NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|492410701|ref|WP_005836137|]
View 

MULTISPECIES: undecaprenyl-phosphate glucose phosphotransferase [Bacteroides]

Protein Classification

sugar transferase( domain architecture ID 11496316)

sugar transferase similar to Xanthomonas campestris UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase that catalyzes the transfer of the glucose-1-phosphate moiety from UDP-Glc onto the carrier lipid undecaprenyl phosphate (C55-P), forming a phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-undecaprenol (Glc-PP-C55)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
17-467 1.93e-171

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


:

Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 489.40  E-value: 1.93e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   17 FGDLCLLNIIFISLYHIFDYQtLGNEFTHSLPQLLVLLNLVYLLCNYSNGVILHERIVRPERIVRRAFRNTIFHAALFIS 96
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGS-RGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   97 LATLAEIGTSSLR-FFACFYGIFFICLAVYRLMFRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGY 175
Cdd:TIGR03023  80 LAFLLKTGTEFSRlWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  176 FCDLPSNDFPES-IPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVPNIRNYLHRRMHFELF 254
Cdd:TIGR03023 160 FDDRPDARTSVRgVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  255 GNIPVLTIREEPLTQMeNRLLKRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMR 334
Cdd:TIGR03023 240 GGLPVISLRDSPLDGW-NRFIKRAFDIVLALLVLLLLSP-LLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  335 VNIDSD-KLQATANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHTEEYSHLIDKYMVRHLVKPGITGW 413
Cdd:TIGR03023 318 VHAEGDgVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGW 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 492410701  414 AQVTGYRGETKELWQMEGRVQRDVWYLEHWTFLLDLYIIYKTVRNAVRGeKEAY 467
Cdd:TIGR03023 398 AQVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVG-KNAY 450
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
17-467 1.93e-171

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 489.40  E-value: 1.93e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   17 FGDLCLLNIIFISLYHIFDYQtLGNEFTHSLPQLLVLLNLVYLLCNYSNGVILHERIVRPERIVRRAFRNTIFHAALFIS 96
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGS-RGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   97 LATLAEIGTSSLR-FFACFYGIFFICLAVYRLMFRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGY 175
Cdd:TIGR03023  80 LAFLLKTGTEFSRlWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  176 FCDLPSNDFPES-IPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVPNIRNYLHRRMHFELF 254
Cdd:TIGR03023 160 FDDRPDARTSVRgVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  255 GNIPVLTIREEPLTQMeNRLLKRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMR 334
Cdd:TIGR03023 240 GGLPVISLRDSPLDGW-NRFIKRAFDIVLALLVLLLLSP-LLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  335 VNIDSD-KLQATANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHTEEYSHLIDKYMVRHLVKPGITGW 413
Cdd:TIGR03023 318 VHAEGDgVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGW 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 492410701  414 AQVTGYRGETKELWQMEGRVQRDVWYLEHWTFLLDLYIIYKTVRNAVRGeKEAY 467
Cdd:TIGR03023 398 AQVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVG-KNAY 450
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
129-463 1.97e-99

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 300.88  E-value: 1.97e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 129 FRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGYFCDLPSNDFPESIPYLGQPKEV-VTYLQQHHIE 207
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLlLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 208 QVYCCLPSARSHEIVPIINYCENHLIRfysvpnirnYLHRRMHFELFGNIPVLTIREEPLTQMeNRLLKRAFDLFFSLSF 287
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGY-QRVLKRLFDIVLALLG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 288 LCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMRVNIDSDK--LQATANDPRKTKIGDFIRKTSIDE 365
Cdd:COG2148  151 LILLSP-LLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLgaVFKLKNDPRITRVGRFLRKTSLDE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 366 LPQFINVLLGQMSVVGPRPHMLKHTEEYSHliDKYMVRHLVKPGITGWAQVTGYRGETkelwqMEGRVQRDVWYLEHWTF 445
Cdd:COG2148  230 LPQLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSL 302
                        330
                 ....*....|....*...
gi 492410701 446 LLDLYIIYKTVRNAVRGE 463
Cdd:COG2148  303 WLDLKILLKTVLVVLKGK 320
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
276-461 1.58e-88

