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Conserved domains on  [gi|738089395|ref|WP_036048046|]
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glycosyltransferase family 4 protein [Burkholderia gladioli]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
23-404 1.19e-37

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: 139.98  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  23 KLGVVIELASFDKGGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTvARDAGLRVVGLPAGNPLSAYERVLAE------ 96
Cdd:cd03801    1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPE-ELEDGVIVPLLPSLAALLRARRLLRElrpllr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  97 -DGIDIAMSHFSDTGYPLFEKFRIPNVTYIHNVYAFFSEAQARAFADNDRYVERY----------VSVSRNATRFAVHNL 165
Cdd:cd03801   80 lRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAeallrradavIAVSEALRDELRALG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 166 GVPEAKVETIPNGLILSEheareklTQTLTRAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGnv 245
Cdd:cd03801  160 GIPPEKIVVIPNGVDLER-------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG-- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 246 VYPPHVDALRAYldEQGLSGHILMPGYV--ADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQ 323
Cdd:cd03801  231 GDGPLRAELEEL--ELGLGDRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 324 DDIGILVPNEYGDTielnskrldelayaphqyrtapiLADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYEALI 403
Cdd:cd03801  309 GEGGLVVPPDDVEA-----------------------LADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365

                 .
gi 738089395 404 E 404
Cdd:cd03801  366 R 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
23-404 1.19e-37

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: 139.98  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  23 KLGVVIELASFDKGGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTvARDAGLRVVGLPAGNPLSAYERVLAE------ 96
Cdd:cd03801    1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPE-ELEDGVIVPLLPSLAALLRARRLLRElrpllr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  97 -DGIDIAMSHFSDTGYPLFEKFRIPNVTYIHNVYAFFSEAQARAFADNDRYVERY----------VSVSRNATRFAVHNL 165
Cdd:cd03801   80 lRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAeallrradavIAVSEALRDELRALG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 166 GVPEAKVETIPNGLILSEheareklTQTLTRAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGnv 245
Cdd:cd03801  160 GIPPEKIVVIPNGVDLER-------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG-- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 246 VYPPHVDALRAYldEQGLSGHILMPGYV--ADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQ 323
Cdd:cd03801  231 GDGPLRAELEEL--ELGLGDRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 324 DDIGILVPNEYGDTielnskrldelayaphqyrtapiLADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYEALI 403
Cdd:cd03801  309 GEGGLVVPPDDVEA-----------------------LADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365

                 .
gi 738089395 404 E 404
Cdd:cd03801  366 R 366
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
218-340 3.03e-20

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 86.03  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  218 KGHYLMADAMRHLLARRRDVKILCVGNVVYpphvDALRAYLDeqGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSI 297
Cdd:pfam13692  15 KGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----EELEELAA--GLEDRVIFTGFVEDLAELLAAADVFVLPSLYEGFGL 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 738089395  298 AMNEAMFYRKPMVLSDTGASAEVIEQDDiGILVPNeyGDTIEL 340
Cdd:pfam13692  89 KLLEAMAAGLPVVATDVGGIPELVDGEN-GLLVPP--GDPEAL 128
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
276-408 9.30e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 84.27  E-value: 9.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 276 VAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNEygdtielnskrldelayaphqy 355
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPG---------------------- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738089395 356 rTAPILADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYEALIEDVVR 408
Cdd:COG0438   72 -DPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEELLA 123
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
146-407 2.99e-18

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


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 85.55  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  146 YVERYVSVSRNATRFAVHNLGVPEAKVETIPNGLilsehEAREKLTQTLTRAEL----GLADTDYVFANVASYNLHKGHY 221
Cdd:TIGR03088 136 LIHHYVAVSRDLEDWLRGPVKVPPAKIHQIYNGV-----DTERFHPSRGDRSPIlppdFFADESVVVGTVGRLQAVKDQP 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  222 LMADAMRHLLARRRD----VKILCVGNvvyPPHVDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSI 297
Cdd:TIGR03088 211 TLVRAFALLVRQLPEgaerLRLVIVGD---GPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISN 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  298 AMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNeyGDtielnskrldelayaphqyrtAPILADALERMASNRDEWRE 377
Cdd:TIGR03088 288 TILEAMASGLPVIATAVGGNPELVQHGVTGALVPP--GD---------------------AVALARALQPYVSDPAARRA 344
                         250       260       270
                  ....*....|....*....|....*....|
gi 738089395  378 RGARGRDKIYAHYDFTEIVARYEALIEDVV 407
Cdd:TIGR03088 345 HGAAGRARAEQQFSINAMVAAYAGLYDQLL 374
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
144-372 7.24e-08

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 54.65  E-value: 7.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 144 DRYVERY------------VSVSRNaTRFAVHN----LGVPEAKVETIPNGLILSEHEAREKLTQTLTRAELGLADTDYV 207
Cdd:PRK15179 441 DRYRVEYdiiysellkmrgVALSSN-SQFAAHRyadwLGVDERRIPVVYNGLAPLKSVQDDACTAMMAQFDARTSDARFT 519
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 208 FANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvyPPHVDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFL 287
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGG---GPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFL 596
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 288 LPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNEYGDTIELNskrlDELAYAPHQYRTAPILADALER 367
Cdd:PRK15179 597 LLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTAPDVA----EALARIHDMCAADPGIARKAAD 672

                 ....*
gi 738089395 368 MASNR 372
Cdd:PRK15179 673 WASAR 677
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
23-404 1.19e-37

