAEF 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 121 LEGYGI-KVPISAISNGIDLSRFYPSEEKEQKFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQL----PEYQFIWF 195
Cdd:cd03807  148 HQEQGYaKNKIVVIYNGIDLFKLSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLvethPDLRLLLV 227

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288167 196 GDTPMYsipKNIRQLVKEDHPEN-VIFPGYIkGDVIEgAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIP 269
Cdd:cd03807  228 GRGPER---PNLERLLLELGLEDrVHLLGER-SDVPA-LLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVG 297
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 61-332 1.79e-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: 90.90  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  61 VRKARKLGKKVIYHAHSteedfrnSFIGSNQLAPLVKKYLISLYSKADHLITPTPYSKTLLEGYG-IKVPISAISNGIDL 139
Cdd:cd03798  112 ALLARLYGVPYVVTEHG-------SDINVFPPRSLLRKLLRWALRRAARVIAVSKALAEELVALGvPRDRVDVIPNGVDP 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 140 SRFYPSEEKEQKfreyfkiDEEKKVIICVGLFFERKGITDFIE----VARQLPEYQFIWFGDTPMysiPKNIRQLVKEDH 215
Cdd:cd03798  185 ARFQPEDRGLGL-------PLDAFVILFVGRLIPRKGIDLLLEafarLAKARPDVVLLIVGDGPL---REALRALAEDLG 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 216 PEN-VIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVL------VRDI--PVYQGWLVANENcymghs 286
Cdd:cd03798  255 LGDrVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVatdvggIPEVvgDPETGLLVPPGD------ 328

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488288167 287 IEEFKKYIEGLL--EGKIPSTREAGYQVAEQRSIKQIGYELKEVYETV 332
Cdd:cd03798  329 ADALAAALRRALaePYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 44-316 6.70e-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: 86.11  E-value: 6.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  44 DYDILHINT-----YGvnshRMVRKARKlGKKVIYHAHSTeedfrnSFIGSNQlaPLVKKYLISLY----SKADHLITPT 114
Cdd:cd03808   81 KPDIVHCHTpkpgiLG----RLAARLAG-VPKVIYTVHGL------GFVFTEG--KLLRLLYLLLEklalLFTDKVIFVN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 115 PYSKTLLEGYGI---KVPISAISNGIDLSRFYPSEEKeqkfreyfkIDEEKKVIICVGLFFERKGITDFIEVARQL---- 187
Cdd:cd03808  148 EDDRDLAIKKGIikkKKTVLIPGSGVDLDRFQYSPES---------LPSEKVVFLFVARLLKDKGIDELIEAAKILkkkg 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 188 PEYQFIWFGDTPMY-SIPKNIRQLVKEdhpENVIFPGYIKgDVIEgAYAAANLFFFPSREETEGIVVLEALASQQQVLVR 266
Cdd:cd03808  219 PNVRFLLVGDGELEnPSEILIEKLGLE---GRIEFLGFRS-DVPE-LLAESDVFVLPSYREGLPRSLLEAMAAGRPVITT 293

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 267 DIP-----V---YQGWLVANENcymghsIEEFKKYIEGLLEG--KIPSTREAGYQVAEQR 316
Cdd:cd03808  294 DVPgcrelVidgVNGFLVPPGD------VEALADAIEKLIEDpeLRKEMGEAARKRVEEK 347
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 161-312 1.96e-16

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: 75.39  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  161 EKKVIICVGLFFERKGITDFIEVARQL----PEYQFIWFGDTPMYSIPKNIRQlvKEDHPENVIFPGYIKGDVIEGAYAA 236
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLkeknPNLKLVIAGDGEEEKRLKKLAE--KLGLGDNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  237 ANLFFFPSREETEGIVVLEALASQQQVLVRDIPVY--------QGWLVANENcymghsIEEFKKYIEGLLEGKIPSTR-- 306
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPpevvkdgeTGFLVKPNN------AEALAEAIDKLLEDEELRERlg 152


                  ....*.
gi 488288167  307 EAGYQV 312
Cdd:pfam00534 153 ENARKR 158
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 125-267 9.68e-16

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: 77.02  E-value: 9.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 125 GIKVPISAISNGIDLSRFypseEKEQKFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQLPE----YQFIWFG-DTP 199
Cdd:cd03821  171 GLEPPIAVIPNGVDIPEF----DPGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEqgrdWHLVIAGpDDG 246

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288167 200 MYsiPKNIRQLVKEDHPENVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRD 267
Cdd:cd03821  247 AY--PAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITD 312
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 106-270 1.81e-15

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: 76.25  E-value: 1.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 106 KADHLITPTPYSKT-LLEGYGIKV-PISAISNGIDlsRFYPSEEKEQKFREYFKIDEekKVIICVGLFFERKGITDFIEV 183
Cdd:cd03809  138 RADAIITVSEATRDdIIKFYGVPPeKIVVIPLGVD--PSFFPPESAAVLIAKYLLPE--PYFLYVGTLEPRKNHERLLKA 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 184 ARQLPEYQFIWF-----GDTPMYSipkNIRQLVKE-DHPENVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEAL 257
Cdd:cd03809  214 FALLKKQGGDLKlvivgGKGWEDE---ELLDLVKKlGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAM 290

                        170
                 ....*....|...
gi 488288167 258 ASQQQVLVRDIPV 270
Cdd:cd03809  291 ACGTPVIASNISV 303
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 103-259 2.05e-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: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 103 LYSKADHLITPTP----YSKTLLEGYGIKVPIsaISNGIDLSRFYPSEEKEQKFREyFKIDEEKKVIICVGLFFERKGIT 178
Cdd:cd03800  160 ILEAADRVIASTPqeadELISLYGADPSRINV--VPPGVDLERFFPVDRAEARRAR-LLLPPDKPVVLALGRLDPRKGID 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 179 DFIEVARQLPEYQF-----IWFGD-TPMYSIPK-NIRQLVKEDH-PENVIFPGYIKGDVIEGAYAAANLFFFPSREETEG 250
Cdd:cd03800  237 TLVRAFAQLPELRElanlvLVGGPsDDPLSMDReELAELAEELGlIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFG 316


                 ....*....
gi 488288167 251 IVVLEALAS 259
Cdd:cd03800  317 LTAIEAMAC 325
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 45-258 3.62e-15

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: 75.47  E-value: 3.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  45 YDILHinTYGVNSHRMVRKARKLGKKVIYHAHS--TEEDFRNSFIgsnqlaplvkKYLISLYSKADHLITPTPYSKTLLE 122
Cdd:cd03811   84 PDVVI--SFLGFATYIVAKLAAARSKVIAWIHSslSKLYYLKKKL----------LLKLKLYKKADKIVCVSKGIKEDLI 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 123 GYGIKVP--ISAISNGIDLSRFypseeKEQKFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQL----PEYQFIWFG 196
Cdd:cd03811  152 RLGPSPPekIEVIYNPIDIDRI-----RALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLrkkyPDVKLVILG 226

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288167 197 DTPMYsipKNIRQLVKEDH-PENVIFPGYIkgDVIEGAYAAANLFFFPSREETEGIVVLEALA 258
Cdd:cd03811  227 DGPLR---EELEKLAKELGlAERVIFLGFQ--SNPYPYLKKADLFVLSSRYEGFPNVLLEAMA 284
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
162-299 4.82e-15

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 71.00  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  162 KKVIICVG-LFFERKGITDFIE----VARQLPEYQFIWFGDTPMYSIPKNIRQLvkedhPENVIFPGYIKgDVIEgAYAA 236
Cdd:pfam13692   1 RPVILFVGrLHPNVKGVDYLLEavplLRKRDNDVRLVIVGDGPEEELEELAAGL-----EDRVIFTGFVE-DLAE-LLAA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  237 ANLFFFPSREETEGIVVLEALASQQQVLVRDIP-----VYQ--GWLVANENcymghsIEEFKKYIEGLLE 299
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGgipelVDGenGLLVPPGD------PEALAEAILRLLE 137
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 98-258 6.73e-15

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 74.68  E-value: 6.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  98 KYLISLYSKAD-HLITPTPYSKTLLEGYGI--KVPISAISNGIDLSRFYPSEEKeqKFREYFKIDEEKKVIICV--GLFF 172
Cdd:cd03825  128 RRKREALAKKRlTIVAPSRWLADMVRRSPLlkGLPVVVIPNGIDTEIFAPVDKA--KARKRLGIPQDKKVILFGaeSVTK 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 173 ERKGITDFIEVARQLPEYQ--FIW-FGDTPMysipknirQLVKEDHPenVIFPGYIKGDV-IEGAYAAANLFFFPSREET 248
Cdd:cd03825  206 PRKGFDELIEALKLLATKDdlLLVvFGKNDP--------QIVILPFD--IISLGYIDDDEqLVDIYSAADLFVHPSLADN 275