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 267.69  E-value: 1.58e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  276 KRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMRVNIDSDK-LQATANDPRKTKI 354
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSP-LLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGpLFKLKNDPRITRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  355 GDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHteEYSHLIDKYMVRHLVKPGITGWAQVTGYRGETKelwqMEGRVQ 434
Cdd:pfam02397  80 GRFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLE 153
                         170       180
                  ....*....|....*....|....*..
gi 492410701  435 RDVWYLEHWTFLLDLYIIYKTVRNAVR 461
Cdd:pfam02397 154 LDLYYIENWSLWLDLKILLKTVKVVLK 180
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
106-456 4.47e-85

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 268.90  E-value: 4.47e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 106 SSLRFFACFYGIFFICLAVYRLMFRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGYFCDLPSNDfp 185
Cdd:PRK10124 106 TQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHDPKPGG-- 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 186 ESIPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVPNIR--NYLHRRMhfELFGNIPVLTIR 263
Cdd:PRK10124 184 VSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFtfNILHSRL--EEMNGVPVVPLY 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 264 EEPLTQMeNRLLKRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMRVNIDSDKL- 342
Cdd:PRK10124 262 DTPLSGI-NRLLKRAEDIVLASLILLLISP-VLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVt 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 343 QATANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHTEEYSHLIDKYMVRHLVKPGITGWAQVTGYRGE 422
Cdd:PRK10124 340 QATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGE 419
                        330       340       350
                 ....*....|....*....|....*....|....
gi 492410701 423 TKELWQMEGRVQRDVWYLEHWTFLLDLYIIYKTV 456
Cdd:PRK10124 420 TDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTV 453
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
17-467 1.93e-171

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 489.40  E-value: 1.93e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   17 FGDLCLLNIIFISLYHIFDYQtLGNEFTHSLPQLLVLLNLVYLLCNYSNGVILHERIVRPERIVRRAFRNTIFHAALFIS 96
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGS-RGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   97 LATLAEIGTSSLR-FFACFYGIFFICLAVYRLMFRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGY 175
Cdd:TIGR03023  80 LAFLLKTGTEFSRlWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  176 FCDLPSNDFPES-IPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVPNIRNYLHRRMHFELF 254
Cdd:TIGR03023 160 FDDRPDARTSVRgVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  255 GNIPVLTIREEPLTQMeNRLLKRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMR 334
Cdd:TIGR03023 240 GGLPVISLRDSPLDGW-NRFIKRAFDIVLALLVLLLLSP-LLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  335 VNIDSD-KLQATANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHTEEYSHLIDKYMVRHLVKPGITGW 413
Cdd:TIGR03023 318 VHAEGDgVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGW 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 492410701  414 AQVTGYRGETKELWQMEGRVQRDVWYLEHWTFLLDLYIIYKTVRNAVRGeKEAY 467
Cdd:TIGR03023 398 AQVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVG-KNAY 450
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
17-467 5.15e-146

exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model.


Pssm-ID: 274398 [Multi-domain]  Cd Length: 445  Bit Score: 424.31  E-value: 5.15e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   17 FGDLCLLNIIFISLYHIFDYQTLGNEFTHSLPQLLVLLNLVYLLCNYsnGVILHERIVRPERIVRRAFRNTIFHAALFIS 96
Cdd:TIGR03025   1 LADLLALVLAFLLAFLLLGLGLLPPPDFYSLLLLLLLLLFLILFALS--GLYRSWRGRSLLEELARVLLAWLVAFLLLLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   97 LATLAEIGTSSLRFFACFYGIFFICLAVYRLMFRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGYF 176
Cdd:TIGR03025  79 LAFLFKSFDFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  177 CDLPSND-FPESIPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVPNIRNYLHRRMHFELFG 255
Cdd:TIGR03025 159 DDRPSDRvEVAGLPVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEELG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  256 NIPVLTIREEPLTQmENRLLKRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMRV 335
Cdd:TIGR03025 239 GVPLLSLSNFPLSG-LNRALKRLFDIVLSLLALLLLSP-LMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  336 NIDSDK--LQATANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHTEEYSHLIDKYMVRHLVKPGITGW 413
Cdd:TIGR03025 317 DAEEGGgpVQATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGW 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 492410701  414 AQVTGyRGETKElwqMEGRVQRDVWYLEHWTFLLDLYIIYKTVRNAVRGeKEAY 467
Cdd:TIGR03025 397 AQVSG-RGETST---MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTG-KGAY 445
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
129-463 1.97e-99