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: 139.98  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  23 KLGVVIELASFDKGGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTvARDAGLRVVGLPAGNPLSAYERVLAE------ 96
Cdd:cd03801    1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPE-ELEDGVIVPLLPSLAALLRARRLLRElrpllr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  97 -DGIDIAMSHFSDTGYPLFEKFRIPNVTYIHNVYAFFSEAQARAFADNDRYVERY----------VSVSRNATRFAVHNL 165
Cdd:cd03801   80 lRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAeallrradavIAVSEALRDELRALG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 166 GVPEAKVETIPNGLILSEheareklTQTLTRAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGnv 245
Cdd:cd03801  160 GIPPEKIVVIPNGVDLER-------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG-- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 246 VYPPHVDALRAYldEQGLSGHILMPGYV--ADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQ 323
Cdd:cd03801  231 GDGPLRAELEEL--ELGLGDRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 324 DDIGILVPNEYGDTielnskrldelayaphqyrtapiLADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYEALI 403
Cdd:cd03801  309 GEGGLVVPPDDVEA-----------------------LADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365

                 .
gi 738089395 404 E 404
Cdd:cd03801  366 R 366
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
32-402 8.11e-35

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: 132.06  E-value: 8.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  32 SFDKGGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTVARDAGLRVVGLPAGNPLSA-----YERVLAEDGIDIAMSHF 106
Cdd:cd03807    8 GLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAAGVPVVCLGLSSGKDPgvllrLAKLIRKRNPDVVHTWM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 107 SDTGY--PLFEKFR--IPNVTYIHNVYAFFSE-----AQARAFADNDRYVeryVSVSRNATRFaVHNLGVPEAKVETIPN 177
Cdd:cd03807   88 YHADLigGLAAKLAggVKVIWSVRSSNIPQRLtrlvrKLCLLLSKFSPAT---VANSSAVAEF-HQEQGYAKNKIVVIYN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 178 GLILSEHEAREKLTqTLTRAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvyPPHVDALRAY 257
Cdd:cd03807  164 GIDLFKLSPDDASR-ARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGR---GPERPNLERL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 258 LDEQGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEqDDIGILVPNEYGDT 337
Cdd:cd03807  240 LLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD-DGTGFLVPAGDPQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738089395 338 ielnskrldelayaphqyrtapiLADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYEAL 402
Cdd:cd03807  319 -----------------------LADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETL 360
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
32-358 8.28e-28

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: 112.45  E-value: 8.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  32 SFDKGGLEKVVLDSAIAFDRSRFDVTIVT-----------PGKVGHLGTVARDAGLRVVGLPAGnpLSAYERVLAEDGID 100
Cdd:cd03811    8 SLSGGGAERVLLNLANALDKRGYDVTLVLlrdegdldkqlNGDVKLIRLLIRVLKLIKLGLLKA--ILKLKRILKRAKPD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 101 IAMSHFSDTGY--PLFEKFRIPNVTYIHNVY--AFFSEAQARAFADNDRYVERYVSVSRNATRFAVHNLGVPEAKVETIP 176
Cdd:cd03811   86 VVISFLGFATYivAKLAAARSKVIAWIHSSLskLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPEKIEVIY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 177 NGLILSEHEAREKLTQTLTRaelglaDTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNVvyPPHvDALRA 256
Cdd:cd03811  166 NPIDIDRIRALAKEPILNEP------EDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDG--PLR-EELEK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 257 YLDEQGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNEYGD 336
Cdd:cd03811  237 LAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAA 316
                        330       340       350
                 ....*....|....*....|....*....|..
gi 738089395 337 ----------TIELNSKRLDELAYAPHQYRTA 358
Cdd:cd03811  317 alagilaallQKKLDAALRERLAKAQEAVFRE 348
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
33-377 1.03e-24

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: 103.97  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  33 FDKGGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTVARDAGLRVVGLP---AGNPLSAYERVLAEDGIDIAMSHfSDT 109
Cdd:cd03819    8 LEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPllrALLGNVRLARLIRRERIDLIHAH-SRA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 110 ----GYPLFEKFRIPNVTYIHNVYAFFSEAQARAFADNdRYVERYVSVSRNATRFAVHNLGVPEAKVETIPNGLILSEHE 185
Cdd:cd03819   87 pawlGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVR-ARGDRVIAVSELVRDHLIEALGVDPERIRVIPNGVDTDRFP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 186 AREKltqTLTRAELGLADTDYVFANVASYNLHKGHYLMADAMRhLLARRRDVKILCVGNvvyPPHVDALRAYLDEQGLSG 265
Cdd:cd03819  166 PEAE---AEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAA-ELKDEPDFRLLVAGD---GPERDEIRRLVERLGLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 266 HILMPGYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNeyGDTielnskrl 345
Cdd:cd03819  239 RVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPP--GDA-------- 308
                        330       340       350
                 ....*....|....*....|....*....|..
gi 738089395 346 DELAYAPHQYRTAPILADALERMASNRDEWRE 377
Cdd:cd03819  309 EALADAIRAAKLLPEAREKLQAAAALTEAVRE 340
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
36-400 2.64e-23

