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Conserved domains on  [gi|446641838|ref|WP_000719184|]
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MULTISPECIES: glycosyltransferase [Staphylococcus]

Protein Classification

glycosyltransferase; glycosyltransferase family protein( domain architecture ID 13559117)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds| glycosyltransferase family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 190-487 2.89e-108

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: 324.64  E-value: 2.89e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 190 KTYVLVNKKEFKNNLALCVYYLEKLIKDsKDSIMICDGPGSFPKMFNTNHKNAQKYGVIHVNHHENFDDT--GAFKKSEK 267
Cdd:cd04949   27 KEHTRPYKIIFLNEQELFAFFIEQLNLQ-KGDIFISDRPTLTGQVILNTKGPAKKGAVLHNEHVKNNDDPehSLIKNFYK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 268 YIIENANKINGVIVLTEAQRLDILNQFD-VENIFTISNFVKIHNAPK---HFQTEKIVGHISRMVPTKRIDLLIEVAELV 343
Cdd:cd04949  106 YVFENLNKYDAIIVSTEQQKQDLSERFNkYPPIFTIPVGYVDQLDTAesnHERKSNKIITISRLAPEKQLDHLIEAVAKA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 344 VKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFD 423
Cdd:cd04949  186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYD 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446641838 424 IKYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKAREnIIEKYSTESILEKW 487
Cdd:cd04949  266 VKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK-IAEKYSTENVMEKW 328
Glyco_trans_A_1 super family cl37583
Glycosyl transferase 1 domain A; Glyco_trans_A_1 is family of found predominantly at the ...
 14-210 9.96e-05

Glycosyl transferase 1 domain A; Glyco_trans_A_1 is family of found predominantly at the N-terminus of various prokaryotic alpha-glucosyltransferases. According to whether the domain exists as a whole molecule or as a half molecule determines the number of sugar residues that the molecule transfers. Two-domain proteins are processive in that they transfer more than one sugar residue, processively; single domain proteins transfer just one sugar moiety.


The actual alignment was detected with superfamily member pfam09318:

Pssm-ID: 370428  Cd Length: 199  Bit Score: 43.49  E-value: 9.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838   14 NKGGMTSSMFNRSKEF-YDADIPADIVTFDYKGNYDEIIKALKKQGKMDRR-TKMYNVFEYFKQI-SNNKHFKSNKLLYK 90
Cdd:pfam09318  10 KYGGLTKSLLLRAKLFgEECNINTFFLTFRFDLEFSQKIDEIFDKGIIDKKfTKIINLFDDFLIPnCNGKEQYEERIGLD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838   91 HISERLKNTieiEESKGISRYFDITTGTY-IAYIRKSKSEKVIDFFKDNKRIERfsfidnkvhmKETFNVDNKVCYQVFY 169
Cdd:pfam09318  90 QIKKHAGMG---KFAKTLLRLFDHEDNEMrMIRNEDGEQIEIVDYFHDKNQLEK----------REEYNKNGNLHKVSHF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446641838  170 D-EKGYPYISRNINANNGAVGKTYVLVNKKEFKNNLALCVYY 210
Cdd:pfam09318 157 DqELGKMYLEEFINDNNHIYLDKGYADLKEEADSKLRDIIWY 198
 
Name Accession Description Interval E-value
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 190-487 2.89e-108

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: 324.64  E-value: 2.89e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 190 KTYVLVNKKEFKNNLALCVYYLEKLIKDsKDSIMICDGPGSFPKMFNTNHKNAQKYGVIHVNHHENFDDT--GAFKKSEK 267
Cdd:cd04949   27 KEHTRPYKIIFLNEQELFAFFIEQLNLQ-KGDIFISDRPTLTGQVILNTKGPAKKGAVLHNEHVKNNDDPehSLIKNFYK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 268 YIIENANKINGVIVLTEAQRLDILNQFD-VENIFTISNFVKIHNAPK---HFQTEKIVGHISRMVPTKRIDLLIEVAELV 343
Cdd:cd04949  106 YVFENLNKYDAIIVSTEQQKQDLSERFNkYPPIFTIPVGYVDQLDTAesnHERKSNKIITISRLAPEKQLDHLIEAVAKA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 344 VKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFD 423
Cdd:cd04949  186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYD 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446641838 424 IKYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKAREnIIEKYSTESILEKW 487
Cdd:cd04949  266 VKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK-IAEKYSTENVMEKW 328
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
318-459 1.99e-32

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 120.69  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838  318 EKIVGHISRMVP-TKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKdKIAKMIedKNLERNVFLKGYTTTPQKCLEDFKLV 396
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELA--AGLEDRVIFTGFVEDLAELLAAADVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446641838  397 VSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIeDNKNGYLIENHNINDMADKILQLVNN 459
Cdd:pfam13692  78 VLPSLYEGFGLKLLEAMAAGLPVVATDVG-GIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 367-493 5.55e-25

