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Conserved domains on  [gi|663530336|gb|AIF20325|]
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putative glycosyl transferase [uncultured marine thaumarchaeote KM3_89_C12]

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 ...
 14-345 8.64e-32

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: 122.65  E-value: 8.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  14 HLKEFGENLKKKGVECklvidTSVYTGFPSKDMTKWFETKGKFNDLIKQFQPDAVFVDRQTNFGLVASKLKIpLFVHLRG 93
Cdd:cd03801   19 HVRELARALAARGHDV-----TVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDV-VHAHGLL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  94 DVWSESVMAKQ-------TLH--KSTTDRSVIWFRERIAKKCF---ENSTSILPICKYLENKVKEHF--PKNKTDVLYQG 159
Cdd:cd03801   93 AALLAALLALLlgaplvvTLHgaEPGRLLLLLAAERRLLARAEallRRADAVIAVSEALRDELRALGgiPPEKIVVIPNG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 160 IEPSNWYSQKGLNLKHP-------CVGLIQNanilEKAKE--LEVLPKVLEAFPKIMFYWVG-DGPY-KEIILSKLEKYK 228
Cdd:cd03801  173 VDLERFSPPLRRKLGIPpdrpvllFVGRLSP----RKGVDllLEALAKLLRRGPDVRLVIVGgDGPLrAELEELELGLGD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 229 NFQWMGKLEYPEkVRQFLSEIDIYALLT---GIdmsPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLI 305
Cdd:cd03801  249 RVRFLGFVPDEE-LPALYAAADVFVLPSryeGF---GLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALA 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 663530336 306 DKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd03801  325 DALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 14-345 8.64e-32

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: 122.65  E-value: 8.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  14 HLKEFGENLKKKGVECklvidTSVYTGFPSKDMTKWFETKGKFNDLIKQFQPDAVFVDRQTNFGLVASKLKIpLFVHLRG 93
Cdd:cd03801   19 HVRELARALAARGHDV-----TVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDV-VHAHGLL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  94 DVWSESVMAKQ-------TLH--KSTTDRSVIWFRERIAKKCF---ENSTSILPICKYLENKVKEHF--PKNKTDVLYQG 159
Cdd:cd03801   93 AALLAALLALLlgaplvvTLHgaEPGRLLLLLAAERRLLARAEallRRADAVIAVSEALRDELRALGgiPPEKIVVIPNG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 160 IEPSNWYSQKGLNLKHP-------CVGLIQNanilEKAKE--LEVLPKVLEAFPKIMFYWVG-DGPY-KEIILSKLEKYK 228
Cdd:cd03801  173 VDLERFSPPLRRKLGIPpdrpvllFVGRLSP----RKGVDllLEALAKLLRRGPDVRLVIVGgDGPLrAELEELELGLGD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 229 NFQWMGKLEYPEkVRQFLSEIDIYALLT---GIdmsPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLI 305
Cdd:cd03801  249 RVRFLGFVPDEE-LPALYAAADVFVLPSryeGF---GLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALA 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 663530336 306 DKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd03801  325 DALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 233-351 4.60e-28

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 105.84  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 233 MGKLEyPEK-----VRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDK 307
Cdd:COG0438    1 MGRLV-PRKgldllLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 663530336 308 ISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQIMNKYVK 351
Cdd:COG0438   80 ILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEELLA 123
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
193-314 1.32e-21

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 89.11  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  193 LEVLPKVLEAFPKIMFYWVGDGPYKEIILSKLEKYKNFQWMGKLEypeKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMK 272
Cdd:pfam13692  21 LEAVPLLRKRDNDVRLVIVGDGPEEELEELAAGLEDRVIFTGFVE---DLAELLAAADVFVLPSLYEGFGLKLLEAMAAG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 663530336  273 KPVVATNVGGIPELIkNNVTGFLIEKGNSLDLIDKISVLVDD 314
Cdd:pfam13692  98 LPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 191-341 1.10e-14

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 74.75  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 191 KELEVLPKVLEAFPKIMFYWVGDGPYKEiilsKLEKY---KNFQWMGKLEyPEKVRQFLSEIDIYALLTGIDMSPLTLLE 267
Cdd:PLN02871 276 KNLDFLKRVMERLPGARLAFVGDGPYRE----ELEKMfagTPTVFTGMLQ-GDELSQAYASGDVFVMPSESETLGFVVLE 350

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530336 268 AQLMKKPVVATNVGGIPELI---KNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKnFSWEIITEK 341
Cdd:PLN02871 351 AMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEK-WDWRAATRK 426
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 14-345 8.64e-32