                        170
                 ....*....|
gi 488288167 249 EGIVVLEALA 258
Cdd:cd03825  276 LPNTLLEAMA 285
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 46-259 9.36e-15

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 74.75  E-value: 9.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  46 DILHINTYGVnshrMVRKARKLGKKV------IYHAHSTeedfrnSFIGSNQLAPLVKKY--LIS-LYSKADHLITPTPY 116
Cdd:PLN02871 146 DLIHASSPGI----MVFGALFYAKLLcvplvmSYHTHVP------VYIPRYTFSWLVKPMwdIIRfLHRAADLTLVTSPA 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 117 SKTLLEGYGIKVP--ISAISNGIDLSRFYP---SEEKEQKFREYfkiDEEKKVIICVGLFFERKGITDFIEVARQLPEYQ 191
Cdd:PLN02871 216 LGKELEAAGVTAAnrIRVWNKGVDSESFHPrfrSEEMRARLSGG---EPEKPLIVYVGRLGAEKNLDFLKRVMERLPGAR 292

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 192 FIWFGDTPMYSipknirQLvkEDHPE--NVIFPGYIKGDVIEGAYAAANLFFFPSREETEGIVVLEALAS 259
Cdd:PLN02871 293 LAFVGDGPYRE------EL--EKMFAgtPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMAS 354
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
44-140 2.93e-14

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 69.87  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167   44 DYDILHINTYGVNSHRMVRKARKLGKKVIYHAHSTEEDFRNSFIGSNQLAPLVKKYLISLYSKADHLITPTPYSK-TLLE 122
Cdd:pfam13439  71 RPDVVHAHSPFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVAdELRR 150

                          90
                  ....*....|....*....
gi 488288167  123 GYGIK-VPISAISNGIDLS 140
Cdd:pfam13439 151 LYGVPpEKIRVIPNGVDLE 169
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 127-267 1.25e-13

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: 70.94  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 127 KVPISAISNGIDLSRFYPSEEKEQKFREYFKIDEEKKVIICVGLFFERKGITD----FIEVARQLPEYQFIWFGDTPMYs 202
Cdd:cd04951  153 KNKSVPVYNGIDLNKFKKDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNlllaISELILSKNDFKLLIAGDGPLR- 231

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288167 203 ipKNIRQLVKEDH-PENVIFPGYIkgDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRD 267
Cdd:cd04951  232 --NELERLICNLNlVDRVILLGQI--SNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATD 293
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 44-333 1.81e-13

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: 70.08  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  44 DYDILHintygVNSHRMVR----KARKLGKKVIYHAHsteedfrnsfiGSNQLAPLVKKYLISLYSKADHLITPTPYSK- 118
Cdd:cd03819   76 RIDLIH-----AHSRAPAWlgwlASRLTGVPLVTTVH-----------GSYLATYHPKDFALAVRARGDRVIAVSELVRd 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 119 TLLEGYGI-KVPISAISNGIDLSRFYPSEEKEQkfREYFKIDEEKKVIICVGLFFERKGITDFIEVARQLPEYQFIWF-- 195
Cdd:cd03819  140 HLIEALGVdPERIRVIPNGVDTDRFPPEAEAEE--RAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLlv 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 196 -GDTP-MYSIPKNIRQLVKEDHpenVIFPGYIKgDVIEgAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDI----- 268
Cdd:cd03819  218 aGDGPeRDEIRRLVERLGLRDR---VTFTGFRE-DVPA-ALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVggare 292

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288167 269 ---PVYQGWLVANENcymghsIEEFKKYIEGLLEGkiPSTREAgyqvaeqrsIKQIGYELKEVYETVL 333
Cdd:cd03819  293 ivvHGRTGLLVPPGD------AEALADAIRAAKLL--PEAREK---------LQAAAALTEAVRELLL 343
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 60-316 1.04e-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: 68.14  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  60 MVRKARKLGKKVIYHAHSTEED--FRNSFIGSNQLAPLVKKYLISLYSKADHLITPTPYSKTLLEGYGIKV-PISAISNG 136
Cdd:cd03794  115 ALLLKKLRGAPFILDVRDLWPEslIALGVLKKGSLLKLLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKeKIIVIPNW 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 137 IDLSRFYPSEEKEQKFReyfKIDEEKKVIICVGLFFERKGITDFIEVARQLPEY---QFIWFGDTPMYSipkNIRQLVKE 213
Cdd:cd03794  195 ADLEEFKPPPKDELRKK---LGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRpdiRFLFVGDGDEKE---RLKELAKA 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 214 DHPENVIFPGYIKGDVIEGAYAAA--NLFFFPSREETEGIV---VLEALASQQQVLVRDIPVYQ--------GWLVANEN 280
Cdd:cd03794  269 RGLDNVTFLGRVPKEEVPELLSAAdvGLVPLKDNPANRGSSpskLFEYMAAGKPILASDDGGSDlaveingcGLVVEPGD 348

