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Conserved domains on  [gi|1816124943|ref|WP_163255994|]
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glycosyltransferase [Clostridium sporogenes]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
80-358 4.71e-59

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03798:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 376  Bit Score: 195.29  E-value: 4.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEE-TNQYTTK-N 154
Cdd:cd03798    96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEElVALGVPRdR 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 155 IEITPFGVNIDTFKPCADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELN 233
Cdd:cd03798   175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 234 IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDEL 313
Cdd:cd03798   255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1816124943 314 EEAIERLIEDDNLRINMGKTGRRFVEdNFNIEDNFNNVDTIYKSI 358
Cdd:cd03798   333 AAALRRALAEPYLRELGEAARARVAE-RFSWVKAADRIAAAYRDV 376
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
2-140 3.16e-40

Glycosyl transferase 4-like;


:

Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 138.61  E-value: 3.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943   2 KICYLADANSTHTKKWCRFFKNKGYDIDVISLNDGEID-----GVTVHSFNKDldkiRKGssfnKISYIKYFSdIKKIIE 76
Cdd:pfam13477   1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816124943  77 KIKPDVVHAHYATSYGLLGAL----SGFHPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTS 140
Cdd:pfam13477  72 KIKPDVVHVHYAKPYGLLAGLaarlSGFPPVVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
 
Name Accession Description Interval E-value
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
80-358 4.71e-59

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: 195.29  E-value: 4.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEE-TNQYTTK-N 154
Cdd:cd03798    96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEElVALGVPRdR 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 155 IEITPFGVNIDTFKPCADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELN 233
Cdd:cd03798   175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 234 IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDEL 313
Cdd:cd03798   255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1816124943 314 EEAIERLIEDDNLRINMGKTGRRFVEdNFNIEDNFNNVDTIYKSI 358
Cdd:cd03798   333 AAALRRALAEPYLRELGEAARARVAE-RFSWVKAADRIAAAYRDV 376
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
177-337 4.43e-46

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: 154.74  E-value: 4.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 177 KENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRF 256
Cdd:pfam00534   1 KKKIIL-FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 257 DVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRR 336
Cdd:pfam00534  80 DVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157

                  .
gi 1816124943 337 F 337
Cdd:pfam00534 158 R 158
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
2-140 3.16e-40

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 138.61  E-value: 3.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943   2 KICYLADANSTHTKKWCRFFKNKGYDIDVISLNDGEID-----GVTVHSFNKDldkiRKGssfnKISYIKYFSdIKKIIE 76
Cdd:pfam13477   1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816124943  77 KIKPDVVHAHYATSYGLLGAL----SGFHPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTS 140
Cdd:pfam13477  72 KIKPDVVHVHYAKPYGLLAGLaarlSGFPPVVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
245-359 2.79e-29

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 109.31  E-value: 2.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 245 NQEKVIEAF-NRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIED 323
Cdd:COG0438     9 GLDLLLEALlAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1816124943 324 DNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYKSII 359
Cdd:COG0438    87 PELRRRLGEAARERAEERFSWEAIAERLLALYEELL 122
mycothiol_MshA TIGR03449
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ...
133-331 5.20e-29

D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.


Pssm-ID: 132490 [Multi-domain]  Cd Length: 405  Bit Score: 115.99  E-value: 5.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 133 ADI-IMSTSKVMAEETNQY--TTKNIEITPFGVNIDTFKPcADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFA 202
Cdd:TIGR03449 164 ADRlIANTDEEARDLVRHYdaDPDRIDVVAPGADLERFRP-GDRATERARLglpldtkVVAFVGRIQPLKAPDVLLRAVA 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 203 KVKQKHNNIKLEIAGVG-------DQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAV 275
Cdd:TIGR03449 243 ELLDRDPDRNLRVIVVGgpsgsglATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVPSY--NESFGLVAM 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1816124943 276 EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMG 331
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMG 376
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
131-339 1.46e-16

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 80.53  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 131 SKADIIMSTSKVMAEE--TNQYTT-KNIEITPFGVNIDTFKPCADKYEKKENL--------VIGTVKTLepkyGIEYLVR 199
Cdd:PLN02871  204 RAADLTLVTSPALGKEleAAGVTAaNRIRVWNKGVDSESFHPRFRSEEMRARLsggepekpLIVYVGRL----GAEKNLD 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 200 AFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNikdhVKFLGFINQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQA 279
Cdd:PLN02871  280 FLKRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPS--ESETLGFVVLEAMA 353
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816124943 280 CGTPVIVSNVGGLPE---ATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVE 339
Cdd:PLN02871  354 SGVPVVAARAGGIPDiipPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVE 416
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
227-290 7.93e-03

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


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 37.99  E-value: 7.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816124943 227 NLCNELNIKDHVKFLGFinqEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVG 290
Cdd:NF038011  358 SLVASLGLQDKVKFLGF---QKIDDLLPQVGLMVLSSI--SEALPLVVLEAFAAGVPVVTTDVG 416
 
Name Accession Description Interval E-value
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
80-358 4.71e-59