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: 122.65  E-value: 8.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  14 HLKEFGENLKKKGVECklvidTSVYTGFPSKDMTKWFETKGKFNDLIKQFQPDAVFVDRQTNFGLVASKLKIpLFVHLRG 93
Cdd:cd03801   19 HVRELARALAARGHDV-----TVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDV-VHAHGLL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  94 DVWSESVMAKQ-------TLH--KSTTDRSVIWFRERIAKKCF---ENSTSILPICKYLENKVKEHF--PKNKTDVLYQG 159
Cdd:cd03801   93 AALLAALLALLlgaplvvTLHgaEPGRLLLLLAAERRLLARAEallRRADAVIAVSEALRDELRALGgiPPEKIVVIPNG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 160 IEPSNWYSQKGLNLKHP-------CVGLIQNanilEKAKE--LEVLPKVLEAFPKIMFYWVG-DGPY-KEIILSKLEKYK 228
Cdd:cd03801  173 VDLERFSPPLRRKLGIPpdrpvllFVGRLSP----RKGVDllLEALAKLLRRGPDVRLVIVGgDGPLrAELEELELGLGD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 229 NFQWMGKLEYPEkVRQFLSEIDIYALLT---GIdmsPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLI 305
Cdd:cd03801  249 RVRFLGFVPDEE-LPALYAAADVFVLPSryeGF---GLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALA 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 663530336 306 DKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd03801  325 DALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 22-343 1.16e-30

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: 119.24  E-value: 1.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  22 LKKKGVECkLVIDTSVYTGFPSKDMTKWFetkgKFNDLIKQFQPDAVFvdrqTNF-------GLVASKLKIPLFVH-LRG 93
Cdd:cd03808   44 LKELGVKV-IDIPILRRGINPLKDLKALF----KLYKLLKKEKPDIVH----CHTpkpgilgRLAARLAGVPKVIYtVHG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  94 dvwsesvmakqtLHKSTTDRSVIWF----RERIAKKCfenSTSILPICKYLENK-VKEHFPKNKTDVLYQGIEPS---NW 165
Cdd:cd03808  115 ------------LGFVFTEGKLLRLlyllLEKLALLF---TDKVIFVNEDDRDLaIKKGIIKKKKTVLIPGSGVDldrFQ 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 166 YSQKGLNLKHPCVGLIqnANILeKAKELEVLpkvLEAF-------PKIMFYWVGDG---PYKEIILSKLEKYKNFQWMGk 235
Cdd:cd03808  180 YSPESLPSEKVVFLFV--ARLL-KDKGIDEL---IEAAkilkkkgPNVRFLLVGDGeleNPSEILIEKLGLEGRIEFLG- 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 236 leYPEKVRQFLSEIDIYALLT---GIdmsPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLV 312
Cdd:cd03808  253 --FRSDVPELLAESDVFVLPSyreGL---PRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLI 327

                        330       340       350
                 ....*....|....*....|....*....|.
gi 663530336 313 DDKIKREGMGEEGKKFVEKNFSWEIITEKFL 343
Cdd:cd03808  328 EDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 233-351 4.60e-28

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 105.84  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 233 MGKLEyPEK-----VRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDK 307
Cdd:COG0438    1 MGRLV-PRKgldllLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 663530336 308 ISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQIMNKYVK 351
Cdd:COG0438   80 ILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEELLA 123
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 59-343 6.08e-28

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: 112.44  E-value: 6.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  59 LIKQFQPDAVFVDRQTNF----GLVASKL-KIPLFVHLRgDVWSESVMAKQTLHKSttdrSVIWFRERIAKKCFENSTSI 133
Cdd:cd03794   93 LVREERPDVIIAYSPPITlglaALLLKKLrGAPFILDVR-DLWPESLIALGVLKKG----SLLKLLKKLERKLYRLADAI 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 134 LPICKYLENKVKEH-FPKNKTDVLYQGIEPSNWYSQKGLNL--KHPC-----------VGLIQN-ANILEKAKELEVLPK 198
Cdd:cd03794  168 IVLSPGLKEYLLRKgVPKEKIIVIPNWADLEEFKPPPKDELrkKLGLddkfvvvyagnIGKAQGlETLLEAAERLKRRPD 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 199 vleafpkIMFYWVGDGPYKEII--LSKLEKYKNFQWMGKLEYpEKVRQFLSEIDIyALLTGID------MSPLTLLEAQL 270
Cdd:cd03794  248 -------IRFLFVGDGDEKERLkeLAKARGLDNVTFLGRVPK-EEVPELLSAADV-GLVPLKDnpanrgSSPSKLFEYMA 318

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663530336 271 MKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFL 343
Cdd:cd03794  319 AGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 59-345 2.05e-23

