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Conserved domains on  [gi|503726187|ref|WP_013960263|]
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glycosyltransferase family 4 protein [Roseobacter litoralis]

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
PubMed:  12691742|10521532|16037492
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 ...
 53-412 3.30e-40

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: 146.91  E-value: 3.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  53 LHDRLKARVNYLPEYLEDDPPRVRRALFSARRLPGFKDAVRCFRAdyardqtenrIRRFGqacVLAHELPQDVtgLYAHF 132
Cdd:cd03801   26 ALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRL----------LRELR---PLLRLRKFDV--VHAHG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 133 LHTPSsVARYAAILTGLPWSFSAHAKDIWTSPDWELREK--LSAQSFGAQFGA---TCTAFGAEHLRSL-ADRTDRVDLV 206
Cdd:cd03801   91 LLAAL-LAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARAEALLRRADaviAVSEALRDELRALgGIPPEKIVVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 207 YHGLDLTRFPDPPDRKARKPDAPLALMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIG-GGTLKDQMQDLAAakGVA 284
Cdd:cd03801  170 PNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPdVRLVIVGgDGPLRAELEELEL--GLG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 285 DRITWRGACDQPEVIAEMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVD-DAPD 363
Cdd:cd03801  248 DRVRFLGFVPDEELPALYAAADVFVLPSR------YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpDDVE 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 503726187 364 SLAQAIRDFAARQDKGRAFADAAYIRLKTEFqmqpGINQLTKRLRAMMR 412
Cdd:cd03801  322 ALADALLRLLADPELRARLGRAARERVAERF----SWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 53-412 3.30e-40

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: 146.91  E-value: 3.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  53 LHDRLKARVNYLPEYLEDDPPRVRRALFSARRLPGFKDAVRCFRAdyardqtenrIRRFGqacVLAHELPQDVtgLYAHF 132
Cdd:cd03801   26 ALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRL----------LRELR---PLLRLRKFDV--VHAHG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 133 LHTPSsVARYAAILTGLPWSFSAHAKDIWTSPDWELREK--LSAQSFGAQFGA---TCTAFGAEHLRSL-ADRTDRVDLV 206
Cdd:cd03801   91 LLAAL-LAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARAEALLRRADaviAVSEALRDELRALgGIPPEKIVVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 207 YHGLDLTRFPDPPDRKARKPDAPLALMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIG-GGTLKDQMQDLAAakGVA 284
Cdd:cd03801  170 PNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPdVRLVIVGgDGPLRAELEELEL--GLG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 285 DRITWRGACDQPEVIAEMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVD-DAPD 363
Cdd:cd03801  248 DRVRFLGFVPDEELPALYAAADVFVLPSR------YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpDDVE 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 503726187 364 SLAQAIRDFAARQDKGRAFADAAYIRLKTEFqmqpGINQLTKRLRAMMR 412
Cdd:cd03801  322 ALADALLRLLADPELRARLGRAARERVAERF----SWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 234-389 7.18e-29

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: 110.44  E-value: 7.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  234 SVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPS 312
Cdd:pfam00534   7 FVGRLEPEKGLDLLIKAFALLKEKNPnLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPS 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503726187  313 RiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDD-APDSLAQAIRDFAARQDKGRAFADAAYIR 389
Cdd:pfam00534  87 R------YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEELRERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 300-414 3.03e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 77.34  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 300 AEMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDDA-PDSLAQAIRDFAARQDK 378
Cdd:COG0438   16 ALLAAADVFVLPSR------SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGdPEALAEAILRLLEDPEL 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503726187 379 GRAFADAAYIRLKTEFqmqpGINQLTKRLRAMMRDA 414
Cdd:COG0438   90 RRRLGEAARERAEERF----SWEAIAERLLALYEEL 121
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
191-357 2.55e-09

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 58.57  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 191 EHLRSLADRTDRVDLVYHGLDLTRFPDPPDRKarkpDAPLALMSVGRLVEK--KGFDRLIEALALLpdTLPWHWTHIGGG 268
Cdd:PRK09922 146 EQMMARGISAQRISVIYNPVEIKTIIIPPPER----DKPAVFLYVGRLKFEgqKNVKELFDGLSQT--TGEWQLHIIGDG 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 269 TLKDQMQDLAAAKGVADRITWRGACDQP--EVIAEMRTSDLFVLPSRIaadgdrDGLPNVLMEAASQRLPILATPVSAIP 346
Cdd:PRK09922 220 SDFEKCKAYSRELGIEQRIIWHGWQSQPweVVQQKIKNVSALLLTSKF------EGFPMTLLEAMSYGIPCISSDCMSGP 293

                        170
                 ....*....|..
gi 503726187 347 E-FIDTGVHGIL 357
Cdd:PRK09922 294 RdIIKPGLNGEL 305
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 53-412 3.30e-40

