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Conserved domains on  [gi|1267305034|ref|WP_098152966|]
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glycosyltransferase [Bacillus wiedmannii]

Protein Classification

glycosyltransferase; glycosyltransferase family 4 protein( domain architecture ID 10133480)

bifunctional glycosyltransferase containing N-terminal family 2 and C-terminal family 4 glycosyltransferase domains, catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds| glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

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 ...
6-362 1.66e-30

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: 123.42  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034   6 KIIYVSHDAHFH--GAQLLSLHTIKALKENfHYSVAIISIGTGILIHDFQKYGPVYCLEEDYPTEKRVELLIKKL----L 79
Cdd:cd03801     1 KILLLSPELPPPvgGAERHVRELARALAAR-GHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELrpllR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034  80 SQDYTFAICSTVISGDIVTLLAK-HNIKVISLIHELPHLIQQYSAEGKARNIAQFAY------KIVFPSQYVYEKFRTIT 152
Cdd:cd03801    80 LRKFDVVHAHGLLAALLAALLALlLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEAllrradAVIAVSEALRDELRALG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 153 QLDHQKCHILPQGLfnhnpyknNIAKARSELRKKHNLPLDSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVGR 232
Cdd:cd03801   160 GIPPEKIVVIPNGV--------DLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 233 TD------VHFFNTLSPRytAHFTLVEPTPDI-GLYNAgADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVT 305
Cdd:cd03801   232 DGplraelEELELGLGDR--VRFLGFVPDEELpALYAA-ADVFVLPSRYEGFGLVVLEAMAAGLPVVAT-DVGGLPEVVE 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 306 EQTGALVDFLNLPQVL-ERIYEFIGDEDLRLQKGRFGQELIEKDFNFLHYIYQLLNLL 362
Cdd:cd03801   308 DGEGGLVVPPDDVEALaDALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
370-597 1.26e-26

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd04196:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 214  Bit Score: 108.10  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 370 SVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLSNENKPHLKvqqIINDKNSGSVfKQWIKGVS 449
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIIL---IRNGKNLGVA-RNFESLLQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 450 AATGDYIWIAEADDLCDQTFLEEVIQGFHINGDVTLSYTQSKQIDEQGNILANHYLDYTNDidkgkwkssyfrkGIDEIQ 529
Cdd:cd04196    77 AADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGESFFEYQKI-------------KPGTSF 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 530 DTLLIKNTIPNvSSVVFKNIDIKSTEKQLEKFKVAGDWFFYVSILKEGNIYFNPKPLNYHRRHTNSVT 597
Cdd:cd04196   144 NNLLFQNVVTG-CTMAFNRELLELALPFPDADVIMHDWWLALLASAFGKVVFLDEPLILYRQHGNNVV 210
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
6-362 1.66e-30

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: 123.42  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034   6 KIIYVSHDAHFH--GAQLLSLHTIKALKENfHYSVAIISIGTGILIHDFQKYGPVYCLEEDYPTEKRVELLIKKL----L 79
Cdd:cd03801     1 KILLLSPELPPPvgGAERHVRELARALAAR-GHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELrpllR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034  80 SQDYTFAICSTVISGDIVTLLAK-HNIKVISLIHELPHLIQQYSAEGKARNIAQFAY------KIVFPSQYVYEKFRTIT 152
Cdd:cd03801    80 LRKFDVVHAHGLLAALLAALLALlLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEAllrradAVIAVSEALRDELRALG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 153 QLDHQKCHILPQGLfnhnpyknNIAKARSELRKKHNLPLDSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVGR 232
Cdd:cd03801   160 GIPPEKIVVIPNGV--------DLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 233 TD------VHFFNTLSPRytAHFTLVEPTPDI-GLYNAgADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVT 305
Cdd:cd03801   232 DGplraelEELELGLGDR--VRFLGFVPDEELpALYAA-ADVFVLPSRYEGFGLVVLEAMAAGLPVVAT-DVGGLPEVVE 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 306 EQTGALVDFLNLPQVL-ERIYEFIGDEDLRLQKGRFGQELIEKDFNFLHYIYQLLNLL 362
Cdd:cd03801   308 DGEGGLVVPPDDVEALaDALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
370-597 1.26e-26

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 108.10  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 370 SVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLSNENKPHLKvqqIINDKNSGSVfKQWIKGVS 449
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIIL---IRNGKNLGVA-RNFESLLQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 450 AATGDYIWIAEADDLCDQTFLEEVIQGFHINGDVTLSYTQSKQIDEQGNILANHYLDYTNDidkgkwkssyfrkGIDEIQ 529
Cdd:cd04196    77 AADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGESFFEYQKI-------------KPGTSF 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 530 DTLLIKNTIPNvSSVVFKNIDIKSTEKQLEKFKVAGDWFFYVSILKEGNIYFNPKPLNYHRRHTNSVT 597
Cdd:cd04196   144 NNLLFQNVVTG-CTMAFNRELLELALPFPDADVIMHDWWLALLASAFGKVVFLDEPLILYRQHGNNVV 210
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
368-522 7.14e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 105.55  E-value: 7.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsNENKPHLKVqqIINDKNSGsVFKQWIKG 447
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILREL--AAKDPRIRV--IRLERNRG-KGAARNAG 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267305034 448 VSAATGDYIWIAEADDLCDQTFLEEVIQGFHING-DVTLSYTQSKQIDEQGNILANHYLDYTNDIDKGKWKSSYFR 522
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPaDLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFR 153
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
370-475 2.85e-24