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 99.68  E-value: 5.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 367 MIEDKNLErnVFLKGYtttpqkcLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNI 446
Cdd:COG0438    4 LVPRKGLD--LLLEAL-------LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446641838 447 NDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNLFNS 493
Cdd:COG0438   74 EALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEE 120
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
299-490 4.72e-11

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 64.35  E-value: 4.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 299 IFTISNFVKIHN----APKHFQTEKIVgHISRMVPT--KRI-DLLIEVAELvvkkDNAVKFHIYGEGSVKDKIAKMIEDK 371
Cdd:PRK09922 158 ISVIYNPVEIKTiiipPPERDKPAVFL-YVGRLKFEgqKNVkELFDGLSQT----TGEWQLHIIGDGSDFEKCKAYSREL 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 372 NLERNVFLKGYTTTPQKCLEDFKLVVS----TSQYEGQGLSMIEAMISKRPVVAFDIKYGPSDFIEDNKNGYLIENHNIN 447
Cdd:PRK09922 233 GIEQRIIWHGWQSQPWEVVQQKIKNVSalllTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDIIKPGLNGELYTPGNID 312

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446641838 448 DMADKILQLVNNDVLaaeFGSKARENIIEKYSTESILEKWLNL 490
Cdd:PRK09922 313 EFVGKLNKVISGEVK---YQHDAIPNSIERFYEVLYFKNLNNA 352
Glyco_trans_A_1 pfam09318
Glycosyl transferase 1 domain A; Glyco_trans_A_1 is family of found predominantly at the ...
 14-210 9.96e-05

Glycosyl transferase 1 domain A; Glyco_trans_A_1 is family of found predominantly at the N-terminus of various prokaryotic alpha-glucosyltransferases. According to whether the domain exists as a whole molecule or as a half molecule determines the number of sugar residues that the molecule transfers. Two-domain proteins are processive in that they transfer more than one sugar residue, processively; single domain proteins transfer just one sugar moiety.


Pssm-ID: 370428  Cd Length: 199  Bit Score: 43.49  E-value: 9.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838   14 NKGGMTSSMFNRSKEF-YDADIPADIVTFDYKGNYDEIIKALKKQGKMDRR-TKMYNVFEYFKQI-SNNKHFKSNKLLYK 90
Cdd:pfam09318  10 KYGGLTKSLLLRAKLFgEECNINTFFLTFRFDLEFSQKIDEIFDKGIIDKKfTKIINLFDDFLIPnCNGKEQYEERIGLD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838   91 HISERLKNTieiEESKGISRYFDITTGTY-IAYIRKSKSEKVIDFFKDNKRIERfsfidnkvhmKETFNVDNKVCYQVFY 169
Cdd:pfam09318  90 QIKKHAGMG---KFAKTLLRLFDHEDNEMrMIRNEDGEQIEIVDYFHDKNQLEK----------REEYNKNGNLHKVSHF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446641838  170 D-EKGYPYISRNINANNGAVGKTYVLVNKKEFKNNLALCVYY 210
Cdd:pfam09318 157 DqELGKMYLEEFINDNNHIYLDKGYADLKEEADSKLRDIIWY 198
 
Name Accession Description Interval E-value
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 190-487 2.89e-108

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: 324.64  E-value: 2.89e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 190 KTYVLVNKKEFKNNLALCVYYLEKLIKDsKDSIMICDGPGSFPKMFNTNHKNAQKYGVIHVNHHENFDDT--GAFKKSEK 267
Cdd:cd04949   27 KEHTRPYKIIFLNEQELFAFFIEQLNLQ-KGDIFISDRPTLTGQVILNTKGPAKKGAVLHNEHVKNNDDPehSLIKNFYK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 268 YIIENANKINGVIVLTEAQRLDILNQFD-VENIFTISNFVKIHNAPK---HFQTEKIVGHISRMVPTKRIDLLIEVAELV 343
Cdd:cd04949  106 YVFENLNKYDAIIVSTEQQKQDLSERFNkYPPIFTIPVGYVDQLDTAesnHERKSNKIITISRLAPEKQLDHLIEAVAKA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 344 VKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFD 423
Cdd:cd04949  186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYD 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446641838 424 IKYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKAREnIIEKYSTESILEKW 487
Cdd:cd04949  266 VKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK-IAEKYSTENVMEKW 328
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 208-487 1.21e-51

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: 178.97  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 208 VYYLEKLIKDSKDSIMICDGPGSFpKMFNTNHKNAQKYGVIHVNHHENFDdTGAFKKSEKYIIENANKIngvIVLTEAQR 287
Cdd:cd03820   76 VRRLRKYLKNNKPDVVISFRTSLL-TFLALIGLKSKLIVWEHNNYEAYNK-GLRRLLLRRLLYKRADKI---VVLTEADK 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 288 LDILNQFDvENIFTISNFVKIHNAPKHFQ-TEKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAK 366
Cdd:cd03820  151 LKKYKQPN-SNVVVIPNPLSFPSEEPSTNlKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEK 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 367 MIEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKYGPSDFIEDNKNGYLIENHNI 446
Cdd:cd03820  230 LIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPSEIIEDGENGLLVPNGDV 309

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446641838 447 NDMADKILQLVNNDVLAAEFGSKARENiIEKYSTESILEKW 487
Cdd:cd03820  310 DALAEALLRLMEDEELRKKMGKNARKN-AERFSIEKIIKQW 349
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 248-492 3.88e-38

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: 143.06  E-value: 3.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 248 IHVNHHENFDDTGAFKKSE-KYIIENANKINGVIVLTEAQRLDI--LNQFDVENIFTISNFV-------KIHNAPKHFQT 317
Cdd:cd03801  112 LHGAEPGRLLLLLAAERRLlARAEALLRRADAVIAVSEALRDELraLGGIPPEKIVVIPNGVdlerfspPLRRKLGIPPD 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 318 EKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYG-EGSVKDKIAKMieDKNLERNVFLKGYTTTPQK--CLEDFK 394
Cdd:cd03801  192 RPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEEL--ELGLGDRVRFLGFVPDEELpaLYAAAD 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 395 LVVSTSQYEGQGLSMIEAMISKRPVVAFDIkYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENI 474
Cdd:cd03801  270 VFVLPSRYEGFGLVVLEAMAAGLPVVATDV-GGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERV 348

                        250
                 ....*....|....*...
gi 446641838 475 IEKYSTESILEKWLNLFN 492
Cdd:cd03801  349 AERFSWERVAERLLDLYR 366
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 240-486 1.44e-33

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: 130.02  E-value: 1.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 240 KNAQKYGVIHVNH--HENFDDTGA----FKKSEKYIIENANKIngvIVLTEAQRLDILNQF--DVENIFTIS----NFVK 307
Cdd:cd03808  101 RLAGVPKVIYTVHglGFVFTEGKLlrllYLLLEKLALLFTDKV---IFVNEDDRDLAIKKGiiKKKKTVLIPgsgvDLDR 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 308 IHNAPKHFQTEKIV-GHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTP 386
Cdd:cd03808  178 FQYSPESLPSEKVVfLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDV 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 387 QKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEF 466
Cdd:cd03808  258 PELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVP-GCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEM 336

                        250       260
                 ....*....|....*....|
gi 446641838 467 GSKARENIIEKYSTESILEK 486
Cdd:cd03808  337 GEAARKRVEEKFDEEKVVNK 356
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 167-483 9.83e-33

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: 127.47  E-value: 9.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 167 VFYDEKGYPYISRNINANNGAVGKtyvlVNKKEFKNNLALCVYYLEKLIKDSKDsiMICDGPGSFPKMFNtnhKNAQKYG 246
Cdd:cd03811   36 LLRDEGDLDKQLNGDVKLIRLLIR----VLKLIKLGLLKAILKLKRILKRAKPD--VVISFLGFATYIVA---KLAAARS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 247 VIHVNHHENFDDTGAFKKSEKYIIENANKINGVIVLTEAQRLDILNQFDV--ENIFTISNFVKIHN----APKHFQTE-- 318
Cdd:cd03811  107 KVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSppEKIEVIYNPIDIDRiralAKEPILNEpe 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 319 --KIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLV 396
Cdd:cd03811  187 dgPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLF 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 397 VSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNINDMAdKILQLVNNDVLAAEFGSKARENIIE 476
Cdd:cd03811  267 VLSSRYEGFPNVLLEAMALGTPVVSTDCP-GPREILDDGENGLLVPDGDAAALA-GILAALLQKKLDAALRERLAKAQEA 344


                 ....*..
gi 446641838 477 KYSTESI 483
Cdd:cd03811  345 VFREYTI 351
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
318-459 1.99e-32

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 120.69  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838  318 EKIVGHISRMVP-TKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKdKIAKMIedKNLERNVFLKGYTTTPQKCLEDFKLV 396
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELA--AGLEDRVIFTGFVEDLAELLAAADVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446641838  397 VSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIeDNKNGYLIENHNINDMADKILQLVNN 459
Cdd:pfam13692  78 VLPSLYEGFGLKLLEAMAAGLPVVATDVG-GIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 317-472 2.84e-32

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: 120.84  E-value: 2.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838  317 TEKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQK--CLEDFK 394
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLpeLLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446641838  395 LVVSTSQYEGQGLSMIEAMISKRPVVAFDIkYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARE 472
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDV-GGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 367-493 5.55e-25

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 99.68  E-value: 5.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 367 MIEDKNLErnVFLKGYtttpqkcLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNI 446
Cdd:COG0438    4 LVPRKGLD--LLLEAL-------LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446641838 447 NDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNLFNS 493
Cdd:COG0438   74 EALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEE 120
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 239-488 1.36e-22

