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Conserved domains on  [gi|818621103|gb|KKS69342|]
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hypothetical protein UV39_C0013G0003 [Candidatus Azambacteria bacterium GW2011_GWA2_42_62]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 3-376 4.95e-66

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.


The actual alignment was detected with superfamily member cd03808:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 358  Bit Score: 214.00  E-value: 4.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSefGGAQHFMFNLGFN-IQNEYKILVCAGadGGGEFLKILQANNIPCKELKHLRRSICPIDDLLCVMDIAQI 81
Cdd:cd03808    1 KILFIVNVD--GGFQSFRLPLIKAlVKKGYEVHVIAP--DGDKLSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  82 IKNFAPDIVFISSSKAGALGTAAAifcrWFGRKFTLIYRID-WAFNDPRPALERKIYIVIENFLSKFRDIIIQNDQFDLR 160
Cdd:cd03808   77 LKKEKPDIVHCHTPKPGILGRLAA----RLAGVPKVIYTVHgLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 161 TA-KINGIKPKLGFKIIHNGIDgnaldfLDKndarnfFHNKLNtDLNQFDLIIGTIANYYKTKGLSYLLDAMAELSKTK- 238
Cdd:cd03808  153 LAiKKGIIKKKKTVLIPGSGVD------LDR------FQYSPE-SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGp 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 239 NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIP 318
Cdd:cd03808  220 NVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCR 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 818621103 319 EILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKY 376
Cdd:cd03808  300 ELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 3-376 4.95e-66

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: 214.00  E-value: 4.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSefGGAQHFMFNLGFN-IQNEYKILVCAGadGGGEFLKILQANNIPCKELKHLRRSICPIDDLLCVMDIAQI 81
Cdd:cd03808    1 KILFIVNVD--GGFQSFRLPLIKAlVKKGYEVHVIAP--DGDKLSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  82 IKNFAPDIVFISSSKAGALGTAAAifcrWFGRKFTLIYRID-WAFNDPRPALERKIYIVIENFLSKFRDIIIQNDQFDLR 160
Cdd:cd03808   77 LKKEKPDIVHCHTPKPGILGRLAA----RLAGVPKVIYTVHgLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 161 TA-KINGIKPKLGFKIIHNGIDgnaldfLDKndarnfFHNKLNtDLNQFDLIIGTIANYYKTKGLSYLLDAMAELSKTK- 238
Cdd:cd03808  153 LAiKKGIIKKKKTVLIPGSGVD------LDR------FQYSPE-SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGp 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 239 NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIP 318
Cdd:cd03808  220 NVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCR 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 818621103 319 EILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKY 376
Cdd:cd03808  300 ELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 209-362 5.52e-41

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: 142.03  E-value: 5.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  209 DLIIGTIANYYKTKGLSYLLDAMAELSKTK-NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDA--YKYLKACDI 285
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNpNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEdlPELLKIADV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818621103  286 FVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQR 362
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 279-384 5.52e-33

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 119.71  E-value: 5.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 279 YLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGIS 358
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*.
gi 818621103 359 AKQRAKNQFALNTMLSKYRQLFRAII 384
Cdd:COG0438   97 ARERAEERFSWEAIAERLLALYEELL 122
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 210-381 1.41e-32

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 125.99  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  210 LIIGTIANYYKTKGLSYLLDAMAELSK-----TKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACD 284
Cdd:TIGR03088 195 VVVGTVGRLQAVKDQPTLVRAFALLVRqlpegAERLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALD 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  285 IFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAK 364
Cdd:TIGR03088 275 LFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAE 354

                         170
                  ....*....|....*..
gi 818621103  365 NQFALNTMLSKYRQLFR 381
Cdd:TIGR03088 355 QQFSINAMVAAYAGLYD 371
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 222-361 5.15e-14

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 73.21  E-value: 5.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 222 KGLSYLLDAMAELSktkNIGCILVGDGPERKILEKIIKqrGLeNRVF---LAG-QISDAYKYLkacDIFVLPSAKEGFPW 297
Cdd:PLN02871 276 KNLDFLKRVMERLP---GARLAFVGDGPYREELEKMFA--GT-PTVFtgmLQGdELSQAYASG---DVFVMPSESETLGF 346

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818621103 298 TILEAMLAGLPIIATKVGAIPEILEN---GVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQ 361
Cdd:PLN02871 347 VVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAARE 413
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 262-380 1.36e-05

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 46.85  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 262 GLENRV-FLAGQ-ISDaykYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILEN--------GVNGWIVE 331
Cdd:NF038011 364 GLQDKVkFLGFQkIDD---LLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIEGldeedralGAAGEVVA 440

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 818621103 332 SENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKYRQLF 380
Cdd:NF038011 441 IADPQALARAALDLLRDPQRWQAAQAAGLARVERYYTEELMFDRYRELY 489
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 3-376 4.95e-66

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: 214.00  E-value: 4.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSefGGAQHFMFNLGFN-IQNEYKILVCAGadGGGEFLKILQANNIPCKELKHLRRSICPIDDLLCVMDIAQI 81
Cdd:cd03808    1 KILFIVNVD--GGFQSFRLPLIKAlVKKGYEVHVIAP--DGDKLSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  82 IKNFAPDIVFISSSKAGALGTAAAifcrWFGRKFTLIYRID-WAFNDPRPALERKIYIVIENFLSKFRDIIIQNDQFDLR 160
Cdd:cd03808   77 LKKEKPDIVHCHTPKPGILGRLAA----RLAGVPKVIYTVHgLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 161 TA-KINGIKPKLGFKIIHNGIDgnaldfLDKndarnfFHNKLNtDLNQFDLIIGTIANYYKTKGLSYLLDAMAELSKTK- 238
Cdd:cd03808  153 LAiKKGIIKKKKTVLIPGSGVD------LDR------FQYSPE-SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGp 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 239 NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIP 318
Cdd:cd03808  220 NVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCR 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 818621103 319 EILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKY 376
Cdd:cd03808  300 ELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 3-381 3.48e-57

