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Conserved domains on  [gi|1267023523|gb|ATM86485|]
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glycosyl transferase family 1 [Yersinia frederiksenii]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133419)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Escherichia coli alpha-1,3-mannosyltransferase WfcD that may transfer UDP, ADP, GDP, or CMP-linked sugars

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 3-358 5.06e-176

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: 493.33  E-value: 5.06e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPDsFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPINLEVASTPFSFQALEDFKK 82
Cdd:cd03795     1 KVLHVFKFYYPD-IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  83 LAQQADIIHYHFPFPFMDMVHFVASLNKPTVVSYHSDIVKQKNILKLYSPLMNRFLGDVSKIVAASPNYVATSETLKKFA 162
Cdd:cd03795    80 LAKEYDIIHYHFPNPLADLLLFFSGAKKPVVVHWHSDIVKQKKLLKLYKPLMTRFLRRADRIIATSPNYVETSPTLREFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 163 DKVCVIPYGLDEKSYPVSDPERLAFWRNKFGQRFFLFVGAFRYYKGLHILIEAAKNSSYPIVIVGAGPIESELKRQVLAL 242
Cdd:cd03795   160 NKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVIGGEGPLKPDLEAQIELN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 243 NISNISFLGAVSDEDKAALLSLCYAVVFPSHLRSEAFGITLLEGAMYGKPLISSEIGTGTTFININQKTGLVIPPSDPIA 322
Cdd:cd03795   240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDA 319

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1267023523 323 LRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMV 358
Cdd:cd03795   320 LAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
 
Name Accession Description Interval E-value
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 3-358 5.06e-176

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: 493.33  E-value: 5.06e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPDsFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPINLEVASTPFSFQALEDFKK 82
Cdd:cd03795     1 KVLHVFKFYYPD-IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  83 LAQQADIIHYHFPFPFMDMVHFVASLNKPTVVSYHSDIVKQKNILKLYSPLMNRFLGDVSKIVAASPNYVATSETLKKFA 162
Cdd:cd03795    80 LAKEYDIIHYHFPNPLADLLLFFSGAKKPVVVHWHSDIVKQKKLLKLYKPLMTRFLRRADRIIATSPNYVETSPTLREFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 163 DKVCVIPYGLDEKSYPVSDPERLAFWRNKFGQRFFLFVGAFRYYKGLHILIEAAKNSSYPIVIVGAGPIESELKRQVLAL 242
Cdd:cd03795   160 NKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVIGGEGPLKPDLEAQIELN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 243 NISNISFLGAVSDEDKAALLSLCYAVVFPSHLRSEAFGITLLEGAMYGKPLISSEIGTGTTFININQKTGLVIPPSDPIA 322
Cdd:cd03795   240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDA 319

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1267023523 323 LRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMV 358
Cdd:cd03795   320 LAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 193-347 1.62e-35

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: 127.39  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 193 GQRFFLFVGAFRYYKGLHILIEAAK-----NSSYPIVIVGAGPIESELKRQVLALNIS-NISFLGAVSDEDKAALLSLCY 266
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFAllkekNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVSDEDLPELLKIAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 267 AVVFPSHlrSEAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARA 346
Cdd:pfam00534  81 VFVLPSR--YEGFGIVLLEAMACGLPVIASDVG-GPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157


                  .
gi 1267023523 347 R 347
Cdd:pfam00534 158 R 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 260-370 2.98e-25

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 98.91  E-value: 2.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 260 ALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAK 339
Cdd:COG0438    16 ALLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1267023523 340 FGDNARARYLEHFTSEKMVSSYIELYNDIVS 370
Cdd:COG0438    93 LGEAARERAEERFSWEAIAERLLALYEELLA 123
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
133-362 1.36e-09

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 59.22  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 133 LMNRFlgD-VSKIvaaSPNYVATSETLKKFADKVCVIPYGLD-EKSYPVSDPERLAFwRNKFG----QRFFLFVGAFRYY 206
Cdd:PRK10307  168 LLRRF--DnVSTI---SRSMMNKAREKGVAAEKVIFFPNWSEvARFQPVADADVDAL-RAQLGlpdgKKIVLYSGNIGEK 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 207 KGLHILIEAAKN----SSYPIVIVGAGPIESELKRQVLALNISNISFLGAVSDEDKAALLSL--CYAV---------VFP 271
Cdd:PRK10307  242 QGLELVIDAARRlrdrPDLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMadCHLLpqkagaadlVLP 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 272 SHLRseafGItLLEGamyGKPLISSEIGT--GTTFINInqktGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYL 349
Cdd:PRK10307  322 SKLT----NM-LASG---RNVVATAEPGTelGQLVEGI----GVCVEPESVEALVAAIAALARQALLRPKLGTVAREYAE 389

                         250
                  ....*....|...
gi 1267023523 350 EHFTSEKMVSSYI 362
Cdd:PRK10307  390 RTLDKENVLRQFI 402
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 277-339 3.19e-03

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: 39.76  E-value: 3.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267023523  277 EAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAK 339
Cdd:TIGR02468  582 EPFGLTLIEAAAHGLPMVATKNG-GPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLWAE 643
 
Name Accession Description Interval E-value
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 3-358 5.06e-176

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: 493.33  E-value: 5.06e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPDsFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPINLEVASTPFSFQALEDFKK 82
Cdd:cd03795     1 KVLHVFKFYYPD-IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  83 LAQQADIIHYHFPFPFMDMVHFVASLNKPTVVSYHSDIVKQKNILKLYSPLMNRFLGDVSKIVAASPNYVATSETLKKFA 162
Cdd:cd03795    80 LAKEYDIIHYHFPNPLADLLLFFSGAKKPVVVHWHSDIVKQKKLLKLYKPLMTRFLRRADRIIATSPNYVETSPTLREFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 163 DKVCVIPYGLDEKSYPVSDPERLAFWRNKFGQRFFLFVGAFRYYKGLHILIEAAKNSSYPIVIVGAGPIESELKRQVLAL 242
Cdd:cd03795   160 NKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVIGGEGPLKPDLEAQIELN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 243 NISNISFLGAVSDEDKAALLSLCYAVVFPSHLRSEAFGITLLEGAMYGKPLISSEIGTGTTFININQKTGLVIPPSDPIA 322
Cdd:cd03795   240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDA 319

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1267023523 323 LRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMV 358
Cdd:cd03795   320 LAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-366 4.59e-62