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: 99.38  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 239 HKNAQKYGV-----IHVNHHENFDDTGAFKKSEKYIIENANKIngVIVLTEAQRLDILNQFDVENIFTISNFVKIHN--- 310
Cdd:cd03798  112 ALLARLYGVpyvvtEHGSDINVFPPRSLLRKLLRWALRRAARV--IAVSKALAEELVALGVPRDRVDVIPNGVDPARfqp 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 311 ---APKHFQTEKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGytTTPQ 387
Cdd:cd03798  190 edrGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTG--RLPH 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 388 KCLEDF----KLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLA 463
Cdd:cd03798  268 EQVPAYyracDVFVLPSRHEGFGLVLLEAMACGLPVVATDVG-GIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLR 346

                        250       260
                 ....*....|....*....|....*
gi 446641838 464 AEfGSKARENIIEKYSTESILEKWL 488
Cdd:cd03798  347 EL-GEAARARVAERFSWVKAADRIA 370
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 290-491 6.19e-22

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: 97.00  E-value: 6.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 290 ILNQFDVENiFTISNFVKIHNAPKHF--QTEKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKM 367
Cdd:cd03807  161 IYNGIDLFK-LSPDDASRARARRRLGlaEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERL 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 368 IEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIkyGPSDFIEDNKNGYLIENHNIN 447
Cdd:cd03807  240 LLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDV--GGAAELVDDGTGFLVPAGDPQ 317

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446641838 448 DMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNLF 491
Cdd:cd03807  318 ALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLY 361
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 274-491 1.74e-20

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: 92.80  E-value: 1.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 274 NKINGVIVLTEAQRLDILNQFDVEN-IFTISNFV------KIHNAPKHFQT-----EKIVGHISRMVPTKRIDLLIEVAE 341
Cdd:cd04962  140 NKSDRVTAVSSSLRQETYELFDVDKdIEVIHNFIdedvfkRKPAGALKRRLlappdEKVVIHVSNFRPVKRIDDVVRVFA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 342 LVVKKDNAvKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVA 421
Cdd:cd04962  220 RVRRKIPA-KLLLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVS 298

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 422 FDIKyGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNLF 491
Cdd:cd04962  299 SNAG-GIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYY 367
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 252-484 1.61e-19

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 90.03  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 252 HHENFDDTGAFKKSEKYIIENANKINGVIVLTEAQRlDILNQFDVE-NIFTISN--------FVKIHNAPKHF---QTEK 319
Cdd:cd03817  124 HYIPKGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIK-DTLREYGVKgPIEVIPNgidldkfeKPLNTEERRKLglpPDEP 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 320 IVGHISRMVPTKRIDLLIEVAELVvKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYtttpqkcLEDFKLV--- 396
Cdd:cd03817  203 ILLYVGRLAKEKNIDFLLRAFAEL-KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGF-------VPREELPeyy 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 397 ------VSTSQYEGQGLSMIEAMISKRPVVAFDiKYGPSDFIEDNKNGYLIENHNINdMADKILQLVNNDVLAAEFGSKA 470
Cdd:cd03817  275 kaadlfVFASTTETQGLVYLEAMAAGLPVVAAK-DPAASELVEDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNA 352

                        250
                 ....*....|....
gi 446641838 471 RENIIEKYSTESIL 484
Cdd:cd03817  353 EISAREFAFAKSVE 366
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 240-488 2.92e-18

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: 86.63  E-value: 2.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 240 KNAQKYGVIHVN--HHENFDDTGAFKKS---------EKYIIENANKIngvIVLTEAQRLDILNQ-FDVENIFTISNFV- 306
Cdd:cd03794  120 KLRGAPFILDVRdlWPESLIALGVLKKGsllkllkklERKLYRLADAI---IVLSPGLKEYLLRKgVPKEKIIVIPNWAd 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 307 ---------KIHNAPKHFQTEKIVGHISRMVPTKRIDLLIEVAELVVKKDNaVKFHIYGEGSVKDKIAKMIEDKNLErNV 377
Cdd:cd03794  197 leefkpppkDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRPD-IRFLFVGDGDEKERLKELAKARGLD-NV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 378 FLKGYTttPQKCLE------DFKLV--VSTSQYEGQGLS-MIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNIND 448
Cdd:cd03794  275 TFLGRV--PKEEVPellsaaDVGLVplKDNPANRGSSPSkLFEYMAAGKPILASDDG-GSDLAVEINGCGLVVEPGDPEA 351

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446641838 449 MADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWL 488
Cdd:cd03794  352 LADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 323-441 1.41e-17

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: 82.07  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 323 HISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKC---LEDFKLVVST 399
Cdd:cd01635  115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLellLAAADVFVLP 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446641838 400 SQYEGQGLSMIEAMISKRPVVAFDIkYGPSDFIEDNKNGYLI 441
Cdd:cd01635  195 SRSEGFGLVLLEAMAAGKPVIATDV-GGIPEFVVDGENGLLV 235
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 318-489 1.76e-15