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 99.78  E-value: 2.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 370 SVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLsnENKPHLKVqqIINDKNSGsVFKQWIKGVS 449
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYA--KKDPRVRV--IRLPENRG-KAGARNAGLR 75
                          90       100
                  ....*....|....*....|....*.
gi 1267305034 450 AATGDYIWIAEADDLCDQTFLEEVIQ 475
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVE 101
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
263-363 3.47e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 75.03  E-value: 3.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 263 AGADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVTE-QTGALVDFLNLPQVLERIYEFIGDEDLRLQKGRFG 341
Cdd:COG0438    19 AAADVFVLPSRSEGFGLVLLEAMAAGLPVIAT-DVGGLPEVIEDgETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAA 97
                          90       100
                  ....*....|....*....|..
gi 1267305034 342 QELIEKDFNFLHYIYQLLNLLD 363
Cdd:COG0438    98 RERAEERFSWEAIAERLLALYE 119
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
194-330 2.36e-15

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 73.31  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 194 KIILGVG-FADHRKGIDLFSLIAYSVRKVHTNIHFIWVGRTDVHFFNTLSPRYTAHFTLVEPTPDIGLYNAGADLYLLTS 272
Cdd:pfam13692   2 PVILFVGrLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAGLEDRVIFTGFVEDLAELLAAADVFVLPS 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 273 REDPFPNVVLEALDTKVPVIGFkNAGGFEDVVTEQTGALVDFLNLPQVLERIYEFIGD 330
Cdd:pfam13692  82 LYEGFGLKLLEAMAAGLPVVAT-DVGGIPELVDGENGLLVPPGDPEALAEAILRLLED 138
PRK10073 PRK10073
putative glycosyl transferase; Provisional
368-464 1.04e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 72.77  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsNENKPHLkvqQIINDKNSG-SVFKQwiK 446
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHY--AENYPHV---RLLHQANAGvSVARN--T 79
                          90
                  ....*....|....*...
gi 1267305034 447 GVSAATGDYIWIAEADDL 464
Cdd:PRK10073   80 GLAVATGKYVAFPDADDV 97
PHA01630 PHA01630
putative group 1 glycosyl transferase
132-321 1.99e-08

putative group 1 glycosyl transferase


Pssm-ID: 164861  Cd Length: 331  Bit Score: 56.33  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 132 QFAYKIVFPSQYVYEKFRTITQLDHQKCHILPQglfNHNPyknniaKARSELRKKHNLPLdskIILGVGFADHRKGIDLF 211
Cdd:PHA01630   93 QPVDEIVVPSQWSKNAFYTSGLKIPQPIYVIPH---NLNP------RMFEYKPKEKPHPC---VLAILPHSWDRKGGDIV 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 212 SLIAYSVRKVHTNIHFIwvgrtdVHFFNTLSPRYTAHFTLVEPTPDIGLYN--AGADLYLLTSREDPFPNVVLEALDTKV 289
Cdd:PHA01630  161 VKIFHELQNEGYDFYFL------IKSSNMLDPRLFGLNGVKTPLPDDDIYSlfAGCDILFYPVRGGAFEIPVIEALALGL 234
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1267305034 290 PVIGFKNAGGFEDVVTEQTGALVDFLNLPQVL 321
Cdd:PHA01630  235 DVVVTEKGAWSEWVLSNLDVYWIKSGRKPKLW 266
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
6-362 1.66e-30

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: 123.42  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034   6 KIIYVSHDAHFH--GAQLLSLHTIKALKENfHYSVAIISIGTGILIHDFQKYGPVYCLEEDYPTEKRVELLIKKL----L 79
Cdd:cd03801     1 KILLLSPELPPPvgGAERHVRELARALAAR-GHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELrpllR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034  80 SQDYTFAICSTVISGDIVTLLAK-HNIKVISLIHELPHLIQQYSAEGKARNIAQFAY------KIVFPSQYVYEKFRTIT 152
Cdd:cd03801    80 LRKFDVVHAHGLLAALLAALLALlLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEAllrradAVIAVSEALRDELRALG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 153 QLDHQKCHILPQGLfnhnpyknNIAKARSELRKKHNLPLDSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVGR 232
Cdd:cd03801   160 GIPPEKIVVIPNGV--------DLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 233 TD------VHFFNTLSPRytAHFTLVEPTPDI-GLYNAgADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVT 305
Cdd:cd03801   232 DGplraelEELELGLGDR--VRFLGFVPDEELpALYAA-ADVFVLPSRYEGFGLVVLEAMAAGLPVVAT-DVGGLPEVVE 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 306 EQTGALVDFLNLPQVL-ERIYEFIGDEDLRLQKGRFGQELIEKDFNFLHYIYQLLNLL 362
Cdd:cd03801   308 DGEGGLVVPPDDVEALaDALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
370-597 1.26e-26

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 108.10  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 370 SVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLSNENKPHLKvqqIINDKNSGSVfKQWIKGVS 449
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIIL---IRNGKNLGVA-RNFESLLQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 450 AATGDYIWIAEADDLCDQTFLEEVIQGFHINGDVTLSYTQSKQIDEQGNILANHYLDYTNDidkgkwkssyfrkGIDEIQ 529
Cdd:cd04196    77 AADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGESFFEYQKI-------------KPGTSF 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 530 DTLLIKNTIPNvSSVVFKNIDIKSTEKQLEKFKVAGDWFFYVSILKEGNIYFNPKPLNYHRRHTNSVT 597
Cdd:cd04196   144 NNLLFQNVVTG-CTMAFNRELLELALPFPDADVIMHDWWLALLASAFGKVVFLDEPLILYRQHGNNVV 210
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
368-522 7.14e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 105.55  E-value: 7.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsNENKPHLKVqqIINDKNSGsVFKQWIKG 447
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILREL--AAKDPRIRV--IRLERNRG-KGAARNAG 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267305034 448 VSAATGDYIWIAEADDLCDQTFLEEVIQGFHING-DVTLSYTQSKQIDEQGNILANHYLDYTNDIDKGKWKSSYFR 522
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPaDLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFR 153
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
370-475 2.85e-24