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 300.88  E-value: 1.97e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 129 FRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGYFCDLPSNDFPESIPYLGQPKEV-VTYLQQHHIE 207
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLlLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 208 QVYCCLPSARSHEIVPIINYCENHLIRfysvpnirnYLHRRMHFELFGNIPVLTIREEPLTQMeNRLLKRAFDLFFSLSF 287
Cdd:COG2148   81 IIVLLALLLRELLLLLLLLLLRLLGVV---------AELGRVSLSELGGLPLLSVRGPPLSGY-QRVLKRLFDIVLALLG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 288 LCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMRVNIDSDK--LQATANDPRKTKIGDFIRKTSIDE 365
Cdd:COG2148  151 LILLSP-LLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLgaVFKLKNDPRITRVGRFLRKTSLDE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 366 LPQFINVLLGQMSVVGPRPHMLKHTEEYSHliDKYMVRHLVKPGITGWAQVTGYRGETkelwqMEGRVQRDVWYLEHWTF 445
Cdd:COG2148  230 LPQLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSL 302
                        330
                 ....*....|....*...
gi 492410701 446 LLDLYIIYKTVRNAVRGE 463
Cdd:COG2148  303 WLDLKILLKTVLVVLKGK 320
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
276-461 1.58e-88

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 267.69  E-value: 1.58e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  276 KRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMRVNIDSDK-LQATANDPRKTKI 354
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSP-LLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGpLFKLKNDPRITRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  355 GDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHteEYSHLIDKYMVRHLVKPGITGWAQVTGYRGETKelwqMEGRVQ 434
Cdd:pfam02397  80 GRFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLE 153
                         170       180
                  ....*....|....*....|....*..
gi 492410701  435 RDVWYLEHWTFLLDLYIIYKTVRNAVR 461
Cdd:pfam02397 154 LDLYYIENWSLWLDLKILLKTVKVVLK 180
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
106-456 4.47e-85

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 268.90  E-value: 4.47e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 106 SSLRFFACFYGIFFICLAVYRLMFRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGYFCDLPSNDfp 185
Cdd:PRK10124 106 TQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHDPKPGG-- 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 186 ESIPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVPNIR--NYLHRRMhfELFGNIPVLTIR 263
Cdd:PRK10124 184 VSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFtfNILHSRL--EEMNGVPVVPLY 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 264 EEPLTQMeNRLLKRAFDLFFSLSFLCTVFPfVYIIIGTTIKLSSSGPIFFKQKRSGENGKEFWCYKFRSMRVNIDSDKL- 342
Cdd:PRK10124 262 DTPLSGI-NRLLKRAEDIVLASLILLLISP-VLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVt 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 343 QATANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVVGPRPHMLKHTEEYSHLIDKYMVRHLVKPGITGWAQVTGYRGE 422
Cdd:PRK10124 340 QATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGE 419
                        330       340       350
                 ....*....|....*....|....*....|....
gi 492410701 423 TKELWQMEGRVQRDVWYLEHWTFLLDLYIIYKTV 456
Cdd:PRK10124 420 TDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTV 453
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
81-463 4.20e-68

Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein has been characterized as the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. This model includes the enterobacterial enzymes, where the function is presumed to be identical to the S. typhimurium enzyme as well as a somewhat broader group which are likely to catalyze the same or highly similar reactions based on a phylogenetic tree-building analysis of the broader sugar transferase family. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. The most likely heterogeneity would be in the precise nature of the sugar molecule transferred.