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: 99.98  E-value: 2.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  36 GGLEKVVLDSAIAFDRSRFDVTIVTPGkVGHLGTVARDAGLRVVGLP---AG-NPLS------AYERVLAEDGIDIAMSH 105
Cdd:cd03808   10 GGFQSFRLPLIKALVKKGYEVHVIAPD-GDKLSDELKELGVKVIDIPilrRGiNPLKdlkalfKLYKLLKKEKPDIVHCH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 106 FSDTG-YPLFEKFRIPNVTYIHNV--YAFFSEAQAR-----------AFADNDRYVeryvSVSRNATRFAVHNLGVPEAK 171
Cdd:cd03808   89 TPKPGiLGRLAARLAGVPKVIYTVhgLGFVFTEGKLlrllyllleklALLFTDKVI----FVNEDDRDLAIKKGIIKKKK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 172 VETIP-NGLILSEHEAREKltqtltraelGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvyPPH 250
Cdd:cd03808  165 TVLIPgSGVDLDRFQYSPE----------SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGD---GEL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 251 VDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILV 330
Cdd:cd03808  232 ENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLV 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 331 PNeyGDTIElnskrldelayaphqyrtapiLADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYE 400
Cdd:cd03808  312 PP--GDVEA---------------------LADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
23-406 1.09e-22

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 98.61  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  23 KLGVVIELASFDKGGLEKVVLDsaiafDRSRFDVTIVTPGKVGHLGTVARDAGLRVVGlPAGNPLSAYERVLAEDGIDia 102
Cdd:cd03798   29 RRGVDVEVLAPAPWGPAAARLL-----RKLLGEAVPPRDGRRLLPLKPRLRLLAPLRA-PSLAKLLKRRRRGPPDLIH-- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 103 mSHFSDTGYPLFEKFR----IPNVTYIH----NVYAFfSEAQARAFADNDRYVERYVSVSRNATRFAVhNLGVPEAKVET 174
Cdd:cd03798  101 -AHFAYPAGFAAALLArlygVPYVVTEHgsdiNVFPP-RSLLRKLLRWALRRAARVIAVSKALAEELV-ALGVPRDRVDV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 175 IPNGLILSEHEAREkltqtltrAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvyPPHVDAL 254
Cdd:cd03798  178 IPNGVDPARFQPED--------RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGD---GPLREAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 255 RAYLDEQGLSGHILMPGYV--ADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPn 332
Cdd:cd03798  247 RALAEDLGLGDRVTFTGRLphEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVP- 325
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738089395 333 eygdtielnSKRLDELAYAphqyrtapiLADALermasNRDEWRERGARGRDKIYAHYDFTEIVARYEALIEDV 406
Cdd:cd03798  326 ---------PGDADALAAA---------LRRAL-----AEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
106-384 1.27e-22

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: 98.20  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 106 FSDTGYPLFEKFRIPNVTYIHNVyAFFSEAQARAFADNDRY----------VERYVSVSRNATRFAVHNLGVPEAKVETI 175
Cdd:cd03809   89 HSPHNTAPLLLKGCPQVVTIHDL-IPLRYPEFFPKRFRLYYrlllpislrrADAIITVSEATRDDIIKFYGVPPEKIVVI 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 176 PNGlilSEHEAREKLTQTLTRAELGLADtDYVFAnVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvYPPHVDALR 255
Cdd:cd03809  168 PLG---VDPSFFPPESAAVLIAKYLLPE-PYFLY-VGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGG--KGWEDEELL 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 256 AYLDEQGLSGHILMPGYVAD--VAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEqdDIGILV-PN 332
Cdd:cd03809  241 DLVKKLGLGGRVRFLGYVSDedLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAG--DAALYFdPL 318
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738089395 333 EYGDtielnskrldelayaphqyrtapiLADALERMASNRDEWRERGARGRD 384
Cdd:cd03809  319 DPES------------------------IADAILRLLEDPSLREELIRKGLE 346
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
218-340 3.03e-20

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 86.03  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  218 KGHYLMADAMRHLLARRRDVKILCVGNVVYpphvDALRAYLDeqGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSI 297
Cdd:pfam13692  15 KGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----EELEELAA--GLEDRVIFTGFVEDLAELLAAADVFVLPSLYEGFGL 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 738089395  298 AMNEAMFYRKPMVLSDTGASAEVIEQDDiGILVPNeyGDTIEL 340
Cdd:pfam13692  89 KLLEAMAAGLPVVATDVGGIPELVDGEN-GLLVPP--GDPEAL 128
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
276-408 9.30e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 84.27  E-value: 9.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 276 VAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNEygdtielnskrldelayaphqy 355
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPG---------------------- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738089395 356 rTAPILADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYEALIEDVVR 408
Cdd:COG0438   72 -DPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEELLA 123
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
204-332 2.37e-18

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: 81.55  E-value: 2.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  204 TDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvyPPHVDALRAYLDEQGLSGHILMPGYV--ADVAAVHR 281
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGD---GEEEKRLKKLAEKLGLGDNVIFLGFVsdEDLPELLK 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 738089395  282 IADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPN 332
Cdd:pfam00534  78 IADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKP 128
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
146-407 2.99e-18

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


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 85.55  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  146 YVERYVSVSRNATRFAVHNLGVPEAKVETIPNGLilsehEAREKLTQTLTRAEL----GLADTDYVFANVASYNLHKGHY 221
Cdd:TIGR03088 136 LIHHYVAVSRDLEDWLRGPVKVPPAKIHQIYNGV-----DTERFHPSRGDRSPIlppdFFADESVVVGTVGRLQAVKDQP 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  222 LMADAMRHLLARRRD----VKILCVGNvvyPPHVDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSI 297
Cdd:TIGR03088 211 TLVRAFALLVRQLPEgaerLRLVIVGD---GPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISN 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  298 AMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNeyGDtielnskrldelayaphqyrtAPILADALERMASNRDEWRE 377
Cdd:TIGR03088 288 TILEAMASGLPVIATAVGGNPELVQHGVTGALVPP--GD---------------------AVALARALQPYVSDPAARRA 344
                         250       260       270
                  ....*....|....*....|....*....|
gi 738089395  378 RGARGRDKIYAHYDFTEIVARYEALIEDVV 407
Cdd:TIGR03088 345 HGAAGRARAEQQFSINAMVAAYAGLYDQLL 374
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
32-321 7.91e-16