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 99.78  E-value: 2.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 370 SVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLsnENKPHLKVqqIINDKNSGsVFKQWIKGVS 449
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYA--KKDPRVRV--IRLPENRG-KAGARNAGLR 75
                          90       100
                  ....*....|....*....|....*.
gi 1267305034 450 AATGDYIWIAEADDLCDQTFLEEVIQ 475
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVE 101
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
371-490 1.05e-21

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 92.18  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLSNENKPHLkvqqIINDKNSGsVFKQWIKGVSA 450
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIR----VINEENQG-LAAARNAGLKA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1267305034 451 ATGDYIWIAEADDLCDQTFLEEVIQGFHINGDVTLSYTQS 490
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPG 115
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
118-369 1.96e-21

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: 96.25  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 118 IQQYSAEGKARNIAQFAYK----------IVFPSQYVYEKFRTITQLDHQKCHILPQGLFNHNPYKnniaKARSELRKKH 187
Cdd:cd03825   112 LNSYPPAKKDLSRQLFRRKrealakkrltIVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAP----VDKAKARKRL 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 188 NLPLDSKIIL--GVGFADHRKGIDLFsliAYSVRKVHT--NIHFIWVGRTDVHF----FNTLS-PRYTAHFTLVEptpdi 258
Cdd:cd03825   188 GIPQDKKVILfgAESVTKPRKGFDEL---IEALKLLATkdDLLLVVFGKNDPQIvilpFDIISlGYIDDDEQLVD----- 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 259 gLYNAgADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVT-EQTGALVDFLNLPQVLERIYEFIGDEDLRLQK 337
Cdd:cd03825   260 -IYSA-ADLFVHPSLADNLPNTLLEAMACGTPVVAF-DTGGSPEIVQhGVTGYLVPPGDVQALAEAIEWLLANPKERESL 336
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1267305034 338 GRFGQELIEKDFNFLHYIYQLLNLldhnYKKI 369
Cdd:cd03825   337 GERARALAENHFDQRVQAQRYLEL----YKDL 364
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
6-349 1.21e-20

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: 93.92  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034   6 KIIYVSHDAHFHGAQLLSLHTIKALKENFHYSVAIISIGTGILIHDFQKYG-PVYCLEEDYPTEKRVELLIKKLLSQD-- 82
Cdd:cd03807     1 KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAAGvPVVCLGLSSGKDPGVLLRLAKLIRKRnp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034  83 ---YTFAICSTVISGdIVTLLAkHNIKVISLIHELphLIQQYSAeGKARNIAQFAYKivFPSQYVYEKFRTitQLDHQKC 159
Cdd:cd03807    81 dvvHTWMYHADLIGG-LAAKLA-GGVKVIWSVRSS--NIPQRLT-RLVRKLCLLLSK--FSPATVANSSAV--AEFHQEQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 160 HILPQGL---FNH-NPYKNNI-AKARSELRKKHNLPLDSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVGR-- 232
Cdd:cd03807   152 GYAKNKIvviYNGiDLFKLSPdDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRgp 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 233 -TDVHFFNTLSPRYTAHFTLVEPTPDI-GLYNAgADLYLLTSREDPFPNVVLEALDTKVPVIGfKNAGGFEDVVTEQTGA 310
Cdd:cd03807   232 eRPNLERLLLELGLEDRVHLLGERSDVpALLPA-MDIFVLSSRTEGFPNALLEAMACGLPVVA-TDVGGAAELVDDGTGF 309
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1267305034 311 LVDFLNlPQVL-ERIYEFIGDEDLRLQKGRFGQELIEKDF 349
Cdd:cd03807   310 LVPAGD-PQALaDAIRALLEDPEKRARLGRAARERIANEF 348
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
370-598 2.04e-18

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 83.75  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 370 SVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIfkqLLSNENKPHlkvqQIINDKNSGsVFKQWIKGVS 449
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDI---IKKYEDKIT----YWISEPDKG-IYDAMNKGIA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 450 AATGDYIWIAEADDLCDQTFLEEVIQGFHINGDVTLSYtqskqideqgnilANHYLDYTNDIDKGKWKSSYFRKgideiq 529
Cdd:cd06433    73 LATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVY-------------GDVLLVDENGRVIGRRRPPPFLD------ 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267305034 530 DTLLIKNTIPNvSSVVFKnidiKSTEKQL----EKFKVAGDWFFYVSILKEGNI-YFNPKPLNYHRRHTNSVTR 598
Cdd:cd06433   134 KFLLYGMPICH-QATFFR----RSLFEKYggfdESYRIAADYDLLLRLLLAGKIfKYLPEVLAAFRLGGVSSTS 202
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
6-350 7.84e-18

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: 85.34  E-value: 7.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034   6 KIIYVSHDAHfhGAQLLSLHTIKALKENfHYSVAIISIGTGILIHDFQKYGPVYcleEDYPTEKR----------VELLI 75
Cdd:cd03808     1 KILFIVNVDG--GFQSFRLPLIKALVKK-GYEVHVIAPDGDKLSDELKELGVKV---IDIPILRRginplkdlkaLFKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034  76 KKLLSQDYTFAICSTVISGDIVTLLAK--HNIKVISLIHELPHLiqqYSAEGKARNIAQFAYKIVFP--------SQYVY 145
Cdd:cd03808    75 KLLKKEKPDIVHCHTPKPGILGRLAARlaGVPKVIYTVHGLGFV---FTEGKLLRLLYLLLEKLALLftdkvifvNEDDR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 146 EKFRTITQLDHQKCHILPQGLFNHNPYKNniakarselrKKHNLPLDSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNI 225
Cdd:cd03808   152 DLAIKKGIIKKKKTVLIPGSGVDLDRFQY----------SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNV 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 226 HFIWVGRTDVHFFNTLSPR---YTAHFTLVEPTPDI-GLYNAgADLYLLTSREDPFPNVVLEALDTKVPVIGFKNAGGFE 301
Cdd:cd03808   222 RFLLVGDGELENPSEILIEklgLEGRIEFLGFRSDVpELLAE-SDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRE 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1267305034 302 DVVTEQTGALVDFLNLPQVLERIYEFIGDEDLRLQKGRFGQELIEKDFN 350
Cdd:cd03808   301 LVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFD 349
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
363-477 1.14e-17