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: 146.91  E-value: 3.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  53 LHDRLKARVNYLPEYLEDDPPRVRRALFSARRLPGFKDAVRCFRAdyardqtenrIRRFGqacVLAHELPQDVtgLYAHF 132
Cdd:cd03801   26 ALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRL----------LRELR---PLLRLRKFDV--VHAHG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 133 LHTPSsVARYAAILTGLPWSFSAHAKDIWTSPDWELREK--LSAQSFGAQFGA---TCTAFGAEHLRSL-ADRTDRVDLV 206
Cdd:cd03801   91 LLAAL-LAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARAEALLRRADaviAVSEALRDELRALgGIPPEKIVVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 207 YHGLDLTRFPDPPDRKARKPDAPLALMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIG-GGTLKDQMQDLAAakGVA 284
Cdd:cd03801  170 PNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPdVRLVIVGgDGPLRAELEELEL--GLG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 285 DRITWRGACDQPEVIAEMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVD-DAPD 363
Cdd:cd03801  248 DRVRFLGFVPDEELPALYAAADVFVLPSR------YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpDDVE 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 503726187 364 SLAQAIRDFAARQDKGRAFADAAYIRLKTEFqmqpGINQLTKRLRAMMR 412
Cdd:cd03801  322 ALADALLRLLADPELRARLGRAARERVAERF----SWERVAERLLDLYR 366
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 193-393 3.23e-36

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: 135.56  E-value: 3.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 193 LRSLADRTDRVDLVYHGLDLTRFPDPPDRKA-RKPDAPLALMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTL 270
Cdd:cd03811  151 IRLGPSPPEKIEVIYNPIDIDRIRALAKEPIlNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPdVKLVILGDGPL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 271 KDQMQDLAAAKGVADRITWRGACDQPevIAEMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFID 350
Cdd:cd03811  231 REELEKLAKELGLAERVIFLGFQSNP--YPYLKKADLFVLSSR------YEGFPNVLLEAMALGTPVVSTDCPGPREILD 302

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503726187 351 TGVHGILVDDAPDSL----AQAIRDFAARQDKGRAFADA--AYIRLKTE 393
Cdd:cd03811  303 DGENGLLVPDGDAAAlagiLAALLQKKLDAALRERLAKAqeAVFREYTI 351
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 19-414 3.38e-36

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: 136.36  E-value: 3.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  19 SETFIAQELVALEDAGLTLELWSLRHPTdektHPLHDRLKarvnylPEYLEDDPPRVRRALFSARRLPGFKDAVRCFRAD 98
Cdd:cd03798   16 RGIFVRRQVRALSRRGVDVEVLAPAPWG----PAAARLLR------KLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  99 YARDQtenrirrfgqacvlAHELPQDVtgLYAHFLHTPSSVARYAAILTGLPWSFSAHAKDIWTSPDWELREKLSAQSFG 178
Cdd:cd03798   86 KLLKR--------------RRRGPPDL--IHAHFAYPAGFAAALLARLYGVPYVVTEHGSDINVFPPRSLLRKLLRWALR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 179 --AQFGATCTAFGAEHLRSLADRtDRVDLVYHGLDLTRFpDPPDRKARKPDAPLALMSVGRLVEKKGFDRLIEALALLPD 256
Cdd:cd03798  150 raARVIAVSKALAEELVALGVPR-DRVDVIPNGVDPARF-QPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAK 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 257 TLPwhwtHI-----GGGTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSRiaadgdRDGLPNVLMEAA 331
Cdd:cd03798  228 ARP----DVvllivGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSR------HEGFGLVLLEAM 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 332 SQRLPILATPVSAIPEFIDTGVHGILVDDA-PDSLAQAIRDFAARQDKgRAFADAAYIRLKTEFqmqpGINQLTKRLRAM 410
Cdd:cd03798  298 ACGLPVVATDVGGIPEVVGDPETGLLVPPGdADALAAALRRALAEPYL-RELGEAARARVAERF----SWVKAADRIAAA 372


                 ....
gi 503726187 411 MRDA 414
Cdd:cd03798  373 YRDV 376
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 7-403 2.00e-34

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: 131.03  E-value: 2.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187   7 RLAVLVKGWPRLSETFIAQELVALEDAGLTLELWSLRHPTDEKTHPLHDRLK-ARVNYLPeyleddpprvrrALFSARRL 85
Cdd:cd03799    1 KIAFIVDEFPVLSETFILNQITGLIDRGHEVDIYAVNPGDLVKRHPDVEKYNvPSLNLLY------------AIVGLNKK 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  86 PGFkDAVRCfradyardqtenrirRFGQACVLAHELPQDVtGLYAHFLhtpsSVARYAAIltglPWSFSAHAKDIWtspd 165
Cdd:cd03799   69 GAY-DIIHC---------------QFGPLGALGALLRRLK-VLKGKLV----TSFRGYDI----SMYVILEGNKVY---- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 166 welrEKLSAQsfGAQFGATCTAFGAEhLRSLADRTDRVDLVYHGLDLTRFPDPPDRKArkPDAPLALMSVGRLVEKKGFD 245
Cdd:cd03799  120 ----PQLFAQ--GDLFLPNCELFKHR-LIALGCDEKKIIVHRSGIDCNKFRFKPRYLP--LDGKIRILTVGRLTEKKGLE 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 246 RLIEALALLPDTLP-WHWTHIGGGTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSRIAADGDRDGLP 324
Cdd:cd03799  191 YAIEAVAKLAQKYPnIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGDQDGPP 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 325 NVLMEAASQRLPILATPVSAIPEFIDTGVHGILVD--DApDSLAQAIRDFAARQDKGRAFADAAYIRLKTEFQMQPGINQ 402
Cdd:cd03799  271 NTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPerDA-EAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDE 349