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: 190.99  E-value: 3.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSEFGGAQ-------HFMFNLGFNIqneykILVCAGADGggEFLKILQANNIPckeLKHLrrSICPIDDLLCV 75
Cdd:cd03807    1 KVAHVITGLNVGGAEtmllrllEHMDKSRFEH-----VVISLTGDG--VLGEELLAAGVP---VVCL--GLSSGKDPGVL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  76 MDIAQIIKNFAPDIVFISSSKAGALGTAAAIFCRwfGRK-FTLIYRIdwafNDPRPALerKIYIVIENFLSKFRDIIIQN 154
Cdd:cd03807   69 LRLAKLIRKRNPDVVHTWMYHADLIGGLAAKLAG--GVKvIWSVRSS----NIPQRLT--RLVRKLCLLLSKFSPATVAN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 155 DQFDLRTAKiNGIKPKLGFKIIHNGIDGNALDFLDKNDARNffhnKLNTDLNQFDLIIGTIANYYKTKGLSYLLDAMAEL 234
Cdd:cd03807  141 SSAVAEFHQ-EQGYAKNKIVVIYNGIDLFKLSPDDASRARA----RRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALL 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 235 SKT-KNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATK 313
Cdd:cd03807  216 VEThPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATD 295

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818621103 314 VGAIPEILENGVnGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKYRQLFR 381
Cdd:cd03807  296 VGGAAELVDDGT-GFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-381 7.35e-46

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: 161.55  E-value: 7.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSE--FGGAQHFMFNLGFNIQNE-YKILVCAGADGGGEFLKILQANNIPCKELKHLRRSICPIDDllcvmDIA 79
Cdd:cd03801    1 KILLLSPELPppVGGAERHVRELARALAARgHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLR-----ELR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  80 QIIKNFAPDIVFISSskagaLGTAAAIFCRWFGRKFTLIYRIDWAFNDPRPALERKIYIVIEN--FLSKFRDIIIQNDQF 157
Cdd:cd03801   76 PLLRLRKFDVVHAHG-----LLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARaeALLRRADAVIAVSEA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 158 DLRTAKINGIKPKLGFKIIHNGIDgnaldfldkndaRNFFHNKLNTDLNQF--DLIIGTIANYYKTKGLSYLLDAMAEL- 234
Cdd:cd03801  151 LRDELRALGGIPPEKIVVIPNGVD------------LERFSPPLRRKLGIPpdRPVLLFVGRLSPRKGVDLLLEALAKLl 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 235 SKTKNIGCILVG-DGPERKILEKIikQRGLENRVFLAGQISDA--YKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIA 311
Cdd:cd03801  219 RRGPDVRLVIVGgDGPLRAELEEL--ELGLGDRVRFLGFVPDEelPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVA 296

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 312 TKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKYRQLFR 381
Cdd:cd03801  297 TDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 3-352 3.42e-44

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: 156.36  E-value: 3.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSEFGGAQHFMFNLGFNIQNE-YKILVCAGADGGGEFLKILQANNIPCKELKHLRrsICPIDDLLCVMDIAQI 81
Cdd:cd03811    1 KILFVIPSLSGGGAERVLLNLANALDKRgYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLK--LIKLGLLKAILKLKRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  82 IKNFAPDIVFissskagalgtaaaifcrWFGRKFTLIYRIDWAFNDPRPALERKIYIVIENFLSKFRDIIIQNDQFDL-- 159
Cdd:cd03811   79 LKRAKPDVVI------------------SFLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKiv 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 160 -------RTAKINGIKPKLGFKIIHNGIDGNALDFLDKNDARNFFHNKLNtdlnqfdliIGTIANYYKTKGLSYLLDAMA 232
Cdd:cd03811  141 cvskgikEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILNEPEDGPV---------ILAVGRLDPQKGHDLLIEAFA 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 233 ELSKT-KNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIA 311
Cdd:cd03811  212 KLRKKyPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVS 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 818621103 312 TKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDR 352
Cdd:cd03811  292 TDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDA 332
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 209-362 5.52e-41

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: 142.03  E-value: 5.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  209 DLIIGTIANYYKTKGLSYLLDAMAELSKTK-NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDA--YKYLKACDI 285
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNpNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEdlPELLKIADV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818621103  286 FVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQR 362
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
211-344 6.60e-38

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 133.41  E-value: 6.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  211 IIGTIANYYK-TKGLSYLLDAMAELSKTKN-IGCILVGDGPERKILEKIikqRGLENRVFLAGQISDAYKYLKACDIFVL 288
Cdd:pfam13692   3 VILFVGRLHPnVKGVDYLLEAVPLLRKRDNdVRLVIVGDGPEEELEELA---AGLEDRVIFTGFVEDLAELLAAADVFVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 818621103  289 PSAKEGFPWTILEAMLAGLPIIATKVGAIPEILEnGVNGWIVESENQKQIVEKILW 344
Cdd:pfam13692  80 PSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEALAEAILR 134
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 211-383 2.76e-36

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


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 135.97  E-value: 2.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 211 IIGTIANYYKTKGLSYLLDAMAEL-SKTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQIS--DAYKYLKACDIFV 287
Cdd:cd03798  202 VILFVGRLIPRKGIDLLLEAFARLaKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPheQVPAYYRACDVFV 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 288 LPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSfGISAKQRAKNQF 367
Cdd:cd03798  282 LPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLREL-GEAARARVAERF 360

                        170
                 ....*....|....*.
gi 818621103 368 ALNTMLSKYRQLFRAI 383
Cdd:cd03798  361 SWVKAADRIAAAYRDV 376
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 4-352 3.27e-35

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: 132.48  E-value: 3.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   4 ILFIVTQSEFGGAQHFMFNLGFNI-QNEYKILVcagADGGGEFLKILQANNIPCKELKhLRRSICPIDDLLcvmdIAQII 82
Cdd:cd03819    1 ILMLTPALEIGGAETYILDLARALaERGHRVLV---VTAGGPLLPRLRQIGIGLPGLK-VPLLRALLGNVR----LARLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  83 KNFAPDIVFISSSKAGALGtaaAIFCRWFGRKFTLIYRIDWA--FNDPRPALERKIYIvienflskFRDIIIQNDQFDLR 160
Cdd:cd03819   73 RRERIDLIHAHSRAPAWLG---WLASRLTGVPLVTTVHGSYLatYHPKDFALAVRARG--------DRVIAVSELVRDHL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 161 TAKINGIKPKLgfKIIHNGIDgnALDFLDKNDARNFFHNKLNTDlnqfDLIIGTIANYYKTKGLSYLLDAMAELSKTKNI 240
Cdd:cd03819  142 IEALGVDPERI--RVIPNGVD--TDRFPPEAEAEERAQLGLPEG----KPVVGYVGRLSPEKGWLLLVDAAAELKDEPDF 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 241 GCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEI 320
Cdd:cd03819  214 RLLVAGDGPERDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREI 293