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: 99.31  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  59 LIKQFQPDAV--FVDRQTNFGLVASKL--KIPLFVHLRgdvwsesvmakQTLHKSTTDRSVIWFRERIAKkcfensTSIL 134
Cdd:cd03807   74 LIRKRNPDVVhtWMYHADLIGGLAAKLagGVKVIWSVR-----------SSNIPQRLTRLVRKLCLLLSK------FSPA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 135 PICkyLENKVKE-----HFPKNKTDVLYQGIEPSNW-YSQKGLNLKHPCVGLIQNANI------LEKAKE----LEVLPK 198
Cdd:cd03807  137 TVA--NSSAVAEfhqeqGYAKNKIVVIYNGIDLFKLsPDDASRARARRRLGLAEDRRVigivgrLHPVKDhsdlLRAAAL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 199 VLEAFPKIMFYWVGDGPYKEIILSKLEKYKNFQWMGKLEYPEKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVAT 278
Cdd:cd03807  215 LVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVAT 294

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530336 279 NVGGIPELIkNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd03807  295 DVGGAAELV-DDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETL 360
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
193-314 1.32e-21

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 89.11  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  193 LEVLPKVLEAFPKIMFYWVGDGPYKEIILSKLEKYKNFQWMGKLEypeKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMK 272
Cdd:pfam13692  21 LEAVPLLRKRDNDVRLVIVGDGPEEELEELAAGLEDRVIFTGFVE---DLAELLAAADVFVLPSLYEGFGLKLLEAMAAG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 663530336  273 KPVVATNVGGIPELIkNNVTGFLIEKGNSLDLIDKISVLVDD 314
Cdd:pfam13692  98 LPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 193-328 2.16e-20

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: 86.56  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  193 LEVLPKVLEAFPKIMFYWVGDGPYKEIILSKLEKY---KNFQWMGKLEYPEkVRQFLSEIDIYALLTGIDMSPLTLLEAQ 269
Cdd:pfam00534  21 IKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLglgDNVIFLGFVSDED-LPELLKIADVFVLPSRYEGFGIVLLEAM 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 663530336  270 LMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKF 328
Cdd:pfam00534 100 ACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 8-345 3.43e-20

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


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 90.52  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336   8 SPEKFFHLKEFgeNLKKKGVECKLVIDTSVYTGFPSKDMTKWFETKGKFNDLIKQF---QPDAVFVDRQTNFGLVASKLK 84
Cdd:cd03798   38 APAPWGPAAAR--LLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKRRrrgPPDLIHAHFAYPAGFAAALLA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  85 iplfvhlrgdvWSESVMAKQTLHKSttDRSVI----WFReRIAKKCFENSTSILPICKYLENKVKEH-FPKNKTDVLYQG 159
Cdd:cd03798  116 -----------RLYGVPYVVTEHGS--DINVFpprsLLR-KLLRWALRRAARVIAVSKALAEELVALgVPRDRVDVIPNG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 160 IEPSNWY---SQKGLNLKHPCVGLIQNaniLEKAKELEVLpkvLEAF-------PKIMFYWVGDGP---YKEIILSKLEK 226
Cdd:cd03798  182 VDPARFQpedRGLGLPLDAFVILFVGR---LIPRKGIDLL---LEAFarlakarPDVVLLIVGDGPlreALRALAEDLGL 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 227 YKNFQWMGKLEYpEKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLID 306
Cdd:cd03798  256 GDRVTFTGRLPH-EQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAA 334

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 663530336 307 KISVLVDDKIKREgMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd03798  335 ALRRALAEPYLRE-LGEAARARVAERFSWVKAADRIAAA 372
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 127-333 3.02e-18

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: 84.42  E-value: 3.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 127 FENSTSILPICKYLENK-VKEHFPKNKTDVLYQGIEPSNWYSQKGLNLKHPCVGLIQNANILEKaKELEV----LPKVLE 201
Cdd:cd03799  123 FAQGDLFLPNCELFKHRlIALGCDEKKIIVHRSGIDCNKFRFKPRYLPLDGKIRILTVGRLTEK-KGLEYaieaVAKLAQ 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 202 AFPKIMFYWVGDGPYKEII---LSKLEKYKNFQWMGKLEYPEKVRqFLSEIDIYaLLTGI-------DMSPLTLLEAQLM 271
Cdd:cd03799  202 KYPNIEYQIIGDGDLKEQLqqlIQELNIGDCVKLLGWKPQEEIIE-ILDEADIF-IAPSVtaadgdqDGPPNTLKEAMAM 279

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663530336 272 KKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNF 333
Cdd:cd03799  280 GLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEY 341
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 128-345 8.56e-17