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: 195.29  E-value: 4.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEE-TNQYTTK-N 154
Cdd:cd03798    96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEElVALGVPRdR 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 155 IEITPFGVNIDTFKPCADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELN 233
Cdd:cd03798   175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 234 IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDEL 313
Cdd:cd03798   255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1816124943 314 EEAIERLIEDDNLRINMGKTGRRFVEdNFNIEDNFNNVDTIYKSI 358
Cdd:cd03798   333 AAALRRALAEPYLRELGEAARARVAE-RFSWVKAADRIAAAYRDV 376
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
11-356 4.43e-57

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: 190.06  E-value: 4.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  11 STHTKKWCRFFKNKGYDIDVISLNDGEIDGVTVHSFNKDLDKIRKGSSFNKISYIKYFSdikKIIEKIKPDVVHAHYATS 90
Cdd:cd03801    17 ERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR---PLLRLRKFDVVHAHGLLA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  91 --YGLLGALSGFHPYIISVWGSDVYDFPKGSYIKRKMV---EYNLSKADIIMSTSKVMAEETNQY---TTKNIEITPFGV 162
Cdd:cd03801    94 alLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLaraEALLRRADAVIAVSEALRDELRALggiPPEKIVVIPNGV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 163 NIDTFKPC--ADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGV-GDQKDFLLNLcnELNIKDHVK 239
Cdd:cd03801   174 DLERFSPPlrRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGdGPLRAELEEL--ELGLGDRVR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 240 FLGFINQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIER 319
Cdd:cd03801   252 FLGFVPDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLR 329
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1816124943 320 LIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03801   330 LLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
2-345 1.18e-46

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: 162.38  E-value: 1.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943   2 KICYLADANS---THTKKWCRFFKNKGYDIDVISLNDGEID------GVTVHSFNkdldkiRKGSSFNKISYIKYFSDIK 72
Cdd:cd03808     1 KILFIVNVDGgfqSFRLPLIKALVKKGYEVHVIAPDGDKLSdelkelGVKVIDIP------ILRRGINPLKDLKALFKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  73 KIIEKIKPDVVHAHyaTS----YGLLGALSGFHPYIISV---WGsdvYDFPKGSYIKR--KMVE-YNLSKADIIMSTSKV 142
Cdd:cd03808    75 KLLKKEKPDIVHCH--TPkpgiLGRLAARLAGVPKVIYTvhgLG---FVFTEGKLLRLlyLLLEkLALLFTDKVIFVNED 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 143 MAEETNQY---TTKNIEITP-FGVNIDTFKPcADKYEKKENLVIGTV-KTLEPKyGIEYLVRAFAKVKQKHNNIKLEIAG 217
Cdd:cd03808   150 DRDLAIKKgiiKKKKTVLIPgSGVDLDRFQY-SPESLPSEKVVFLFVaRLLKDK-GIDELIEAAKILKKKGPNVRFLLVG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 218 VGDQKDFLLNLCNELNIKDHVKFLGFInqEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATS 297
Cdd:cd03808   228 DGELENPSEILIEKLGLEGRIEFLGFR--SDVPELLAESDVFVLPS--YREGLPRSLLEAMAAGRPVITTDVPGCRELVI 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1816124943 298 PNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03808   304 DGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEE 351
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
177-337 4.43e-46

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: 154.74  E-value: 4.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 177 KENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRF 256
Cdd:pfam00534   1 KKKIIL-FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 257 DVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRR 336
Cdd:pfam00534  80 DVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157

                  .
gi 1816124943 337 F 337
Cdd:pfam00534 158 R 158
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
18-356 5.72e-42

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: 150.16  E-value: 5.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  18 CRFFKNKGYDIDVISL-NDGEI------DGVTVHSFNKDLDKirkgSSFNKISYIKYFSDIKkiiekikPDVVHAH--YA 88
Cdd:cd03807    22 LEHMDKSRFEHVVISLtGDGVLgeellaAGVPVVCLGLSSGK----DPGVLLRLAKLIRKRN-------PDVVHTWmyHA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  89 TSYGLLGA-LSGFHPYIISVWGSDvyDFPKGSYIKRKMvEYNLSKADI-IMSTSKVMAEETNQ--YTTKNIEITPFGVNI 164
Cdd:cd03807    91 DLIGGLAAkLAGGVKVIWSVRSSN--IPQRLTRLVRKL-CLLLSKFSPaTVANSSAVAEFHQEqgYAKNKIVVIYNGIDL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 165 DTFKPCADK--------YEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKD 236
Cdd:cd03807   168 FKLSPDDASrararrrlGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLED 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 237 HVKFLGfiNQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEaTSPNNSSLLVNKKSVDELEEA 316
Cdd:cd03807   248 RVHLLG--ERSDVPALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVGGAAE-LVDDGTGFLVPAGDPQALADA 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1816124943 317 IERLIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03807   323 IRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
2-140 3.16e-40

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 138.61  E-value: 3.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943   2 KICYLADANSTHTKKWCRFFKNKGYDIDVISLNDGEID-----GVTVHSFNKDldkiRKGssfnKISYIKYFSdIKKIIE 76
Cdd:pfam13477   1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816124943  77 KIKPDVVHAHYATSYGLLGAL----SGFHPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTS 140
Cdd:pfam13477  72 KIKPDVVHVHYAKPYGLLAGLaarlSGFPPVVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-345 3.50e-37