                        330       340       350
                 ....*....|....*....|....*....|..
gi 818621103 321 LENGVNGWIVESENQKQIVEKILWFSAHPDDR 352
Cdd:cd03819  294 VVHGRTGLLVPPGDAEALADAIRAAKLLPEAR 325
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 279-384 5.52e-33

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 119.71  E-value: 5.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 279 YLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGIS 358
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*.
gi 818621103 359 AKQRAKNQFALNTMLSKYRQLFRAII 384
Cdd:COG0438   97 ARERAEERFSWEAIAERLLALYEELL 122
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 173-372 6.36e-33

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 126.23  E-value: 6.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 173 FKIIHNGIDGNALDFldknDARNFFHNKLNTDLNQFDLIIGTIANYyktKGLSYLLDAMAELsktkNIGCILVGDGPERK 252
Cdd:cd03795  162 VRVIPLGIDKNVYNI----PRVDFENIKREKKGKKIFLFIGRLVYY---KGLDYLIEAAQYL----NYPIVIGGEGPLKP 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 253 ILEKIIKQRGLENrVFLAGQISDA--YKYLKACDIFVLPS--AKEGFPWTILEAMLAGLPIIATKVG-AIPEILENGVNG 327
Cdd:cd03795  231 DLEAQIELNLLDN-VKFLGRVDDEekVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETG 309

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 818621103 328 WIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTM 372
Cdd:cd03795  310 LVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKM 354
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 210-381 1.41e-32

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 125.99  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  210 LIIGTIANYYKTKGLSYLLDAMAELSK-----TKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACD 284
Cdd:TIGR03088 195 VVVGTVGRLQAVKDQPTLVRAFALLVRqlpegAERLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALD 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  285 IFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAK 364
Cdd:TIGR03088 275 LFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAE 354

                         170
                  ....*....|....*..
gi 818621103  365 NQFALNTMLSKYRQLFR 381
Cdd:TIGR03088 355 QQFSINAMVAAYAGLYD 371
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 3-380 8.76e-32

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 123.32  E-value: 8.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSEFGGAQHFMFNLGFNIQ---NEYKILVCAGADgggeFLKILQANNIpckeLKHLRRSICPIDDLLCVMDIA 79
Cdd:cd04951    1 KILYVITGLGLGGAEKQTVLLADQMFirgHDVNIVYLTGEV----EVKPLNNNII----IYNLGMDKNPRSLLKALLKLK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  80 QIIKNFAPDIVFissskagALGTAAAIFCRwFGRKFTLIYR-IDWAFNDPRPALERKIYIVIENFLSKFRDIIIQN--DQ 156
Cdd:cd04951   73 KIISAFKPDVVH-------SHMFHANIFAR-FLRMLYPIPLlICTAHNKNEGGRIRMFIYRLTDFLCDITTNVSREalDE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 157 FDLRTAKingikPKLGFKIIHNGIDGNALDFldKNDARNFFHNKLNTDLNQFdlIIGTIANYYKTKGLSYLLDAMAELSK 236
Cdd:cd04951  145 FIAKKAF-----SKNKSVPVYNGIDLNKFKK--DINVRLKIRNKLNLKNDEF--VILNVGRLTEAKDYPNLLLAISELIL 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 237 TK-NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVG 315
Cdd:cd04951  216 SKnDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAG 295

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818621103 316 AIPEILENgvNGWIVESENQKQIVEKILWFSAH-PDDRHSFGISAKQRAKnQFALNTMLSKYRQLF 380
Cdd:cd04951  296 GVAEVVGD--HNYVVPVSDPQLLAEKIKEIFDMsDEERDILGNKNEYIAK-NFSINTIVNEWERLY 358
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 80-378 1.55e-31

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: 122.35  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  80 QIIKNFAPDIVFissSKAGALGTAAAIFcrWFGRKFTLIYRID-WAFNDPRPALERKIYIVienflsKFRDIIIQNDQFD 158
Cdd:cd03820   81 KYLKNNKPDVVI---SFRTSLLTFLALI--GLKSKLIVWEHNNyEAYNKGLRRLLLRRLLY------KRADKIVVLTEAD 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 159 LRTAKINGIKPklgFKIIHNGIDGNALDFLDKNDARNFfhnklntdlnqfdLIIGTIANYyktKGLSYLLDAMAELSKtK 238
Cdd:cd03820  150 KLKKYKQPNSN---VVVIPNPLSFPSEEPSTNLKSKRI-------------LAVGRLTYQ---KGFDLLIEAWALIAK-K 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 239 NIGCIL--VGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIAT--KV 314
Cdd:cd03820  210 HPDWKLriYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFdcPT 289

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818621103 315 GAiPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKnQFALNTMLSKYRQ 378
Cdd:cd03820  290 GP-SEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAE-RFSIEKIIKQWEE 351
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 175-383 7.99e-31

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: 120.90  E-value: 7.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 175 IIHNGIDGNALDFLDKNDARNffhnKLNTDLNQFdlIIGTIANYY--KTKGLSYLLDAMAELSKTKNIGCILVG-DGPER 251
Cdd:cd03825  165 VIPNGIDTEIFAPVDKAKARK----RLGIPQDKK--VILFGAESVtkPRKGFDELIEALKLLATKDDLLLVVFGkNDPQI 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 252 KILE-KIIKQRGLENRVFLAgqisDAYKylkACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIV 330
Cdd:cd03825  239 VILPfDIISLGYIDDDEQLV----DIYS---AADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLV 311

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 818621103 331 ESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKYRQLFRAI 383
Cdd:cd03825  312 PPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 139-348 1.27e-29

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: 117.77  E-value: 1.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 139 VIENFLSKF---RDIIIQNDQFDLRTAKINGIKPKlgFKIIHNGIDGNALDFLDKNDARNffHNKLNTDlnqfDLIIGTI 215
Cdd:cd03817  136 VVRKLVRRFynhTDAVIAPSEKIKDTLREYGVKGP--IEVIPNGIDLDKFEKPLNTEERR--KLGLPPD----EPILLYV 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 216 ANYYKTKGLSYLLDAMAELSKTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDA--YKYLKACDIFVLPSAKE 293
Cdd:cd03817  208 GRLAKEKNIDFLLRAFAELKKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREelPEYYKAADLFVFASTTE 287

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 818621103 294 GFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENqkqivEKILWFSAH 348
Cdd:cd03817  288 TQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPND-----ETLAEKLLH 337
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 175-379 2.15e-26