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: 80.47  E-value: 8.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 128 ENSTSILPICKYLENKVKEHFPKNK-TDVLYQGIEPSNWYSQKGLNLK-----HPCVGLIQNANILEKAKE----LEVLP 197
Cdd:cd04962  140 NKSDRVTAVSSSLRQETYELFDVDKdIEVIHNFIDEDVFKRKPAGALKrrllaPPDEKVVIHVSNFRPVKRiddvVRVFA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 198 KVLEAFP-KIMFywVGDGPYKEIILSKLEKY---KNFQWMGKLEypeKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMKK 273
Cdd:cd04962  220 RVRRKIPaKLLL--VGDGPERVPAEELARELgveDRVLFLGKQD---DVEELLSIADLFLLPSEKESFGLAALEAMACGV 294

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663530336 274 PVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDK-ISVLVDDKIKREgMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd04962  295 PVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSaLSILEDDELYNR-MGRAARKRAAERFDPERIVPQYEAY 366
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 55-319 1.39e-15

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 76.63  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  55 KFNDLIKQFQPDAVFV--DRQTNFGLVASKLKIPLFVHLRGDVWSESVMakqtlhksttdrsviWFRERIAKKCFENSTS 132
Cdd:cd03811   74 KLKRILKRAKPDVVISflGFATYIVAKLAAARSKVIAWIHSSLSKLYYL---------------KKKLLLKLKLYKKADK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 133 ILPICKYLENKVKEHFP--KNKTDVLYQGIEPSNwysQKGLNLKHPCVGLIQNANI-----LEKAKELEVLPKVLEAFPK 205
Cdd:cd03811  139 IVCVSKGIKEDLIRLGPspPEKIEVIYNPIDIDR---IRALAKEPILNEPEDGPVIlavgrLDPQKGHDLLIEAFAKLRK 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 206 IM----FYWVGDGPYKEiilsKLEKYKNfqwmgKLEYPEKVRqFLSEI-DIYALLTGIDM---------SPLTLLEAQLM 271
Cdd:cd03811  216 KYpdvkLVILGDGPLRE----ELEKLAK-----ELGLAERVI-FLGFQsNPYPYLKKADLfvlssryegFPNVLLEAMAL 285

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663530336 272 KKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKRE 319
Cdd:cd03811  286 GTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAA 333
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 233-345 2.70e-15

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


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 76.22  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 233 MGKLEYPEKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLV 312
Cdd:cd03825  248 LGYIDDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLL 327

                         90       100       110
                 ....*....|....*....|....*....|...
gi 663530336 313 DDKIKREGMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd03825  328 ANPKERESLGERARALAENHFDQRVQAQRYLEL 360
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 191-341 1.10e-14

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 74.75  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 191 KELEVLPKVLEAFPKIMFYWVGDGPYKEiilsKLEKY---KNFQWMGKLEyPEKVRQFLSEIDIYALLTGIDMSPLTLLE 267
Cdd:PLN02871 276 KNLDFLKRVMERLPGARLAFVGDGPYRE----ELEKMfagTPTVFTGMLQ-GDELSQAYASGDVFVMPSESETLGFVVLE 350

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530336 268 AQLMKKPVVATNVGGIPELI---KNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKnFSWEIITEK 341
Cdd:PLN02871 351 AMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEK-WDWRAATRK 426
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 193-296 4.86e-14

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: 70.90  E-value: 4.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 193 LEVLPKVLEAFPKIMFYWVGDGP---YKEIILSKLEKYKNFQWMGKLEYPEKVRQFLSEIDIYALLTGIDMSPLTLLEAQ 269
Cdd:cd01635  129 LEALALLKARLPDLVLVLVGGGGereEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAM 208

                         90       100
                 ....*....|....*....|....*..
gi 663530336 270 LMKKPVVATNVGGIPELIKNNVTGFLI 296
Cdd:cd01635  209 AAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 46-345 9.88e-14

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: 71.21  E-value: 9.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  46 MTKWFETKGKFNDLIKQFQPDAVFVDRQTNFGL----VASKLKIPLFVHLRgDVWSESvmAKQTLHKSTTDRsviwfreR 121
Cdd:cd03823   78 ETYNPGLRRLLARLLEDFRPDVVHTHNLSGLGAslldAARDLGIPVVHTLH-DYWLLC--PRQFLFKKGGDA-------V 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 122 IAkkcfeNStsilpicKYLENKVKEH--FPKNKTdVLYQGIEPSN-WYSQKGLNLKHPCVGLIqnaNILEKAKELEVLpk 198
Cdd:cd03823  148 LA-----PS-------RFTANLHEANglFSARIS-VIPNAVEPDLaPPPRRRPGTERLRFGYI---GRLTEEKGIDLL-- 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 199 vLEAF-----PKIMFYWVGDGPYKEIILSKLEKYKNFqwMGKLEYpEKVRQFLSEIDIyALLTGI--DMSPLTLLEAQLM 271
Cdd:cd03823  210 -VEAFkrlprEDIELVIAGHGPLSDERQIEGGRRIAF--LGRVPT-DDIKDFYEKIDV-LVVPSIwpEPFGLVVREAIAA 284