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 488288167 281 cymghsIEEFKKYIEGLLEGkiPSTR----EAGYQVAEQR 316
Cdd:cd03794  349 ------PEALADAILELLDD--PELRramgENGRELAEEK 380
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 44-269 3.46e-12

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: 66.54  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  44 DYDILHINTygvNSHRMV--RKARKLGKKV-IYHAHSTE-EDFRNSFIGSNQLAPLVKKYlislyskADHLITPTPYSKT 119
Cdd:cd03812   80 KYDIVHVHG---SSSNGIilLLAAKAGVPVrIAHSHNTKdSSIKLRKIRKNVLKKLIERL-------STKYLACSEDAGE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 120 LLEGYGIKVPISAISNGIDLSRFYPSEEKEQKFREYfKIDEEKKVIICVGLFFERKGITDFIEVARQLPE----YQFIWF 195
Cdd:cd03812  150 WLFGEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKL-LILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKknpnVKLVLV 228

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288167 196 GDTPMYSipkNIRQLVKE-DHPENVIFPGYiKGDVIEgAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIP 269
Cdd:cd03812  229 GEGELKE---KIKEKVKElGLEDKVIFLGF-RNDVSE-ILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTI 298
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 223-334 3.78e-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: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 223 GYIKG--DVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIPVYQGWLVANENCYM--GHSIEEFKKYIEGLL 298
Cdd:COG0438    5 VPRKGldLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLvpPGDPEALAEAILRLL 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488288167 299 E--GKIPSTREAGYQVAEQR-SIKQIGYELKEVYETVLS 334
Cdd:COG0438   85 EdpELRRRLGEAARERAEERfSWEAIAERLLALYEELLA 123
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 67-282 8.45e-11

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: 61.27  E-value: 8.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  67 LGKKVIYHAHSTEEDFRNSFIGSNQLAPLVKKYLISLYSKADHLI---TPTPYSKTLLEGYGIKVPISAISNGIDLSRfY 143
Cdd:cd01635   15 LELHVRALARALAALGHEVTVLALLLLALRRILKKLLELKPDVVHahsPHAAALAALLAARLLGIPIVVTVHGPDSLE-S 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 144 PSEEKEQKFREYFKIDEEKKViiCVGLFFERKGITDFIE----VARQLPEYQFIWFGDTPMYsiPKNIRQLVKEDHPENV 219
Cdd:cd01635   94 TRSELLALARLLVSLPLADKV--SVGRLVPEKGIDLLLEalalLKARLPDLVLVLVGGGGER--EEEEALAAALGLLERV 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288167 220 IFPG-YIKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIPVYQGWLVANENCY 282
Cdd:cd01635  170 VIIGgLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 124-332 2.33e-09

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: 58.13  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 124 YGIKVPISAISNGIDLSRFyPSEEKEQKFREYFKIDEEkKVIICVGLFFERKGITDFIEV----ARQLPEyQFIWFGDTP 199
Cdd:cd04962  160 FDVDKDIEVIHNFIDEDVF-KRKPAGALKRRLLAPPDE-KVVIHVSNFRPVKRIDDVVRVfarvRRKIPA-KLLLVGDGP 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 200 MYSipkNIRQLVKEDHPEN-VIFPGyiKGDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDIPVYQGWLVAN 278
Cdd:cd04962  237 ERV---PAEELARELGVEDrVLFLG--KQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHG 311

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488288167 279 ENCYMGH--SIEEFKKYIEGLLEGKIPS---TREAGYQVAEQRSIKQIGYELKEVYETV 332
Cdd:cd04962  312 ETGFLSDvgDVDAMAKSALSILEDDELYnrmGRAARKRAAERFDPERIVPQYEAYYRRL 370
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 103-299 2.14e-08