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: 78.05  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 318 EKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGS---------VKDKIAKM--IEDKnlernvflkgYTTTP 386
Cdd:cd03800  220 KPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSddplsmdreELAELAEElgLIDR----------VRFPG 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 387 QKCLEDF-------KLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNINDMADKILQLVNN 459
Cdd:cd03800  290 RVSRDDLpelyraaDVFVVPSLYEPFGLTAIEAMACGTPVVATAVG-GLQDIVRDGRTGLLVDPHDPEALAAALRRLLDD 368

                        170       180       190
                 ....*....|....*....|....*....|
gi 446641838 460 DVLAAEFGSKARENIIEKYSTESILEKWLN 489
Cdd:cd03800  369 PALWQRLSRAGLERARAHYTWESVADQLLT 398
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 320-473 2.43e-15

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: 77.01  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 320 IVGHISRMVPTKRIDLLIEVAELVvKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVVST 399
Cdd:cd03819  184 VVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLP 262

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446641838 400 SQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKAREN 473
Cdd:cd03819  263 SLHEEFGRVALEAMACGTPVVATDVG-GAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALT 335
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 289-485 9.89e-13

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: 69.28  E-value: 9.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 289 DILNQFdVENIFTISNFVKIHNAPK---------HFQTEKI-VGHISRMVPTKRIDLLIEVAELVVKKDnaVKFHIYGEG 358
Cdd:cd03823  153 FTANLH-EANGLFSARISVIPNAVEpdlappprrRPGTERLrFGYIGRLTEEKGIDLLVEAFKRLPRED--IELVIAGHG 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 359 SvkDKIAKMIEDKnlERNVFLKGYTTTPqkcLEDFK-----LVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIE 433
Cdd:cd03823  230 P--LSDERQIEGG--RRIAFLGRVPTDD---IKDFYekidvLVVPSIWPEPFGLVVREAIAAGLPVIASDLG-GIAELIQ 301

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446641838 434 DNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILE 485
Cdd:cd03823  302 PGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLK 353
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 316-493 1.62e-12

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


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 68.90  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 316 QTEKIVGHISRMV--PTKRIDLLIEVAELVVKKDNAVkFHIYGEGSVKDKIAKMiedknlerNVFLKGYTTtpqkclEDF 393
Cdd:cd03825  191 QDKKVILFGAESVtkPRKGFDELIEALKLLATKDDLL-LVVFGKNDPQIVILPF--------DIISLGYID------DDE 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 394 KLV---------VSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAA 464
Cdd:cd03825  256 QLVdiysaadlfVHPSLADNLPNTLLEAMACGTPVVAFDTG-GSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERE 334

                        170       180
                 ....*....|....*....|....*....
gi 446641838 465 EFGSKARENIIEKYSTESILEKWLNLFNS 493
Cdd:cd03825  335 SLGERARALAENHFDQRVQAQRYLELYKD 363
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 291-493 2.12e-12

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: 68.24  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 291 LNQFDveniFTISNFVKIHNAPKHFQTEKIVGHISRMVPTK-RIDLLIEVAELVVKKDNAvKFHIYGEGSVKDKIAKMIE 369
Cdd:cd04951  165 LNKFK----KDINVRLKIRNKLNLKNDEFVILNVGRLTEAKdYPNLLLAISELILSKNDF-KLLIAGDGPLRNELERLIC 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 370 DKNLERNVFLKGYTTTPQKCLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKngYLIENHNINDM 449
Cdd:cd04951  240 NLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAG-GVAEVVGDHN--YVVPVSDPQLL 316

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446641838 450 ADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNLFNS 493
Cdd:cd04951  317 AEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLYSG 360
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 298-481 3.14e-12

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: 67.68  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 298 NIFTISNFVKIHNAPKhfqtEKIVGHISRMVPTKRIDLLIEVAelvvKKDNAVKFhIYGEGSVKDKIAKMIEdKNLERNV 377
Cdd:cd03795  175 NIPRVDFENIKREKKG----KKIFLFIGRLVYYKGLDYLIEAA----QYLNYPIV-IGGEGPLKPDLEAQIE-LNLLDNV 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 378 FLKGYTTTPQK----CLEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDIKYGPSDFIEDNKNGYLIENHNINDMADKI 453
Cdd:cd03795  245 KFLGRVDDEEKviylHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDALAEAI 324

                        170       180
                 ....*....|....*....|....*...
gi 446641838 454 LQLVNNDVLAAEFGSKARENIIEKYSTE 481
Cdd:cd03795  325 DKLLSDEELRESYGENAKKRFEELFTAE 352
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 267-489 6.23e-12

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: 67.00  E-value: 6.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 267 KYIIENANKIngvIVLTEAQRLDILNQFDV--ENIFTISNFVKIHNAP---------KHFQTEKIVGHISRMVPTKRIDL 335
Cdd:cd03809  133 PISLRRADAI---ITVSEATRDDIIKFYGVppEKIVVIPLGVDPSFFPpesaavliaKYLLPEPYFLYVGTLEPRKNHER 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 336 LIEVAELVVKKDNAVKFHIYGE-GSVKDKIAKMIEDKNLERNVFLKGYTTTPQ--KCLEDFKLVVSTSQYEGQGLSMIEA 412
Cdd:cd03809  210 LLKAFALLKKQGGDLKLVIVGGkGWEDEELLDLVKKLGLGGRVRFLGYVSDEDlpALYRGARAFVFPSLYEGFGLPVLEA 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 413 MISKRPVVAFDIK-----YGPSdfiednknGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENiIEKYSTESILEKW 487
Cdd:cd03809  290 MACGTPVIASNISvlpevAGDA--------ALYFDPLDPESIADAILRLLEDPSLREELIRKGLER-AKKFSWEKTAEKT 360