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663530336 272 KKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDkikrEGMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:cd03823  285 GLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTD----PALLERLRAGAEPPRSTESQAEEYLKL 354
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 263-344 2.80e-13

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: 70.35  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 263 LTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKF 342
Cdd:cd03800  317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQL 396


                 ..
gi 663530336 343 LQ 344
Cdd:cd03800  397 LT 398
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 193-342 6.72e-13

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


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 68.80  E-value: 6.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 193 LEVLPKVLEAFPKIMFYWVGDGPYKEIILSKLEKYknfQWMGKLEYP---EKVRQFLSEIDIYALLTGIDMSPLTLLEAQ 269
Cdd:cd03820  200 IEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKL---GLEDRVKLLgptKNIAEEYANSSIFVLSSRYEGFPMVLLEAM 276

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663530336 270 LMKKPVVATN-VGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKnFSWEIITEKF 342
Cdd:cd03820  277 AYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAER-FSIEKIIKQW 349
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 58-342 6.27e-12

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: 66.15  E-value: 6.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  58 DLIKQFQPDAVFVdrQTNFGL------VASKLKIPlFVHlrgdvwsesvmakqTLHKSTTD---------RSVIWFRERI 122
Cdd:cd03817   78 DRIKELGPDIIHT--HTPFSLgklglrIARKLKIP-IVH--------------TYHTMYEDylhyipkgkLLVKAVVRKL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 123 AKKcFENSTSILpIC--KYLENKVKEHFPKNKTDVLYQGIEPSNWYS--QKGLNLKHpcvGLIQNANIL--------EKA 190
Cdd:cd03817  141 VRR-FYNHTDAV-IApsEKIKDTLREYGVKGPIEVIPNGIDLDKFEKplNTEERRKL---GLPPDEPILlyvgrlakEKN 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 191 KE--LEVLPKVLEAfPKIMFYWVGDGPYKE-----IILSKLEKYKNFqwMGKLEYpEKVRQFLSEIDIYALLTGIDMSPL 263
Cdd:cd03817  216 IDflLRAFAELKKE-PNIKLVIVGDGPEREelkelARELGLADKVIF--TGFVPR-EELPEYYKAADLFVFASTTETQGL 291

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663530336 264 TLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNsldlidkisVLVDDKIKREGMGEEGKKFVEKNFswEIITEKF 342
Cdd:cd03817  292 VYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPND---------ETLAEKLLHLRENLELLRKLSKNA--EISAREF 359
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 266-342 7.26e-12

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 66.07  E-value: 7.26e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530336 266 LEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKgNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKF 342
Cdd:cd03805  317 LEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 116-342 1.27e-11

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: 65.43  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 116 IWFRERIAKKCFENSTSILPICKYLEN-KVKEHFPKNKTDVLYQGIEPSNWysqKGLNLKHPC-----VGLIQNaniLEK 189
Cdd:cd03813  231 IRFFERLGKLAYQQADKIISLYEGNRRrQIRLGADPDKTRVIPNGIDIQRF---APAREERPEkeppvVGLVGR---VVP 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 190 AKELEVLPK----VLEAFPKIMFYWVG----DGPY----KEIILSkLEKYKNFQWMGkleyPEKVRQFLSEIDIYALLTG 257
Cdd:cd03813  305 IKDVKTFIRafklVRRAMPDAEGWLIGpedeDPEYaqecKRLVAS-LGLENKVKFLG----FQNIKEYYPKLGLLVLTSI 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 258 IDMSPLTLLEAQLMKKPVVATNVGGIPELI-----KNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKN 332
Cdd:cd03813  380 SEGQPLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459

                        250
                 ....*....|
gi 663530336 333 FSWEIITEKF 342
Cdd:cd03813  460 YTLEGMIDSY 469
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 142-323 2.49e-11

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: 63.91  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 142 NKVKEH------FPKNKTDVLYQGIEPSN--------WYSQKGLNLKHPCVGLIQNaniLEKAKELEVLPKVLEAFPKIM 207
Cdd:cd03819  135 ELVRDHliealgVDPERIRVIPNGVDTDRfppeaeaeERAQLGLPEGKPVVGYVGR---LSPEKGWLLLVDAAAELKDEP 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 208 ---FYWVGDGPYKEIILSKLEKYKNFQWMGKLEYPEKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVATNVGGIP 284
Cdd:cd03819  212 dfrLLVAGDGPERDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAR 291

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 663530336 285 ELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGE 323
Cdd:cd03819  292 EIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQA 330
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 193-341 3.22e-11