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 108.31  E-value: 2.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 175 IIHN-GIDGNALDFLDKNDARnffHNKLNtdlnqfdliIGTIANYYKTKGLSYLLDAMAEL-SKTKNIGCILVGDGPERK 252
Cdd:cd03799  151 IVHRsGIDCNKFRFKPRYLPL---DGKIR---------ILTVGRLTEKKGLEYAIEAVAKLaQKYPNIEYQIIGDGDLKE 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 253 ILEKIIKQRGLENRVFLAG--QISDAYKYLKACDIFVLPSA------KEGFPWTILEAMLAGLPIIATKVGAIPEILENG 324
Cdd:cd03799  219 QLQQLIQELNIGDCVKLLGwkPQEEIIEILDEADIFIAPSVtaadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDG 298

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 818621103 325 VNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMlskYRQL 379
Cdd:cd03799  299 VSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKL---NDEL 350
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 78-376 2.32e-26

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: 108.97  E-value: 2.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  78 IAQIIKNFAPDIVFISSSKAgALGTAAAIFCRWFGRKFTLIYR---IDWAFNDP--RPALERKIYIVIENF-LSKFRDII 151
Cdd:cd03794   90 LKLLVREERPDVIIAYSPPI-TLGLAALLLKKLRGAPFILDVRdlwPESLIALGvlKKGSLLKLLKKLERKlYRLADAII 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 152 IQNDQF--DLRTAKINGIKpklgFKIIHNGIDgnaLDFLDKNDARNFFHNKLNTDlnqfDLIIGTIANYYKTKGLSYLLD 229
Cdd:cd03794  169 VLSPGLkeYLLRKGVPKEK----IIVIPNWAD---LEEFKPPPKDELRKKLGLDD----KFVVVYAGNIGKAQGLETLLE 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 230 AMAELSKTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKY-LKACDIFVLPSAKE-----GFPWTILEAM 303
Cdd:cd03794  238 AAERLKRRPDIRFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPElLSAADVGLVPLKDNpanrgSSPSKLFEYM 317

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818621103 304 LAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKY 376
Cdd:cd03794  318 AAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 3-310 2.70e-24

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 102.37  E-value: 2.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVTQSEFGGAQHFMFNLGFNI-QNEYKILVCAGADGGGEFLKILQANNipCKELKHLRRSICPIddlLCVMDIAQI 81
Cdd:cd03812    1 KILHIVGGMNVGGIETFLMNLYRKLdKSKIEFDFLATSDDKGEYDEELEELG--GKIFYIPPKKKNII---KYFIKLLKL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  82 IKNFAPDIVFI-SSSKAGALGTAAAIFcrwfGRKftliYRIDWAFNDPRpalERKIYIVIENFLskFRDIIIQNDqfdlr 160
Cdd:cd03812   76 IKKEKYDIVHVhGSSSNGIILLLAAKA----GVP----VRIAHSHNTKD---SSIKLRKIRKNV--LKKLIERLS----- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 161 TAKIN----------GIKPKLGFKIIHNGIDGNALDFLDKN-DARNFFHNKLNtdlnqfDLIIGTIANYYKTKGLSYLLD 229
Cdd:cd03812  138 TKYLAcsedagewlfGEVENGKFKVIPNGIDIEKYKFNKEKrRKRRKLLILED------KLVLGHVGRFNEQKNHSFLID 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 230 AMAEL-SKTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLP 308
Cdd:cd03812  212 IFEELkKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLP 291


                 ..
gi 818621103 309 II 310
Cdd:cd03812  292 CL 293
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 159-381 1.07e-23

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: 100.89  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 159 LRTAKINGIKPKLGFKIIHNGIDgnaLDFLDKNDARNFFHNKLNTDLNQfdlIIGTIANYYKTKGLSYLLDAMAELSKTK 238
Cdd:cd04962  152 LRQETYELFDVDKDIEVIHNFID---EDVFKRKPAGALKRRLLAPPDEK---VVIHVSNFRPVKRIDDVVRVFARVRRKI 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 239 NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIP 318
Cdd:cd04962  226 PAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIP 305

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818621103 319 EILENGVNGWIVE-------SENQKQIVEkilwfsahpDDRHS--FGISAKQRAKNQFALNTMLSKYRQLFR 381
Cdd:cd04962  306 EVVKHGETGFLSDvgdvdamAKSALSILE---------DDELYnrMGRAARKRAAERFDPERIVPQYEAYYR 368
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 174-381 3.80e-23

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


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 100.49  E-value: 3.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 174 KIIHNGIDGNALDfldknDARNFFHNKLNtdlnqfdLIIGTIANYYKTKGLSYLLDAMAELSKtKNIGCI--LVGDGPER 251
Cdd:cd03813  270 RVIPNGIDIQRFA-----PAREERPEKEP-------PVVGLVGRVVPIKDVKTFIRAFKLVRR-AMPDAEgwLIGPEDED 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 252 KILEK----IIKQRGLENRVFLAG--QISDAYKYLkacDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGV 325
Cdd:cd03813  337 PEYAQeckrLVASLGLENKVKFLGfqNIKEYYPKL---GLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGAD 413

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818621103 326 N-----GWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKYRQLFR 381
Cdd:cd03813  414 DalgqaGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 222-330 5.70e-23

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: 96.32  E-value: 5.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 222 KGLSYLLDAMAELSKTK-NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISD---AYKYLKACDIFVLPSAKEGFPW 297
Cdd:cd01635  123 KGIDLLLEALALLKARLpDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDdevLELLLAAADVFVLPSRSEGFGL 202

                         90       100       110
                 ....*....|....*....|....*....|...
gi 818621103 298 TILEAMLAGLPIIATKVGAIPEILENGVNGWIV 330
Cdd:cd01635  203 VLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 3-382 3.60e-22