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: 137.86  E-value: 3.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943   2 KICYLAD-------ANSTHTKKWCRFFKNKGYDIDVI------------SLNDGEIDGVTVHSF-------NKDLDKIRK 55
Cdd:cd03794     1 KILLISQyypppkgAAAARVYELAKELVRRGHEVTVLtpspnyplgrifAGATETKDGIRVIRVklgpikkNGLIRRLLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  56 GSSFNKISYIKYFsdikkiIEKIKPDVVHAH--YATSYGLLGALSGFH--PYIISV------WGSDVYDFPKGSYIK--R 123
Cdd:cd03794    81 YLSFALAALLKLL------VREERPDVIIAYspPITLGLAALLLKKLRgaPFILDVrdlwpeSLIALGVLKKGSLLKllK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 124 KMVEYNLSKADIIMSTSKVMAEETNQ--YTTKNIEITPFGVNIDTFKPCADKYEKKEN-----LVIGTVKTLEPKYGIEY 196
Cdd:cd03794   155 KLERKLYRLADAIIVLSPGLKEYLLRkgVPKEKIIVIPNWADLEEFKPPPKDELRKKLglddkFVVVYAGNIGKAQGLET 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 197 LVRAFAKVKQkHNNIKLEIAGVGDQKDFLLNLCNELNIKDhVKFLGFINQEKVIEAFNRFDVAVFPstLDSESFGVAAV- 275
Cdd:cd03794   235 LLEAAERLKR-RPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVGLVP--LKDNPANRGSSp 310
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816124943 276 ----EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03794   311 sklfEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSRE 384
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
17-344 3.65e-37

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: 137.10  E-value: 3.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  17 WCRFFKNKGYDIDVISLNDG----EIDGVTVHSFNKDLDKIRKGSSFNKISYIKYFSdikkIIEKIKPDVVHAHYATSYG 92
Cdd:cd03811    21 LANALDKRGYDVTLVLLRDEgdldKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR----ILKRAKPDVVISFLGFATY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  93 LLGALSGFHPYIISVWGSDvYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEE---TNQYTTKNIEITPFGVNIDTFKP 169
Cdd:cd03811    97 IVAKLAAARSKVIAWIHSS-LSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDlirLGPSPPEKIEVIYNPIDIDRIRA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 170 CADK---YEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFinQ 246
Cdd:cd03811   176 LAKEpilNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGF--Q 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 247 EKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDEL---EEAIERLIED 323
Cdd:cd03811   254 SNPYPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALagiLAALLQKKLD 331
                         330       340
                  ....*....|....*....|.
gi 1816124943 324 DNLRINMGKtGRRFVEDNFNI 344
Cdd:cd03811   332 AALRERLAK-AQEAVFREYTI 351
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
4-358 4.80e-37

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: 137.03  E-value: 4.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943   4 CYLADAN--STHTKKWCRFFKNKGYDIDVISLNDGEidgvtvHSFNKDLDKIRKGSSFNKISY-----IKYFSDIKKIIE 76
Cdd:cd03817     8 TYLPQVNgvATSVRNLARALEKRGHEVYVITPSDPG------AEDEEEVVRYRSFSIPIRKYHrqhipFPFKKAVIDRIK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  77 KIKPDVVHAHYATSYGLLGALSG----------FHpyiiSVWGSDVYDFPKGSYIKRKMVE------YNlsKADIIMSTS 140
Cdd:cd03817    82 ELGPDIIHTHTPFSLGKLGLRIArklkipivhtYH----TMYEDYLHYIPKGKLLVKAVVRklvrrfYN--HTDAVIAPS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 141 KVMAEETNQY-TTKNIEITPFGVNIDTFKPCADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKQKhNNIKL 213
Cdd:cd03817   156 EKIKDTLREYgVKGPIEVIPNGIDLDKFEKPLNTEERRKLGlppdepILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 214 EIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLP 293
Cdd:cd03817   235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFAST--TETQGLVYLEAMAAGLPVVAAKDPAAS 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816124943 294 EATSPNNSSLLVnKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNIEDnfnnVDTIYKSI 358
Cdd:cd03817   313 ELVEDGENGFLF-EPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKS----VEKLYEEV 372
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
80-343 4.92e-36

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: 135.06  E-value: 4.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAHYATSyGLLGAL----SG------FH-------PYIIsvwGSDVYDFPKgsyikRKMVEYN-LSKAD-IIMSTS 140
Cdd:cd03800   102 YDLIHSHYWDS-GLVGALlarrLGvplvhtFHslgrvkyRHLG---AQDTYHPSL-----RITAEEQiLEAADrVIASTP 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 141 KVMAEETNQYTTK--NIEITPFGVNIDTFKPCADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFAKVKQKHNNI 211
Cdd:cd03800   173 QEADELISLYGADpsRINVVPPGVDLERFFPVDRAEARRARLllppdkpVVLALGRLDPRKGIDTLVRAFAQLPELRELA 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 212 KLEIAGvGDQKDFLLN-------LCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd03800   253 NLVLVG-GPSDDPLSMdreelaeLAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSL--YEPFGLTAIEAMACGTPV 329
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1816124943 285 IVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFN 343
Cdd:cd03800   330 VATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYT 388
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
121-345 6.12e-36