                 .
gi 503726187 403 L 403
Cdd:cd03799  350 L 350
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 201-397 7.33e-30

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: 118.57  E-value: 7.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 201 DRVDLVYHGLDLTRF-PDPPDRKARKPDAPLA-----LMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTLKDQ 273
Cdd:cd03807  156 NKIVVIYNGIDLFKLsPDDASRARARRRLGLAedrrvIGIVGRLHPVKDHSDLLRAAALLVETHPdLRLLLVGRGPERPN 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 274 MQDLAAAKGVADRITWRGAC-DQPEViaeMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTG 352
Cdd:cd03807  236 LERLLLELGLEDRVHLLGERsDVPAL---LPAMDIFVLSSR------TEGFPNALLEAMACGLPVVATDVGGAAELVDDG 306

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 503726187 353 VhGILVD-DAPDSLAQAIRDFAARQDKGRAFADAAYIRLKTEFQMQ 397
Cdd:cd03807  307 T-GFLVPaGDPQALADAIRALLEDPEKRARLGRAARERIANEFSID 351
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 74-358 9.42e-30

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: 115.19  E-value: 9.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  74 RVRRALFSARRLPGFKDAVRCfradyardqtENRIRRFGQACVLAHELPQDVtglYAHFLHTPSSVARYAAILTGLPWSF 153
Cdd:cd01635   17 LHVRALARALAALGHEVTVLA----------LLLLALRRILKKLLELKPDVV---HAHSPHAAALAALLAARLLGIPIVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 154 SAHAKDIWTSPDWELreklsaqsfgaqfgatctaFGAEHLRSLADRTDRVdlvyhgldltrfpdppdrkarkpdaplalm 233
Cdd:cd01635   84 TVHGPDSLESTRSEL-------------------LALARLLVSLPLADKV------------------------------ 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 234 SVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEM-RTSDLFVLP 311
Cdd:cd01635  115 SVGRLVPEKGIDLLLEALALLKARLPdLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLlAAADVFVLP 194

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 503726187 312 SRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILV 358
Cdd:cd01635  195 SR------SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 234-389 7.18e-29

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: 110.44  E-value: 7.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  234 SVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPS 312
Cdd:pfam00534   7 FVGRLEPEKGLDLLIKAFALLKEKNPnLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPS 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503726187  313 RiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDD-APDSLAQAIRDFAARQDKGRAFADAAYIR 389
Cdd:pfam00534  87 R------YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 148-383 8.64e-27

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: 110.23  E-value: 8.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 148 GLPWSFSAHAKDIWTSPDW-----------ELREKLsAQSFGAQFGATctafgAEHLRSLADR----TDRVDLVYHGLDL 212
Cdd:cd05844  104 GVPLVVTFHGFDITTSRAWlaaspgwpsqfQRHRRA-LQRPAALFVAV-----SGFIRDRLLArglpAERIHVHYIGIDP 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 213 TRFPdPPDRKARKPdaplALMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTLKDQMQDLAAAkgvADRITWRG 291
Cdd:cd05844  178 AKFA-PRDPAERAP----TILFVGRLVEKKGCDVLIEAFRRLAARHPtARLVIAGDGPLRPALQALAAA---LGRVRFLG 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 292 ACDQPEVIAEMRTSDLFVLPSRIAADGDRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDDA-PDSLAQAI- 369
Cdd:cd05844  250 ALPHAEVQDWMRRAEIFCLPSVTAASGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGdVDALADALq 329

                        250       260
                 ....*....|....*....|
gi 503726187 370 -----RDFAARQD-KGRAFA 383
Cdd:cd05844  330 alladRALADRMGgAARAFV 349
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
232-371 2.70e-25

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 99.89  E-value: 2.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  232 LMSVGRLVEK-KGFDRLIEALALL-PDTLPWHWTHIGGGTLKDQMqdlAAAKGVADRITWRGAcdQPEVIAEMRTSDLFV 309
Cdd:pfam13692   4 ILFVGRLHPNvKGVDYLLEAVPLLrKRDNDVRLVIVGDGPEEELE---ELAAGLEDRVIFTGF--VEDLAELLAAADVFV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503726187  310 LPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDtGVHGILVDDA-PDSLAQAIRD 371
Cdd:pfam13692  79 LPSL------YEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGdPEALAEAILR 134
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 202-391 5.00e-25