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: 63.47  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 193 LEVLPKVLEAFPKIMFYWVGDGPYKEIILSKLEKYKnfqwmgkLEYPEKVRQFLSEIDI-----YALLTGIDMS--PLTL 265
Cdd:cd04949  179 IEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELH-------LEDNVFLKGYHSNLDQeyqdaYLSLLTSQMEgfGLTL 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530336 266 LEAQLMKKPVVATNVG-GIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKnFSWEIITEK 341
Cdd:cd04949  252 MEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEK-YSTENVMEK 327
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
128-349 3.99e-11

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 63.66  E-value: 3.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 128 ENSTSILPiCKYLENKVKEHFPKNKTDVLYQGIEPSNWYSQKGLNLKhpcvgliQNANILEKAKEL----EVLPK----- 198
Cdd:PRK15484 139 KNAKIIVP-SQFLKKFYEERLPNADISIVPNGFCLETYQSNPQPNLR-------QQLNISPDETVLlyagRISPDkgill 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 199 VLEAFPK-------IMFYWVGD---------GPYKEIILSKLEKYKNFQWMGKLEYPEKVRQFLSEIDIYALLTGIDMS- 261
Cdd:PRK15484 211 LMQAFEKlatahsnLKLVVVGDptasskgekAAYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAf 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 262 PLTLLEAQLMKKPVVATNVGGIPELIKNNVTGF-LIEKGNSLDLIDKISVLVDDKiKREGMGEEGKKFVEKNFSWEIITE 340
Cdd:PRK15484 291 CMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADP-ELTQIAEQAKDFVFSKYSWEGVTQ 369


                 ....*....
gi 663530336 341 KFLQIMNKY 349
Cdd:PRK15484 370 RFEEQIHNW 378
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 145-348 2.73e-10

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: 60.92  E-value: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 145 KEHFPKNKTDVLYQGIEPS--NWYSQKGLNLKHPC-----VGLIQNANILEKAKE----LEVLPKVLEAFPKIMFYWVGD 213
Cdd:cd04951  148 KKAFSKNKSVPVYNGIDLNkfKKDINVRLKIRNKLnlkndEFVILNVGRLTEAKDypnlLLAISELILSKNDFKLLIAGD 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 214 GPYKEIILSKLEKYKNFQWMGKLEYPEKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVATNVGGIPELIKNnvTG 293
Cdd:cd04951  228 GPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HN 305

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663530336 294 FLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQIMNK 348
Cdd:cd04951  306 YVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLYSG 360
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 193-345 3.07e-10

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 61.59  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 193 LEVLPKVLEAFPKIMFYWVGDGPYKEIILSKLEKYKNFQWMGKLEYPEKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMK 272
Cdd:PRK15179 536 VEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSG 615

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663530336 273 KPVVATNVGGIPELIKNNVTGFLIEKGN--SLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQI 345
Cdd:PRK15179 616 VPVVTTLAGGAGEAVQEGVTGLTLPADTvtAPDVAEALARIHDMCAADPGIARKAADWASARFSLNQMIASTVRC 690
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 148-341 4.77e-10

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: 60.16  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 148 FPKNKTDVLYQGIEPSNWysqkglnlkHP-CVG----LIQNANILEKAKELEVLpkvLEAF-------PKIMFYWVGDGP 215
Cdd:cd05844  163 LPAERIHVHYIGIDPAKF---------APrDPAerapTILFVGRLVEKKGCDVL---IEAFrrlaarhPTARLVIAGDGP 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 216 YKEIILSKLEKYKNFQWMGKLEYPEkVRQFLSEIDIYALLTGIDMS------PLTLLEAQLMKKPVVATNVGGIPELIKN 289
Cdd:cd05844  231 LRPALQALAAALGRVRFLGALPHAE-VQDWMRRAEIFCLPSVTAASgdseglGIVLLEAAACGVPVVSSRHGGIPEAILD 309

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663530336 290 NVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEK 341
Cdd:cd05844  310 GETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAK 361
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 150-337 6.58e-10

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: 59.60  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 150 KNKTDVLYQGIEPS--NWYSQKGLNLKHPCVG--LIQNANILEKAKELEVLpkvLEAFPKIMFYWV--GDGPYKEIILSK 223
Cdd:cd03795  159 KNKVRVIPLGIDKNvyNIPRVDFENIKREKKGkkIFLFIGRLVYYKGLDYL---IEAAQYLNYPIVigGEGPLKPDLEAQ 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 224 LE--KYKNFQWMGKLEYPEKVrQFLSEIDIYAL--LTGIDMSPLTLLEAQLMKKPVVATNVG-GIPELIKNNVTGFLIEK 298
Cdd:cd03795  236 IElnLLDNVKFLGRVDDEEKV-IYLHLCDVFVFpsVLRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPP 314

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 663530336 299 GNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEI 337
Cdd:cd03795  315 KDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEK 353
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 193-344 6.88e-10