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: 134.03  E-value: 6.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 121 IKRKMVEYNLSKADIIMSTSKVMAEETNQYT---TKNIEITPFGVNIDTFKPCADKYEKKEN-------LVIGTvktLEP 190
Cdd:cd03809   127 YYRLLLPISLRRADAIITVSEATRDDIIKFYgvpPEKIVVIPLGVDPSFFPPESAAVLIAKYllpepyfLYVGT---LEP 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 191 KYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDF-LLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSES 269
Cdd:cd03809   204 RKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEeLLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSL--YEG 281
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816124943 270 FGVAAVEAQACGTPVIVSNVGGLPEATSPnnSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEdNFNIE 345
Cdd:cd03809   282 FGLPVLEAMACGTPVIASNISVLPEVAGD--AALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWE 354
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
13-345 1.32e-34

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: 130.57  E-value: 1.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  13 HTKKWCRFFK---NKGYDIDVISLNDGEIDGVTVhsfnKDLDKIRKGSSFNKISYIK---------YFSDIKKIIEKIKP 80
Cdd:cd03821    16 PVKVVLRLAAalaALGHEVTIVSTGDGYESLVVE----ENGRYIPPQDGFASIPLLRqgagrtdfsPGLPNWLRRNLREY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  81 DVVHAHYATSYGLLGAL---SGFH-PYIISVWGS-DVYDFPKgSYIKRKMVEY-----NLSKADIIMSTSKVMAEETN-- 148
Cdd:cd03821    92 DVVHIHGVWTYTSLAACklaRRRGiPYVVSPHGMlDPWALQQ-KHWKKRIALHlierrNLNNAALVHFTSEQEADELRrf 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 149 QYTTKnIEITPFGVNIDTFKPcADKYEKKENL-----VIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQK- 222
Cdd:cd03821   171 GLEPP-IAVIPNGVDIPEFDP-GLRDRRKHNGledrrIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAy 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 223 DFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSs 302
Cdd:cd03821   249 PAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSY--SENFGNVVAEALACGLPVVITDKCGLSELVEAGCG- 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1816124943 303 lLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFV--EDNFNIE 345
Cdd:cd03821   326 -VVVDPNVSSLAEALAEALRDPADRKRLGEMARRARqvEENFSWE 369
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
23-345 1.57e-34

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: 130.05  E-value: 1.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  23 NKGYDIDVISLNDGEI-------DGVTVhsfnKDLDKIRKGSSFNKISYIKYFSDIKKIIEKIKPDVVhahYATSYGLLG 95
Cdd:cd03820    28 KKGYDVTIISLDSAEKppfyeldDNIKI----KNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVV---ISFRTSLLT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  96 ALSGF-HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEETNQYTTKNIEITPfgvNIDTFKPCADKY 174
Cdd:cd03820   101 FLALIgLKSKLIVWEHNNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKKYKQPNSNVVVIP---NPLSFPSEEPST 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 175 EKKENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFinQEKVIEAFN 254
Cdd:cd03820   178 NLKSKRIL-AVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGP--TKNIAEEYA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 255 RFDVAVFPStlDSESFGVAAVEAQACGTPVIVSN-VGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKT 333
Cdd:cd03820   255 NSSIFVLSS--RYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKN 332
                         330
                  ....*....|..
gi 1816124943 334 GRRFVEDnFNIE 345
Cdd:cd03820   333 ARKNAER-FSIE 343
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
21-344 2.24e-34

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: 129.49  E-value: 2.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  21 FKNKGYDIDVISLNDGeiDGVTVHSfnkDLDKIRKgSSFNKISYIKYFSDIKKIiekikpDVVHAHYATSyGLLGAL--- 97
Cdd:cd03799    24 LIDRGHEVDIYAVNPG--DLVKRHP---DVEKYNV-PSLNLLYAIVGLNKKGAY------DIIHCQFGPL-GALGALlrr 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  98 ---------SGFHPYIISVW----GSDVYD--FPKGS-------YIKRKMVEYNLSKADIIMSTSKVmaeETNQYTtkni 155
Cdd:cd03799    91 lkvlkgklvTSFRGYDISMYvileGNKVYPqlFAQGDlflpnceLFKHRLIALGCDEKKIIVHRSGI---DCNKFR---- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 156 eitpfgvnidtFKPCADKYEKKenLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIK 235
Cdd:cd03799   164 -----------FKPRYLPLDGK--IRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 236 DHVKFLGFINQEKVIEAFNRFDVAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVD 311
Cdd:cd03799   231 DCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAE 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1816124943 312 ELEEAIERLIEDDNLRINMGKTGRRFVEDNFNI 344
Cdd:cd03799   311 AIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDI 343
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
181-323 4.20e-34