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: 203.15  E-value: 4.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFyKTYYPDSFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYcSPINLEVASTPFSFQALEDFKK 82
Cdd:cd03801     1 KILLL-SPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVP-LLPSLAALLRARRLLRELRPLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  83 LAQQADIIHYHFPFPFMDMVHFVASLNKPTVVSYHSDIVKQKNilkLYSPLMNRFLGDVSKIVAASPNYVATSETLKKF- 161
Cdd:cd03801    79 RLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLL---LLLAAERRLLARAEALLRRADAVIAVSEALRDEl 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 162 -------ADKVCVIPYGLDEKSYpvSDPERLAFWRNKfGQRFFLFVGAFRYYKGLHILIEAA-----KNSSYPIVIVGA- 228
Cdd:cd03801   156 ralggipPEKIVVIPNGVDLERF--SPPLRRKLGIPP-DRPVLLFVGRLSPRKGVDLLLEALakllrRGPDVRLVIVGGd 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 229 GPIESELKRQVLALNiSNISFLGAVSDEDKAALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGTGTTFInIN 308
Cdd:cd03801   233 GPLRAELEELELGLG-DRVRFLGFVPDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVV-ED 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267023523 309 QKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSYIELYN 366
Cdd:cd03801   309 GEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 193-347 1.62e-35

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: 127.39  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 193 GQRFFLFVGAFRYYKGLHILIEAAK-----NSSYPIVIVGAGPIESELKRQVLALNIS-NISFLGAVSDEDKAALLSLCY 266
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFAllkekNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVSDEDLPELLKIAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 267 AVVFPSHlrSEAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARA 346
Cdd:pfam00534  81 VFVLPSR--YEGFGIVLLEAMACGLPVIASDVG-GPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157


                  .
gi 1267023523 347 R 347
Cdd:pfam00534 158 R 158
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 3-362 6.42e-33

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: 126.69  E-value: 6.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPDSfGGVEQVIFQLCEGGASRGIDSTVLS-------LSRRGTITNQKIGSHTVYCSPINLEVASTP---- 71
Cdd:cd03794     1 KILLISQYYPPPK-GAAAARVYELAKELVRRGHEVTVLTpspnyplGRIFAGATETKDGIRVIRVKLGPIKKNGLIrrll 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  72 ----FSFQALEDFKKLAQQADIIHYHFPFPFMDMVHFVAS--LNKPTVVSYHS---------DIVKQKNILKLYSPLMNR 136
Cdd:cd03794    80 nylsFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKklRGAPFILDVRDlwpeslialGVLKKGSLLKLLKKLERK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 137 FLGDVSKIVAASPNYVATSETLKKFADKVCVIPYGLDEKSYPVSDPERLAFWRNKfGQRF-FLFVGAFRYYKGLHILIEA 215
Cdd:cd03794   160 LYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLGL-DDKFvVVYAGNIGKAQGLETLLEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 216 AKN-SSYP---IVIVGAGPIESELKRQVLALNISNISFLGAVSDEDKAALLSLCYAVVFP---SHLRSEAFGITLLEGAM 288
Cdd:cd03794   239 AERlKRRPdirFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPlkdNPANRGSSPSKLFEYMA 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267023523 289 YGKPLISSeIGTGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSYI 362
Cdd:cd03794   319 AGKPILAS-DDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 21-356 1.57e-32

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: 124.77  E-value: 1.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  21 QVIFQLCEGGASRGIDSTVLSLSRRG----TITNQKIGSHTVYCSPINLEVASTPFsFQALEDFKKLA-----QQADIIH 91
Cdd:cd03819     3 MLTPALEIGGAETYILDLARALAERGhrvlVVTAGGPLLPRLRQIGIGLPGLKVPL-LRALLGNVRLArlirrERIDLIH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  92 YHFPFPfmDMVHFVAS--LNKPTVVSYHSDIVKQKNILKLYSPLMNRflgdVSKIVAASPNyvaTSETLKK----FADKV 165
Cdd:cd03819    82 AHSRAP--AWLGWLASrlTGVPLVTTVHGSYLATYHPKDFALAVRAR----GDRVIAVSEL---VRDHLIEalgvDPERI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 166 CVIPYGLDEKSY-PVSDPERLAFWRNKFGQRFFLFVGAFRYYKGLHILIEAA----KNSSYPIVIVGAGPIESELKRQVL 240
Cdd:cd03819   153 RVIPNGVDTDRFpPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAaelkDEPDFRLLVAGDGPERDEIRRLVE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 241 ALNISN-ISFLGAvsDEDKAALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGTGTTFINiNQKTGLVIPPSD 319
Cdd:cd03819   233 RLGLRDrVTFTGF--REDVPAALAASDVVVLPS--LHEEFGRVALEAMACGTPVVATDVGGAREIVV-HGRTGLLVPPGD 307

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1267023523 320 PIALRTAMDQLWNDVELAAKFGdnARARYLEHFTSEK 356
Cdd:cd03819   308 AEALADAIRAAKLLPEAREKLQ--AAAALTEAVRELL 342
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 17-361 2.42e-32

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: 124.24  E-value: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  17 GGVEQVIFQLCEGGASRGIDstVLSLSRRGTITNQKIGSHTVYCSPINLEVAST-PFS-FQALEDFKKL--AQQADIIHY 92
Cdd:cd03808    10 GGFQSFRLPLIKALVKKGYE--VHVIAPDGDKLSDELKELGVKVIDIPILRRGInPLKdLKALFKLYKLlkKEKPDIVHC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  93 HFPFPFMdMVHFVASLNKP-----TVVSYHSDIVKQKNILKLYSPLMNRFLGDVSKIVAASPNY--VATSETLKKFADKV 165
Cdd:cd03808    88 HTPKPGI-LGRLAARLAGVpkviyTVHGLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDrdLAIKKGIIKKKKTV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 166 CVIPYGLDEKSYPVSDPERLafwRNKFgqrFFLFVGAFRYYKGLHILIEAAKN--SSYP---IVIVGAGPIESELKRQVL 240
Cdd:cd03808   167 LIPGSGVDLDRFQYSPESLP---SEKV---VFLFVARLLKDKGIDELIEAAKIlkKKGPnvrFLLVGDGELENPSEILIE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 241 ALNIS-NISFLGAVSDedKAALLSLCYAVVFPSHlrSEAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSD 319
Cdd:cd03808   241 KLGLEgRIEFLGFRSD--VPELLAESDVFVLPSY--REGLPRSLLEAMAAGRPVITTDVP-GCRELVIDGVNGFLVPPGD 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1267023523 320 PIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSY 361
Cdd:cd03808   316 VEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 15-365 1.66e-31