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: 105.01  E-value: 5.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 202 RVDLVYHGLDLTRFPDPPDRKARKpdaplaLMSVGRLVEKKGFDRLIEALALLPDTLP-WHWtHI-GGGTLKDQMQDLAA 279
Cdd:cd03820  160 NVVVIPNPLSFPSEEPSTNLKSKR------ILAVGRLTYQKGFDLLIEAWALIAKKHPdWKL-RIyGDGPEREELEKLID 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 280 AKGVADRITWRGACDQPEViaEMRTSDLFVLPSRIaadgdrDGLPNVLMEAASQRLPILAtpvSAIP----EFIDTGVHG 355
Cdd:cd03820  233 KLGLEDRVKLLGPTKNIAE--EYANSSIFVLSSRY------EGFPMVLLEAMAYGLPIIS---FDCPtgpsEIIEDGENG 301

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 503726187 356 ILVDDA-PDSLAQAIRDFAARQDKGRAFADAAYIRLK 391
Cdd:cd03820  302 LLVPNGdVDALAEALLRLMEDEELRKKMGKNARKNAE 338
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 70-389 3.18e-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: 102.43  E-value: 3.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187  70 DDPPRVRRALFSARRLPGFKdaVRCFRADYARDQTENRIRRFgqacvlahelpqDVTGLYAHFLhTPSSVARYAAILTGL 149
Cdd:cd03819   36 AGGPLLPRLRQIGIGLPGLK--VPLLRALLGNVRLARLIRRE------------RIDLIHAHSR-APAWLGWLASRLTGV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 150 PWSFSAHAKDIWTSPDWELRekLSAQSFGAQFGATCtAFGAEHL--RSLADRtDRVDLVYHGLDLTRFPDPPDRKAR--- 224
Cdd:cd03819  101 PLVTTVHGSYLATYHPKDFA--LAVRARGDRVIAVS-ELVRDHLieALGVDP-ERIRVIPNGVDTDRFPPEAEAEERaql 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 225 --KPDAPLALMsVGRLVEKKGFDRLIEALALLPDTLPWHWTHIGGGTLKDQMQDLAAAKGVADRITWRGACDQpeVIAEM 302
Cdd:cd03819  177 glPEGKPVVGY-VGRLSPEKGWLLLVDAAAELKDEPDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFRED--VPAAL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 303 RTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDD-APDSLAQAIRDF----AARQD 377
Cdd:cd03819  254 AASDVVVLPSL------HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAkllpEAREK 327

                        330
                 ....*....|..
gi 503726187 378 KGRAFADAAYIR 389
Cdd:cd03819  328 LQAAAALTEAVR 339
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 132-394 7.28e-24

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: 101.52  E-value: 7.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 132 FLHTPSSV--ARYAAIL----------TGLPWSFSAHA--KDIWTspdweLREKLsaqsfgAQFGATCTAFGAEHLRSLA 197
Cdd:cd03808   86 HCHTPKPGilGRLAARLagvpkviytvHGLGFVFTEGKllRLLYL-----LLEKL------ALLFTDKVIFVNEDDRDLA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 198 ----DRTDRVDLVYHG--LDLTRFPdpPDRKARKPDAPLALMsVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTL 270
Cdd:cd03808  155 ikkgIIKKKKTVLIPGsgVDLDRFQ--YSPESLPSEKVVFLF-VARLLKDKGIDELIEAAKILKKKGPnVRFLLVGDGEL 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 271 KDQMQDLAAAKGVADRITWRGAC-DQPEVIAEmrtSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFI 349
Cdd:cd03808  232 ENPSEILIEKLGLEGRIEFLGFRsDVPELLAE---SDVFVLPSY------REGLPRSLLEAMAAGRPVITTDVPGCRELV 302

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 503726187 350 DTGVHGILVDDA-PDSLAQAIRDFAARQDKGRAFADAAYIRLKTEF 394
Cdd:cd03808  303 IDGVNGFLVPPGdVEALADAIEKLIEDPELRKEMGEAARKRVEEKF 348
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 190-394 1.49e-21

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: 95.77  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 190 AEHLRSL--ADRtDRVDLVYHGLDLTRF-PDPPD-----RKARKPDAPLALmSVGRLVEKKGFDRLIEALALLPDTLPWH 261
Cdd:cd03800  175 ADELISLygADP-SRINVVPPGVDLERFfPVDRAearraRLLLPPDKPVVL-ALGRLDPRKGIDTLVRAFAQLPELRELA 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 262 WTHIGGGTLKD-------QMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSRIAADGdrdglpNVLMEAASQR 334
Cdd:cd03800  253 NLVLVGGPSDDplsmdreELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFG------LTAIEAMACG 326

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503726187 335 LPILATPVSAIPEFIDTGVHGILVDD-APDSLAQAIRDFAARQDKGRAFADAAYIRLKTEF 394
Cdd:cd03800  327 TPVVATAVGGLQDIVRDGRTGLLVDPhDPEALAAALRRLLDDPALWQRLSRAGLERARAHY 387
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 186-369 9.70e-20

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: 90.03  E-value: 9.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 186 TAFGAEHLRSLADrTDRVDLVYHGLDLTRFPDPPDRKARK-----PDAPLALMsVGRLVEKKGFDRLIEALALLPDTLPW 260
Cdd:cd03817  155 SEKIKDTLREYGV-KGPIEVIPNGIDLDKFEKPLNTEERRklglpPDEPILLY-VGRLAKEKNIDFLLRAFAELKKEPNI 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 261 HWTHIGGGTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSriaadgDRDGLPNVLMEAASQRLPILAT 340
Cdd:cd03817  233 KLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFAS------TTETQGLVYLEAMAAGLPVVAA 306