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 122.62  E-value: 4.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 181 VIGTVKTLEPKY-GIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDfLLNLCNELNikDHVKFLGFINQekVIEAFNRFDVA 259
Cdd:pfam13692   3 VILFVGRLHPNVkGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLE--DRVIFTGFVED--LAELLAAADVF 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816124943 260 VFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNsSLLVNKKSVDELEEAIERLIED 323
Cdd:pfam13692  78 VLPSL--YEGFGLKLLEAMAAGLPVVATDVGGIPELVDGEN-GLLVPPGDPEALAEAILRLLED 138
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
81-345 8.34e-34

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: 128.24  E-value: 8.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  81 DVVHAHYATSYgllgALSGFH---------PYIISVWGSDV----YDFPKGSYIKrkmveYNLSKADIIMSTSKVMAEET 147
Cdd:cd04962    86 DVLHAHYAIPH----ASCAYLareilgekiPIVTTLHGTDItlvgYDPSLQPAVR-----FSINKSDRVTAVSSSLRQET 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 148 NQY--TTKNIEITPFGVNIDTFKPCADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVkQKHNNIKLEIAGVG 219
Cdd:cd04962   157 YELfdVDKDIEVIHNFIDEDVFKRKPAGALKRRLLappdekVVIHVSNFRPVKRIDDVVRVFARV-RRKIPAKLLLVGDG 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 220 DQKDFLLNLCNELNIKDHVKFLGfiNQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPN 299
Cdd:cd04962   236 PERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPS--EKESFGLAALEAMACGVPVVSSNAGGIPEVVKHG 311
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1816124943 300 NSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd04962   312 ETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPE 357
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
18-345 2.07e-33

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


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 127.01  E-value: 2.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  18 CRFFKNKGYDIDVISLNDgEIDGVTVHSFNkdlDKIRKGSSFNKI-------SYIKYFsdikkIIEKIKPDVVHAHYATS 90
Cdd:cd03795    24 AEGLKKKGIEVDVLCFSK-EKETPEKEENG---IRIHRVKSFLNVastpfspSYIKRF-----KKLAKEYDIIHYHFPNP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  91 YG-LLGALSGFH-PYIISvWGSDVydfpkgsyIKRKMVE--YN------LSKADIIMSTSKVMAEETNQYT--TKNIEIT 158
Cdd:cd03795    95 LAdLLLFFSGAKkPVVVH-WHSDI--------VKQKKLLklYKplmtrfLRRADRIIATSPNYVETSPTLRefKNKVRVI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 159 PFGVNIDTFKPCADKYEKKENLVIGT-----VKTLEPKYGIEYLVRAfakvkQKHNNIKLEIAGVGDQKDFLLNLCnELN 233
Cdd:cd03795   166 PLGIDKNVYNIPRVDFENIKREKKGKkiflfIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPLKPDLEAQI-ELN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 234 IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDSESFGVAAVEAQACGTPVIVSNVGGlpeATSPNN----SSLLVNKKS 309
Cdd:cd03795   240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGT---GVPYVNnngeTGLVVPPKD 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1816124943 310 VDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03795   317 PDALAEAIDKLLSDEELRESYGENAKKRFEELFTAE 352
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
245-359 2.79e-29

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 109.31  E-value: 2.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 245 NQEKVIEAF-NRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIED 323
Cdd:COG0438     9 GLDLLLEALlAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1816124943 324 DNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYKSII 359
Cdd:COG0438    87 PELRRRLGEAARERAEERFSWEAIAERLLALYEELL 122
mycothiol_MshA TIGR03449
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ...
133-331 5.20e-29

D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.


Pssm-ID: 132490 [Multi-domain]  Cd Length: 405  Bit Score: 115.99  E-value: 5.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 133 ADI-IMSTSKVMAEETNQY--TTKNIEITPFGVNIDTFKPcADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFA 202
Cdd:TIGR03449 164 ADRlIANTDEEARDLVRHYdaDPDRIDVVAPGADLERFRP-GDRATERARLglpldtkVVAFVGRIQPLKAPDVLLRAVA 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 203 KVKQKHNNIKLEIAGVG-------DQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAV 275
Cdd:TIGR03449 243 ELLDRDPDRNLRVIVVGgpsgsglATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVPSY--NESFGLVAM 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1816124943 276 EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMG 331
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMG 376
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
80-339 1.98e-28

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: 113.22  E-value: 1.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAHyATSYGLLGAL---SGFHPYIISVWGSD-VYDFPKGSYI-KRKMVEYnlskaDIIMSTSKVMAEETNQYTTKN 154
Cdd:cd03819    77 IDLIHAH-SRAPAWLGWLasrLTGVPLVTTVHGSYlATYHPKDFALaVRARGDR-----VIAVSELVRDHLIEALGVDPE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 155 -IEITPFGVNIDTFKP-----CADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKqKHNNIKLEIAGVGDQKDFLLN 227
Cdd:cd03819   151 rIRVIPNGVDTDRFPPeaeaeERAQLGLPEGkPVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLLVAGDGPERDEIRR 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 228 LCNELNIKDHVKFLGFInqEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNK 307
Cdd:cd03819   230 LVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSL--HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPP 305
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1816124943 308 KSVDELEEAIERLIEDDNLRinmGKTGRRFVE 339
Cdd:cd03819   306 GDAEALADAIRAAKLLPEAR---EKLQAAAAL 334
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
155-344 1.55e-27