Pssm-ID: 274395 [Multi-domain]  Cd Length: 456  Bit Score: 224.55  E-value: 4.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   81 RRAFRNTIFHAALFISLATLAEIGT-SSLRFFACFYGIFFICLAVYRLMFRYLLKRYREYGgnsRTVVLVGSNKNMAELY 159
Cdd:TIGR03022  65 RRLTLATFALFLFILALAFFTKVSEpYSRLVFLLAWGLALVLVPLARILVRKLLSRRGWWG---RPAVIIGAGQNAAILY 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  160 QEMAGDPTTGFRISGYFCDLPSND--FPESIPYLGQpKEVVTYLQQHHIEQVYCCLPSARS---HEIVPII--NYCENHL 232
Cdd:TIGR03022 142 RALQSNPQLGLRPLAVVDTDPAASgrLLTGLPVVGA-DDALRLYARTRYAYVIVAMPGTQAedmARLVRKLgaLHFRNVL 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  233 IR--FYSVPNIRnylhrRMHFELfGNIPVLTIREEPLTQmENRLLKRAFDLFFSLSFLCTVFPFVyIIIGTTIKLSSSGP 310
Cdd:TIGR03022 221 IVpsLFGLPNLW-----ISPRFI-GGVLGLRVRNNLLLP-SARLIKRTLDLVLSLLALPLLLPLL-LVIALLIRLDSKGP 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  311 IFFKQKRSGENGKEFWCYKFRSMRVNIDS----------------DKLQATANDPRKTKIGDFIRKTSIDELPQFINVLL 374
Cdd:TIGR03022 293 AFYKQERVGRNGKLFKCYKFRTMVMNSDQvleellaadpelraewEEYHKLRNDPRITRIGKFLRKTSLDELPQLWNVLK 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  375 GQMSVVGPRPHMLKHTEEYSHLIDKYmvrHLVKPGITGWAQVTGyRGETkelwQMEGRVQRDVWYLEHWTFLLDLYIIYK 454
Cdd:TIGR03022 373 GDMSLVGPRPYLTSELSRYGEALELY---LRVRPGITGLWQVSG-RNET----TYDERVYLDVWYIKNWSLWLDIVILAK 444

                  ....*....
gi 492410701  455 TVRNAVRGE 463
Cdd:TIGR03022 445 TIKVVLRRK 453
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
81-463 2.08e-53

sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the family of bacterial sugar transferases (pfam02397). 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 (notable exceptions appear to include Magnetococcus sp. MC-1 and Myxococcus xanthus DK 1622 ). These genes are generally found near one or more of the PrsK, PrsR or PrsT genes that have been related to the PEP-CTERM system by phylogenetic profiling methods. 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. These proteins are homologs of the EpsB protein found in Methylobacillus sp. strain 12S, which is also associated with a PEP-CTERM system, but of a distinct type. A name which appears attached to a number of genes (by transitive annotation) in this family is "undecaprenyl-phosphate galactose phosphotransferase", which comes from relatively distant characterized enterobacterial homologs, and is considerably more specific than warranted from the currently available evidence.


Pssm-ID: 274390 [Multi-domain]  Cd Length: 442  Bit Score: 185.28  E-value: 2.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   81 RRAFRNTIFHAALFISLATLAeigtSSLRFFacFYGIFF---------ICLAVY-RLMFRYLLKRYREYGGNSRTVVLVG 150
Cdd:TIGR03013  58 REDFRGIIARLAISLLVSFLA----LSFIFY--FYPEFYlgrgllalaIVLAGSlVLLSRLFFLKILGLQGLKRRILVLG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  151 SNKNMAELYQEMAGDPTTGFRISGYFcdlPSNDFPESIPY---LGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINY 227
Cdd:TIGR03013 132 TGPRAREIARLRRSSDRRGHEIVGFV---PLPDEPAYVPSehvIENGDGLVEYVLRHRIDEIVIALDERRGSLPVDELLE 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  228 CENHLIRFYSVPNIRNYLHRRMHFELFgnIPVLTIREEPLTQMENR-LLKRAFDLFFSLSFLCTVFPfVYIIIGTTIKLS 306
Cdd:TIGR03013 209 CKLSGIEVVDAPSFFERETGKIAIDLI--YPSWLIFSNGFRNSSLRrITKRSFDVVASLILLILTLP-VMLFTALAIKLE 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  307 SSGPIFFKQKRSGENGKEFWCYKFRSMRVNIDSDKLQ-ATANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVVGPRPH 385
Cdd:TIGR03013 286 SGGPVLYRQERVGLNGRPFNLIKFRSMRADAEKNGAVwAQKDDPRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPE 365
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492410701  386 MLKHTEEYSHLIDKYMVRHLVKPGITGWAQVTGYRGETKElwQMEGRVQRDVWYLEHWTFLLDLYIIYKTVRNAVRGE 463
Cdd:TIGR03013 366 RPEFVEKLSEEIPYYNERHRVKPGITGWAQIKYPYGASVA--DAKEKLRYDLYYIKNMSLLLDLIILIQTFEVVLFGK 441
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
80-461 6.13e-41