                        170       180
                 ....*....|....*....|....*....
gi 503726187 341 PVSAIPEFIDTGVHGILVDDAPDSLAQAI 369
Cdd:cd03817  307 KDPAASELVEDGENGFLFEPNDETLAEKL 335
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 150-385 1.07e-19

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: 89.74  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 150 PWSFS-AHAKDIWTspdWELREKlsaQSFGAQFGATCTAFG-AEHLRSLADRTdRVDLVYHGLDLTRFpDPPDRKARK-- 225
Cdd:cd03821  128 PWALQqKHWKKRIA---LHLIER---RNLNNAALVHFTSEQeADELRRFGLEP-PIAVIPNGVDIPEF-DPGLRDRRKhn 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 226 --PDAPLALMsVGRLVEKKGFDRLIEALA-LLPDTLPWHWTHIG-GGTLKDQMQDLAAAKGVADRITWRGACDQPEVIAE 301
Cdd:cd03821  200 glEDRRIILF-LGRIHPKKGLDLLIRAARkLAEQGRDWHLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWAL 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 302 MRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVhGILVDDAPDSLAQAIRDF-------AA 374
Cdd:cd03821  279 YASADLFVLPSY------SENFGNVVAEALACGLPVVITDKCGLSELVEAGC-GVVVDPNVSSLAEALAEAlrdpadrKR 351

                        250
                 ....*....|.
gi 503726187 375 RQDKGRAFADA 385
Cdd:cd03821  352 LGEMARRARQV 362
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 190-394 2.19e-19

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: 89.32  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 190 AEHLRSLADRTDRVDLVYHGLDLTRFPDPPD---RKARKPDAPLALMSVGRLVEKKGFDRLIEALALLPDTLPWHWTHIG 266
Cdd:cd03794  175 KEYLLRKGVPKEKIIVIPNWADLEEFKPPPKdelRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRPDIRFLFVG 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 267 GGTLKDQMQDLAAAKGVaDRITWRGACDQPEVIAEMRTSD--LFVLPSRIAADGdrdGLPNVLMEAASQRLPILATPVSA 344
Cdd:cd03794  255 DGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADvgLVPLKDNPANRG---SSPSKLFEYMAAGKPILASDDGG 330

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503726187 345 IPEFIDTGVHGILVD-DAPDSLAQAIRDFAARQDKGRAFADAAYIRLKTEF 394
Cdd:cd03794  331 SDLAVEINGCGLVVEpGDPEALADAILELLDDPELRRAMGENGRELAEEKF 381
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 300-414 3.03e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 77.34  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 300 AEMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDDA-PDSLAQAIRDFAARQDK 378
Cdd:COG0438   16 ALLAAADVFVLPSR------SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGdPEALAEAILRLLEDPEL 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503726187 379 GRAFADAAYIRLKTEFqmqpGINQLTKRLRAMMRDA 414
Cdd:COG0438   90 RRRLGEAARERAEERF----SWEAIAERLLALYEEL 121
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 199-395 1.73e-15

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: 77.37  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 199 RTDRVDLVYHGLdltRFPDPPDRKARKPDAPLALMSVGRLVEKKGFDRLIEALALLPDtLPWHWTHIGGGTLKDqmqdlA 278
Cdd:cd03823  164 FSARISVIPNAV---EPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPR-EDIELVIAGHGPLSD-----E 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 279 AAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSRIAadgdrDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILV 358
Cdd:cd03823  235 RQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWP-----EPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLF 309

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 503726187 359 -DDAPDSLAQAIRDFAARQDKGRAFADAAYIRLKTEFQ 395
Cdd:cd03823  310 aPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQ 347
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 186-387 1.86e-15

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 77.33  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 186 TAFGAEHLRSLADRtdRVDLVYHGLDLTRF-PDPPDRKARK----PDAPLaLMSVGRLVEKKGFDRLIEALALLPDTLPW 260
Cdd:cd03814  153 SPSIARELEGHGFE--RVRLWPRGVDTELFhPSRRDAALRRrlgpPGRPL-LLYVGRLAPEKNLEALLDADLPLAASPPV 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 261 HWTHIGGGTLKDQMQDlaaakgVADRITWRGACDQPEVIAEMRTSDLFVLPSRiaadgdRDGLPNVLMEAASQRLPILAT 340
Cdd:cd03814  230 RLVVVGDGPARAELEA------RGPDVIFTGFLTGEELARAYASADVFVFPSR------TETFGLVVLEAMASGLPVVAA 297

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 503726187 341 PVSAIPEFIDTGVHGILVDD-APDSLAQAIRDFAARQDKGRAFADAAY 387
Cdd:cd03814  298 DAGGPRDIVRPGGTGALVEPgDAAAFAAALRALLEDPELRRRMAARAR 345
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 220-394 2.05e-14

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: 73.85  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 220 DRKARKPDaplaLMSVGRLVEKKGFDRLIEALALL-PDTLpwhwthIGG-GTLKDQMQDLaAAKGVADRITWRGACDQPE 297
Cdd:cd03795  186 REKKGKKI----FLFIGRLVYYKGLDYLIEAAQYLnYPIV------IGGeGPLKPDLEAQ-IELNLLDNVKFLGRVDDEE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 298 VIAEMRTSDLFVLPSRIAADGdrDGLpnVLMEAASQRLPILATPV-SAIPEFIDTGVHGILVDDA-PDSLAQAIRDFAAR 375
Cdd:cd03795  255 KVIYLHLCDVFVFPSVLRSEA--FGI--VLLEAMMCGKPVISTNIgTGVPYVNNNGETGLVVPPKdPDALAEAIDKLLSD 330

                        170
                 ....*....|....*....
gi 503726187 376 QDKGRAFADAAYIRLKTEF 394
Cdd:cd03795  331 EELRESYGENAKKRFEELF 349
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 193-383 4.26e-14

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: 73.17  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 193 LRSLADRTDRVDLVYHGLDLTRFPDPPD---RKARKPDAPLALMsVGRLVEKKGFDRLIEALALLPDTLPWHWTHI--GG 267
Cdd:cd03809  154 IKFYGVPPEKIVVIPLGVDPSFFPPESAavlIAKYLLPEPYFLY-VGTLEPRKNHERLLKAFALLKKQGGDLKLVIvgGK 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 268 GTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSRIAadgdRDGLPnVLmEAASQRLPILATPVSAIPE 347
Cdd:cd03809  233 GWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYE----GFGLP-VL-EAMACGTPVIASNISVLPE 306

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503726187 348 FidTGVHGILVD-DAPDSLAQAIR----DFAARQ---DKGRAFA 383
Cdd:cd03809  307 V--AGDAALYFDpLDPESIADAILrlleDPSLREeliRKGLERA 348
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 227-373 1.92e-12

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 68.26  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 227 DAPLALMSVGRLVEKKGFDRLIEALALLPDTLPW---HWTHIGGGTLKDQMQDLAAAKGVADRITWRGACDQPEVIA--E 301
Cdd:cd04946  222 EGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSiciSWTHIGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQlyK 301

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503726187 302 MRTSDLFVLPSriaadgDRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDD--APDSLAQAIRDFA 373
Cdd:cd04946  302 ENDVDVFVNVS------ESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLDKdpTPNEIVSSIMKFY 369
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 194-395 5.70e-12

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: 66.59  E-value: 5.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 194 RSLADRTDRVDLVYHGLDLTRFPDPPDRKARK-----PDAPLALM-SVGRLVEKKGFDRLIEALALLPDTLPWHWTHIGG 267
Cdd:cd03825  154 RSPLLKGLPVVVIPNGIDTEIFAPVDKAKARKrlgipQDKKVILFgAESVTKPRKGFDELIEALKLLATKDDLLLVVFGK 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 268 GTLKDQMQDLAaakgvadriTWR-GACDQPEVIAEMRTS-DLFVLPSRiaadgdRDGLPNVLMEAASQRLPILATPVSAI 345
Cdd:cd03825  234 NDPQIVILPFD---------IISlGYIDDDEQLVDIYSAaDLFVHPSL------ADNLPNTLLEAMACGTPVVAFDTGGS 298

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503726187 346 PEFIDTGVHGILVD--DAPDsLAQAIRDFAARQDKGRAFADAAyiRLKTEFQ 395
Cdd:cd03825  299 PEIVQHGVTGYLVPpgDVQA-LAEAIEWLLANPKERESLGERA--RALAENH 347
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 190-394 1.75e-11

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: 65.07  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 190 AEHLRSLADRTDRVDLVYHGLDLTRF---PDPPDRKAR--KPDAPLaLMSVGRLVEKKGFDRLIEALALLPDTLPWHWTH 264
Cdd:cd04962  153 RQETYELFDVDKDIEVIHNFIDEDVFkrkPAGALKRRLlaPPDEKV-VIHVSNFRPVKRIDDVVRVFARVRRKIPAKLLL 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 265 IGGGTLKDQMQDLAAAKGVADRITWRGacDQPEVIAEMRTSDLFVLPSriaadgDRDGLPNVLMEAASQRLPILATPVSA 344
Cdd:cd04962  232 VGDGPERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPS------EKESFGLAALEAMACGVPVVSSNAGG 303

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503726187 345 IPEFIDTGVHGIL-----VDDAPDSLAQAIRDfaarQDKGRAFADAAYIRLKTEF 394
Cdd:cd04962  304 IPEVVKHGETGFLsdvgdVDAMAKSALSILED----DELYNRMGRAARKRAAERF 354
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 197-402 1.83e-09

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: 59.27  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 197 ADRtDRVDLVYHGLDLTRFPDPPDRKARKPdaPLALMSVGRLVEKKGFDRLIEALALL----PDTLPWhwthIGGGTLKD 272
Cdd:cd03813  264 ADP-DKTRVIPNGIDIQRFAPAREERPEKE--PPVVGLVGRVVPIKDVKTFIRAFKLVrramPDAEGW----LIGPEDED 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 273 QM-----QDLAAAKGVADRITWRGACDQPEVIAEMrtsDLFVLPSrIAadgdrDGLPNVLMEAASQRLPILATPVSAIPE 347
Cdd:cd03813  337 PEyaqecKRLVASLGLENKVKFLGFQNIKEYYPKL---GLLVLTS-IS-----EGQPLVILEAMASGVPVVATDVGSCRE 407