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 78.10  E-value: 7.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  32 SFDKGGLEKVVLDSAIAFDRSRFDVTIV-TPGKVGHLGTVARDAGLRVVGLPAG--NPLSAYERVL---AEDGIDIAMSH 105
Cdd:cd03812    8 GMNVGGIETFLMNLYRKLDKSKIEFDFLaTSDDKGEYDEELEELGGKIFYIPPKkkNIIKYFIKLLkliKKEKYDIVHVH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 106 ---FSDTGYPLFEKFRIP-----------NVTYIHNVYAFFSEAQARAFADNdryverYVSVSRNATR--FAVHNLGvpe 169
Cdd:cd03812   88 gssSNGIILLLAAKAGVPvriahshntkdSSIKLRKIRKNVLKKLIERLSTK------YLACSEDAGEwlFGEVENG--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 170 aKVETIPNG-----LILSEhEAREKltqtltRAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGN 244
Cdd:cd03812  159 -KFKVIPNGidiekYKFNK-EKRRK------RRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGE 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738089395 245 VvypPHVDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVI 321
Cdd:cd03812  231 G---ELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDI 304
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
153-331 6.14e-15

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: 75.56  E-value: 6.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 153 VSRNATRFAVHNLGVPEAKVETIPNGLILSEHEaREKLTQTLTRAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLA 232
Cdd:cd04951  137 VSREALDEFIAKKAFSKNKSVPVYNGIDLNKFK-KDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELIL 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 233 RRRDVKILCVGNvvyPPHVDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLS 312
Cdd:cd04951  216 SKNDFKLLIAGD---GPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVAT 292
                        170
                 ....*....|....*....
gi 738089395 313 DTGASAEVIeqDDIGILVP 331
Cdd:cd04951  293 DAGGVAEVV--GDHNYVVP 309
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
171-406 2.18e-14

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


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 73.91  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 171 KVETIPNGL---ILSEHEAREkltqtlTRAELGLADTDYV--FANVASYNLHKGHYLMADAMRhLLARRRDVKILCVGNv 245
Cdd:cd03825  162 PVVVIPNGIdteIFAPVDKAK------ARKRLGIPQDKKVilFGAESVTKPRKGFDELIEALK-LLATKDDLLLVVFGK- 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 246 vypphvdalrayLDEQ--GLSGHILMPGYVADVAAVHRI---ADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEV 320
Cdd:cd03825  234 ------------NDPQivILPFDIISLGYIDDDEQLVDIysaADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEI 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 321 IEQDDIGILVPNeyGDTIElnskrldelayaphqyrtapiLADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYE 400
Cdd:cd03825  302 VQHGVTGYLVPP--GDVQA---------------------LAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYL 358

                 ....*.
gi 738089395 401 ALIEDV 406
Cdd:cd03825  359 ELYKDL 364
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
36-401 8.32e-13

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 69.19  E-value: 8.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  36 GGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTVARDAGLRVVGLPAG---------NPLSAYER---VLAEDGIDIAM 103
Cdd:cd03820   13 GGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRkyshfklllKYFKKVRRlrkYLKNNKPDVVI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 104 S-HFSDTGYPLFEKFRIPNVTYIHNVYAFFSEAQARAFAD--NDRYVERYVSVSRNAtrfAVHNLGVPEAKVETIPNGLI 180
Cdd:cd03820   93 SfRTSLLTFLALIGLKSKLIVWEHNNYEAYNKGLRRLLLRrlLYKRADKIVVLTEAD---KLKKYKQPNSNVVVIPNPLS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 181 LSEHEAREKLTQTltraelgladtdyVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvyPPHVDALRAYLDE 260
Cdd:cd03820  170 FPSEEPSTNLKSK-------------RILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGD---GPEREELEKLIDK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 261 QGLSGHILMPGYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSD--TGASaEVIEQDDIGILVPNeyGDti 338
Cdd:cd03820  234 LGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDcpTGPS-EIIEDGENGLLVPN--GD-- 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738089395 339 elnskrldelayaphqyrtAPILADALERMASNRDEWRERGARGRDKIyAHYDFTEIVARYEA 401
Cdd:cd03820  309 -------------------VDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEKIIKQWEE 351
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
211-330 9.00e-13

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: 67.43  E-value: 9.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 211 VASYNLHKGHYLMADAMRHLLARRRDVKILCVGNVVYPPHVDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFLLPS 290
Cdd:cd01635  116 VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPS 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 738089395 291 FIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILV 330
Cdd:cd01635  196 RSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
27-333 9.32e-12

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: 65.85  E-value: 9.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  27 VIELASFDKGGLEKVVLDSAIAFDRSRFDVTIVTPGkvghlgtvarDAGLRVVGLPAGNPLSayeRVLAEDGIDIAMSHF 106
Cdd:cd03821    5 VTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTG----------DGYESLVVEENGRYIP---PQDGFASIPLLRQGA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 107 SDTGYPLF------EKFRIPNVTYIHNVYAFFSEAQARAFADNDR-YV---------------------ERYVSVSRNAT 158
Cdd:cd03821   72 GRTDFSPGlpnwlrRNLREYDVVHIHGVWTYTSLAACKLARRRGIpYVvsphgmldpwalqqkhwkkriALHLIERRNLN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 159 RFA-VHNLG----------VPEAKVETIPNGLILSEHEAREKLtqtltRAELGLADTDYVFANVASYNLHKGHYLMADAM 227
Cdd:cd03821  152 NAAlVHFTSeqeadelrrfGLEPPIAVIPNGVDIPEFDPGLRD-----RRKHNGLEDRRIILFLGRIHPKKGLDLLIRAA 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 228 RHLLARRRDVKILCVGnvvYPPH-VDALRAYLDEQGLSGHILMPGYVADVA--AVHRIADAFLLPSFIEGWSIAMNEAMF 304
Cdd:cd03821  227 RKLAEQGRDWHLVIAG---PDDGaYPAFLQLQSSLGLGDRVTFTGPLYGEAkwALYASADLFVLPSYSENFGNVVAEALA 303
                        330       340
                 ....*....|....*....|....*....
gi 738089395 305 YRKPMVLSDTGASAEVIEQDDIGILVPNE 333
Cdd:cd03821  304 CGLPVVITDKCGLSELVEAGCGVVVDPNV 332
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
112-399 1.19e-11

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: 65.48  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 112 PLFEKFRIPNVTYIHNVYAFFS--EAQARAFADNDRYVERYVSVSRNATRFAVHNLGVPEAKVETIPNGLIL--SEHEAR 187
Cdd:cd03822   98 GLLLHLRIPVITTLHTVLDLSDpgKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPAVNIEVIPHGVPEvpQDPTTA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 188 EKltqtltrAELGLADTdYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVG----NVVYPPHVDALRAYLDEQGL 263
Cdd:cd03822  178 LK-------RLLLPEGK-KVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelhpSLARYEGERYRKAAIEELGL 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 264 SGHILMPGYVADVAAVHRI---ADAFLLP--SFIEGWSIAMNEAMFYRKPMVLSDTGaSAEVIEQDDIGILVPneygdti 338
Cdd:cd03822  250 QDHVDFHNNFLPEEEVPRYisaADVVVLPylNTEQSSSGTLSYAIACGKPVISTPLR-HAEELLADGRGVLVP------- 321
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738089395 339 elnskrldelayaphqYRTAPILADALERMASN---RDEWRERGARgrdkiYAHYDFTEIVARY 399
Cdd:cd03822  322 ----------------FDDPSAIAEAILRLLEDderRQAIAERAYA-----YARAMTWESIADR 364
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
34-401 1.19e-11

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: 65.72  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  34 DKGGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTVARDA-GLRVVGLPAGNP-------LSAY--------ERVLAED 97
Cdd:cd03800   19 DTGGQNVYVLELARALAELGYQVDIFTRRISPADPEVVEIApGARVIRVPAGPPeylpkeeLWPYleefadglLRFIARE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  98 GI--DIAMSHFSDTGYP---LFEKFRIPNVTYIHN---VYAFFSEAQARAFADNDRYVE--------RYVSVSRNATRFA 161
Cdd:cd03800   99 GGryDLIHSHYWDSGLVgalLARRLGVPLVHTFHSlgrVKYRHLGAQDTYHPSLRITAEeqileaadRVIASTPQEADEL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 162 VHNLGVPEAKVETIPNGL------ILSEHEARekltqtltRAELGL-ADTDYVFAnVASYNLHKGHYLMADAMRHLLARR 234
Cdd:cd03800  179 ISLYGADPSRINVVPPGVdlerffPVDRAEAR--------RARLLLpPDKPVVLA-LGRLDPRKGIDTLVRAFAQLPELR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 235 RDVKILCVGNVVYPPHVD---ALRAYLDEQGLSGHILMPGYV--ADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPM 309
Cdd:cd03800  250 ELANLVLVGGPSDDPLSMdreELAELAEELGLIDRVRFPGRVsrDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPV 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 310 VLSDTGASAEVIEQDDIGILVPneygdtielnskrldelAYAPHQyrtapiLADALERMASNRDEWRERGARGRDKIYAH 389
Cdd:cd03800  330 VATAVGGLQDIVRDGRTGLLVD-----------------PHDPEA------LAAALRRLLDDPALWQRLSRAGLERARAH 386
                        410
                 ....*....|..
gi 738089395 390 YDFTEIVARYEA 401
Cdd:cd03800  387 YTWESVADQLLT 398
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
118-406 1.42e-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: 59.29  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 118 RIPNVTYIHN-----VYAFFSEAQARAFADNDRyvERYVSVSrNATRFAVHNLGVPEAKVETIPNglILSEHEAREKLTQ 192
Cdd:cd04962  110 KIPIVTTLHGtditlVGYDPSLQPAVRFSINKS--DRVTAVS-SSLRQETYELFDVDKDIEVIHN--FIDEDVFKRKPAG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 193 TLTRAELGLADtDYVFANVASYNLHKGhylMADAMR--HLLARRRDVKILCVGNvvyPPHVDALRAYLDEQGLSGHILMP 270
Cdd:cd04962  185 ALKRRLLAPPD-EKVVIHVSNFRPVKR---IDDVVRvfARVRRKIPAKLLLVGD---GPERVPAEELARELGVEDRVLFL 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 271 GYVADVAAVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPneYGDtIELNSKrldelay 350
Cdd:cd04962  258 GKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSD--VGD-VDAMAK------- 327
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738089395 351 aphqyRTAPILADalermasnRDEWRERGARGRDKIYAHYDFTEIVARYEALIEDV 406
Cdd:cd04962  328 -----SALSILED--------DELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
118-399 1.77e-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: 55.81  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 118 RIPNVTYIHNVYAFFSEAQARAFADND-------RYVERY--------VSVSRNATRFAVhNLGVPEAKVETIPNGlilS 182
Cdd:cd03794  120 KLRGAPFILDVRDLWPESLIALGVLKKgsllkllKKLERKlyrladaiIVLSPGLKEYLL-RKGVPKEKIIVIPNW---A 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 183 EHEAREKLTQTLTRAELGLADT-DYVFA-NVASYNlhkGHYLMADAMRhLLARRRDVKILCVGNVvypPHVDALRAYLDE 260
Cdd:cd03794  196 DLEEFKPPPKDELRKKLGLDDKfVVVYAgNIGKAQ---GLETLLEAAE-RLKRRPDIRFLFVGDG---DEKERLKELAKA 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 261 QGLSGHILMPgYV--ADVAAVHRIADAFLLP---SFIEGWSIA--MNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNE 333
Cdd:cd03794  269 RGLDNVTFLG-RVpkEEVPELLSAADVGLVPlkdNPANRGSSPskLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPG 347
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738089395 334 ygdtielnskRLDELAyaphqyrtapilaDALERMASNRDEWRERGARGRDKIYAHYDfTEIVARY 399
Cdd:cd03794  348 ----------DPEALA-------------DAILELLDDPELRRAMGENGRELAEEKFS-REKLADR 389
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
36-178 2.60e-08

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 53.31  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395   36 GGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLGTVARDaGLRVVGLPAGNP---------LSAYERVLAEDGIDIAMSHF 106
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVR-VVRVPRVPLPLPprllrslafLRRLRRLLRRERPDVVHAHS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  107 SDTGYP----LFEKFRIPNVTYIHNVYAFFSEAQARAFADND----------RYVERYVSVSRNATRFAVHNLGVPEAKV 172
Cdd:pfam13439  80 PFPLGLaalaARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRllrrlerrllRRADRVIAVSEAVADELRRLYGVPPEKI 159

                  ....*.
gi 738089395  173 ETIPNG 178
Cdd:pfam13439 160 RVIPNG 165
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
36-387 4.29e-08

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: 54.64  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  36 GGLEKVVLDSAIAFDRSRFDVTIVTPGkVGHLGTVARDAGLRVVGLPAGNPLSA--------------------YERVLA 95
Cdd:cd03823   15 GGAEISVHDLAEALVAEGHEVAVLTAG-VGPPGQATVARSVVRYRRAPDETLPLalkrrgyelfetynpglrrlLARLLE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  96 EDGIDIAMSHfSDTGYPL-----FEKFRIPNVTYIHNvYAFFSEAQARAFADNDRYVeryvSVSRnATRFAVHNLGVPEA 170
Cdd:cd03823   94 DFRPDVVHTH-NLSGLGAslldaARDLGIPVVHTLHD-YWLLCPRQFLFKKGGDAVL----APSR-FTANLHEANGLFSA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 171 KVETIPNGLIlSEHEAREKLTQTLTRAelgladtdyVFANVASYNLHKGHYLMADAMRHLlaRRRDVKILCVGnvvyppH 250
Cdd:cd03823  167 RISVIPNAVE-PDLAPPPRRRPGTERL---------RFGYIGRLTEEKGIDLLVEAFKRL--PREDIELVIAG------H 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 251 VDALRAYLDEQGLSGHILmpGYV--ADVAAVHRIADAFLLPS-FIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIG 327
Cdd:cd03823  229 GPLSDERQIEGGRRIAFL--GRVptDDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNG 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 328 ILVPneYGDTielnskrlDELAYAPHQYRTAPILADALERMASNRDEWRERgARGRDKIY 387
Cdd:cd03823  307 LLFA--PGDA--------EDLAAAMRRLLTDPALLERLRAGAEPPRSTESQ-AEEYLKLY 355
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
144-372 7.24e-08

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 54.65  E-value: 7.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 144 DRYVERY------------VSVSRNaTRFAVHN----LGVPEAKVETIPNGLILSEHEAREKLTQTLTRAELGLADTDYV 207
Cdd:PRK15179 441 DRYRVEYdiiysellkmrgVALSSN-SQFAAHRyadwLGVDERRIPVVYNGLAPLKSVQDDACTAMMAQFDARTSDARFT 519
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 208 FANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNvvyPPHVDALRAYLDEQGLSGHILMPGYVADVAAVHRIADAFL 287
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGG---GPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFL 596
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 288 LPSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNEYGDTIELNskrlDELAYAPHQYRTAPILADALER 367
Cdd:PRK15179 597 LLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTAPDVA----EALARIHDMCAADPGIARKAAD 672

                 ....*
gi 738089395 368 MASNR 372
Cdd:PRK15179 673 WASAR 677
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
61-402 2.45e-07

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: 52.45  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  61 PGKVGHLGTVARDAGLRVVGLPAGNPLSAYERVLAEDGIDIAMSHFSDTG---YPLFEKFRIPNVTYIHNVYAFFSEAQA 137
Cdd:cd05844   44 GVALRALGGSGPLRWLRQMAQRLLGWSAPRLGGAAGLAPALVHAHFGRDGvyaLPLARALGVPLVVTFHGFDITTSRAWL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 138 RAFADNDRYVER-----------YVSVSRnATRFAVHNLGVPEAKVETIPNGLILSEhearekltqtLTRAELGlADTDY 206
Cdd:cd05844  124 AASPGWPSQFQRhrralqrpaalFVAVSG-FIRDRLLARGLPAERIHVHYIGIDPAK----------FAPRDPA-ERAPT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 207 vFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNVVYPPHVDALRAYLDE---QGLSGHilmpgyvADVAAVHRIA 283
Cdd:cd05844  192 -ILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAALGRvrfLGALPH-------AEVQDWMRRA 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 284 DAFLLPSFI------EGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNeygdtielnskrldelayaphqyRT 357
Cdd:cd05844  264 EIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPE-----------------------GD 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 738089395 358 APILADALERMASNRDEWRERGARGRDKIYAHYDFTEIVARYEAL 402
Cdd:cd05844  321 VDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAKLEAI 365
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
43-313 2.63e-07