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 96.63  E-value: 3.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   3 KILFIVT---QSEFGGAQHFMFNLGFNIQNE-YKILVCAGADGG------GEFLKILQANNIPCKELKHLRRSICPIDDL 72
Cdd:cd03823    1 KILLVNSlypPQRVGGAEISVHDLAEALVAEgHEVAVLTAGVGPpgqatvARSVVRYRRAPDETLPLALKRRGYELFETY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  73 LCVM--DIAQIIKNFAPDIVFISSskagALG-TAAAIF-CRWFGRKFTLIYRiDWAFNDPRPALERKIyivienflskfR 148
Cdd:cd03823   81 NPGLrrLLARLLEDFRPDVVHTHN----LSGlGASLLDaARDLGIPVVHTLH-DYWLLCPRQFLFKKG-----------G 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 149 DIIIQNDQFDLRTAKINGIKPKLgFKIIHNGIDGN--ALDFLDKNDARNFFhnklntdlnqfdLIIGTIANYyktKGLSY 226
Cdd:cd03823  145 DAVLAPSRFTANLHEANGLFSAR-ISVIPNAVEPDlaPPPRRRPGTERLRF------------GYIGRLTEE---KGIDL 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 227 LLDAmAELSKTKNIGCILVGDGPErkileKIIKQRGLENRVFLAGQIS--DAYKYLKACDIFVLPSA-KEGFPWTILEAM 303
Cdd:cd03823  209 LVEA-FKRLPREDIELVIAGHGPL-----SDERQIEGGRRIAFLGRVPtdDIKDFYEKIDVLVVPSIwPEPFGLVVREAI 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 304 LAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPD--DRHSFGISAKQRAKNQfalntmLSKYRQLFR 381
Cdd:cd03823  283 AAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPAllERLRAGAEPPRSTESQ------AEEYLKLYR 356


                 .
gi 818621103 382 A 382
Cdd:cd03823  357 D 357
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 78-364 2.91e-20

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: 91.20  E-value: 2.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  78 IAQIIKNFAPDIVFISSSkaGALGTAAAIFCRWFGRKFTLIYRIDW----AFNDPRPaLERKIYivieNFLSKFrdiiiq 153
Cdd:cd03814   76 VRRLIKEFQPDIIHIATP--GPLGLAALRAARRLGLPVVTSYHTDFpeylSYYTLGP-LSWLAW----AYLRWF------ 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 154 ndqfdlrtakingikpklgfkiiHNGIDGN------ALDFLDKNDARNFFHNKLNTDLNQFD------------------ 209
Cdd:cd03814  143 -----------------------HNPFDTTlvpspsIARELEGHGFERVRLWPRGVDTELFHpsrrdaalrrrlgppgrp 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 210 --LIIGTIANYyktKGLSYLLDAMAELSKTKNIGCILVGDGPERKILEkiikQRGLeNRVFLAGQISDAY-KYLKACDIF 286
Cdd:cd03814  200 llLYVGRLAPE---KNLEALLDADLPLAASPPVRLVVVGDGPARAELE----ARGP-DVIFTGFLTGEELaRAYASADVF 271

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818621103 287 VLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAK 364
Cdd:cd03814  272 VFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAE 349
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 222-367 2.84e-19

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: 88.45  E-value: 2.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 222 KGLSYLLDAMAELSKTKNIGCILVGDGPERKI-------LEKIIKQRGLENRVFLAGQISDA--YKYLKACDIFVLPSAK 292
Cdd:cd03800  233 KGIDTLVRAFAQLPELRELANLVLVGGPSDDPlsmdreeLAELAEELGLIDRVRFPGRVSRDdlPELYRAADVFVVPSLY 312

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818621103 293 EGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQF 367
Cdd:cd03800  313 EPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHY 387
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 87-361 7.42e-18

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: 84.34  E-value: 7.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  87 PDIVFISsskaGALGTAAAIFCRWfGRKFTLIYRID-------WAFnDPRPALERKIYIVIENFLSKFRDIIIQNDQFDL 159
Cdd:cd03821   91 YDVVHIH----GVWTYTSLAACKL-ARRRGIPYVVSphgmldpWAL-QQKHWKKRIALHLIERRNLNNAALVHFTSEQEA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 160 RTAKINGIKPKLgfKIIHNGIDgnaLDFLDKNDARNFFHNKLNTDlnQFDLIIGTIanyYKTKGLSYLLDAMAELS-KTK 238
Cdd:cd03821  165 DELRRFGLEPPI--AVIPNGVD---IPEFDPGLRDRRKHNGLEDR--RIILFLGRI---HPKKGLDLLIRAARKLAeQGR 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 239 NIGCILVG--DGPERKILeKIIKQRGLENRVFLAGQISDAYKY--LKACDIFVLPSAKEGFPWTILEAMLAGLP-IIATK 313
Cdd:cd03821  235 DWHLVIAGpdDGAYPAFL-QLQSSLGLGDRVTFTGPLYGEAKWalYASADLFVLPSYSENFGNVVAEALACGLPvVITDK 313

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 818621103 314 VGaIPEILENGvNGWIVESENQkQIVEKILWFSAHPDDRHSFGISAKQ 361
Cdd:cd03821  314 CG-LSELVEAG-CGVVVDPNVS-SLAEALAEALRDPADRKRLGEMARR 358
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 173-343 1.55e-17

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 83.18  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 173 FKIIHNGIDgnALDFLDKNDARNFFHNKLNTDlnqFDLIIGTIANYyktKGLSYLLDAMAELsKTKNIGCILV---GDGP 249
Cdd:cd03809  164 IVVIPLGVD--PSFFPPESAAVLIAKYLLPEP---YFLYVGTLEPR---KNHERLLKAFALL-KKQGGDLKLVivgGKGW 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 250 ERKILEKIIKQRGLENRVFLAGQISDA--YKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENgvNG 327
Cdd:cd03809  235 EDEELLDLVKKLGLGGRVRFLGYVSDEdlPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGD--AA 312

                        170
                 ....*....|....*.
gi 818621103 328 WIVESENQKQIVEKIL 343
Cdd:cd03809  313 LYFDPLDPESIADAIL 328
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 228-367 3.14e-16

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


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 79.81  E-value: 3.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 228 LDAMAELSKTKNIGCILVGDGPERKILEKIIKQRgLEN-RVFLAGQI--SDAYKYLK--ACDIFVLPSAKEGFPWTILEA 302
Cdd:cd04946  246 LNSLCVAHPSICISWTHIGGGPLKERLEKLAENK-LENvKVNFTGEVsnKEVKQLYKenDVDVFVNVSESEGIPVSIMEA 324

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818621103 303 MLAGLPIIATKVGAIPEILENGVNGWIVESE-NQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQF 367
Cdd:cd04946  325 ISFGIPVIATNVGGTREIVENETNGLLLDKDpTPNEIVSSIMKFYLDGGDYKTMKISARECWEERF 390
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 211-365 4.52e-15

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


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 75.42  E-value: 4.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 211 IIGTIANYYKTKGLSYLLDAMAELSKT-KNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLP 289
Cdd:cd04949  162 KIITISRLAPEKQLDHLIEAVAKAVKKvPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLT 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818621103 290 SAKEGFPWTILEAMLAGLPIIATKV--GAiPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKN 365
Cdd:cd04949  242 SQMEGFGLTLMEAIGHGLPVVSYDVkyGP-SELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEK 318
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 222-321 1.54e-14

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


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 74.58  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 222 KGLSYLLDAMAEL-SKTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQI--SDAYKYLKACDIFVLPSAKEGFPWT 298
Cdd:cd03796  206 KGIDLLVGIIPRIcKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVphEEVRDVLVQGHIFLNTSLTEAFCIA 285

                         90       100
                 ....*....|....*....|...
gi 818621103 299 ILEAMLAGLPIIATKVGAIPEIL 321
Cdd:cd03796  286 IVEAASCGLLVVSTRVGGIPEVL 308
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 222-361 5.15e-14

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 73.21  E-value: 5.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 222 KGLSYLLDAMAELSktkNIGCILVGDGPERKILEKIIKqrGLeNRVF---LAG-QISDAYKYLkacDIFVLPSAKEGFPW 297
Cdd:PLN02871 276 KNLDFLKRVMERLP---GARLAFVGDGPYREELEKMFA--GT-PTVFtgmLQGdELSQAYASG---DVFVMPSESETLGF 346

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818621103 298 TILEAMLAGLPIIATKVGAIPEILEN---GVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQ 361
Cdd:PLN02871 347 VVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAARE 413
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 211-380 1.01e-11

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: 65.81  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 211 IIGTIANYYKTKGLSYLLDAMAELsKTKNIGC--ILVG----DGPE-RKILEKIIKQRGLENRVFL-----AGQISDAYk 278
Cdd:cd03792  199 YILQVARFDPSKDPLGVIDAYKLF-KRRAEEPqlVICGhgavDDPEgSVVYEEVMEYAGDDHDIHVlrlppSDQEINAL- 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 279 yLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVES--ENQKQIVEKIlwfsAHPDDRHSFG 356
Cdd:cd03792  277 -QRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSveGAAVRILRLL----TDPELRRKMG 351

                        170       180
                 ....*....|....*....|....
gi 818621103 357 ISAKQRAKNQFALNTMLSKYRQLF 380
Cdd:cd03792  352 LAAREHVRDNFLITGNLRAWLYLI 375
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 220-371 1.30e-11

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


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 65.55  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 220 KTKGLSYLLDAMAELS-KTKNIGCILVGDGPERKILEKIikQRGLENRVFLAGQ-ISDAYKYLKACDIFVLPSA------ 291
Cdd:cd05844  200 EKKGCDVLIEAFRRLAaRHPTARLVIAGDGPLRPALQAL--AAALGRVRFLGALpHAEVQDWMRRAEIFCLPSVtaasgd 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 292 KEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNT 371
Cdd:cd05844  278 SEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRV 357
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 129-380 2.92e-11

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 65.06  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 129 RPALERKIYIVIENFLSKFRDI-IIQNDQFDL-RTAKINGIkPKLGFKIIHNGIDGNALDFLDKNDARNFFHNKLNTDLN 206
Cdd:PRK15179 439 RPDRYRVEYDIIYSELLKMRGVaLSSNSQFAAhRYADWLGV-DERRIPVVYNGLAPLKSVQDDACTAMMAQFDARTSDAR 517

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 207 QfdlIIGTIANYYKTKGLSYLLDAMAELSKTK-NIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDI 285
Cdd:PRK15179 518 F---TVGTVMRVDDNKRPFLWVEAAQRFAASHpKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNA 594

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 286 FVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWI-----VESENQKQIVEKIlwfsaHPDDRHSFGIS-- 358
Cdd:PRK15179 595 FLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTlpadtVTAPDVAEALARI-----HDMCAADPGIArk 669

                        250       260
                 ....*....|....*....|..
gi 818621103 359 AKQRAKNQFALNTMLSKYRQLF 380
Cdd:PRK15179 670 AADWASARFSLNQMIASTVRCY 691
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 272-377 1.02e-10

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 62.77  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 272 QISDAYKYLKAcdIFVLPsakegfpWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWFSAHPDD 351
Cdd:cd03818  299 QLSDAHVYLTY--PFVLS-------WSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDR 369

                         90       100
                 ....*....|....*....|....*.
gi 818621103 352 RHSFGISAKQRAKNQFALNTMLSKYR 377
Cdd:cd03818  370 AAALRRAARRTVERSDSLDVCLARYL 395
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
243-331 1.26e-10

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 63.18  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 243 ILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILE 322
Cdd:PRK15490 433 VLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFI 512


                 ....*....
gi 818621103 323 NGVNGWIVE 331
Cdd:PRK15490 513 EGVSGFILD 521
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
78-347 6.63e-09

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 57.03  E-value: 6.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  78 IAQIIKNFAPDIVfISSSKAGALgtAAAIFCRWFGRKFTLIYRIDWAFNDPRPALERKI-----YIVIEnflSKFRDIII 152
Cdd:PRK09922  76 FSKWLKETQPDIV-ICIDVISCL--YANKARKKSGKQFKIFSWPHFSLDHKKHAECKKItcadyHLAIS---SGIKEQMM 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 153 QndqFDLRTAKINgikpklgfkIIHNGIDGNA--LDFLDKNDARNFFHnklntdlnqfdliIGTIaNYYKTKGLSYLLDA 230
Cdd:PRK09922 150 A---RGISAQRIS---------VIYNPVEIKTiiIPPPERDKPAVFLY-------------VGRL-KFEGQKNVKELFDG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 231 MAELskTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYL----KACDIFVLPSAKEGFPWTILEAMLAG 306
Cdd:PRK09922 204 LSQT--TGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVqqkiKNVSALLLTSKFEGFPMTLLEAMSYG 281

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 818621103 307 LPIIATKVGAIPE-ILENGVNGWIVESENQKQIVEKILWFSA 347
Cdd:PRK09922 282 IPCISSDCMSGPRdIIKPGLNGELYTPGNIDEFVGKLNKVIS 323
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 156-381 5.32e-08

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 54.31  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 156 QFDLRTAKIngiKPKLGFKIIHNGIDGNALDFLDKNDARNFFHNKLntdlnqfdlIIGTIANYYKTKGLSYLLDAMAEL- 234
Cdd:cd03822  146 RFLLVRIKL---IPAVNIEVIPHGVPEVPQDPTTALKRLLLPEGKK---------VILTFGFIGPGKGLEILLEALPELk 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 235 SKTKNIGCILVG-DGPE------RKILEKIIKQRGLENRVFLAGQI---SDAYKYLKACDIFVLP--SAKEGFPWTILEA 302
Cdd:cd03822  214 AEFPDVRLVIAGeLHPSlaryegERYRKAAIEELGLQDHVDFHNNFlpeEEVPRYISAADVVVLPylNTEQSSSGTLSYA 293

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818621103 303 MLAGLPIIATKVGAIPEILENGvNGWIVESENQKQIVEKILWFSAHPDDRHSFgISAKQRAKNQFALNTMLSKYRQLFR 381
Cdd:cd03822  294 IACGKPVISTPLRHAEELLADG-RGVLVPFDDPSAIAEAILRLLEDDERRQAI-AERAYAYARAMTWESIADRYLRLFN 370
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
169-328 2.00e-07

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 52.48  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 169 PKLGFKIIHNGIDGNALDFLDKNDARNffhnKLNTDLNqfDLIIGTIANYYKTKGLSYLLDAMAELSKT-KNIGCILVGD 247
Cdd:PRK15484 159 PNADISIVPNGFCLETYQSNPQPNLRQ----QLNISPD--ETVLLYAGRISPDKGILLLMQAFEKLATAhSNLKLVVVGD 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 248 GPERKILEKIIKQR-------GLENRVFLAGQIS--DAYKYLKACDIFVLPSA-KEGFPWTILEAMLAGLPIIATKVGAI 317
Cdd:PRK15484 233 PTASSKGEKAAYQKkvleaakRIGDRCIMLGGQPpeKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTKGGI 312

                        170
                 ....*....|.
gi 818621103 318 PEILENGVNGW 328
Cdd:PRK15484 313 TEFVLEGITGY 323
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 127-372 2.37e-07

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


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 52.21  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 127 DPRPALERKIYIV----IENFLSKFRDIIIQNDQFdlrTAKINgikpKLGFKIIHNGIDGN-----ALDFLDKNDARNFF 197
Cdd:cd03805  130 AQRKSLLKRLYRKpfdwLEEFTTGMADQIVVNSNF---TAGVF----KKTFPSLAKNPPEVlypcvDTDSFDSTSEDPDP 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 198 HNKLntdLNQFDLIIGTIANYYKTKGLSYLLDAMAELSKTKNIG---CILVGDGPERKILEKII----------KQRGLE 264
Cdd:cd03805  203 GDLI---AKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPEFenvRLVIAGGYDPRVAENVEyleelqrlaeELLNVE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 265 NRV-FLAgQISDAYKY--LKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESeNQKQIVEK 341
Cdd:cd03805  280 DQVlFLR-SISDSQKEqlLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEA 357

                        250       260       270
                 ....*....|....*....|....*....|.
gi 818621103 342 ILWFSAHPDDRHSFGISAKQRAKNQFALNTM 372
Cdd:cd03805  358 MLKLANDPDLADRMGAAGRKRVKEKFSREAF 388
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 299-383 4.15e-07

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


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 51.52  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 299 ILEAMLAGLPIIATKVGAIPEILENGVNGWIVES-ENQKQIVEKILWFsahpdDRHsfgiSAKQRAKNQFALNTMLSKYR 377
Cdd:cd03802  257 MIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSvEEMAEAIANIDRI-----DRA----ACRRYAEDRFSAARMADRYE 327


                 ....*.
gi 818621103 378 QLFRAI 383
Cdd:cd03802  328 ALYRKV 333
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 243-351 4.91e-07

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


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 51.13  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 243 ILVGDGPERKILEKIIKqrglENRVFLaGQISDAYK--YLKACDIFVLPsAKEGFPWTILEAMLAGLPIIATKVGAIPEI 320
Cdd:cd03804  229 VVIGDGPDLDRLRAMAS----PNVEFL-GYQPDEVLkeLLSKARAFVFA-AEEDFGIVPVEAQACGTPVIAFGKGGALET 302

                         90       100       110
                 ....*....|....*....|....*....|.
gi 818621103 321 LENGVNGWIVESENQKQIVEKILWFSAHPDD 351
Cdd:cd03804  303 VRPGPTGILFGEQTVESLKAAVEEFEQNFDR 333
PLN00142 PLN00142
sucrose synthase
 231-345 6.48e-07

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 51.52  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 231 MAELSKTKNI-----------------------GCILVGDGPERKILEKIIKQRGLENRVFLAGQI------------SD 275
Cdd:PLN00142 579 MARLDRVKNLtglvewygknkrlrelvnlvvvgGFIDPSKSKDREEIAEIKKMHSLIEKYNLKGQFrwiaaqtnrvrnGE 658

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818621103 276 AYKYLkaCD---IFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKILWF 345
Cdd:PLN00142 659 LYRYI--ADtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKIADF 729
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
223-386 2.36e-06

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 49.20  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 223 GLSYLLDAMAELSKTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAY-KYLKACDIFVLP----SAKEGFPw 297
Cdd:PRK10307 243 GLELVIDAARRLRDRPDLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLpALLKMADCHLLPqkagAADLVLP- 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 298 TILEAMLA-GLPIIATkvgAIPE------ILENGVngwIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALN 370
Cdd:PRK10307 322 SKLTNMLAsGRNVVAT---AEPGtelgqlVEGIGV---CVEPESVEALVAAIAALARQALLRPKLGTVAREYAERTLDKE 395

                        170
                 ....*....|....*.
gi 818621103 371 TMLSKYRQLFRAIIDK 386
Cdd:PRK10307 396 NVLRQFIADIRGLVAE 411
PLN02605 PLN02605
monogalactosyldiacylglycerol synthase
 278-350 4.70e-06

monogalactosyldiacylglycerol synthase


Pssm-ID: 215325 [Multi-domain]  Cd Length: 382  Bit Score: 48.43  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 278 KYLKACDIFVlpsAKEGfPWTILEAMLAGLPIIAT------KVGAIPEILENGVNgwiVESENQKQIVEKIL-WFSAHPD 350
Cdd:PLN02605 278 EWMGACDCII---TKAG-PGTIAEALIRGLPIILNgyipgqEEGNVPYVVDNGFG---AFSESPKEIARIVAeWFGDKSD 350
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 262-380 1.36e-05

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 46.85  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 262 GLENRV-FLAGQ-ISDaykYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILEN--------GVNGWIVE 331
Cdd:NF038011 364 GLQDKVkFLGFQkIDD---LLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIEGldeedralGAAGEVVA 440

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 818621103 332 SENQKQIVEKILWFSAHPDDRHSFGISAKQRAKNQFALNTMLSKYRQLF 380
Cdd:NF038011 441 IADPQALARAALDLLRDPQRWQAAQAAGLARVERYYTEELMFDRYRELY 489
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
 228-368 2.28e-05