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503726187 348 FI-----DTGVHGILVDDA-PDSLAQAI----RDFAARQdkgrAFADAAYIRLKTEFQMQPGINQ 402
Cdd:cd03813  408 LIygaddALGQAGLVVPPAdPEALAEALikllRDPELRQ----AFGEAGRKRVEKYYTLEGMIDS 468
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
191-357 2.55e-09

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 58.57  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 191 EHLRSLADRTDRVDLVYHGLDLTRFPDPPDRKarkpDAPLALMSVGRLVEK--KGFDRLIEALALLpdTLPWHWTHIGGG 268
Cdd:PRK09922 146 EQMMARGISAQRISVIYNPVEIKTIIIPPPER----DKPAVFLYVGRLKFEgqKNVKELFDGLSQT--TGEWQLHIIGDG 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 269 TLKDQMQDLAAAKGVADRITWRGACDQP--EVIAEMRTSDLFVLPSRIaadgdrDGLPNVLMEAASQRLPILATPVSAIP 346
Cdd:PRK09922 220 SDFEKCKAYSRELGIEQRIIWHGWQSQPweVVQQKIKNVSALLLTSKF------EGFPMTLLEAMSYGIPCISSDCMSGP 293

                        170
                 ....*....|..
gi 503726187 347 E-FIDTGVHGIL 357
Cdd:PRK09922 294 RdIIKPGLNGEL 305
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 194-387 4.33e-09

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: 57.78  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 194 RSLADRTDRVDLVYHGLDLTRFPDPPDRKARK-PDAPLALMSVGRLVEKKGFDRLIEALALLPDTLPWHWTHIGGGTLKD 272
Cdd:cd03822  151 RIKLIPAVNIEVIPHGVPEVPQDPTTALKRLLlPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPS 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 273 QMQD--------LAAAKGVADRITW-RGACDQPEVIAEMRTSDLFVLPSRiaaDGDRdGLPNVLMEAASQRLPILATPVS 343
Cdd:cd03822  231 LARYegeryrkaAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPYL---NTEQ-SSSGTLSYAIACGKPVISTPLR 306

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503726187 344 AIPEFIDTGVHGILVDDAPDSLAQAIRDFAARQDKGRAFADAAY 387
Cdd:cd03822  307 HAEELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAY 350
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 205-380 4.53e-09

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: 57.84  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 205 LVYHGLDLTRFPDPPDRKARKPDA------PLALMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTLKDQMQDL 277
Cdd:cd04951  158 PVYNGIDLNKFKKDINVRLKIRNKlnlkndEFVILNVGRLTEAKDYPNLLLAISELILSKNdFKLLIAGDGPLRNELERL 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 278 AAAKGVADRITWRGACDQpevIAE-MRTSDLFVLPSRIaadgdrDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGI 356
Cdd:cd04951  238 ICNLNLVDRVILLGQISN---ISEyYNAADLFVLSSEW------EGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVV 308

                        170       180
                 ....*....|....*....|....
gi 503726187 357 LVDDaPDSLAQAIRDFAARQDKGR 380
Cdd:cd04951  309 PVSD-PQLLAEKIKEIFDMSDEER 331
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 202-369 1.96e-07

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 53.11  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 202 RVDLVYHGL-DLTRFPDPPDRK------ARKPDAPLALMSVGRLVEKKGFDRLIEALALLPDTLPW-HWTHIGGGTLKDQ 273
Cdd:PRK15179 483 RIPVVYNGLaPLKSVQDDACTAmmaqfdARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKvRFIMVGGGPLLES 562

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 274 MQDLAAAKGVADRITWRGACDQpeVIAEMRTSDLFVLPSRIaadgdrDGLPNVLMEAASQRLPILATPVSAIPEFIDTGV 353
Cdd:PRK15179 563 VREFAQRLGMGERILFTGLSRR--VGYWLTQFNAFLLLSRF------EGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGV 634

                        170       180
                 ....*....|....*....|
gi 503726187 354 HGILVD----DAPDsLAQAI 369
Cdd:PRK15179 635 TGLTLPadtvTAPD-VAEAL 653
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
265-370 4.73e-07

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 52.01  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 265 IGGGTLKDQMQDLAAAKGVADRITWRGAcdQPEVIAEMRTSDLFVLPSRIaadgdrDGLPNVLMEAASQRLPILATPVSA 344
Cdd:PRK15490 435 VGDGDLRAEAQKRAEQLGILERILFVGA--SRDVGYWLQKMNVFILFSRY------EGLPNVLIEAQMVGVPVISTPAGG 506

                         90       100
                 ....*....|....*....|....*..
gi 503726187 345 IPEFIDTGVHGILVDDAPD-SLAQAIR 370
Cdd:PRK15490 507 SAECFIEGVSGFILDDAQTvNLDQACR 533
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 232-387 4.92e-07