                 ..
gi 446641838 488 LN 489
Cdd:cd03809  361 LE 362
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 317-492 1.03e-11

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


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 66.58  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 317 TEKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDK-------------------NLERNV 377
Cdd:cd03792  196 ERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPEGSVVYEEvmeyagddhdihvlrlppsDQEINA 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 378 FLKGYTttpqkcledfkLVVSTSQYEGQGLSMIEAMISKRPVVAFD---IKYgpsdFIEDNKNGYLIenhninDMADK-- 452
Cdd:cd03792  276 LQRAAT-----------VVLQLSTREGFGLTVSEALWKGKPVIATPaggIPL----QVIDGETGFLV------NSVEGaa 334

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446641838 453 --ILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNLFN 492
Cdd:cd03792  335 vrILRLLTDPELRRKMGLAAREHVRDNFLITGNLRAWLYLIA 376
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
299-490 4.72e-11

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 64.35  E-value: 4.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 299 IFTISNFVKIHN----APKHFQTEKIVgHISRMVPT--KRI-DLLIEVAELvvkkDNAVKFHIYGEGSVKDKIAKMIEDK 371
Cdd:PRK09922 158 ISVIYNPVEIKTiiipPPERDKPAVFL-YVGRLKFEgqKNVkELFDGLSQT----TGEWQLHIIGDGSDFEKCKAYSREL 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 372 NLERNVFLKGYTTTPQKCLEDFKLVVS----TSQYEGQGLSMIEAMISKRPVVAFDIKYGPSDFIEDNKNGYLIENHNIN 447
Cdd:PRK09922 233 GIEQRIIWHGWQSQPWEVVQQKIKNVSalllTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDIIKPGLNGELYTPGNID 312

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446641838 448 DMADKILQLVNNDVLaaeFGSKARENIIEKYSTESILEKWLNL 490
Cdd:PRK09922 313 EFVGKLNKVISGEVK---YQHDAIPNSIERFYEVLYFKNLNNA 352
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 318-486 4.75e-11

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: 64.23  E-value: 4.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 318 EKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVV 397
Cdd:cd03812  191 KLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFL 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 398 STSQYEGQGLSMIEAMISKRPVVAfdikygpSDFI-EDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENIIE 476
Cdd:cd03812  271 FPSLYEGLPLVAVEAQASGLPCLL-------SDTItKECDITNNVEFLPLNETPSTWAEKILKLIKRKRRINKEINKEKK 343

                        170
                 ....*....|
gi 446641838 477 KYSTESILEK 486
Cdd:cd03812  344 ELGYDDESLE 353
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 271-491 4.91e-11

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


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 64.66  E-value: 4.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 271 ENANKIngvIVLTE-AQRLDILNQFDVENIFTISNFVKIH---NAPKhFQTEKI---VGHISRMVPTKRIDLLIEVAELV 343
Cdd:cd03813  243 QQADKI---ISLYEgNRRRQIRLGADPDKTRVIPNGIDIQrfaPARE-ERPEKEppvVGLVGRVVPIKDVKTFIRAFKLV 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 344 VKKDNAVKFHIYG---EGSVKDKIAK-MIEDKNLERNVFLKGytttPQKCLEDFK---LVVSTSQYEGQGLSMIEAMISK 416
Cdd:cd03813  319 RRAMPDAEGWLIGpedEDPEYAQECKrLVASLGLENKVKFLG----FQNIKEYYPklgLLVLTSISEGQPLVILEAMASG 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 417 RPVVAFD------IKYGPSDFIedNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLNL 490
Cdd:cd03813  395 VPVVATDvgscreLIYGADDAL--GQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKL 472


                 .
gi 446641838 491 F 491
Cdd:cd03813  473 Y 473
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 406-486 4.20e-10

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: 61.16  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 406 GLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENiIEKYSTESILE 485
Cdd:cd03814  281 GLVVLEAMASGLPVVAADAG-GPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAE-AERYSWEAFLD 358


                 .
gi 446641838 486 K 486
Cdd:cd03814  359 N 359
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 308-492 7.39e-10