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). 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: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 46.16  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 228 LDAMAE-LSKTKNIGCILVGDGPERKILEKIIKQRGLENRVFLAGQISDAYKYLKACDIFVlpsAKEGfPWTILEAMLAG 306
Cdd:cd17507  212 VKETVEaLLDSLRAGQVLVVCGKNKKLYEKLSGLEEDYINVRVLGYVDDMNELMAASDLVI---TKPG-GLTISEALARG 287

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818621103 307 LPIIATK------VGAIPEILENGVNGWIVESENQKQIVEKILwfsaHPDDRHSFGISAKQRAKNQFA 368
Cdd:cd17507  288 LPVIIYDpipgqeEENADFLENNGAGIIARDPEELLEIVARLI----DPPSLLRMMSEAAKELKPPAA 351
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 285-343 9.54e-05

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 44.77  E-value: 9.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 818621103   285 IFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVESENQKQIVEKIL 343
Cdd:TIGR02468  574 VFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALL 632
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
 225-332 1.25e-04

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 43.80  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 225 SYLLDAMAELSKTK--------NIGCILVGDGPERKILEKIIKQRGLEN----RVFLAgqISDAYKYLKACDIFV-LPSA 291
Cdd:cd03816  244 SILLDALKAYESSAatepallpSLLCIITGKGPLKEMYLELIKELKLKKvtirTPWLS--AEDYPRLLASADLGVcLHTS 321

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 818621103 292 KEG--FPWTILEAMLAGLPIIATKVGAIPEILENGVNGWIVES 332
Cdd:cd03816  322 SSGldLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGD 364
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 266-322 2.27e-04

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 42.77  E-value: 2.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 818621103  266 RVFLAGQISDA-YKYLKAC-DIFVLPSAKEGFPWTILEAMLAGLPIIATkvgAIPEILE 322
Cdd:TIGR04047 258 PVVITGPVPDAdLPALYRCaDAFAFPSLKEGFGLVVLEALASGIPVVAS---DIAPFTE 313
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
299-367 4.92e-04

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 38.74  E-value: 4.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818621103  299 ILEAMLAGLPIIATKVGAIPEILENGVNGWIVESEnqKQIVEKILWFSAHPDDRHSFGISAKQRAKNQF 367
Cdd:pfam13524  16 VFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDP--EELAEKIRYLLEHPEERRAIAAAGRERVLAEH 82
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
14-181 6.83e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 40.21  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   14 GGAQHFMFNLGFNIQNE-YKILVCAGADGGGEFLKILQANNIPCKELKHLRRsicPIDDLLCVMDIAQIIKNFAPDIVFI 92
Cdd:pfam13439   1 GGVERYVLELARALARRgHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPR---LLRSLAFLRRLRRLLRRERPDVVHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103   93 SSskAGALGTAAAIFCRWFGRKFTLIY---RIDWAFNDPRPALERKIYIVIENFLSKFRDIIIQNDQFDLRT-AKINGIK 168
Cdd:pfam13439  78 HS--PFPLGLAALAARLRLGIPLVVTYhglFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADElRRLYGVP 155

                         170
                  ....*....|...
gi 818621103  169 PKLgFKIIHNGID 181
Cdd:pfam13439 156 PEK-IRVIPNGVD 167
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
57-363 9.40e-04

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 40.68  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103  57 KELKHLRRSICPIDDLLCVMDIAQIIKNFAPDIVFISSskagalGTAAAIFCRwfGRKFTLIYridWAFNDPrPALERKI 136
Cdd:COG4641   20 AALGHEVTFLEPDDPWHDPLYAAELLDAFRPDLVLVIS------GVELVAALR--ARGIPTVF---WDTDDP-VTLDRFR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 137 YIvienfLSKFrDIIIQNDQFDLRTAKINGIkPKLGFkiIHNGIDGNaldfldkndarnfFHNKLNTDlNQFDLIIGTIA 216
Cdd:COG4641   88 EL-----LPLY-DLVFTFDGDCVEEYRALGA-RRVFY--LPFAADPE-------------LHRPVPPE-ARFRYDVAFVG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 217 NYY--KTKGLSYLLDAMAELsktkniGCILVGDG-PERKILEKIIKQRGLENRvflagqisDAYKYLKACDIFV-LPSAK 292
Cdd:COG4641  145 NYYpdRRARLEELLLAPAGL------RLKIYGPGwPKLALPANVRRGGHLPGE--------EHPAAYASSKITLnVNRMA 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818621103 293 EgFPWTI----LEAMLAGLPIIATKVGAIPEILENGVNgwIVESENQKQIVEKILWFSAHPDDRHSFGISAKQRA 363
Cdd:COG4641  211 A-SPDSPtrrtFEAAACGAFLLSDPWEGLEELFEPGEE--VLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRV 282
PHA01630 PHA01630
putative group 1 glycosyl transferase
 275-336 2.15e-03

putative group 1 glycosyl transferase


Pssm-ID: 164861  Cd Length: 331  Bit Score: 39.77  E-value: 2.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818621103 275 DAYKYLKACDIFVLPSAKEGFPWTILEAMLAGLPIIATKVGAIPE-ILENGVNGWIVESENQK 336
Cdd:PHA01630 202 DIYSLFAGCDILFYPVRGGAFEIPVIEALALGLDVVVTEKGAWSEwVLSNLDVYWIKSGRKPK 264
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 222-381 3.47e-03

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 39.47  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 222 KGLSYLLDAMAELSKtKNIGCILVGDGPERkiLEKiiKQRGLENR------------VFLAGQIsdaYkylKACDIFVLP 289
Cdd:cd03791  307 KGVDLILDALPELLE-EGGQLVVLGSGDPE--YEQ--AFRELAERypgkvavvigfdEALAHRI---Y---AGADFFLMP 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818621103 290 SAKEGFPWTILEAMLAGLPIIATKVGA-----IPEILENGV-NGWIVESENQKQIVEK----ILWFsAHPDDRHSFgisa 359
Cdd:cd03791  376 SRFEPCGLVQMYAMRYGTLPIVRRTGGladtvFDYDPETGEgTGFVFEDYDAEALLAAlrraLALY-RNPELWRKL---- 450

                        170       180
                 ....*....|....*....|...
gi 818621103 360 KQRAKNQ-FALNTMLSKYRQLFR 381
Cdd:cd03791  451 QKNAMKQdFSWDKSAKEYLELYR 473
 
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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