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 84.02  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 363 DHNYKKISVIIPNYNYEKYLPDRVKSILNQTYP--LYELIFLDDASTDNSVSIFKQLlsNENKPHLKVqqIINDKNSGSV 440
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIAREL--AAEYPRVRV--IERPENGGKA 100
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1267305034 441 fKQWIKGVSAATGDYIWIAEADDLCDQTFLEEVIQGF 477
Cdd:COG1215   101 -AALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF 136
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
263-363 3.47e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 75.03  E-value: 3.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 263 AGADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVTE-QTGALVDFLNLPQVLERIYEFIGDEDLRLQKGRFG 341
Cdd:COG0438    19 AAADVFVLPSRSEGFGLVLLEAMAAGLPVIAT-DVGGLPEVIEDgETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAA 97
                          90       100
                  ....*....|....*....|..
gi 1267305034 342 QELIEKDFNFLHYIYQLLNLLD 363
Cdd:COG0438    98 RERAEERFSWEAIAERLLALYE 119
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
194-330 2.36e-15

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 73.31  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 194 KIILGVG-FADHRKGIDLFSLIAYSVRKVHTNIHFIWVGRTDVHFFNTLSPRYTAHFTLVEPTPDIGLYNAGADLYLLTS 272
Cdd:pfam13692   2 PVILFVGrLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAGLEDRVIFTGFVEDLAELLAAADVFVLPS 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267305034 273 REDPFPNVVLEALDTKVPVIGFkNAGGFEDVVTEQTGALVDFLNLPQVLERIYEFIGD 330
Cdd:pfam13692  82 LYEGFGLKLLEAMAAGLPVVAT-DVGGIPELVDGENGLLVPPGDPEALAEAILRLLED 138
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
368-475 2.59e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.03  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsneNKPHLKVqqIINDKNSGSVfKQWIKG 447
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL----AFPRVRV--IRNPENLGFA-AARNLG 76
                          90       100
                  ....*....|....*....|....*...
gi 1267305034 448 VSAATGDYIWIAEADDLCDQTFLEEVIQ 475
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEPDWLERLLA 104
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
86-351 3.67e-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: 77.40  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034  86 AICSTVISGDIVTLLAKHNIKVISLIHE-LPHLIQQYSAEGKARNIAQFAYKIVFPSQYVYEKFRTITQLDHQKCHILPQ 164
Cdd:cd03811    87 VISFLGFATYIVAKLAAARSKVIAWIHSsLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPEKIEVIYN 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 165 GLFNHNPyknnIAKARSELrkkHNLPLDSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVG----RTDVHFF-N 239
Cdd:cd03811   167 PIDIDRI----RALAKEPI---LNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGdgplREELEKLaK 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 240 TLSprYTAHFTLVEPTPDIGLYNAGADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVTEQTGALV----DFL 315
Cdd:cd03811   240 ELG--LAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVST-DCPGPREILDDGENGLLvpdgDAA 316
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1267305034 316 NLPQVLERIYEFIGDEDLRLQKGRfGQELIEKDFNF 351
Cdd:cd03811   317 ALAGILAALLQKKLDAALRERLAK-AQEAVFREYTI 351
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
128-334 6.42e-14

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: 73.94  E-value: 6.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 128 RNIAQFAYkIVFPSQYVYEKFRTItqLDHQKCHILPQGLFNhnpyknNIAKARSELRKKHNLPLDSKIILGVGFADHRKG 207
Cdd:cd03821   148 RNLNNAAL-VHFTSEQEADELRRF--GLEPPIAVIPNGVDI------PEFDPGLRDRRKHNGLEDRRIILFLGRIHPKKG 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 208 IDLFSLIAYSVRKVHTNIHFIWVG---------RTDVHFFNtLSPRytahFTLVEPTPD---IGLYnAGADLYLLTSRED 275
Cdd:cd03821   219 LDLLIRAARKLAEQGRDWHLVIAGpddgaypafLQLQSSLG-LGDR----VTFTGPLYGeakWALY-ASADLFVLPSYSE 292
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267305034 276 PFPNVVLEALDTKVPVIGFKNAgGFEDVVTEQTGALVDfLNLPQVLERIYEFIGDEDLR 334
Cdd:cd03821   293 NFGNVVAEALACGLPVVITDKC-GLSELVEAGCGVVVD-PNVSSLAEALAEALRDPADR 349
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
368-591 9.70e-14

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 70.31  E-value: 9.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNY-EKYLPDRVKSILNQTYPLYELIFLDDASTDNSVsifKQLLSNENKPHLKVQQIINDKNSGsvfkqwI- 445
Cdd:cd04184     2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEV---KRVLKKYAAQDPRIKVVFREENGG------Is 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 446 ----KGVSAATGDYIWIAEADDLCDQTFLEEVIQGFHINGDVTLSYTQSKQIDEQGNILANHYldytndidKGKWksSYf 521
Cdd:cd04184    73 aatnSALELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFF--------KPDW--SP- 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267305034 522 rkgideiqDTLLIKNTIPNVssVVFKnidiKSTEKQL----EKFKVAGDWFFYVSILKEG-NIYFNPKPLnYHRR 591
Cdd:cd04184   142 --------DLLLSQNYIGHL--LVYR----RSLVRQVggfrEGFEGAQDYDLVLRVSEHTdRIAHIPRVL-YHWR 201
PRK10073 PRK10073
putative glycosyl transferase; Provisional
368-464 1.04e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 72.77  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsNENKPHLkvqQIINDKNSG-SVFKQwiK 446
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHY--AENYPHV---RLLHQANAGvSVARN--T 79
                          90
                  ....*....|....*...
gi 1267305034 447 GVSAATGDYIWIAEADDL 464
Cdd:PRK10073   80 GLAVATGKYVAFPDADDV 97
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
189-313 3.53e-13