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 152.47  E-value: 6.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  80 VRRAFRNTIFHAALFISLATLAEIGTSSLRFFACfYGIFFICLAVYRLMFRYLLKRYreyGGNSRTVVLVGSNKNMAELY 159
Cdd:PRK15204  87 LKEIFRTIVIFAIFDLALIAFTKWQFSRYVWVFC-WTFALILVPFFRALTKHLLNKL---GIWKKKTIILGSGQNARGAY 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 160 QEMAGDPTTGFRISGYFCDLPSNDFPESIPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVP 239
Cdd:PRK15204 163 SALQSEEMMGFDVIAFFDTDASDAEINMLPVIKDTEIIWDLNRTGDVHYILAYEYTELEKTHFWLRELSKHHCRSVTVVP 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 240 NIRNY--LHRRMHFELFGNIPVLTIREEpLTQMENRLLKRAFDLFFSLSFLCTVFPF-VYIIIGTTiklSSSGPIFFKQK 316
Cdd:PRK15204 243 SFRGLplYNTDMSFIFSHEVMLLRIQNN-LAKRSSRFLKRTFDIVCSIMILIIASPLmIYLWYKVT---RDGGPAIYGHQ 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 317 RSGENGKEFWCYKFRSMRVN--------IDSDKLQAT--------ANDPRKTKIGDFIRKTSIDELPQFINVLLGQMSVV 380
Cdd:PRK15204 319 RVGRHGKLFPCYKFRSMVMNsqevlkelLANDPIARAewekdfklKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLV 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 381 GPRPHMLKHTEEYSHLIDKYMvrhLVKPGITGWAQVTGyRGETkelwQMEGRVQRDVWYLEHWTFLLDLYIIYKTVRNAV 460
Cdd:PRK15204 399 GPRPIVSDELERYCDDVDYYL---MAKPGMTGLWQVSG-RNDV----DYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVL 470

                 .
gi 492410701 461 R 461
Cdd:PRK15204 471 R 471
CoA_binding_3 pfam13727
CoA-binding domain;
63-239 3.57e-29

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 112.75  E-value: 3.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701   63 YSNGVILHERIVRPERIVRRAFRNTIFhAALFISLATLAEIGTSSLRFFACFYGIFFICLAVYRLMFRYLLKRYREYGGN 142
Cdd:pfam13727   1 PAFGVYQSWRGRSLLRELRRVLSAWLL-VFLLLALLSFSLHDIFSRLWLAYWAVSGIALLILSRLLLRAVLRRYRRHGRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701  143 SRTVVLVGsnkNMAELYQEMAGDPTTGFRISGYFCDLPSNDFPE--SIPYLGQPKEVVTYLQQHHIEQVYCCLPSARSHE 220
Cdd:pfam13727  80 NRRVVAVG---GGLELARQIRANPWLGFRVVGVFDDRDDDRVPEvaGVPVLGNLADLVEYVRETRVDEVYLALPLSAEAR 156
                         170
                  ....*....|....*....
gi 492410701  221 IVPIINYCENHLIRFYSVP 239
Cdd:pfam13727 157 ILRLVKELRDDPVNIRLIP 175
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
123-241 1.26e-20

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 87.29  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492410701 123 AVYRLMFRYLLKRYREYGGNSRTVVLVGSNKNMAELYQEMAGDPTTGFRISGYFCDLPS--NDFPESIPYLGQPKEVVTY 200
Cdd:COG1086    1 LLLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVDDDPDkrGRRIEGVPVLGTLDDLPEL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 492410701 201 LQQHHIEQVYCCLPSARSHEIVPIINYCENHLIRFYSVPNI 241
Cdd:COG1086   81 VRRLGVDEVIIALPSASRERLRELLEQLEDLGVKVKIVPDL 121
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH