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Conserved domains on  [gi|991971941|gb|AMH30717|]
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beta-1,6-galactofuranosyltransferase [Escherichia coli K-12]

Protein Classification

sugar transferase( domain architecture ID 11484490)

sugar transferase similar to Escherichia coli beta-1,6-galactofuranosyltransferase WbbI that is involved in the transfer of galactofuranose (Galf) onto an alpha-D-gluco-configured acceptor substrate to form a beta-1,6-linkage

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09814 PRK09814
sugar transferase;
1-327 3.27e-114

sugar transferase;


:

Pssm-ID: 236626 [Multi-domain]  Cd Length: 333  Bit Score: 333.86  E-value: 3.27e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941   1 MYFLNDLNFSRRDAGFKARKDALDIAS--DYENISVVNIPLWGGVVQRIISSVKlsTFLCGLENKDVLIFNFPMAKPFWH 78
Cdd:PRK09814   3 VHITNLYGMSGNSAALKAKNDVTKIAKqlGFEELGIYFYNIKRDSLSERSKRLD--GILASLKPGDIVIFQFPTWNGFEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941  79 ILSFFHRLLK--FRIVPLIHDIDELRGGGGS-----DSVRLATCDMVISHNPQMTKYLSKY-MSQDKIKDIKIFDYLvsS 150
Cdd:PRK09814  81 DRLFVDKLKKkqVKIIILIHDIEPLRFDSNYylmkeEIDMLNLADVLIVHSKKMKDRLVEEgLTTDKIIVQGIFDYL--N 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 151 DVEHRDVTDKQRGVIYAGNLSrhKCSFI--YTEGCDFTLFGVNYE---NKDNPKYLGSFDAQSPEKINLPGmqFGLIWDG 225
Cdd:PRK09814 159 DIELVKTPSFQKKINFAGNLE--KSPFLknWSQGIKLTVFGPNPEdleNSANISYKGWFDPEELPNELSKG--FGLVWDG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 226 DsveTCSGAFGDYLKFNNPHKTSLYLSMELPVFIWDKAALADFIVDNRIGYAVGSIKEMQEIVDSMTIETYKQISENTKI 305
Cdd:PRK09814 235 D---TNDGEYGEYYKYNNPHKLSLYLAAGLPVIVWSKAAIADFIVENGLGFVVDSLEELPEIIDNITEEEYQEMVENVKK 311

                        330       340
                 ....*....|....*....|..
gi 991971941 306 ISQKIRTGSYFRDVLEEVIDDL 327
Cdd:PRK09814 312 ISKLLRNGYFTKKALVDAIKEL 333
 
Name Accession Description Interval E-value
PRK09814 PRK09814
sugar transferase;
1-327 3.27e-114

sugar transferase;


Pssm-ID: 236626 [Multi-domain]  Cd Length: 333  Bit Score: 333.86  E-value: 3.27e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941   1 MYFLNDLNFSRRDAGFKARKDALDIAS--DYENISVVNIPLWGGVVQRIISSVKlsTFLCGLENKDVLIFNFPMAKPFWH 78
Cdd:PRK09814   3 VHITNLYGMSGNSAALKAKNDVTKIAKqlGFEELGIYFYNIKRDSLSERSKRLD--GILASLKPGDIVIFQFPTWNGFEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941  79 ILSFFHRLLK--FRIVPLIHDIDELRGGGGS-----DSVRLATCDMVISHNPQMTKYLSKY-MSQDKIKDIKIFDYLvsS 150
Cdd:PRK09814  81 DRLFVDKLKKkqVKIIILIHDIEPLRFDSNYylmkeEIDMLNLADVLIVHSKKMKDRLVEEgLTTDKIIVQGIFDYL--N 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 151 DVEHRDVTDKQRGVIYAGNLSrhKCSFI--YTEGCDFTLFGVNYE---NKDNPKYLGSFDAQSPEKINLPGmqFGLIWDG 225
Cdd:PRK09814 159 DIELVKTPSFQKKINFAGNLE--KSPFLknWSQGIKLTVFGPNPEdleNSANISYKGWFDPEELPNELSKG--FGLVWDG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 226 DsveTCSGAFGDYLKFNNPHKTSLYLSMELPVFIWDKAALADFIVDNRIGYAVGSIKEMQEIVDSMTIETYKQISENTKI 305
Cdd:PRK09814 235 D---TNDGEYGEYYKYNNPHKLSLYLAAGLPVIVWSKAAIADFIVENGLGFVVDSLEELPEIIDNITEEEYQEMVENVKK 311

                        330       340
                 ....*....|....*....|..
gi 991971941 306 ISQKIRTGSYFRDVLEEVIDDL 327
Cdd:PRK09814 312 ISKLLRNGYFTKKALVDAIKEL 333
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 20-302 2.18e-04

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: 42.71  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941  20 KDALDIASDYENISVVNIPL----WGGVVQRIIS----SVKLSTFLCGLENK-DVLI-FNFPmakPFWHILSFFHRllKF 89
Cdd:cd03794   47 RIFAGATETKDGIRVIRVKLgpikKNGLIRRLLNylsfALAALLKLLVREERpDVIIaYSPP---ITLGLAALLLK--KL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941  90 RIVPLIHDIDEL-------RGGGGSDSVR----------LATCDMVISHNPQMTKYLS-KYMSQDKIK------DIKIFD 145
Cdd:cd03794  122 RGAPFILDVRDLwpesliaLGVLKKGSLLkllkklerklYRLADAIIVLSPGLKEYLLrKGVPKEKIIvipnwaDLEEFK 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 146 YLVSSDVEHRDVTDKQRGVIYAGN----------------LSRHKCS--FIYTEGCDFTLFG--VNYENKDNPKYLGSfd 205
Cdd:cd03794  202 PPPKDELRKKLGLDDKFVVVYAGNigkaqgletlleaaerLKRRPDIrfLFVGDGDEKERLKelAKARGLDNVTFLGR-- 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 206 aQSPEKIN--LPGMQFGLIwdgdsvetcSGAFGDYLKFNNPHKTSLYLSMELPVFIWDKAALADFIVDNRIGYAV--GSI 281
Cdd:cd03794  280 -VPKEEVPelLSAADVGLV---------PLKDNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVepGDP 349

                        330       340
                 ....*....|....*....|...
gi 991971941 282 KEMQEIVDSMT--IETYKQISEN 302
Cdd:cd03794  350 EALADAILELLddPELRRAMGEN 372
 
Name Accession Description Interval E-value
PRK09814 PRK09814
sugar transferase;
1-327 3.27e-114

sugar transferase;


Pssm-ID: 236626 [Multi-domain]  Cd Length: 333  Bit Score: 333.86  E-value: 3.27e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941   1 MYFLNDLNFSRRDAGFKARKDALDIAS--DYENISVVNIPLWGGVVQRIISSVKlsTFLCGLENKDVLIFNFPMAKPFWH 78
Cdd:PRK09814   3 VHITNLYGMSGNSAALKAKNDVTKIAKqlGFEELGIYFYNIKRDSLSERSKRLD--GILASLKPGDIVIFQFPTWNGFEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941  79 ILSFFHRLLK--FRIVPLIHDIDELRGGGGS-----DSVRLATCDMVISHNPQMTKYLSKY-MSQDKIKDIKIFDYLvsS 150
Cdd:PRK09814  81 DRLFVDKLKKkqVKIIILIHDIEPLRFDSNYylmkeEIDMLNLADVLIVHSKKMKDRLVEEgLTTDKIIVQGIFDYL--N 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 151 DVEHRDVTDKQRGVIYAGNLSrhKCSFI--YTEGCDFTLFGVNYE---NKDNPKYLGSFDAQSPEKINLPGmqFGLIWDG 225
Cdd:PRK09814 159 DIELVKTPSFQKKINFAGNLE--KSPFLknWSQGIKLTVFGPNPEdleNSANISYKGWFDPEELPNELSKG--FGLVWDG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 226 DsveTCSGAFGDYLKFNNPHKTSLYLSMELPVFIWDKAALADFIVDNRIGYAVGSIKEMQEIVDSMTIETYKQISENTKI 305
Cdd:PRK09814 235 D---TNDGEYGEYYKYNNPHKLSLYLAAGLPVIVWSKAAIADFIVENGLGFVVDSLEELPEIIDNITEEEYQEMVENVKK 311

                        330       340
                 ....*....|....*....|..
gi 991971941 306 ISQKIRTGSYFRDVLEEVIDDL 327
Cdd:PRK09814 312 ISKLLRNGYFTKKALVDAIKEL 333
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 20-302 2.18e-04

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: 42.71  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941  20 KDALDIASDYENISVVNIPL----WGGVVQRIIS----SVKLSTFLCGLENK-DVLI-FNFPmakPFWHILSFFHRllKF 89
Cdd:cd03794   47 RIFAGATETKDGIRVIRVKLgpikKNGLIRRLLNylsfALAALLKLLVREERpDVIIaYSPP---ITLGLAALLLK--KL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941  90 RIVPLIHDIDEL-------RGGGGSDSVR----------LATCDMVISHNPQMTKYLS-KYMSQDKIK------DIKIFD 145
Cdd:cd03794  122 RGAPFILDVRDLwpesliaLGVLKKGSLLkllkklerklYRLADAIIVLSPGLKEYLLrKGVPKEKIIvipnwaDLEEFK 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 146 YLVSSDVEHRDVTDKQRGVIYAGN----------------LSRHKCS--FIYTEGCDFTLFG--VNYENKDNPKYLGSfd 205
Cdd:cd03794  202 PPPKDELRKKLGLDDKFVVVYAGNigkaqgletlleaaerLKRRPDIrfLFVGDGDEKERLKelAKARGLDNVTFLGR-- 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991971941 206 aQSPEKIN--LPGMQFGLIwdgdsvetcSGAFGDYLKFNNPHKTSLYLSMELPVFIWDKAALADFIVDNRIGYAV--GSI 281
Cdd:cd03794  280 -VPKEEVPelLSAADVGLV---------PLKDNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVepGDP 349

                        330       340
                 ....*....|....*....|...
gi 991971941 282 KEMQEIVDSMT--IETYKQISEN 302
Cdd:cd03794  350 EALADAILELLddPELRRAMGEN 372
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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