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: 71.64  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 189 LPLDSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVGR-------TDVHFFNTLSPRytAHFTLVEPTPDIGLY 261
Cdd:cd03798   196 LPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDgplrealRALAEDLGLGDR--VTFTGRLPHEQVPAY 273
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1267305034 262 NAGADLYLLTSREDPFPNVVLEALDTKVPVIGfKNAGGFEDVVTEQ-TGALVD 313
Cdd:cd03798   274 YRACDVFVLPSRHEGFGLVLLEAMACGLPVVA-TDVGGIPEVVGDPeTGLLVP 325
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
368-475 8.52e-13

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 68.80  E-value: 8.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYP--LYELIFLDDASTDNSVSIFKQLLSNenkpHLKVQQIINDKNSGSvfKQWI 445
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYAAK----DPRIRLIDNPKRIQS--AGLN 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1267305034 446 KGVSAATGDYIWIAEADDLCDQTFLEEVIQ 475
Cdd:cd02525    75 IGIRNSRGDIIIRVDAHAVYPKDYILELVE 104
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
371-483 1.68e-12

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 65.66  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLSNenkphlkVQQIINDKNSGsvF----KQwik 446
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE-------VRLIRNGENLG--FgagnNQ--- 68
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1267305034 447 GVSAATGDYIWIAEADDLCDQTFLEEVIQGFHINGDV 483
Cdd:cd04186    69 GIREAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDV 105
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
199-312 3.62e-12

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: 66.66  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 199 VGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVGRTDVHFFNTLSPRYTAH------FTLVEPTPDIGLYNAGADLYLLTS 272
Cdd:cd01635   116 VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLlervviIGGLVDDEVLELLLAAADVFVLPS 195
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1267305034 273 REDPFPNVVLEALDTKVPVIGFKNAGGFEDVVTEQTGALV 312
Cdd:cd01635   196 RSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
371-479 7.27e-12

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 64.42  E-value: 7.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLP---DRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLsnENKPHLKVqqIINDKNSGsvfKQW--I 445
Cdd:cd04187     1 IVVPVYNEEENLPelyERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELA--ARDPRVKV--IRLSRNFG---QQAalL 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1267305034 446 KGVSAATGDYIwIAEADDLCDQ-----TFLEEVIQGFHI 479
Cdd:cd04187    74 AGLDHARGDAV-ITMDADLQDPpelipEMLAKWEEGYDV 111
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
371-483 1.55e-11

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 63.40  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLSNENKPHLkvqqIINDKNSGSvfkqwiK---- 446
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVL----VVRDKENGG------Kagal 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1267305034 447 --GVSAATGDYIWIAEADDLCDQTFLEEVIQGFHINGDV 483
Cdd:cd06423    71 naGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKV 109
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
192-343 3.81e-11

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: 61.91  E-value: 3.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 192 DSKIILGVGFADHRKGIDLFSLIAYSVRKVHTNIHFIWVGrtDVHFFNTLSPRYTA-------HFTLVEPTPDIGLYNAG 264
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG--DGEEEKRLKKLAEKlglgdnvIFLGFVSDEDLPELLKI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 265 ADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVTE-QTGALVDFLNLPQVLERIYEFIGDEDLRLQKGRFGQE 343
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIAS-DVGGPPEVVKDgETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
100-347 9.08e-11

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: 63.80  E-value: 9.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 100 LAKHNIKVISLIHELPHLIQQYSAEGKARN-IAQFAYKIVfpsqyvyekfrTITQLDHQKCHilpQGLFNHNPYKNNIAk 178
Cdd:cd03820   104 LIGLKSKLIVWEHNNYEAYNKGLRRLLLRRlLYKRADKIV-----------VLTEADKLKKY---KQPNSNVVVIPNPL- 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 179 arSELRKKHNLPLDSKIILGVGFADHRKGIDL----FSLIAysvrkvhtNIHFIW----VG----RTD-VHFFNTLSPRY 245
Cdd:cd03820   169 --SFPSEEPSTNLKSKRILAVGRLTYQKGFDLlieaWALIA--------KKHPDWklriYGdgpeREElEKLIDKLGLED 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 246 TAHFTlvEPTPDIGLYNAGADLYLLTSREDPFPNVVLEALDTKVPVIGFKNAGGFEDVVTEQ-TGALVDFLNLPQVLERI 324
Cdd:cd03820   239 RVKLL--GPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPSEIIEDGeNGLLVPNGDVDALAEAL 316
                         250       260
                  ....*....|....*....|...
gi 1267305034 325 YEFIGDEDLRLQKGRFGQELIEK 347
Cdd:cd03820   317 LRLMEDEELRKKMGKNARKNAER 339
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
371-462 2.71e-10

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 60.77  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTYP--LYELIFLDDASTDNSVSIFKQLLSNENkPHLKVQQIINDKNSGSvfKQWI-KG 447
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPkeKFEVILVDDHSTDGTVQILEFAAAKPN-FQLKILNNSRVSISGK--KNALtTA 77
                          90
                  ....*....|....*
gi 1267305034 448 VSAATGDYIWIAEAD 462
Cdd:cd04192    78 IKAAKGDWIVTTDAD 92
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
369-477 1.95e-09

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 58.15  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 369 ISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLSNEnkPHLKVQQIINDKNSGSVFKQW--IK 446
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARF--PDVRLRVIRNARLLGPTGKSRglNH 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1267305034 447 GVSAATGDYIWIAEADDLCDQTFLEEVIQGF 477
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF 112
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
368-477 1.15e-08

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 56.44  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYP--LYELIFLDDASTDNSVSIFKQLLSNenkphlKVQQIINDKNSG--SVFKq 443
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDYPrdRLEIIVVSDGSTDGTAEIAREYADK------GVKLLRFPERRGkaAALN- 102
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1267305034 444 wiKGVSAATGDYIWIAEADDLCDQTFLEEVIQGF 477
Cdd:cd06439   103 --RALALATGEIVVFTDANALLDPDALRLLVRHF 134
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
371-462 1.20e-08

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 55.27  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLP---DRVKSILNQTYPlYELIFLDDASTDNSVSIFKQLLSNENKPHLkvqqIINDKNSGsvfKQW--I 445
Cdd:cd04179     1 VVIPAYNEEENIPelvERLLAVLEEGYD-YEIIVVDDGSTDGTAEIARELAARVPRVRV----IRLSRNFG---KGAavR 72
                          90
                  ....*....|....*..
gi 1267305034 446 KGVSAATGDYIWIAEAD 462
Cdd:cd04179    73 AGFKAARGDIVVTMDAD 89
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
179-313 1.38e-08

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: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 179 ARSELRKKHNLPLDSKIILGVGfadhR----KGIDLFsLIAYSVRKVHTNIHFIWVG-----------RTDVHFFNTLSP 243
Cdd:cd03814   184 RRDAALRRRLGPPGRPLLLYVG----RlapeKNLEAL-LDADLPLAASPPVRLVVVGdgparaelearGPDVIFTGFLTG 258
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267305034 244 R-YTAHFtlveptpdiglynAGADLYLLTSREDPFPNVVLEALDTKVPVIGFkNAGGFEDVVTEQ-TGALVD 313
Cdd:cd03814   259 EeLARAY-------------ASADVFVFPSRTETFGLVVLEAMASGLPVVAA-DAGGPRDIVRPGgTGALVE 316
PHA01630 PHA01630
putative group 1 glycosyl transferase
132-321 1.99e-08

putative group 1 glycosyl transferase


Pssm-ID: 164861  Cd Length: 331  Bit Score: 56.33  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 132 QFAYKIVFPSQYVYEKFRTITQLDHQKCHILPQglfNHNPyknniaKARSELRKKHNLPLdskIILGVGFADHRKGIDLF 211
Cdd:PHA01630   93 QPVDEIVVPSQWSKNAFYTSGLKIPQPIYVIPH---NLNP------RMFEYKPKEKPHPC---VLAILPHSWDRKGGDIV 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 212 SLIAYSVRKVHTNIHFIwvgrtdVHFFNTLSPRYTAHFTLVEPTPDIGLYN--AGADLYLLTSREDPFPNVVLEALDTKV 289
Cdd:PHA01630  161 VKIFHELQNEGYDFYFL------IKSSNMLDPRLFGLNGVKTPLPDDDIYSlfAGCDILFYPVRGGAFEIPVIEALALGL 234
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1267305034 290 PVIGFKNAGGFEDVVTEQTGALVDFLNLPQVL 321
Cdd:PHA01630  235 DVVVTEKGAWSEWVLSNLDVYWIKSGRKPKLW 266
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
371-481 3.38e-07

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 51.41  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLP---DRVKSILNQTYPL-YELIFLDDASTDNSVSIFKQlLSNENKPHLKVqqIINDKNSG---SVfkq 443
Cdd:cd04188     1 VVIPAYNEEKRLPptlEEAVEYLEERPSFsYEIIVVDDGSKDGTAEVARK-LARKNPALIRV--LTLPKNRGkggAV--- 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1267305034 444 wIKGVSAATGDYIWIAEAD---DLCDqtfLEEVIQGFHING 481
Cdd:cd04188    75 -RAGMLAARGDYILFADADlatPFEE---LEKLEEALKTSG 111
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
155-360 4.51e-07

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: 52.63  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 155 DHQKCHILPQG--LFNHNPYknniAKARSELRKKhNLPLDSKIILGVGFADHRKGIDLfsLI-AYSVRKVH---TNIHFI 228
Cdd:cd03800   185 DPSRINVVPPGvdLERFFPV----DRAEARRARL-LLPPDKPVVLALGRLDPRKGIDT--LVrAFAQLPELrelANLVLV 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 229 WVGRTD---------------------VHFFNTLSPRytahftlveptpDIGLYNAGADLYLLTSREDPFPNVVLEALDT 287
Cdd:cd03800   258 GGPSDDplsmdreelaelaeelglidrVRFPGRVSRD------------DLPELYRAADVFVVPSLYEPFGLTAIEAMAC 325
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267305034 288 KVPVIGFKNAGGFEDVVTEQTGALVDFLNLPQVLERIYEFIGDEDLRLQKGRFGQELIEKDFNFLHYIYQLLN 360
Cdd:cd03800   326 GTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT 398
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
134-350 1.04e-06

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: 51.19  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 134 AYKIVFPSQYVYEKFRTITQLDHqKCHILPQGLfNHNPYKNNiakARSELRKKHNLPlDSKIILGVGFADHRKGIDLFSL 213
Cdd:cd03794   164 ADAIIVLSPGLKEYLLRKGVPKE-KIIVIPNWA-DLEEFKPP---PKDELRKKLGLD-DKFVVVYAGNIGKAQGLETLLE 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 214 IAYSVRKvHTNIHFIWVGR----------------TDVHFFNTLSP-RYTAHFTLVeptpDIGLYNAGADLYLLTSredp 276
Cdd:cd03794   238 AAERLKR-RPDIRFLFVGDgdekerlkelakarglDNVTFLGRVPKeEVPELLSAA----DVGLVPLKDNPANRGS---- 308
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267305034 277 FPNVVLEALDTKVPVIGFKNAGGFEDVVTEQTGALVDFLNLPQVLERIYEFIGDEDLRLQKGRFGQELIEKDFN 350
Cdd:cd03794   309 SPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFS 382
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
265-350 1.14e-06

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: 51.20  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 265 ADLYLLTSREDPFPNVVLEALDTKVPVIGfKNAGGFEDVVTE-QTGALVDFLNLPQVLERIYEFIGDEDLRLQKGRFGQE 343
Cdd:cd04962   270 ADLFLLPSEKESFGLAALEAMACGVPVVS-SNAGGIPEVVKHgETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARK 348

                  ....*..
gi 1267305034 344 LIEKDFN 350
Cdd:cd04962   349 RAAERFD 355
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
189-316 1.18e-06

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: 51.20  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 189 LPLDSKIILGVGFADHRKGIDLFSLIAYSVRKvHTNIHFIWVGrtDVH---FFNTLSPRY--TAHFTLVEPTPDIGLYNA 263
Cdd:cd03819   178 LPEGKPVVGYVGRLSPEKGWLLLVDAAAELKD-EPDFRLLVAG--DGPerdEIRRLVERLglRDRVTFTGFREDVPAALA 254
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1267305034 264 GADLYLLTSREDPFPNVVLEALDTKVPVIGFKNAGGFEDVVTEQTGALVDFLN 316
Cdd:cd03819   255 ASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGD 307
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
369-477 2.95e-06

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 48.36  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 369 ISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLLsnENKPHLKVQQIINDKNSGSVFK--QWIK 446
Cdd:cd02520     3 VSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLI--AKYPNVDARLLIGGEKVGINPKvnNLIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1267305034 447 GVSAATGDYIWIAEADDLCDQTFLEEVIQGF 477
Cdd:cd02520    81 GYEEARYDILVISDSDISVPPDYLRRMVAPL 111
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
367-462 3.42e-06

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 49.35  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 367 KKISVIIPNYNYEKYLP---DRVKSILNQTYPLYELIFLDDASTDNSVSIfkqLLSNENKPHLKVQQIINDKNSGSvFKQ 443
Cdd:PRK10714    6 KKVSVVIPVYNEQESLPeliRRTTAACESLGKEYEILLIDDGSSDNSAEM---LVEAAQAPDSHIVAILLNRNYGQ-HSA 81
                          90
                  ....*....|....*....
gi 1267305034 444 WIKGVSAATGDYIWIAEAD 462
Cdd:PRK10714   82 IMAGFSHVTGDLIITLDAD 100
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
369-475 4.82e-06

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 47.95  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 369 ISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsnenkphlkVQQIIN-DKNSGsvfKQWIKG 447
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSA----------GVVVISsPKGRA---RQMNAG 67
                          90       100
                  ....*....|....*....|....*...
gi 1267305034 448 VSAATGDYIWIAEADDLCDQTFLEEVIQ 475
Cdd:cd02522    68 AAAARGDWLLFLHADTRLPPDWDAAIIE 95
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
371-497 7.75e-06

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 47.24  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsnenKPHLKVQQIINDKNSGSV--FKQWIKGV 448
Cdd:cd04185     1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSL-----GDLDNIVYLRLPENLGGAggFYEGVRRA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1267305034 449 SAATGDYIWIAEADDLCDQTFLEEVIQGFHINGdvtLSYTQSKQIDEQG 497
Cdd:cd04185    76 YELGYDWIWLMDDDAIPDPDALEKLLAYADKDN---PQFLAPLVLDPDG 121
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
369-463 9.36e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 47.68  E-value: 9.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 369 ISVIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTdnSVSIFKQLLSNENKPhlKVQQIINDKNSG--SVFKQwik 446
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTALNDP--RITYIHNDINSGacAVRNQ--- 79
                          90
                  ....*....|....*..
gi 1267305034 447 GVSAATGDYIWIAEADD 463
Cdd:PRK10018   80 AIMLAQGEYITGIDDDD 96
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
263-347 2.96e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 47.01  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 263 AGADLYLLTSREDPFPNVVLEALDTKVPVIGFKnAGGFEDVVTEQ----TGALVDFLNLPQVLERIYEFIGDEDLRLQKG 338
Cdd:PLN02871  330 ASGDVFVMPSESETLGFVVLEAMASGVPVVAAR-AGGIPDIIPPDqegkTGFLYTPGDVDDCVEKLETLLADPELRERMG 408

                  ....*....
gi 1267305034 339 RFGQELIEK 347
Cdd:PLN02871  409 AAAREEVEK 417
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
369-474 6.72e-05

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 45.53  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 369 ISVIIPNYNYE-----------KYLPDRVKSILNQTYplyELIFLDDASTDNSVSIFKQLLSNENKPH--LKVQQIINDK 435
Cdd:PTZ00260   72 LSIVIPAYNEEdrlpkmlketiKYLESRSRKDPKFKY---EIIIVNDGSKDKTLKVAKDFWRQNINPNidIRLLSLLRNK 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1267305034 436 NSGSVFKQwikGVSAATGDYIWIAEAD---DLCDQTFLEEVI 474
Cdd:PTZ00260  149 GKGGAVRI---GMLASRGKYILMVDADgatDIDDFDKLEDIM 187
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
371-462 6.96e-05

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 44.45  E-value: 6.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTYPL-YELIFLDDASTDNSVSIFKQLLSNENKPHLKVQqiINDKNSGSVFkqwIKGVS 449
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGIdYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVR--PGKRGLGSAY---IEGFK 75
                          90
                  ....*....|...
gi 1267305034 450 AATGDYIWIAEAD 462
Cdd:cd06442    76 AARGDVIVVMDAD 88
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
370-575 1.03e-04

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 44.58  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 370 SVIIPNYNYEK--YLPDRVKSILNQTYPLYELIFLDDASTDNS---VSIFKQLLSNENKPHLkvqqiinDKNSGSVFKQW 444
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTleeVSSIKDHNLQVYYPNA-------PDTTYSLAASR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 445 IKGVSAATGDYIWIAEADDLCDQTFLEEViqgfhingdvtLSYTQSKQIDEQGNILANHYLDYTNDIDKGKWKS-SYFRK 523
Cdd:pfam10111  74 NRGTSHAIGEYISFIDGDCLWSPDKFEKQ-----------LKIATSLALQENIQAAVVLPVTDLNDESSNFLRRgGDLTA 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267305034 524 GIDEIQDTLLIKNTI-----PNVSSVVFKNIDIKSTEKQLEKFKVAG--DWFFYVSILK 575
Cdd:pfam10111 143 SGDVLRDLLVFYSPLaiffaPNSSNALINRQAFIEVGGFDESFRGHGaeDFDIFLRLAA 201
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
137-313 3.05e-04

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: 43.42  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 137 IVFPSQYVYEKFRtitQLDHQKC-HILPQGlFNHNPYKNniaKARSELRKKHNLPLDSKIILGVGFADHRKGID-LFSLI 214
Cdd:cd03817   151 VIAPSEKIKDTLR---EYGVKGPiEVIPNG-IDLDKFEK---PLNTEERRKLGLPPDEPILLYVGRLAKEKNIDfLLRAF 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 215 AYSVRKVhtNIHFIWVG-----------------RTDVHFFNTLSPRytahftlveptpDIGLYNAGADLYLLTSREDPF 277
Cdd:cd03817   224 AELKKEP--NIKLVIVGdgpereelkelarelglADKVIFTGFVPRE------------ELPEYYKAADLFVFASTTETQ 289
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1267305034 278 PNVVLEALDTKVPVIgFKNAGGFEDVVTE-QTGALVD 313
Cdd:cd03817   290 GLVYLEAMAAGLPVV-AAKDPAASELVEDgENGFLFE 325
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
180-363 4.68e-04

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: 43.08  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 180 RSELRKKHNLPLDSKIILGVGFADHRKGIdlFSLI-AYS-VRKVHTNIHFIWVGR--TDVH-----FFNTLSPRYTAH-- 248
Cdd:cd03792   184 RYYLEKPFVIDPERPYILQVARFDPSKDP--LGVIdAYKlFKRRAEEPQLVICGHgaVDDPegsvvYEEVMEYAGDDHdi 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 249 FTLVEPTPDIgLYNA---GADLYLLTSREDPFPNVVLEALDTKVPVIGFKNAGGFEDVVTEQTGALVDFLNLPQVleRIY 325
Cdd:cd03792   262 HVLRLPPSDQ-EINAlqrAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAV--RIL 338
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1267305034 326 EFIGDEDLRLQKGRFGQELIEKDFNFLHYIYQLLNLLD 363
Cdd:cd03792   339 RLLTDPELRRKMGLAAREHVRDNFLITGNLRAWLYLIA 376
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
368-577 7.25e-04

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 41.51  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILNQTYplyELIFLDDASTDNSVSIFKQLlsnenkphlkvqqiiNDKnsgsVFKQWIKG 447
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVD---EIIVVDSGSTDRTVEIAKEY---------------GAK----VYQRWWDG 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 448 VSA--------ATGDYIWIAEADDLCDQTFLEEVIQGFHINGDVTLSYTQSKQIDEQGNILANHYLDYTNDIdkgkWKSS 519
Cdd:cd02511    59 FGAqrnfalelATNDWVLSLDADERLTPELADEILALLATDDYDGYYVPRRNFFLGRWIRHGGWYPDRQLRL----FRRG 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267305034 520 YFRKGIDEIQDTLLIKNTIPNVSSVVFKNIDIKSTEKQLEKF-----------KVAGDWFFYVSILKEG 577
Cdd:cd02511   135 KARFEDGRVHEQVVVDGGVGIVLKGDILHYGYKSLEEFLEKHnryssleakdlAAKGKKRSLLKGLLLG 203
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
371-456 9.05e-04

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 40.64  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTYPLYELIFLDDASTDNSVSIFKQLlsnENKPHLKVQ------------QIINdknsg 438
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEF---KSQFPIPIKhvwqedegfrkaKIRN----- 72
                          90
                  ....*....|....*...
gi 1267305034 439 svfkqwiKGVSAATGDYI 456
Cdd:cd06420    73 -------KAIAAAKGDYL 83
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
368-462 1.76e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 40.45  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 368 KISVIIPNYNYEKYLPDRVKSILN--QTYPLYELIFLDDASTDNSVSIFKQLLSNENKPHLKVQQIINDKNSGSVFkqwI 445
Cdd:PLN02726   10 KYSIIVPTYNERLNIALIVYLIFKalQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAY---I 86
                          90
                  ....*....|....*..
gi 1267305034 446 KGVSAATGDYIWIAEAD 462
Cdd:PLN02726   87 HGLKHASGDFVVIMDAD 103
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
371-463 3.87e-03

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 39.36  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267305034 371 VIIPNYNYEKYLPDRVKSILNQTY--PLyELIFLDDASTDNSVSI---FKQLLSNENKPHLkVQQIINDKNSGSVFKQwI 445
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFegTL-ELSVFNDASTDKSAEIiekWRKKLEDSGVIVL-VGSHNSPSPKGVGYAK-N 77
                          90
                  ....*....|....*...
gi 1267305034 446 KGVSAATGDYIWIAEADD 463
Cdd:cd06913    78 QAIAQSSGRYLCFLDSDD 95
 
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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