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: 111.39  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 155 IEITPFGVNIDTFKPcadKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELni 234
Cdd:cd05844   168 IHVHYIGIDPAKFAP---RDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL-- 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 235 kDHVKFLGFINQEKVIEAFNRFDVAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSV 310
Cdd:cd05844   243 -GRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDV 321
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1816124943 311 DELEEAIERLIEDDNLRINMGKTGRRFVEDNFNI 344
Cdd:cd05844   322 DALADALQALLADRALADRMGGAARAFVCEQFDI 355
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
81-356 1.05e-25

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: 107.42  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  81 DVVHAHyATSY-GLLGALSGFH---PYIISVWGsdVY------DFPKGS----YIKRKMVEY--NLSK-----ADIIMST 139
Cdd:cd03813   175 DLYHSV-STGYaGLLGALARHRrgiPFLLTEHG--IYtrerkiEILQSTwimgYIKKLWIRFfeRLGKlayqqADKIISL 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 140 SkvmaEETNQYTTK------NIEITPFGVNIDTFKPCADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKL 213
Cdd:cd03813   252 Y----EGNRRRQIRlgadpdKTRVIPNGIDIQRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 214 EIAGVGDQKDFLLNLCNEL----NIKDHVKFLGFINqekVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNV 289
Cdd:cd03813   328 WLIGPEDEDPEYAQECKRLvaslGLENKVKFLGFQN---IKEYYPKLGLLVLTSI--SEGQPLVILEAMASGVPVVATDV 402
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816124943 290 GGLPEA-----TSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03813   403 GSCRELiygadDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
130-358 2.02e-25

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: 105.11  E-value: 2.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 130 LSKADI-IMSTSKVMAEETNQ---YTTKNIEITPFGVNIDTFKPCADKY-------EKKENLVI-GTVKTLEPKYGIEYL 197
Cdd:cd03825   134 LAKKRLtIVAPSRWLADMVRRsplLKGLPVVVIPNGIDTEIFAPVDKAKarkrlgiPQDKKVILfGAESVTKPRKGFDEL 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 198 VRAFAKVkQKHNNIKLEIAGVGDQKDFLLNLcnelnikDHVKFlGFI-NQEKVIEAFNRFDVAVFPSTLDSesFGVAAVE 276
Cdd:cd03825   214 IEALKLL-ATKDDLLLVVFGKNDPQIVILPF-------DIISL-GYIdDDEQLVDIYSAADLFVHPSLADN--LPNTLLE 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 277 AQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFN----IEDNFNnvd 352
Cdd:cd03825   283 AMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDqrvqAQRYLE--- 359

                  ....*.
gi 1816124943 353 tIYKSI 358
Cdd:cd03825   360 -LYKDL 364
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
134-357 5.81e-25

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: 103.95  E-value: 5.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 134 DIIMSTSKVMAE--ETNQYTTKNIEITPFGVNIDTfKPCADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKhnNI 211
Cdd:cd03823   145 DAVLAPSRFTANlhEANGLFSARISVIPNAVEPDL-APPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPRE--DI 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 212 KLEIAGVGDQKDfllnlCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGG 291
Cdd:cd03823   222 ELVIAGHGPLSD-----ERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWP-EPFGLVVREAIAAGLPVIASDLGG 295
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816124943 292 LPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTgrrfVEDNFNIEDNFNNVDTIYKS 357
Cdd:cd03823   296 IAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAG----AEPPRSTESQAEEYLKLYRD 357
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
80-305 1.49e-22

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: 94.78  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMstskvmaeetnqyttknie 156
Cdd:cd01635    55 PDVVHAHSPHAAALAALLAARllgIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVS------------------- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 157 itpfgvnidtfkpcadkyekkenlvigtVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKD 236
Cdd:cd01635   116 ----------------------------VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLE 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 237 HVKFLGFINQEKVIEAFNR-FDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLV 305
Cdd:cd01635   168 RVVIIGGLVDDEVLELLLAaADVFVLPSR--SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
133-340 3.76e-22

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: 96.21  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 133 ADIIMSTSKVMAEETNQYTTKNIEITPFGVNIDTFKPCA------DKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQ 206
Cdd:cd03814   146 FDTTLVPSPSIARELEGHGFERVRLWPRGVDTELFHPSRrdaalrRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAA 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 207 kHNNIKLEIAGVGDQKDfllnlcnELNIKD-HVKFLGFINQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVI 285
Cdd:cd03814   226 -SPPVRLVVVGDGPARA-------ELEARGpDVIFTGFLTGEELARAYASADVFVFPS--RTETFGLVVLEAMASGLPVV 295
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1816124943 286 VSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVED 340
Cdd:cd03814   296 AADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER 350
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
24-328 6.62e-22