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: 54.94  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 103 LYSKADHLITPTpySKTLLEGYGI-KVPISAISNGIDLSRFYPSEEKEQKfreyfkideekkVIICVGLFFERKGITDFI 181
Cdd:cd03820  135 LYKRADKIVVLT--EADKLKKYKQpNSNVVVIPNPLSFPSEEPSTNLKSK------------RILAVGRLTYQKGFDLLI 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 182 EVARQLPEYQFIW----FGDTPMysiPKNIRQLVKEDHPEN-VIFPGYIKGdvIEGAYAAANLFFFPSREETEGIVVLEA 256
Cdd:cd03820  201 EAWALIAKKHPDWklriYGDGPE---REELEKLIDKLGLEDrVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEA 275

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488288167 257 LASQQQVLVRDIPV---------YQGWLVANENcymghsIEEFKKYIEGLLE 299
Cdd:cd03820  276 MAYGLPIISFDCPTgpseiiedgENGLLVPNGD------VDALAEALLRLME 321
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 45-258 4.17e-08

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: 54.20  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  45 YDILHI---NTYGVNSHRMVrkarKLGKKVIYHAHSteedfrnSFIGSNQLAPLVKKYLISLYSKADHLITPTP-YSKT- 119
Cdd:cd03795   84 YDIIHYhfpNPLADLLLFFS----GAKKPVVVHWHS-------DIVKQKKLLKLYKPLMTRFLRRADRIIATSPnYVETs 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 120 -LLEGYGIKVPIsaISNGIDLSRF-YPSEEKEQKFREYFKideeKKVIICVGLFFERKGITDFIEVARQLPEYQFIwFGD 197
Cdd:cd03795  153 pTLREFKNKVRV--IPLGIDKNVYnIPRVDFENIKREKKG----KKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVI-GGE 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288167 198 TPMYsipKNIRQLVKEDHPENVIFPGYIKGDVIEGAYAAANLFFFPSREETE--GIVVLEALA 258
Cdd:cd03795  226 GPLK---PDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEafGIVLLEAMM 285
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 129-332 2.63e-05

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


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 45.36  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 129 PISAISNGIDLSRFYPSEEKEqkfrEYFkideekkviicvgLFFER----KGITDFIEVARQLPEYQFIWFG-DTPMYSi 203
Cdd:cd03802  149 YLTVVHNGLDPADYRFQPDPE----DYL-------------AFLGRiapeKGLEDAIRVARRAGLPLKIAGKvRDEDYF- 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 204 pknirQLVKEDHPENVI-FPGYI----KGDVIEGAYAaanLFFFPSREETEGIVVLEALASQQQV----------LVRDI 268
Cdd:cd03802  211 -----YYLQEPLPGPRIeFIGEVghdeKQELLGGARA---LLFPINWDEPFGLVMIEAMACGTPViayrrgglpeVIQHG 282

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288167 269 PVyqGWLVanencymgHSIEEFKKYIEGLleGKIPstREAGYQVAEQR-SIKQIGYELKEVYETV 332
Cdd:cd03802  283 ET--GFLV--------DSVEEMAEAIANI--DRID--RAACRRYAEDRfSAARMADRYEALYRKV 333
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 136-259 5.40e-05

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: 44.37  E-value: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 136 GIDLSRFYPSEEKEqkfreyfkideEKKVIICVGLFFERKGITDFIE----VARQLPEYQFIWFGDTPMysipknIRQLV 211
Cdd:cd05844  174 GIDPAKFAPRDPAE-----------RAPTILFVGRLVEKKGCDVLIEafrrLAARHPTARLVIAGDGPL------RPALQ 236

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488288167 212 KEDHP-ENVIFPGYIKGDVIEGAYAAANLFFFPS------REETEGIVVLEALAS 259
Cdd:cd05844  237 ALAAAlGRVRFLGALPHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAAC 291
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
110-265 7.82e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 44.01  E-value: 7.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 110 LITPTPYSKTLLEGYGIKVPISAISNGIDLSRFypSEEKEQKFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQLPE 189
Cdd:PRK15484 143 IIVPSQFLKKFYEERLPNADISIVPNGFCLETY--QSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLAT 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 190 YQ----FIWFGDtPMYS-------IPKNIRQLVKEDHPEnVIFPGYIKGDVIEGAYAAANLFFFPSR-EETEGIVVLEAL 257
Cdd:PRK15484 221 AHsnlkLVVVGD-PTASskgekaaYQKKVLEAAKRIGDR-CIMLGGQPPEKMHNYYPLADLVVVPSQvEEAFCMVAVEAM 298