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: 60.38  E-value: 7.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 308 IHNA--PKHF----QTEKIVGHISRMVPTKRIDLLIEVAelvvkKDNAVKFHIYGEGSVKDKiAKMIEDKNLERNVFLKG 381
Cdd:cd03802  153 VHNGldPADYrfqpDPEDYLAFLGRIAPEKGLEDAIRVA-----RRAGLPLKIAGKVRDEDY-FYYLQEPLPGPRIEFIG 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 382 YTTTPQKC--LEDFKLVVSTSQY-EGQGLSMIEAMISKRPVVAFdiKYG-PSDFIEDNKNGYLIEnhNINDMADKILQLv 457
Cdd:cd03802  227 EVGHDEKQelLGGARALLFPINWdEPFGLVMIEAMACGTPVIAY--RRGgLPEVIQHGETGFLVD--SVEEMAEAIANI- 301

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446641838 458 nndvlaAEFGSKA-RENIIEKYSTESILEKWLNLFN 492
Cdd:cd03802  302 ------DRIDRAAcRRYAEDRFSAARMADRYEALYR 331
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 324-481 8.53e-10

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: 60.68  E-value: 8.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 324 ISRMVPTKRIDLLIEV-AELVVKKDNAVKFHIYGEGSVKDKIAKMIE---------DKNLERN---VFLKGYTTTpQKC- 389
Cdd:cd03805  217 INRFERKKNIALAIEAfAKLKQKLPEFENVRLVIAGGYDPRVAENVEyleelqrlaEELLNVEdqvLFLRSISDS-QKEq 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 390 -LEDFKLVVSTSQYEGQGLSMIEAMISKRPVVAFDiKYGPSDFIEDNKNGYLIENhNINDMADKILQLVNNDVLAAEFGS 468
Cdd:cd03805  296 lLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACN-SGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGA 373

                        170
                 ....*....|...
gi 446641838 469 KARENIIEKYSTE 481
Cdd:cd03805  374 AGRKRVKEKFSRE 386
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 324-478 2.45e-09

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: 59.00  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 324 ISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQ--KCLEDFKLVVSTS- 400
Cdd:cd03799  180 VGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEiiEILDEADIFIAPSv 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 401 -----QYEGQGLSMIEAMISKRPVVAfDIKYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENII 475
Cdd:cd03799  260 taadgDQDGPPNTLKEAMAMGLPVIS-TEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVE 338


                 ...
gi 446641838 476 EKY 478
Cdd:cd03799  339 EEY 341
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 325-481 5.36e-09

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


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 58.24  E-value: 5.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 325 SRMVPTKRIDLLIEVAELVVKKDNAVKF---HIyGEGSVKDKIAKMIEDKNLERNVFLKGYTTTpQKCLE-----DFKLV 396
Cdd:cd04946  231 SSIVPVKRIDLIIETLNSLCVAHPSICIswtHI-GGGPLKERLEKLAENKLENVKVNFTGEVSN-KEVKQlykenDVDVF 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 397 VSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFIEDNKNGYLI-ENHNINDMADKILQLVNNDVLAAEFGSKARENII 475
Cdd:cd04946  309 VNVSESEGIPVSIMEAISFGIPVIATNVG-GTREIVENETNGLLLdKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWE 387


                 ....*.
gi 446641838 476 EKYSTE 481
Cdd:cd04946  388 ERFNAE 393
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 253-483 5.84e-08

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: 54.68  E-value: 5.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 253 HENFDDTGAFKKSEKYIIE--NANKINGVIVLT--EAQRLDILN----QFDVENIFTISNFVKIHNAPKHFQT---EKIV 321
Cdd:cd03821  128 PWALQQKHWKKRIALHLIErrNLNNAALVHFTSeqEADELRRFGleppIAVIPNGVDIPEFDPGLRDRRKHNGledRRII 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 322 GHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGS-VKDKIAKMIEDKNLERNVFLKGYTTTPQK--CLEDFKLVVS 398
Cdd:cd03821  208 LFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDgAYPAFLQLQSSLGLGDRVTFTGPLYGEAKwaLYASADLFVL 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 399 TSQYEGQGLSMIEAMISKRPVVAFDiKYGPSDFIEDNkNGYLIENhNINDMADKILQLVNNDVLAAEFGSKARE--NIIE 476
Cdd:cd03821  288 PSYSENFGNVVAEALACGLPVVITD-KCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRDPADRKRLGEMARRarQVEE 364


                 ....*..
gi 446641838 477 KYSTESI 483
Cdd:cd03821  365 NFSWEAV 371
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 293-412 8.02e-07

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


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 51.08  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 293 QFDVENIFTISNFVKIH----NAPKHFQTEKIVGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMI 368
Cdd:cd03796  164 SLDPRIVSVIPNAVDSSdftpDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMR 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446641838 369 EDKNLERNVFLKGYTTTPQKC--LEDFKLVVSTSQYEGQGLSMIEA 412
Cdd:cd03796  244 EKYQLQDRVELLGAVPHEEVRdvLVQGHIFLNTSLTEAFCIAIVEA 289
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 321-492 8.27e-07