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: 95.43  E-value: 6.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  24 KGYDIDVISLNDGEIDgvtvhsfnKDLDKIRKGS-----SFNKISYIKYFSDIKKIIEKIKPDVVHAHYATSYG--LLGA 96
Cdd:cd03812    28 SKIEFDFLATSDDKGE--------YDEELEELGGkifyiPPKKKNIIKYFIKLLKLIKKEKYDIVHVHGSSSNGiiLLLA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  97 LSGFHPYIISVWGSDVYDfpkgSYIKRKMVEYNLSKADIIMST-----SKVMAEET-NQYTTKNIEITPFGVNIDTF--- 167
Cdd:cd03812   100 AKAGVPVRIAHSHNTKDS----SIKLRKIRKNVLKKLIERLSTkylacSEDAGEWLfGEVENGKFKVIPNGIDIEKYkfn 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 168 KPCADKYEKKEN----LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGF 243
Cdd:cd03812   176 KEKRRKRRKLLIledkLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 244 INQekVIEAFNRFDVAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGlPEATSPNNSSLLVNKKSVDELEEAIERLIED 323
Cdd:cd03812   256 RND--VSEILSAMDVFLFPSLY--EGLPLVAVEAQASGLPCLLSDTIT-KECDITNNVEFLPLNETPSTWAEKILKLIKR 330

                  ....*
gi 1816124943 324 DNLRI 328
Cdd:cd03812   331 KRRIN 335
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
129-332 2.83e-20

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: 90.05  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 129 NLSKAD-IIMSTSK---VMAEETNQYttKNIEITPFGVnIDTFKPCADKYEKKENLVIgTVKTLEPKYGIEYLVRAFAKV 204
Cdd:cd04949   110 NLNKYDaIIVSTEQqkqDLSERFNKY--PPIFTIPVGY-VDQLDTAESNHERKSNKII-TISRLAPEKQLDHLIEAVAKA 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 205 KQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEKVIeaFNRFDVAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd04949   186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQE--YQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPV 261
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1816124943 285 IVSNVG-GLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGK 332
Cdd:cd04949   262 VSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSE 310
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
81-322 9.23e-20

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: 89.60  E-value: 9.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  81 DVVHAHYATSY----GLLGA-LSGFHPYII--SVWG-SDVydfpkGSYIKRKMVEYNLSKADIIMSTSKVMAEET---NQ 149
Cdd:cd03796    90 QIVHGHQAFSSlaheALFHArTLGLKTVFTdhSLFGfADA-----SSILTNKLLRFSLADIDHVICVSHTSKENTvlrAS 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 150 YTTKNIEITPFGVNIDTFKPCADKYEKKEnLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLC 229
Cdd:cd03796   165 LDPRIVSVIPNAVDSSDFTPDPSKPDPNK-ITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMR 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 230 NELNIKDHVKFLGFINQEKVIEAFNRFDVavFPSTLDSESFGVAAVEAQACGTPVIVSNVGGLPEATsPNNSSLLVNKKS 309
Cdd:cd03796   244 EKYQLQDRVELLGAVPHEEVRDVLVQGHI--FLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVL-PPDMILLAEPDP 320
                         250
                  ....*....|....*.
gi 1816124943 310 VD---ELEEAIERLIE 322
Cdd:cd03796   321 EDivrKLEEAISILRT 336
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
159-345 3.29e-17

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: 81.57  E-value: 3.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 159 PFGVNIDTFKPCadkYEKKENLV-IGTVKtlePKYGIEYLVRAFAKVkqkhnNIKLEIAGVGDQKD---FLlnlcNELNI 234
Cdd:cd03802   154 HNGLDPADYRFQ---PDPEDYLAfLGRIA---PEKGLEDAIRVARRA-----GLPLKIAGKVRDEDyfyYL----QEPLP 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 235 KDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNkkSVDELE 314
Cdd:cd03802   219 GPRIEFIGEVGHDEKQELLGGARALLFPINWD-EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD--SVEEMA 295
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1816124943 315 EAIERLIEDDNLRInmgktgRRFVEDNFNIE 345
Cdd:cd03802   296 EAIANIDRIDRAAC------RRYAEDRFSAA 320
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
131-339 1.46e-16

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 80.53  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 131 SKADIIMSTSKVMAEE--TNQYTT-KNIEITPFGVNIDTFKPCADKYEKKENL--------VIGTVKTLepkyGIEYLVR 199
Cdd:PLN02871  204 RAADLTLVTSPALGKEleAAGVTAaNRIRVWNKGVDSESFHPRFRSEEMRARLsggepekpLIVYVGRL----GAEKNLD 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 200 AFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNikdhVKFLGFINQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQA 279
Cdd:PLN02871  280 FLKRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPS--ESETLGFVVLEAMA 353
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816124943 280 CGTPVIVSNVGGLPE---ATSPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVE 339
Cdd:PLN02871  354 SGVPVVAARAGGIPDiipPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVE 416
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
80-355 2.67e-16