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: 59.78  E-value: 6.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 193 LEVLPKVLEAFPKIMFYW--VGDGPYKEII---LSKLEKYKNFQWMGKLEYPEkVRQFLSE--IDIYALLTGIDMSPLTL 265
Cdd:cd04946  243 IETLNSLCVAHPSICISWthIGGGPLKERLeklAENKLENVKVNFTGEVSNKE-VKQLYKEndVDVFVNVSESEGIPVSI 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 266 LEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSL-DLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEKFLQ 344
Cdd:cd04946  322 MEAISFGIPVIATNVGGTREIVENETNGLLLDKDPTPnEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYSKFAN 401
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 191-346 4.75e-09

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: 57.30  E-value: 4.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 191 KELEVLPKV---LEAFPKIMFYWVGDGPYKEiilsKLE-KYKNFQWMGKLEYPEkvrqfLSEIdiYALLtgiDM----SP 262
Cdd:cd03814  211 KNLEALLDAdlpLAASPPVRLVVVGDGPARA----ELEaRGPDVIFTGFLTGEE-----LARA--YASA---DVfvfpSR 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 263 -----LTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKnFSWEI 337
Cdd:cd03814  277 tetfgLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER-YSWEA 355


                 ....*....
gi 663530336 338 ITEKFLQIM 346
Cdd:cd03814  356 FLDNLLDYY 364
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 262-333 5.55e-09

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 56.95  E-value: 5.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663530336 262 PLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKG--NSLDLIDKisvLVDDKIKREgMGEEGKKFVEKNF 333
Cdd:cd03792  293 GLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVegAAVRILRL---LTDPELRRK-MGLAAREHVRDNF 362
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 106-344 9.05e-09

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: 56.22  E-value: 9.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 106 LHKSTTDRSVIWFRERIAKKCFENSTSILPICKYLENKVKEHF--PKNKTDVLYQGIEPSNW------YSQKGLNLKHP- 176
Cdd:cd03809  115 RYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFYgvPPEKIVVIPLGVDPSFFppesaaVLIAKYLLPEPy 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 177 --CVGliqnanILEKAKELEVLpkvLEAFPKImfyWVGDGPYKEIILSKLE-KYKNFQWMGKLEYPEKVRQFLSEI---D 250
Cdd:cd03809  195 flYVG------TLEPRKNHERL---LKAFALL---KKQGGDLKLVIVGGKGwEDEELLDLVKKLGLGGRVRFLGYVsdeD 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 251 IYALLTG----IDMS-----PLTLLEAQLMKKPVVATNVGGIPELIKNNvtGFLIEKGNSLDLIDKISVLVDDKIKREGM 321
Cdd:cd03809  263 LPALYRGarafVFPSlyegfGLPVLEAMACGTPVIASNISVLPEVAGDA--ALYFDPLDPESIADAILRLLEDPSLREEL 340

                        250       260
                 ....*....|....*....|...
gi 663530336 322 GEEGKKFVeKNFSWEIITEKFLQ 344
Cdd:cd03809  341 IRKGLERA-KKFSWEKTAEKTLE 362
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 194-341 1.92e-07

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: 52.24  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 194 EVLPKVLEAFPKIMFYWVGDGPyKEIILSK-LEKYK---NFQWMGKLEyPEKVRQFLSEIDIY--ALLT---GIdmsplT 264
Cdd:cd03796  213 GIIPRICKKHPNVRFIIGGDGP-KRIELEEmREKYQlqdRVELLGAVP-HEEVRDVLVQGHIFlnTSLTeafCI-----A 285

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530336 265 LLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKgnSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEIITEK 341
Cdd:cd03796  286 IVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPD--PEDIVRKLEEAISILRTGKHDPWSFHNRVKKMYSWEDVARR 360
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
119-346 3.08e-07

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 52.01  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 119 RERIAKKCFE---NSTSILPICKYLENK--VKEHFPK------NKTDVLYQGI-----EPSN------W--YSQKGLNLK 174
Cdd:PRK15490 319 RKRLFKPEYEplyQALAVVPGVDFMSNNhcVTRHYADwlkleaKHFQVVYNGVlppstEPSSevphkiWqqFTQKTQDAD 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 175 HPCVGLIQNANILEKAKELEVLPKVLEAFPKIMFYWVGDGPYKEIILSKLEKYKNFQWMGKLEYPEKVRQFLSEIDIYAL 254
Cdd:PRK15490 399 TTIGGVFRFVGDKNPFAWIDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFIL 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 255 LTGIDMSPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISV---LVDDKIKREGMGEEGKKFVEK 331
Cdd:PRK15490 479 FSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVSGFILDDAQTVNLDQACRYaekLVNLWRSRTGICQQTQSFLQE 558

                        250
                 ....*....|....*
gi 663530336 332 NFSWEIITEKFLQIM 346
Cdd:PRK15490 559 RFTVEHMVGTFVKTI 573
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 193-334 4.86e-06