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 52.40  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395   43 LDSAIAFDRSRFDVTIVTPGKVGhlGTVARDAGLRVVGLPAGnPLSAYERVLAEDGIDIAMSHFSDTGYPLFEKF----- 117
Cdd:TIGR04047  19 LELAEALTALGHDVTVWALAADG--FGFFRDPPCAVRLVPVA-PAPGDTDAMVEQRIARSIDHLRAHFARGFDVVhaqdc 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  118 -------------RIPN-VTYIHNVYAFFSEA----QARAFADNDRYVeryvSVSRNATRFAVHNLGVpEAKVetIPNGL 179
Cdd:TIGR04047  96 isgnalatlraegLIPGfVRTVHHLDDFDDPRlaacQERAIVEADAVL----CVSAAWAAELRAEWGI-DATV--VPNGV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  180 ILSEHEAREKLTQTLTRAELGLADTDYVFAnVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNVV---YPPHVDALRA 256
Cdd:TIGR04047 169 DAARFSPAADAADAALRRRLGLRGGPYVLA-VGGIEPRKNTIDLLEAFALLRARRPQAQLVIAGGATlfdYDAYRREFRA 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  257 YLDEQGLS-GHILMPGYVADVA--AVHRIADAFLLPSFIEGWSIAMNEAMFYRKPMVLSD 313
Cdd:TIGR04047 248 RAAELGVDpGPVVITGPVPDADlpALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASD 307
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
79-371 1.32e-06

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: 49.97  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  79 VGLPAGNPlSAYERVLAEDGIDI--AMSHFS--DTGYPLFEKFRIPNVTYIHNVYAFFSEAQARAFADNDRYVERYVSVS 154
Cdd:cd03817   66 QHIPFPFK-KAVIDRIKELGPDIihTHTPFSlgKLGLRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKAVVRKLVRRF 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 155 RNATRfAVH-----------NLGVpEAKVETIPNGLilsEHEAREKLTQTLTRAELGLADTDYVFANVASYNLHKGHYLM 223
Cdd:cd03817  145 YNHTD-AVIapsekikdtlrEYGV-KGPIEVIPNGI---DLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFL 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 224 ADAMrHLLARRRDVKILCVGNVVYPPHVDALRAYLdeqGLSGHILMPGYV--ADVAAVHRIADAFLLPSFIEGWSIAMNE 301
Cdd:cd03817  220 LRAF-AELKKEPNIKLVIVGDGPEREELKELAREL---GLADKVIFTGFVprEELPEYYKAADLFVFASTTETQGLVYLE 295
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738089395 302 AMFYRKPMVLSDTGASAEVIEQDDIGILVPN------EYGDTIELNSKRLDELAYAPHQYRTAPILADALERMASN 371
Cdd:cd03817  296 AMAAGLPVVAAKDPAASELVEDGENGFLFEPndetlaEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLYEE 371
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
167-405 6.88e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.86  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 167 VPEAKVETIPNGLILsehEAREKLTQTLTRAELGLADTDYVFANVASYNLHKGHYLMADAMRHLLARRRDVKILCVGNVV 246
Cdd:PRK15484 158 LPNADISIVPNGFCL---ETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPT 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 247 YPPHVDAL---RAYLDE-QGLSGHILMPGYVA--DVAAVHRIADAFLLPS-FIEGWSIAMNEAMFYRKPMVLSDTGASAE 319
Cdd:PRK15484 235 ASSKGEKAayqKKVLEAaKRIGDRCIMLGGQPpeKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITE 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 320 VIEQDDIGilvpneygdtielnskrldelaYAPHQYRTAPILADALERMASNRDEwRERGARGRDKIYAHYDFTEIVARY 399
Cdd:PRK15484 315 FVLEGITG----------------------YHLAEPMTSDSIISDINRTLADPEL-TQIAEQAKDFVFSKYSWEGVTQRF 371

                 ....*.
gi 738089395 400 EALIED 405
Cdd:PRK15484 372 EEQIHN 377
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
34-357 9.44e-06

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: 47.27  E-value: 9.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  34 DKGGLEKVVLDSAIAFDRSRFDVTIVT----PGKVGHLGTVARDAGLRVVGLPAGNPLS-AYERVLAE--DGIDIAMSHF 106
Cdd:cd03795   12 DIGGIEQVIYDLAEGLKKKGIEVDVLCfskeKETPEKEENGIRIHRVKSFLNVASTPFSpSYIKRFKKlaKEYDIIHYHF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 107 SdtgYPL------FEKFRIPNVTYIHN-------VYAFFSEAQARAFADNDRYV---ERYVSVSRNATRFavhnlgvpEA 170
Cdd:cd03795   92 P---NPLadlllfFSGAKKPVVVHWHSdivkqkkLLKLYKPLMTRFLRRADRIIatsPNYVETSPTLREF--------KN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 171 KVETIPNGLILSEHEAREKLTQTLTRAELGladtDYVFANVASYNLHKG-HYLMaDAMRHLlarrrDVKILCVGnvvypp 249
Cdd:cd03795  161 KVRVIPLGIDKNVYNIPRVDFENIKREKKG----KKIFLFIGRLVYYKGlDYLI-EAAQYL-----NYPIVIGG------ 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 250 hVDALRAYLDEQ---GLSGHILMPGYVADVAAVH--RIADAFLLPSFI--EGWSIAMNEAMFYRKPMVLSDTGASAEVIE 322
Cdd:cd03795  225 -EGPLKPDLEAQielNLLDNVKFLGRVDDEEKVIylHLCDVFVFPSVLrsEAFGIVLLEAMMCGKPVISTNIGTGVPYVN 303
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 738089395 323 QDDI-GILVPNeyGDTIELnSKRLDELAYAPHQYRT 357
Cdd:cd03795  304 NNGEtGLVVPP--KDPDAL-AEAIDKLLSDEELRES 336
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
145-399 5.59e-05