                 ....*...
gi 488288167 258 ASQQQVLV 265
Cdd:PRK15484 299 AAGKPVLA 306
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 46-277 1.40e-04

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: 43.09  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  46 DILHINTYGVNSHRMVRKARKLGKKVIYHAHsteeDFrnsfigsnqlaplvkkYLI----SLYSKA-DHLITPTPYSKTL 120
Cdd:cd03823   98 DVVHTHNLSGLGASLLDAARDLGIPVVHTLH----DY----------------WLLcprqFLFKKGgDAVLAPSRFTANL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 121 LEGYGI-KVPISAISNGIDLSRfYPseekeqkfREYFKIDEEKKVIICVGLFFERKGITDFIEVARQLP--EYQFIWFGD 197
Cdd:cd03823  158 HEANGLfSARISVIPNAVEPDL-AP--------PPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPreDIELVIAGH 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 198 TPMysipkniRQLVKEDHPENVIFPGYIKGDVIEGAYAAANLFFFPSR-EETEGIVVLEALASQQQVLVRDI-------- 268
Cdd:cd03823  229 GPL-------SDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLggiaeliq 301


                 ....*....
gi 488288167 269 PVYQGWLVA 277
Cdd:cd03823  302 PGVNGLLFA 310
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
44-136 1.62e-03

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 38.54  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167   44 DYDILHINTYGVNS-HRMVRKARKLgkKVIYHAHSTEEDfrnsfIGSNQLAPLVKKYLISLYSKADHLITPTPYSKTLLE 122
Cdd:pfam13579  71 RPDVVHAHSPTAGLaARLARRRRGV--PLVVTVHGLALD-----YGSGWKRRLARALERRLLRRADAVVVVSEAEAELLR 143

                          90
                  ....*....|....*
gi 488288167  123 GYGI-KVPISAISNG 136
Cdd:pfam13579 144 ALGVpAARVVVVPNG 158
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 72-268 2.55e-03

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: 39.24  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167  72 IYHAHSTEEdfrnsFIGSNQLAPLVKKYLISL--------YSKADHLITPTPYSKTLLEGYG-----IKVpisaISNGID 138
Cdd:cd03813  207 IYTRERKIE-----ILQSTWIMGYIKKLWIRFferlgklaYQQADKIISLYEGNRRRQIRLGadpdkTRV----IPNGID 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 139 LSRFYPSEEKEQKfreyfkidEEKKVIICVGLFFERKGITDFI----EVARQLPEYQFIWFGDT---PMYSipKNIRQLV 211
Cdd:cd03813  278 IQRFAPAREERPE--------KEPPVVGLVGRVVPIKDVKTFIrafkLVRRAMPDAEGWLIGPEdedPEYA--QECKRLV 347

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488288167 212 KE-DHPENVIFPGYikgDVIEGAYAAANLFFFPSREETEGIVVLEALASQQQVLVRDI 268
Cdd:cd03813  348 ASlGLENKVKFLGF---QNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDV 402
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 137-280 6.06e-03

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 38.03  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 137 IDLSRFYPSEEKEqkfrEYFKIdeekkviicVGLFFERKGITDFIEVARQLPeYQFIWFGDTPMYSIPKNIRQlvkedhp 216
Cdd:cd03804  187 VDTDAFAPAADKE----DYYLT---------ASRLVPYKRIDLAVEAFNELP-KRLVVIGDGPDLDRLRAMAS------- 245

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288167 217 ENVIFPGYIKGDVIEGAYAAANLFFFPSrEETEGIVVLEALASQQQVL----------VRDIPVyqGWLVANEN 280
Cdd:cd03804  246 PNVEFLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPVEAQACGTPVIafgkggaletVRPGPT--GILFGEQT 316
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
135-221 8.20e-03

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 37.65  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288167 135 NGIDLSRFYP-SEEKEQKFREYFKIDEEKKVIICVGLFFERKGITDFIEVARQL---PEYQFIWFGDTPmysIPKNIRQL 210
Cdd:PRK10307 201 NWSEVARFQPvADADVDALRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLrdrPDLIFVICGQGG---GKARLEKM 277

                         90
                 ....*....|.
gi 488288167 211 VKEDHPENVIF 221
Cdd:PRK10307 278 AQCRGLPNVHF 288
 
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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