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: 122.04  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  15 SFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKI--GSHtVYCspINLEVASTPFS-FQALEDFKKlaQQADIIH 91
Cdd:cd03807    10 NVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLaaGVP-VVC--LGLSSGKDPGVlLRLAKLIRK--RNPDVVH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  92 YHFPFPfmdmvHFVASL------NKPTVVSYHSDIVKQKNILKLYspLMNRFLGDVSkivaasPNYVATSETLKKF---- 161
Cdd:cd03807    85 TWMYHA-----DLIGGLaaklagGVKVIWSVRSSNIPQRLTRLVR--KLCLLLSKFS------PATVANSSAVAEFhqeq 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 162 ---ADKVCVIPYGLDEKSYPVSDPERLAFWRN---KFGQRFFLFVGAFRYYKGLHILIEAA-----KNSSYPIVIVGAGP 230
Cdd:cd03807   152 gyaKNKIVVIYNGIDLFKLSPDDASRARARRRlglAEDRRVIGIVGRLHPVKDHSDLLRAAallveTHPDLRLLLVGRGP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 231 IESELKRQVLALNISN-ISFLGAVSDedKAALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGtGTTFInINQ 309
Cdd:cd03807   232 ERPNLERLLLELGLEDrVHLLGERSD--VPALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVG-GAAEL-VDD 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267023523 310 KTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSYIELY 365
Cdd:cd03807   306 GTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLY 361
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 17-363 1.01e-30

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: 119.65  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  17 GGVEQVIFQLCEGGASRGIDSTVLSLSRRG---------TITNQKIGSHTVYCSPINLevaSTPFSFQALEDFKKLaQQA 87
Cdd:cd03820    13 GGAERVAINLANHLAKKGYDVTIISLDSAEkppfyelddNIKIKNLGDRKYSHFKLLL---KYFKKVRRLRKYLKN-NKP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  88 DIIhyhFPFPFMDMVhFVAS--LNKPTVVSYHSDIVKQKNIlklYSPLMNRFLG--DVSKIVAASPNYVatSETLKKFAD 163
Cdd:cd03820    89 DVV---ISFRTSLLT-FLALigLKSKLIVWEHNNYEAYNKG---LRRLLLRRLLykRADKIVVLTEADK--LKKYKQPNS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 164 KVCVIPYGLDEKSYPVSDPerlafwrnkFGQRFFLFVGAFRYYKGLHILIEAAKNSS-----YPIVIVGAGPIESELKRQ 238
Cdd:cd03820   160 NVVVIPNPLSFPSEEPSTN---------LKSKRILAVGRLTYQKGFDLLIEAWALIAkkhpdWKLRIYGDGPEREELEKL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 239 VLALNISN-ISFLGAVSDedKAALLSLCYAVVFPShlRSEAFGITLLEgAM-YGKPLISSEIGTGTTFININQKTGLVIP 316
Cdd:cd03820   231 IDKLGLEDrVKLLGPTKN--IAEEYANSSIFVLSS--RYEGFPMVLLE-AMaYGLPIISFDCPTGPSEIIEDGENGLLVP 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1267023523 317 PSDPIALRTAMDQLWNDVELAAKFGDNARARyLEHFTSEKMVSSYIE 363
Cdd:cd03820   306 NGDVDALAEALLRLMEDEELRKKMGKNARKN-AERFSIEKIIKQWEE 351
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 4-368 1.84e-30

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: 119.79  E-value: 1.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   4 VLHFYKTYYPDSFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPINLEVASTPFSF--------- 74
Cdd:cd03798     1 VLILTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPrlrllaplr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  75 -----QALEDFKKLAQqaDIIHYHFPFPFMDMVHFVA-SLNKPTVVSYH-SDIVKQKNiLKLYSPLMNRFLGDVSKIVAA 147
Cdd:cd03798    81 apslaKLLKRRRRGPP--DLIHAHFAYPAGFAAALLArLYGVPYVVTEHgSDINVFPP-RSLLRKLLRWALRRAARVIAV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 148 SPnyvATSETLKKF---ADKVCVIPYGLDEK-SYPVSDPERLAFwrnkfGQRFFLFVGAFRYYKGLHILIEA-----AKN 218
Cdd:cd03798   158 SK---ALAEELVALgvpRDRVDVIPNGVDPArFQPEDRGLGLPL-----DAFVILFVGRLIPRKGIDLLLEAfarlaKAR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 219 SSYPIVIVGAGPIESELKRQVLALNI-SNISFLGAVSDEDKAALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSE 297
Cdd:cd03798   230 PDVVLLIVGDGPLREALRALAEDLGLgDRVTFTGRLPHEQVPAYYRACDVFVLPS--RHEGFGLVLLEAMACGLPVVATD 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267023523 298 IGTGTTFINiNQKTGLVIPPSDPIALRTAMDQLWNDVELAAKfGDNARARYLEHFTSEKMVSSYIELYNDI 368
Cdd:cd03798   308 VGGIPEVVG-DPETGLLVPPGDADALAAALRRALAEPYLREL-GEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 3-353 3.23e-30

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: 118.61  E-value: 3.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYypdSFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPINLEVASTPFSFQALEDFKK 82
Cdd:cd03811     1 KILFVIPSL---SGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  83 LAQQA--DIIH-YHFPFPFmdMVHFVASLNKPTVVSYHSDIVKQKNilklysplMNRFLGDVSKIVAASPNYVATSETLK 159
Cdd:cd03811    78 ILKRAkpDVVIsFLGFATY--IVAKLAAARSKVIAWIHSSLSKLYY--------LKKKLLLKLKLYKKADKIVCVSKGIK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 160 KFA--------DKVCVIPYGLDeksypVSDPERLAF---WRNKFGQRFFLFVGAFRYYKGLHILIEAA-----KNSSYPI 223
Cdd:cd03811   148 EDLirlgpsppEKIEVIYNPID-----IDRIRALAKepiLNEPEDGPVILAVGRLDPQKGHDLLIEAFaklrkKYPDVKL 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 224 VIVGAGPIESELKRQVLALNISN-ISFLGAVSdeDKAALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGtGT 302
Cdd:cd03811   223 VILGDGPLREELEKLAKELGLAErVIFLGFQS--NPYPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCP-GP 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267023523 303 TFININQKTGLVIPPSDPIAL---RTAMDQLWNDVELAAKFGdNARARYLEHFT 353
Cdd:cd03811   298 REILDDGENGLLVPDGDAAALagiLAALLQKKLDAALRERLA-KAQEAVFREYT 350
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 3-365 4.35e-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: 115.84  E-value: 4.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPDSfGGVEQVIFQLCEGGASRGIDSTVLSLSRRGtITNQKIGSHTVYCS---PINLEVASTPFSFQALED 79
Cdd:cd03817     1 KIAIFTDTYLPQV-NGVATSVRNLARALEKRGHEVYVITPSDPG-AEDEEEVVRYRSFSipiRKYHRQHIPFPFKKAVID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  80 FKKLaQQADIIHYHFPFPFMDMVHFVAS-LNKPTVVSYHS-------DIVKQKNILKLY-SPLMNRFLGDVSKIVAASPn 150
Cdd:cd03817    79 RIKE-LGPDIIHTHTPFSLGKLGLRIARkLKIPIVHTYHTmyedylhYIPKGKLLVKAVvRKLVRRFYNHTDAVIAPSE- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 151 yvATSETLKKFADKVC--VIPYGLDEKSYPVSDPERLafwRNKFG----QRFFLFVGAFRYYKGLHILIEAAKNSSYPI- 223
Cdd:cd03817   157 --KIKDTLREYGVKGPieVIPNGIDLDKFEKPLNTEE---RRKLGlppdEPILLYVGRLAKEKNIDFLLRAFAELKKEPn 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 224 ---VIVGAGPIESELKRQVLALNIS-NISFLGAVSDEDKAALLSLCYAVVFPSHlrSEAFGITLLEGAMYGKPLISSEIG 299
Cdd:cd03817   232 iklVIVGDGPEREELKELARELGLAdKVIFTGFVPREELPEYYKAADLFVFAST--TETQGLVYLEAMAAGLPVVAAKDP 309