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: 48.13  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 193 LEVLPKVLEAFPKIMFYWVGD------------GPYKEIILSKLE-KYKNFQWMGKLEYPEKVRQF-LSEIDIYalLTGI 258
Cdd:cd03818  233 MRALPRIQARRPDARVVVVGGdgvsygspppdgGSWKQKMLAELGvDLERVHFVGKVPYDQYVRLLqLSDAHVY--LTYP 310

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663530336 259 DMSPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEKGNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFS 334
Cdd:cd03818  311 FVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDS 386
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 221-348 2.92e-05

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


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 45.36  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 221 LSKLEKYKNFQWMGKLEYPEKVRQFLSEIdiyALLTGIDMS-P--LTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIE 297
Cdd:cd03802  213 LQEPLPGPRIEFIGEVGHDEKQELLGGAR---ALLFPINWDePfgLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD 289

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663530336 298 -KGNSLDLIDKIsvlvdDKIKREGMgeegKKFVEKNFSWEIITEKFLQIMNK 348
Cdd:cd03802  290 sVEEMAEAIANI-----DRIDRAAC----RRYAEDRFSAARMADRYEALYRK 332
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 79-344 5.29e-05

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: 44.67  E-value: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  79 VASKLKIPLFVHLRGDV--WSESvmakqtlHKSTTDRsviWFRERIAKKCFENSTSILPICKYLENKVKEHFPKNKTDVL 156
Cdd:cd03821  110 LARRRGIPYVVSPHGMLdpWALQ-------QKHWKKR---IALHLIERRNLNNAALVHFTSEQEADELRRFGLEPPIAVI 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 157 YQGIEPSNWYSQKGLNLKHPCVG---LIQNANILEKAKELEVL----PKVLEAFPKIMFYWVG-DGPYKEIILSKLEKYk 228
Cdd:cd03821  180 PNGVDIPEFDPGLRDRRKHNGLEdrrIILFLGRIHPKKGLDLLiraaRKLAEQGRDWHLVIAGpDDGAYPAFLQLQSSL- 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 229 NFQ----WMGKLeYPEKVRQFLSEIDIYALLTGIDMSPLTLLEAQLMKKPVVATNVGGIPELIKNNvtGFLIEKGNSLDL 304
Cdd:cd03821  259 GLGdrvtFTGPL-YGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG--CGVVVDPNVSSL 335

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663530336 305 IDKISVLVDDKIKREGMGEEGKKFV--EKNFSWEIITEKFLQ 344
Cdd:cd03821  336 AEALAEALRDPADRKRLGEMARRARqvEENFSWEAVAGQLGE 377
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
 138-288 1.46e-04

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 43.13  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 138 KYLENKVK-EHFPKNKTdvlyqgiEPSNWYSQKglNLKHPCVGLIqnANILEKAkELEVLPKVLEAFPKIMFYWVGdgPY 216
Cdd:cd04950  176 HPIPNGVDvEHFAAARQ-------PLDDPIDLR--EIPGPVLGFF--GAIDEKL-DFDLIEELAKARPQWNFVFIG--PV 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663530336 217 KEIILSKLEKYKNFQWMGKLEYPEkVRQFLSEIDIyALLTGI------DMSPLTLLEAQLMKKPVVATNvggIPELIK 288
Cdd:cd04950  242 VKIDPSSLPRAPNIHWLGPKPYKE-LPAYLAGFDV-ALLPFAlneytrFISPLKLFEYLAAGKPVVATS---IPSVVR 314
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
259-344 2.61e-04

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 39.51  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336  259 DMSPLTLLEAQLMKKPVVATNVGGIPELIKNNVTGFLIEkgNSLDLIDKISVLVDDKIKREGMGEEGKKFVEKNFSWEII 338
Cdd:pfam13524  10 DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHR 87


                  ....*.
gi 663530336  339 TEKFLQ 344
Cdd:pfam13524  88 AEQLLD 93
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 211-337 6.03e-04

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


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 41.50  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530336 211 VGDGPYKEIILSKLEKykNFQWMGKL------EYPEKVRQFL--SEIDIyalltGIdmsplTLLEAQLMKKPVVATNVGG 282
Cdd:cd03804  231 IGDGPDLDRLRAMASP--NVEFLGYQpdevlkELLSKARAFVfaAEEDF-----GI-----VPVEAQACGTPVIAFGKGG 298

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663530336 283 IPELIKNNVTGFLIEKGNSLDLIDKIS--VLVDDKIKREGMGEEGKKFVEKNFSWEI 337
Cdd:cd03804  299 ALETVRPGPTGILFGEQTVESLKAAVEefEQNFDRFKPQAIRANAERFSRARFRQEI 355
 
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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