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: 45.02  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 145 RYVERYVSVSRNATRFAVHnLGVPEAKVETIPNGL-------ILSEHEAREKLTqtltraeLGLadtdyvfanVASYNLH 217
Cdd:cd03813  243 QQADKIISLYEGNRRRQIR-LGADPDKTRVIPNGIdiqrfapAREERPEKEPPV-------VGL---------VGRVVPI 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 218 KGHYLMADAMRHLLARRRDVKILCVG----NVVYPPHVDALRAYLdeqGLSGHILMPGyVADVAAVHRIADAFLLPSFIE 293
Cdd:cd03813  306 KDVKTFIRAFKLVRRAMPDAEGWLIGpedeDPEYAQECKRLVASL---GLENKVKFLG-FQNIKEYYPKLGLLVLTSISE 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 294 GWSIAMNEAMFYRKPMVLSDTGASAEVIE-QDDI----GILVPneygdtielnskrldelayaPHQYRTapiLADALERM 368
Cdd:cd03813  382 GQPLVILEAMASGVPVVATDVGSCRELIYgADDAlgqaGLVVP--------------------PADPEA---LAEALIKL 438
                        250       260       270
                 ....*....|....*....|....*....|.
gi 738089395 369 ASNRDEWRERGARGRDKIYAHYDFTEIVARY 399
Cdd:cd03813  439 LRDPELRQAFGEAGRKRVEKYYTLEGMIDSY 469
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
36-333 7.23e-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: 44.59  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  36 GGLEKVVLDSAIAFDRSRFDVTIVTPGKVGHLG------TVARDAGLRVVGLPAGNPLSAYERVLAEDGIDIAMSHFSDT 109
Cdd:cd03802   18 GGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAplvaviPRALRLDPIPQESKLAELLEALEVQLRASDFDVIHNHSYDW 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 110 GYPLFEKFRIPNVTYIHnvyaFFSEAQARAFADNDRYVeRYVSVSRNAtrfAVHNLGVPEAKVetIPNGLilsehearek 189
Cdd:cd03802   98 LPPFAPLIGTPFVTTLH----GPSIPPSLAIYAAEPPV-NYVSISDAQ---RAATPPIDYLTV--VHNGL---------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 190 ltqtltraelglADTDYVFANVASYNLH--------KGhylMADAMRhlLARRRDVKILCVGNVVYPPHVDalraYLDEQ 261
Cdd:cd03802  158 ------------DPADYRFQPDPEDYLAflgriapeKG---LEDAIR--VARRAGLPLKIAGKVRDEDYFY----YLQEP 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738089395 262 GLSGHILMPGYVADVAAVHRIADAFLL---PSFIEGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNE 333
Cdd:cd03802  217 LPGPRIEFIGEVGHDEKQELLGGARALlfpINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSV 291
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
230-401 3.47e-04

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 42.35  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 230 LLARRRDVKILCVGN--VVY---PPHVDALRAYLDEQgLSG---HILMPGYV--ADVAAVHRIADA--FLLPSFIEGWSi 297
Cdd:cd03818  239 IQARRPDARVVVVGGdgVSYgspPPDGGSWKQKMLAE-LGVdleRVHFVGKVpyDQYVRLLQLSDAhvYLTYPFVLSWS- 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 298 aMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPneYGDTIELNSKRLDELAyaphqyrtapiladalermasNRDEWRE 377
Cdd:cd03818  317 -LLEAMACGCPVIGSDTAPVREVIRDGRNGLLVD--FFDPDALAAAVLELLE---------------------DPDRAAA 372
                        170       180
                 ....*....|....*....|....
gi 738089395 378 RGARGRDKIYAHYDFTEIVARYEA 401
Cdd:cd03818  373 LRRAARRTVERSDSLDVCLARYLA 396
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
36-178 3.49e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 40.85  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395   36 GGLEKVVLDSAIAFDRSRFDVTIVTPGKVGhLGTVARDAGLRVVGLPAGNP---------LSAYERVLAEDGIDIAMSHF 106
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPP-GRPELVGDGVRVHRLPVPPRpspladlaaLRRLRRLLRAERPDVVHAHS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395  107 SDTGYPLFEKFRIPNVTYIHNVYAFFSEAQARAFADNDRYVERYVSvsRNATRF---------AVHNLGVPEAKVETIPN 177
Cdd:pfam13579  80 PTAGLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARALERRLL--RRADAVvvvseaeaeLLRALGVPAARVVVVPN 157

                  .
gi 738089395  178 G 178
Cdd:pfam13579 158 G 158
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
283-391 5.05e-03

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: 38.59  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738089395 283 ADAFLLPSFI------EGWSIAMNEAMFYRKPMVLSDTGASAEVIEQDDIGILVPNeygdtielnskrldelayaphqyR 356
Cdd:cd03799  251 ADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPE-----------------------R 307
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 738089395 357 TAPILADALERMASNRDEWRERGARGRDKIYAHYD 391
Cdd:cd03799  308 DAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYD 342
 
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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