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 51.57  E-value: 8.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 321 VGHISRMVPTKRIDLLIEVAELVVKKDNAVKFHIYGEGSVKDKIAKMIEDKNLERNVFLKGYTTTPQKCLEDFKLVVSTS 400
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLS 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 401 QYEGQGLSMIEAMISKRPVVAfDIKYGPSDFIEDNKNGYLIENHNIN--DMADKILQLVnnDVLAAEFG--SKARENIIE 476
Cdd:PRK15179 600 RFEGLPNVLIEAQFSGVPVVT-TLAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIH--DMCAADPGiaRKAADWASA 676

                        170
                 ....*....|....*.
gi 446641838 477 KYSTESILEKWLNLFN 492
Cdd:PRK15179 677 RFSLNQMIASTVRCYQ 692
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 325-447 7.15e-06

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: 48.05  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 325 SRMVPTKRIDLLIEV-----AELVVkkdnavkfhiYGEGSVKDKIAKMiedknLERNVFLKGYTTTPQ------KC---- 389
Cdd:cd03804  206 SRLVPYKRIDLAVEAfnelpKRLVV----------IGDGPDLDRLRAM-----ASPNVEFLGYQPDEVlkellsKArafv 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446641838 390 ---LEDFklvvstsqyegqGLSMIEAMISKRPVVAFDiKYGPSDFIEDNKNGYLIENHNIN 447
Cdd:cd03804  271 faaEEDF------------GIVPVEAQACGTPVIAFG-KGGALETVRPGPTGILFGEQTVE 318
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 319-479 4.15e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.86  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 319 KIVGHISRMVPTKRIDLLIEVAElvvkKDNAVKFHIYGEGSVKDKIAKMIEDKNLernVF---LKGytttpqkclEDFK- 394
Cdd:PLN02871 264 PLIVYVGRLGAEKNLDFLKRVME----RLPGARLAFVGDGPYREELEKMFAGTPT---VFtgmLQG---------DELSq 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 395 ------LVVSTSQYEGQGLSMIEAMISKRPVVAFDIKyGPSDFI---EDNKNGYLIENHNINDMADKILQLVNNDVLAAE 465
Cdd:PLN02871 328 ayasgdVFVMPSESETLGFVVLEAMASGVPVVAARAG-GIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRER 406

                        170
                 ....*....|....
gi 446641838 466 FGSKARENiIEKYS 479
Cdd:PLN02871 407 MGAAAREE-VEKWD 419
Glyco_trans_A_1 pfam09318
Glycosyl transferase 1 domain A; Glyco_trans_A_1 is family of found predominantly at the ...
 14-210 9.96e-05

Glycosyl transferase 1 domain A; Glyco_trans_A_1 is family of found predominantly at the N-terminus of various prokaryotic alpha-glucosyltransferases. According to whether the domain exists as a whole molecule or as a half molecule determines the number of sugar residues that the molecule transfers. Two-domain proteins are processive in that they transfer more than one sugar residue, processively; single domain proteins transfer just one sugar moiety.


Pssm-ID: 370428  Cd Length: 199  Bit Score: 43.49  E-value: 9.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838   14 NKGGMTSSMFNRSKEF-YDADIPADIVTFDYKGNYDEIIKALKKQGKMDRR-TKMYNVFEYFKQI-SNNKHFKSNKLLYK 90
Cdd:pfam09318  10 KYGGLTKSLLLRAKLFgEECNINTFFLTFRFDLEFSQKIDEIFDKGIIDKKfTKIINLFDDFLIPnCNGKEQYEERIGLD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838   91 HISERLKNTieiEESKGISRYFDITTGTY-IAYIRKSKSEKVIDFFKDNKRIERfsfidnkvhmKETFNVDNKVCYQVFY 169
Cdd:pfam09318  90 QIKKHAGMG---KFAKTLLRLFDHEDNEMrMIRNEDGEQIEIVDYFHDKNQLEK----------REEYNKNGNLHKVSHF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446641838  170 D-EKGYPYISRNINANNGAVGKTYVLVNKKEFKNNLALCVYY 210
Cdd:pfam09318 157 DqELGKMYLEEFINDNNHIYLDKGYADLKEEADSKLRDIIWY 198
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
411-489 3.55e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 36.81  E-value: 3.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446641838  411 EAMISKRPVVAFDIKyGPSDFIEDNKNGYLIENHNinDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKWLN 489
Cdd:pfam13524  18 EAAACGAPLLTDRTP-GLEELFEPGEEILLYRDPE--ELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAEQLLD 93
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 403-478 4.19e-03

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: 39.36  E-value: 4.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446641838 403 EGQGLSMIEAMISKRPVVAfDIKYGPSDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENIIEKY 478
Cdd:cd05844  279 EGLGIVLLEAAACGVPVVS-SRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQF 353
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 408-488 4.21e-03

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 39.27  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641838 408 SMIEAMISKRPVVAFDIKYGPsDFIEDNKNGYLIENHNINDMADKILQLVNNDVLAAEFGSKARENIIEKYSTESILEKW 487
Cdd:cd03818  316 SLLEAMACGCPVIGSDTAPVR-EVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLARY 394


                 .
gi 446641838 488 L 488
Cdd:cd03818  395 L 395
 
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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