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267023523 300 TGTTFINiNQKTGLVIPPsDPIALRTAMDQLWNDVELAAKFGDNARArYLEHFTSEKMVSSYIELY 365
Cdd:cd03817   310 AASELVE-DGENGFLFEP-NDETLAEKLLHLRENLELLRKLSKNAEI-SAREFAFAKSVEKLYEEV 372
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 88-352 2.38e-28

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: 113.70  E-value: 2.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  88 DIIHYHFPFPFMDMVHFVASLNKPTVVSYH-SDIVKQKNILKLYSPLMNRFLGDVSKIVAASPNYVATSETLKKF----- 161
Cdd:cd05844    83 ALVHAHFGRDGVYALPLARALGVPLVVTFHgFDITTSRAWLAASPGWPSQFQRHRRALQRPAALFVAVSGFIRDRllarg 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 162 --ADKVCVIPYGLD-EKSYPVSDPERlafwrnkfgQRFFLFVGAFRYYKGLHILIEA-----AKNSSYPIVIVGAGPIES 233
Cdd:cd05844   163 lpAERIHVHYIGIDpAKFAPRDPAER---------APTILFVGRLVEKKGCDVLIEAfrrlaARHPTARLVIAGDGPLRP 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 234 ELkrQVLALNISNISFLGAVSDEDKAALLSLCYAVVFPSHL----RSEAFGITLLEGAMYGKPLISSEIGTGTTFInINQ 309
Cdd:cd05844   234 AL--QALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAI-LDG 310

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1267023523 310 KTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHF 352
Cdd:cd05844   311 ETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQF 353
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 17-363 5.04e-28

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: 112.46  E-value: 5.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  17 GGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPINLEVASTPFSFQALEDFKKLAQ-QADIIHYHFP 95
Cdd:cd03809    14 TGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKdKPDLLHSPHN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  96 FPFMDMVhfvaslNKPTVVSYHsDIvkqkNILKL---YSPLMNRFLGDVSKIVAASPNYVAT---------SETLKKFAD 163
Cdd:cd03809    94 TAPLLLK------GCPQVVTIH-DL----IPLRYpefFPKRFRLYYRLLLPISLRRADAIITvseatrddiIKFYGVPPE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 164 KVCVIPYGLDEKSYPVSDPERLafwRNKFGQ--RFFLFVGAFRYYKGLHILIEA-----AKNSSYPIVIVGAGPIESE-L 235
Cdd:cd03809   163 KIVVIPLGVDPSFFPPESAAVL---IAKYLLpePYFLYVGTLEPRKNHERLLKAfallkKQGGDLKLVIVGGKGWEDEeL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 236 KRQVLALNIS-NISFLGAVSDEDKAALLSLCYAVVFPSHlrSEAFGITLLEGAMYGKPLISSEIgtgTTFININQKTGLV 314
Cdd:cd03809   240 LDLVKKLGLGgRVRFLGYVSDEDLPALYRGARAFVFPSL--YEGFGLPVLEAMACGTPVIASNI---SVLPEVAGDAALY 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1267023523 315 IPPSDPIALRTAMDQLWNDVELAAKFGDNARARyLEHFTSEKMVSSYIE 363
Cdd:cd03809   315 FDPLDPESIADAILRLLEDPSLREELIRKGLER-AKKFSWEKTAEKTLE 362
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 3-363 5.19e-28

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: 112.85  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHfYKTYYPDSFGGVEQVIFQLCEGGASRGIDSTVLSLSR----------RGTITNQKIGSHTVYCSPINLEvasTPF 72
Cdd:cd03821     1 KILH-VTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDgyeslvveenGRYIPPQDGFASIPLLRQGAGR---TDF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  73 SFQALEDFKKLAQQADIIHYHFPFPFMDMvhFVASLNK----PTVVSYHSDIVK----QKNILK-LYSPL-MNRFLGDVS 142
Cdd:cd03821    77 SPGLPNWLRRNLREYDVVHIHGVWTYTSL--AACKLARrrgiPYVVSPHGMLDPwalqQKHWKKrIALHLiERRNLNNAA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 143 KIVAASPNYVATSETLKkFADKVCVIPYGLDEKSYPVSDPERLAFWRNKfGQRFFLFVGAFRYYKGLHILIEAA-----K 217
Cdd:cd03821   155 LVHFTSEQEADELRRFG-LEPPIAVIPNGVDIPEFDPGLRDRRKHNGLE-DRRIILFLGRIHPKKGLDLLIRAArklaeQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 218 NSSYPIVIVGAGPIESELKRQVLA-LNISN-ISFLGAVSDEDKAALLSLCYAVVFPSHlrSEAFGITLLEGAMYGKPLIS 295
Cdd:cd03821   233 GRDWHLVIAGPDDGAYPAFLQLQSsLGLGDrVTFTGPLYGEAKWALYASADLFVLPSY--SENFGNVVAEALACGLPVVI 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267023523 296 seigtgTTFINI----NQKTGLVIPPSDPiALRTAMDQLWNDVELAAKFGDNARA--RYLEHFTSEKMVSSYIE 363
Cdd:cd03821   311 ------TDKCGLselvEAGCGVVVDPNVS-SLAEALAEALRDPADRKRLGEMARRarQVEENFSWEAVAGQLGE 377
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 72-361 8.20e-27

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: 110.02  E-value: 8.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  72 FSFQALEDFKKLAQQADIIHYHFpfpFM-DMVHFVAS--LNKPTVVSYHS-DIVKQKNILK--LYSPlMNRFLGDvsKIV 145
Cdd:cd03800    87 FADGLLRFIAREGGRYDLIHSHY---WDsGLVGALLArrLGVPLVHTFHSlGRVKYRHLGAqdTYHP-SLRITAE--EQI 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 146 AASPNYVATS---------ETLKKFADKVCVIPYGLDEKSY-PVSDPE----RLAFWRNKFgqrFFLFVGAFRYYKGLHI 211
Cdd:cd03800   161 LEAADRVIAStpqeadeliSLYGADPSRINVVPPGVDLERFfPVDRAEarraRLLLPPDKP---VVLALGRLDPRKGIDT 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 212 LIEA-AKNSSYP----IVIVGaGPI------ESELKRQVLAL--NISNISFLGAVSDEDKAALLSLCYAVVFPSHlrSEA 278
Cdd:cd03800   238 LVRAfAQLPELRelanLVLVG-GPSddplsmDREELAELAEElgLIDRVRFPGRVSRDDLPELYRAADVFVVPSL--YEP 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 279 FGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMV 358
Cdd:cd03800   315 FGLTAIEAMACGTPVVATAVG-GLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVA 393


                  ...
gi 1267023523 359 SSY 361
Cdd:cd03800   394 DQL 396
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 13-368 5.11e-26

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: 106.60  E-value: 5.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  13 PDSFGGVEQVIFQLCEGGASRGIDSTVL------------SLSRRGTITNQKIGSHTVYCSPINLEVastpfsFQALEDF 80
Cdd:cd03802    14 PGKYGGTELVVSALTEGLVRRGHEVTLFapgdshtsaplvAVIPRALRLDPIPQESKLAELLEALEV------QLRASDF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  81 kklaqqaDIIHYHFPFPFMDMVHFVAslnKPTVvsyhsdivkqknilklySPLMNRFLGDVSKIVAA--SPNYVATSETL 158
Cdd:cd03802    88 -------DVIHNHSYDWLPPFAPLIG---TPFV-----------------TTLHGPSIPPSLAIYAAepPVNYVSISDAQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 159 KK---FADKVCVIPYGLDEKSYPVSDPerlafwrnkfGQRFFLFVGafRYY--KGLHILIEAAKNSSYPIVIVGAGPIES 233
Cdd:cd03802   141 RAatpPIDYLTVVHNGLDPADYRFQPD----------PEDYLAFLG--RIApeKGLEDAIRVARRAGLPLKIAGKVRDED 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 234 ELKRQVLALNISNISFLGAVSDEDKAALLSLCYAVVFPShLRSEAFGITLLEGAMYGKPLI------SSEIgtgttfinI 307
Cdd:cd03802   209 YFYYLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPI-NWDEPFGLVMIEAMACGTPVIayrrggLPEV--------I 279

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267023523 308 NQ-KTGLVIPPsdpialrtaMDQLWNDVELAAKF-GDNARARYLEHFTSEKMVSSYIELYNDI 368
Cdd:cd03802   280 QHgETGFLVDS---------VEEMAEAIANIDRIdRAACRRYAEDRFSAARMADRYEALYRKV 333
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
197-333 1.13e-25

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 100.28  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 197 FLFVGAF-RYYKGLHILIEA-----AKNSSYPIVIVGAGPIEsELKRQVLALNiSNISFLGAVsdEDKAALLSLCYAVVF 270
Cdd:pfam13692   4 ILFVGRLhPNVKGVDYLLEAvpllrKRDNDVRLVIVGDGPEE-ELEELAAGLE-DRVIFTGFV--EDLAELLAAADVFVL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267023523 271 PShlRSEAFGITLLEGAMYGKPLISSEIGtGTTFInINQKTGLVIPPSDPIALRTAMDQLWND 333
Cdd:pfam13692  80 PS--LYEGFGLKLLEAMAAGLPVVATDVG-GIPEL-VDGENGLLVPPGDPEALAEAILRLLED 138
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 260-370 2.98e-25

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 98.91  E-value: 2.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 260 ALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAK 339
Cdd:COG0438    16 ALLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1267023523 340 FGDNARARYLEHFTSEKMVSSYIELYNDIVS 370
Cdd:COG0438    93 LGEAARERAEERFSWEAIAERLLALYEELLA 123
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 3-367 1.60e-24

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: 102.79  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPDSFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGS--HTVYCSPINLEVASTPFSFQALE-- 78
Cdd:cd03823     1 KILLVNSLYPPQRVGGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVARSvvRYRRAPDETLPLALKRRGYELFEty 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  79 ---DFKKLAQ-----QADIIHYHFPFPF-MDMVHFVASLNKPTVVSYHSdivkqkniLKLYSPLMNRFLGDVSKIVAASp 149
Cdd:cd03823    81 npgLRRLLARlledfRPDVVHTHNLSGLgASLLDAARDLGIPVVHTLHD--------YWLLCPRQFLFKKGGDAVLAPS- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 150 nyVATSETLKK---FADKVCVIPYGLdekSYPVSDPERLAFWRNKFGqrfFLFVGAFRYYKGLHILIEAAKNS---SYPI 223
Cdd:cd03823   152 --RFTANLHEAnglFSARISVIPNAV---EPDLAPPPRRRPGTERLR---FGYIGRLTEEKGIDLLVEAFKRLpreDIEL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 224 VIVGAGPiESELKRQVLalnISNISFLGAVSDEDKAALLSLCYAVVFPShLRSEAFGITLLEGAMYGKPLISSEIGTGTT 303
Cdd:cd03823   224 VIAGHGP-LSDERQIEG---GRRIAFLGRVPTDDIKDFYEKIDVLVVPS-IWPEPFGLVVREAIAAGLPVIASDLGGIAE 298

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267023523 304 FININqKTGLVIPPSDPIALRTAMDQLWNDVELAAKfgdnARARYLEHFTSEKMVSSYIELYND 367
Cdd:cd03823   299 LIQPG-VNGLLFAPGDAEDLAAAMRRLLTDPALLER----LRAGAEPPRSTESQAEEYLKLYRD 357
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 3-351 1.15e-21

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: 94.67  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPDSfGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSP------INLEVASTPFSFQA 76
Cdd:cd03814     1 RIALVTDTYHPQV-NGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFPlpfypeYRLALPLPRRVRRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  77 LEDFkklaqQADIIHYHFPFPfmdmVHFVAS-----LNKPTVVSYHSDivkqknilkLYSPLMNRFLGDVSKIV------ 145
Cdd:cd03814    80 IKEF-----QPDIIHIATPGP----LGLAALraarrLGLPVVTSYHTD---------FPEYLSYYTLGPLSWLAwaylrw 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 146 ---AASPNYVATSETLKKFADK----VCVIPYGLDEKSYpvsDPE-RLAFWRNKFGQ---RFFLFVGAFRYYKGLHILIE 214
Cdd:cd03814   142 fhnPFDTTLVPSPSIARELEGHgferVRLWPRGVDTELF---HPSrRDAALRRRLGPpgrPLLLYVGRLAPEKNLEALLD 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 215 A----AKNSSYPIVIVGAGPIeselkRQVLALNISNISFLGAVSDEDKAALLSLCYAVVFPShlRSEAFGITLLEgAM-Y 289
Cdd:cd03814   219 AdlplAASPPVRLVVVGDGPA-----RAELEARGPDVIFTGFLTGEELARAYASADVFVFPS--RTETFGLVVLE-AMaS 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267023523 290 GKPLISSEIGTGTTFINiNQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEH 351
Cdd:cd03814   291 GLPVVAADAGGPRDIVR-PGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERY 351
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 144-368 1.15e-19

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: 88.93  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 144 IVAASP---NYVATSETLKKFadKVCVIPYGLD-EKSYPVsdPERLAFWRNKFGQRFF--LFV--GAFRYYKGLHILIEA 215
Cdd:cd03825   141 IVAPSRwlaDMVRRSPLLKGL--PVVVIPNGIDtEIFAPV--DKAKARKRLGIPQDKKviLFGaeSVTKPRKGFDELIEA 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 216 ----AKNSSYPIVIVGAGPieseLKRQVLALNISNISFLGavSDEDKAALLSLCYAVVFPShlRSEAFGITLLEGAMYGK 291
Cdd:cd03825   217 lkllATKDDLLLVVFGKND----PQIVILPFDIISLGYID--DDEQLVDIYSAADLFVHPS--LADNLPNTLLEAMACGT 288

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267023523 292 PLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSYIELYNDI 368
Cdd:cd03825   289 PVVAFDTG-GSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 10-368 3.78e-18

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: 84.71  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  10 TYYPdSFGGVEQVIFQLCEGGASRGIDSTVLSLSR--RGTITNQKIGSHTVycSPINLEVASTPFSFQALEDfkKLAQQA 87
Cdd:cd04962     6 VCYP-SYGGSGVVATELGLELAERGHEVHFISSAIpfRLNLYSGNIFFHEV--EVPNYPLFEYPPYTLALAS--KIVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  88 -----DIIHYHFPFPfmdmvHFVASL--------NKPTVVSYH-SDIVkqknIL---KLYSPLmNRFLGDVSKIVAASPN 150
Cdd:cd04962    81 kehklDVLHAHYAIP-----HASCAYlareilgeKIPIVTTLHgTDIT----LVgydPSLQPA-VRFSINKSDRVTAVSS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 151 YVATsETLKKF--ADKVCVIPYGLDEKSYPVSDPErlAFWRNKF---GQRFFLFVGAFRYYKGLHILIEA----AKNSSY 221
Cdd:cd04962   151 SLRQ-ETYELFdvDKDIEVIHNFIDEDVFKRKPAG--ALKRRLLappDEKVVIHVSNFRPVKRIDDVVRVfarvRRKIPA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 222 PIVIVGAGPIESELKRQVLALNISN-ISFLGAVSDEDKaaLLSLCYAVVFPSHlrSEAFGITLLEGAMYGKPLISSEIGt 300
Cdd:cd04962   228 KLLLVGDGPERVPAEELARELGVEDrVLFLGKQDDVEE--LLSIADLFLLPSE--KESFGLAALEAMACGVPVVSSNAG- 302

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267023523 301 GTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSYIELYNDI 368
Cdd:cd04962   303 GIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
17-173 4.45e-16

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 75.26  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  17 GGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPINLEvASTPFSFQALEDFKKLAQ--QADIIHYHF 94
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLP-PRLLRSLAFLRRLRRLLRreRPDVVHAHS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  95 PFPFM-DMVHFVASLNKPTVVSYHSDI-------VKQKNILKLYSPLMNRFLGDVSKIVAASPnyvATSETLKKF----A 162
Cdd:pfam13439  80 PFPLGlAALAARLRLGIPLVVTYHGLFpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSE---AVADELRRLygvpP 156

                         170
                  ....*....|.
gi 1267023523 163 DKVCVIPYGLD 173
Cdd:pfam13439 157 EKIRVIPNGVD 167
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 144-314 3.38e-15

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: 74.36  E-value: 3.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 144 IVAASPNYVATSETLKKFAD--KVCVIPYGLDEKSYPVSDPERLAFWRNKFGQRFFLFVGAFRYYKGLHILIEAAK---- 217
Cdd:cd01635    58 VHAHSPHAAALAALLAARLLgiPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALAllka 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 218 -NSSYPIVIVGAGPIESELKRQVLAL-NISNISFLGAVSDEDKAALLSLCY-AVVFPShlRSEAFGITLLEGAMYGKPLI 294
Cdd:cd01635   138 rLPDLVLVLVGGGGEREEEEALAAALgLLERVVIIGGLVDDEVLELLLAAAdVFVLPS--RSEGFGLVLLEAMAAGKPVI 215

                         170       180
                  ....*....|....*....|
gi 1267023523 295 SSEIGTGTTFININQKTGLV 314
Cdd:cd01635   216 ATDVGGIPEFVVDGENGLLV 235
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 177-294 4.85e-14

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: 72.32  E-value: 4.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 177 YPVSDPERLAFWRNKfgQRFFLFVGAFRYYKGLHILIEAAKNSSYPIVIVGAGPIESELKrqvlALNISNISFLGAVSDE 256
Cdd:cd03804   184 YPPVDTDAFAPAADK--EDYYLTASRLVPYKRIDLAVEAFNELPKRLVVIGDGPDLDRLR----AMASPNVEFLGYQPDE 257

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1267023523 257 DKAALLSLCYAVVFPShlrSEAFGITLLEGAMYGKPLI 294
Cdd:cd03804   258 VLKELLSKARAFVFAA---EEDFGIVPVEAQACGTPVI 292
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 162-365 7.69e-14

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: 72.37  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 162 ADKVCVIPYGLDEKSYPvsdpERLAFWRNKFGQRFFLfVGAFRYYKGLHILIEAAKNSSYPIV-----IVGAGP----IE 232
Cdd:cd03813   266 PDKTRVIPNGIDIQRFA----PAREERPEKEPPVVGL-VGRVVPIKDVKTFIRAFKLVRRAMPdaegwLIGPEDedpeYA 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 233 SELKRQVLALNISN-ISFLGAVSDEDKAALLSLcyaVVFPShlRSEAFGITLLEGAMYGKPLISSEIGTGTTFI----NI 307
Cdd:cd03813   341 QECKRLVASLGLENkVKFLGFQNIKEYYPKLGL---LVLTS--ISEGQPLVILEAMASGVPVVATDVGSCRELIygadDA 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267023523 308 NQKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSYIELY 365
Cdd:cd03813   416 LGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLY 473
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 3-309 5.69e-12

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: 66.16  E-value: 5.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523   3 KVLHFYKTYYPdsfGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKI---GSHTVYCSPINLEVastPFSFQALED 79
Cdd:cd03812     1 KILHIVGGMNV---GGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEELeelGGKIFYIPPKKKNI---IKYFIKLLK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  80 FKKlAQQADIIHYHFPFPFMDMVHFVASLNKPTVVSY-HSDIVKQKNILKLYSPLMnRFLgdvskIVAASPNYVATSETL 158
Cdd:cd03812    75 LIK-KEKYDIVHVHGSSSNGIILLLAAKAGVPVRIAHsHNTKDSSIKLRKIRKNVL-KKL-----IERLSTKYLACSEDA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 159 ------KKFADKVCVIPYGLDEKSYPVSDPERLAFWRNKFGQRFFLF--VGAFRYYKGLHILIEAA-----KNSSYPIVI 225
Cdd:cd03812   148 gewlfgEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLghVGRFNEQKNHSFLIDIFeelkkKNPNVKLVL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 226 VGAGPIESELKRQVLALNI-SNISFLGAVSDEDKaaLLSLCYAVVFPSHLrsEAFGITLLEGAMYGKPLISSE------- 297
Cdd:cd03812   228 VGEGELKEKIKEKVKELGLeDKVIFLGFRNDVSE--ILSAMDVFLFPSLY--EGLPLVAVEAQASGLPCLLSDtitkecd 303

                         330
                  ....*....|..
gi 1267023523 298 IGTGTTFININQ 309
Cdd:cd03812   304 ITNNVEFLPLNE 315
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 247-357 1.78e-11

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: 64.92  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 247 ISFLGAVSDEDKAALLSLCYAVVF-PSHlrsEAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPsDPIALRT 325
Cdd:cd03805   282 VLFLRSISDSQKEQLLSSALALLYtPSN---EHFGIVPLEAMYAGKPVIACNSG-GPLETVVEGVTGFLCEP-TPEAFAE 356

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1267023523 326 AMDQLWNDVELAAKFGDNARARYLEHFTSEKM 357
Cdd:cd03805   357 AMLKLANDPDLADRMGAAGRKRVKEKFSREAF 388
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 62-366 1.95e-10

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: 61.63  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  62 PINLEVASTPFSFQALEDFKKLaqqaDIIHYHFPFPFMD------MVHFVASLNKPTVVSYHsdivkqkNILKLYSPL-- 133
Cdd:cd03822    55 EIKSWNSNEYFRLLDHLNFKKP----DVVHIQHEFGIFGgkyglyALGLLLHLRIPVITTLH-------TVLDLSDPGkq 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 134 ----MNRFLGDVSKIVAASPNYVATSETLKKF-ADKVCVIPYGLDE-KSYPVSDPERLAFWRNKFgqrFFLFVGAFRYYK 207
Cdd:cd03822   124 alkvLFRIATLSERVVVMAPISRFLLVRIKLIpAVNIEVIPHGVPEvPQDPTTALKRLLLPEGKK---VILTFGFIGPGK 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 208 GLHILIEAA---KNSSYPIVIVGAG---------PIESELKRQVLALNISNISFL--GAVSDEDKAALLSLCYAVVFPSH 273
Cdd:cd03822   201 GLEILLEALpelKAEFPDVRLVIAGelhpslaryEGERYRKAAIEELGLQDHVDFhnNFLPEEEVPRYISAADVVVLPYL 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 274 LRSEAFGITLLEGAMYGKPLISSEIGtgtTFININ-QKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNArARYLEHF 352
Cdd:cd03822   281 NTEQSSSGTLSYAIACGKPVISTPLR---HAEELLaDGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERA-YAYARAM 356

                         330
                  ....*....|....
gi 1267023523 353 TSEKMVSSYIELYN 366
Cdd:cd03822   357 TWESIADRYLRLFN 370
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 15-366 4.78e-10

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


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 60.54  E-value: 4.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  15 SFGGVEQVIFQLCEGGASRGIDSTVLSLSRRGTIT--NQKIGSHtvycspiNLEVASTPFSF-QALEDFKKL--AQQADI 89
Cdd:cd04951    10 GLGGAEKQTVLLADQMFIRGHDVNIVYLTGEVEVKplNNNIIIY-------NLGMDKNPRSLlKALLKLKKIisAFKPDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  90 IHYHfpfpfmdMVH--FVASLNK------PTVVSYHSDIVKQKNILKLYSplMNRFLGDVSKIVAASpnyvATSETLKKF 161
Cdd:cd04951    83 VHSH-------MFHanIFARFLRmlypipLLICTAHNKNEGGRIRMFIYR--LTDFLCDITTNVSRE----ALDEFIAKK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 162 A---DKVCVIPYGLDEKSYPVSDPERLAFwRNKFGQRF----FLFVGAFRYYKGLHILIEA-----AKNSSYPIVIVGAG 229
Cdd:cd04951   150 AfskNKSVPVYNGIDLNKFKKDINVRLKI-RNKLNLKNdefvILNVGRLTEAKDYPNLLLAiseliLSKNDFKLLIAGDG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 230 PIESELKRQVLALNIS-NISFLGAVSdeDKAALLSLCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGTGTTFINin 308
Cdd:cd04951   229 PLRNELERLICNLNLVdRVILLGQIS--NISEYYNAADLFVLSS--EWEGFGLVVAEAMACERPVVATDAGGVAEVVG-- 302

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267023523 309 qKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKMVSSYIELYN 366
Cdd:cd04951   303 -DHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLYS 359
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 196-368 1.03e-09

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


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 59.26  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 196 FFLFVGAFRYYKGLHILIEAAK----NSSYP-IVIVGAGPIE----SELKRQVLAL--NISNISFLGA-VSDEDKAALLS 263
Cdd:cd03792   199 YILQVARFDPSKDPLGVIDAYKlfkrRAEEPqLVICGHGAVDdpegSVVYEEVMEYagDDHDIHVLRLpPSDQEINALQR 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 264 LCYAVVFPShlRSEAFGITLLEGAMYGKPLISSEIGTGTTFInINQKTGLVIPPSDPIALRtaMDQLWNDVELAAKFGDN 343
Cdd:cd03792   279 AATVVLQLS--TREGFGLTVSEALWKGKPVIATPAGGIPLQV-IDGETGFLVNSVEGAAVR--ILRLLTDPELRRKMGLA 353

                         170       180
                  ....*....|....*....|....*
gi 1267023523 344 ARARYLEHFTSEKMVSSYIELYNDI 368
Cdd:cd03792   354 AREHVRDNFLITGNLRAWLYLIAKL 378
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
133-362 1.36e-09

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 59.22  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 133 LMNRFlgD-VSKIvaaSPNYVATSETLKKFADKVCVIPYGLD-EKSYPVSDPERLAFwRNKFG----QRFFLFVGAFRYY 206
Cdd:PRK10307  168 LLRRF--DnVSTI---SRSMMNKAREKGVAAEKVIFFPNWSEvARFQPVADADVDAL-RAQLGlpdgKKIVLYSGNIGEK 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 207 KGLHILIEAAKN----SSYPIVIVGAGPIESELKRQVLALNISNISFLGAVSDEDKAALLSL--CYAV---------VFP 271
Cdd:PRK10307  242 QGLELVIDAARRlrdrPDLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMadCHLLpqkagaadlVLP 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 272 SHLRseafGItLLEGamyGKPLISSEIGT--GTTFINInqktGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYL 349
Cdd:PRK10307  322 SKLT----NM-LASG---RNVVATAEPGTelGQLVEGI----GVCVEPESVEALVAAIAALARQALLRPKLGTVAREYAE 389

                         250
                  ....*....|...
gi 1267023523 350 EHFTSEKMVSSYI 362
Cdd:PRK10307  390 RTLDKENVLRQFI 402
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
17-171 1.56e-06

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 47.40  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  17 GGVEQVIFQLCEGGASRGIDSTVLSLSRRGTITNQKIGSHTVYCSPInLEVASTPFSFQALEDFKKL--AQQADIIHYHF 94
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPV-PPRPSPLADLAALRRLRRLlrAERPDVVHAHS 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267023523  95 PFPFMDMVHFVASLNKPTVVSYHSDIVKQKNILK--LYSPLMNRFLGDVSKIVAASPNYVATSETLKKFADKVCVIPYG 171
Cdd:pfam13579  80 PTAGLAARLARRRRGVPLVVTVHGLALDYGSGWKrrLARALERRLLRRADAVVVVSEAEAELLRALGVPAARVVVVPNG 158
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 164-346 1.72e-06

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: 49.22  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 164 KVCVIPYG-LDEKSYPVSDPERLafwRNKFgqrffLFVGAFRYYKGLHILIEAAK--NSSYPIV---IVGAGPIESELKR 237
Cdd:cd04949   137 PIFTIPVGyVDQLDTAESNHERK---SNKI-----ITISRLAPEKQLDHLIEAVAkaVKKVPEItldIYGYGEEREKLKK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 238 QVLALNISNISFL-GAVSDEDKaaLLSLCYAVVFPSHlrSEAFGITLLEGAMYGKPLISSEIGTG-TTFInINQKTGLVI 315
Cdd:cd04949   209 LIEELHLEDNVFLkGYHSNLDQ--EYQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPVVSYDVKYGpSELI-EDGENGYLI 283

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1267023523 316 PPSDPIALRTAMDQLWNDVELAAKFGDNARA 346
Cdd:cd04949   284 EKNNIDALADKIIELLNDPEKLQQFSEESYK 314
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 87-357 2.25e-04

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: 42.82  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  87 ADIIHYHFPF--PFMDMVHFVASLNKPTVVSYHS-DIVK--QKNILKLYSPLMNRflGDVskivaaspnYVATSETLKKF 161
Cdd:cd03799    71 YDIIHCQFGPlgALGALLRRLKVLKGKLVTSFRGyDISMyvILEGNKVYPQLFAQ--GDL---------FLPNCELFKHR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 162 AdkvcvIPYGLDEKSYPVS----DPERLAFWRNKF---GQRFFLFVGAFRYYKGLHILIEAAKN--SSYPIV---IVGAG 229
Cdd:cd03799   140 L-----IALGCDEKKIIVHrsgiDCNKFRFKPRYLpldGKIRILTVGRLTEKKGLEYAIEAVAKlaQKYPNIeyqIIGDG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 230 PIESELKRQVLALNISN-ISFLGAVSDEDKAALLSLCYAVVFPSHLRS----EAFGITLLEGAMYGKPLISSEIGTGTTF 304
Cdd:cd03799   215 DLKEQLQQLIQELNIGDcVKLLGWKPQEEIIEILDEADIFIAPSVTAAdgdqDGPPNTLKEAMAMGLPVISTEHGGIPEL 294

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1267023523 305 ININqKTGLVIPPSDPIALRTAMDQLWNDVELAAKFGDNARARYLEHFTSEKM 357
Cdd:cd03799   295 VEDG-VSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKL 346
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 89-365 2.62e-04

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: 42.94  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523  89 IIH-----YHFPFPFMDMVHFVASLNKPTVVSYHSDIvkqkNILK---LYSplmnrflgdvSKIVAASPNY---VATSE- 156
Cdd:cd03791   163 TIHnlayqGLFPLDTLAELGLPPELFHIDGLEFYGQI----NFLKagiVYA----------DRVTTVSPTYakeILTPEy 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 157 ------TLKKFADKVCVIPYGLDEKSY-PVSDPErLAF----------WRNK--FGQRFFL----------FVGAFRYYK 207
Cdd:cd03791   229 gegldgVLRARAGKLSGILNGIDYDEWnPATDKL-IPAnysandlegkAENKaaLQKELGLpvdpdaplfgFVGRLTEQK 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 208 GLHILIEAAknssyP--------IVIVGAG--PIESELkRQVLALNISNISFLGAVSDEDkAALLslcYA----VVFPSh 273
Cdd:cd03791   308 GVDLILDAL-----PelleeggqLVVLGSGdpEYEQAF-RELAERYPGKVAVVIGFDEAL-AHRI---YAgadfFLMPS- 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 274 lRSEAFGITLLEgAM-YGKPLISSEIG----TGTTFININQK-TGLVIPPSDPIALRTAMD---QLWNDVELAAKFGDNA 344
Cdd:cd03791   377 -RFEPCGLVQMY-AMrYGTLPIVRRTGgladTVFDYDPETGEgTGFVFEDYDAEALLAALRralALYRNPELWRKLQKNA 454

                         330       340
                  ....*....|....*....|.
gi 1267023523 345 RARyleHFTSEKMVSSYIELY 365
Cdd:cd03791   455 MKQ---DFSWDKSAKEYLELY 472
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
197-301 2.40e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 39.69  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267023523 197 FLFVGAFRYY--KGLHILIEA--AKNSSYPIVIVGAGPIESELKRQVLALNIS-NISFLGAVSD-----EDKAALLSlcy 266
Cdd:PRK09922  183 FLYVGRLKFEgqKNVKELFDGlsQTTGEWQLHIIGDGSDFEKCKAYSRELGIEqRIIWHGWQSQpwevvQQKIKNVS--- 259

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1267023523 267 AVVFPSHLrsEAFGITLLEGAMYGKPLISSEIGTG 301
Cdd:PRK09922  260 ALLLTSKF--EGFPMTLLEAMSYGIPCISSDCMSG 292
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 277-339 3.19e-03

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: 39.76  E-value: 3.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267023523  277 EAFGITLLEGAMYGKPLISSEIGtGTTFININQKTGLVIPPSDPIALRTAMDQLWNDVELAAK 339
Cdd:TIGR02468  582 EPFGLTLIEAAAHGLPMVATKNG-GPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLWAE 643
 
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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