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 51.15  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 232 LMSVGRLVEKKGFDRLIEALALLPDTLPWHWTHI-GGGTLKDQMQDLAAAKGVADRITWRGACDQPEviAEMRTSDLFVL 310
Cdd:cd04949  163 IITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIyGYGEEREKLKKLIEELHLEDNVFLKGYHSNLD--QEYQDAYLSLL 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503726187 311 PSRIaadgdrDGLPNVLMEAASQRLPILATPVSAIP-EFIDTGVHGILVD-DAPDSLAQAIRDFAARQDKGRAFADAAY 387
Cdd:cd04949  241 TSQM------EGFGLTLMEAIGHGLPVVSYDVKYGPsELIEDGENGYLIEkNNIDALADKIIELLNDPEKLQQFSEESY 313
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 201-395 5.44e-07

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: 51.14  E-value: 5.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 201 DRVDLVYHGLDLTR--FPDPPDRKARKP---DAPLALMSVGRLVEKKGFDRLIEALALLPDTLP-WHWTHIGGGTLKDQM 274
Cdd:cd03812  158 GKFKVIPNGIDIEKykFNKEKRRKRRKLlilEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPnVKLVLVGEGELKEKI 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 275 QDLAAAKGVADRITWRGA-CDQPEViaeMRTSDLFVLPSRIaadgdrDGLPNVLMEAASQRLPILATpvSAIPEFIDTG- 352
Cdd:cd03812  238 KEKVKELGLEDKVIFLGFrNDVSEI---LSAMDVFLFPSLY------EGLPLVAVEAQASGLPCLLS--DTITKECDITn 306

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503726187 353 -VHGILVDDAPDSLAQAIRDFAARQDKGRAFADAAYIRLKTEFQ 395
Cdd:cd03812  307 nVEFLPLNETPSTWAEKILKLIKRKRRINKEINKEKKELGYDDE 350
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 201-386 5.16e-05

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: 45.05  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 201 DRVDLVYHGLDLTRFPdpPDRKARKPDAPLALMSVGRLV---------EKKGFDRLIEALALL-------------PDTL 258
Cdd:cd03818  179 DRISVIHDGVDTDRLA--PDPAARLRLLNGTELKAGDPVityvarnlePYRGFHVFMRALPRIqarrpdarvvvvgGDGV 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 259 PWHWTHIGGGTLKDQMqdLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSRiaadgdrdglPNV----LMEAASQR 334
Cdd:cd03818  257 SYGSPPPDGGSWKQKM--LAELGVDLERVHFVGKVPYDQYVRLLQLSDAHVYLTY----------PFVlswsLLEAMACG 324

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503726187 335 LPILATPVSAIPEFIDTGVHGILVD-DAPDSLAQAIRDFAARQDKGRAFADAA 386
Cdd:cd03818  325 CPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDPDRAAALRRAA 377
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 202-381 5.88e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.09  E-value: 5.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 202 RVDLVYHGLDLTRFpDPPDRKAR--------KPDAPLaLMSVGRLVEKKGFDRLIEALALLPDTlpwHWTHIGGGTLKDQ 273
Cdd:PLN02871 230 RIRVWNKGVDSESF-HPRFRSEEmrarlsggEPEKPL-IVYVGRLGAEKNLDFLKRVMERLPGA---RLAFVGDGPYREE 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 274 MQDLAAAKGVadriTWRGACDQPEVIAEMRTSDLFVLPSriaadgDRDGLPNVLMEAASQRLPILATPVSAIPEFI---D 350
Cdd:PLN02871 305 LEKMFAGTPT----VFTGMLQGDELSQAYASGDVFVMPS------ESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQ 374

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 503726187 351 TGVHGIL-----VDDAPDSLAQAIRDFAARQDKGRA 381
Cdd:PLN02871 375 EGKTGFLytpgdVDDCVEKLETLLADPELRERMGAA 410
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
319-394 3.43e-04

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 39.51  E-value: 3.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503726187  319 DRDGLPNVLMEAASQRLPILATPVSAIPEFIDTGVHGILVDDaPDSLAQAIRDFAARQDKGRAFADAAYIRLKTEF 394
Cdd:pfam13524   8 RPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRD-PEELAEKIRYLLEHPEERRAIAAAGRERVLAEH 82
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 192-347 1.42e-03

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 40.68  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 192 HLRSLADrTDRVDLVYHGLDLTRFPdpPDRKARKPDaPLALMSVGRLVEKKGFDRLIEAL----ALLPDTlpwHWTHIGG 267
Cdd:cd03796  160 VLRASLD-PRIVSVIPNAVDSSDFT--PDPSKPDPN-KITIVVISRLVYRKGIDLLVGIIpricKKHPNV---RFIIGGD 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503726187 268 GTLKDQMQDLAAAKGVADRITWRGACDQPEVIAEMRTSDLFVLPSRIAADGdrdglpNVLMEAASQRLPILATPVSAIPE 347
Cdd:cd03796  233 GPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFC------IAIVEAASCGLLVVSTRVGGIPE 306
 
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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