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: 79.03  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAHYatsygllgalsgFHPYIISVWGSDVYDFPK----------GSYIKRKMVEYNLSKADIIMSTSKVMAEE--T 147
Cdd:cd04951    80 PDVVHSHM------------FHANIFARFLRMLYPIPLlictahnkneGGRIRMFIYRLTDFLCDITTNVSREALDEfiA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 148 NQYTTKNIEIT-PFGVNIDTFKPCADKYEKKEN--------LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGV 218
Cdd:cd04951   148 KKAFSKNKSVPvYNGIDLNKFKKDINVRLKIRNklnlkndeFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGD 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 219 GDQKDFLLNLCNELNIKDHVKFLGFINQekVIEAFNRFDVAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATSP 298
Cdd:cd04951   228 GPLRNELERLICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSEW--EGFGLVVAEAMACERPVVATDAGGVAEVVGD 303
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1816124943 299 NNSSLLVNKKSvdELEEAI-ERLIEDDNLRINMGKTgRRFVEDNFNIEDNFNNVDTIY 355
Cdd:cd04951   304 HNYVVPVSDPQ--LLAEKIkEIFDMSDEERDILGNK-NEYIAKNFSINTIVNEWERLY 358
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
80-344 6.01e-16

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


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 78.23  E-value: 6.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  80 PDVVHAH--YATSYGLLGALSGFHPYIISVWGSDVYDfPKGSYIKrkmveYNLSKADI--IMSTSKVMAEETNQYTTKNI 155
Cdd:TIGR03088  82 PDIVHTRnlAALEAQLPAALAGVPARIHGEHGRDVFD-LDGSNWK-----YRWLRRLYrpLIHHYVAVSRDLEDWLRGPV 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 156 EITPF-------GVNIDTFKP--------CADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQK----HNNIKLEIA 216
Cdd:TIGR03088 156 KVPPAkihqiynGVDTERFHPsrgdrspiLPPDFFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQlpegAERLRLVIV 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 217 GVGDQKDFLLNLCNELNIKDHVKFLGfiNQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEAT 296
Cdd:TIGR03088 236 GDGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQALDLFVLPSL--AEGISNTILEAMASGLPVIATAVGGNPELV 311
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1816124943 297 SPNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNI 344
Cdd:TIGR03088 312 QHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSI 359
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
162-319 1.54e-15

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: 76.94  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 162 VNIDTFKPCADKyekKENLVigTVKTLEPKYGIEYLVRAFAKVkqkhnNIKLEIAGVGDQKDFLLNLCnelniKDHVKFL 241
Cdd:cd03804   187 VDTDAFAPAADK---EDYYL--TASRLVPYKRIDLAVEAFNEL-----PKRLVVIGDGPDLDRLRAMA-----SPNVEFL 251
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816124943 242 GFINQEKVIEAFNRFDVAVFPSTldsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIER 319
Cdd:cd03804   252 GYQPDEVLKELLSKARAFVFAAE---EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEE 326
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
190-344 9.11e-14

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: 71.58  E-value: 9.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 190 PKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKD----FLLN--LCNELNIKD-HVKFLGFINQEkvIEAFNRF-DVAVF 261
Cdd:cd03792   208 PSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDpegsVVYEevMEYAGDDHDiHVLRLPPSDQE--INALQRAaTVVLQ 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 262 PSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNkkSVDELEEAIERLIEDDNLRINMGKTGRRFVEDN 341
Cdd:cd03792   286 LST--REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVN--SVEGAAVRILRLLTDPELRRKMGLAAREHVRDN 361

                  ...
gi 1816124943 342 FNI 344
Cdd:cd03792   362 FLI 364
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
116-345 9.54e-14

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: 71.85  E-value: 9.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 116 PKGSYIKR-------KMVEYNLSKADIIMSTSKVMAEETNQyTTKNIEITPFGV-----NIDTFKPCADKYEKKENLVIG 183
Cdd:cd03805   131 QRKSLLKRlyrkpfdWLEEFTTGMADQIVVNSNFTAGVFKK-TFPSLAKNPPEVlypcvDTDSFDSTSEDPDPGDLIAKS 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 184 TVKTL------EPKYGIEYLVRAFAKVKQKHN---NIKLEIAGVGDQK--------DFLLNLCNEL-NIKDHVKFLGFIN 245
Cdd:cd03805   210 NKKFFlsinrfERKKNIALAIEAFAKLKQKLPefeNVRLVIAGGYDPRvaenveylEELQRLAEELlNVEDQVLFLRSIS 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 246 QEKVIEAFNRFDVAVFpsTLDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKsVDELEEAIERLIEDDN 325
Cdd:cd03805   290 DSQKEQLLSSALALLY--TPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPT-PEAFAEAMLKLANDPD 366
                         250       260
                  ....*....|....*....|
gi 1816124943 326 LRINMGKTGRRFVEDNFNIE 345
Cdd:cd03805   367 LADRMGAAGRKRVKEKFSRE 386
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
154-345 6.19e-13

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 69.05  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 154 NIEITPFGVNIDTFKPCADKyEKKENLVIGTVKT-------LEPKYGIEYLVRAFAKVKQKHNNIKLEIAG------VGD 220
Cdd:PRK15484  162 DISIVPNGFCLETYQSNPQP-NLRQQLNISPDETvllyagrISPDKGILLLMQAFEKLATAHSNLKLVVVGdptassKGE 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 221 QKDFLLNLCNELN-IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATSPN 299
Cdd:PRK15484  241 KAAYQKKVLEAAKrIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVE-EAFCMVAVEAMAAGKPVLASTKGGITEFVLEG 319
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1816124943 300 NSSL-LVNKKSVDELEEAIERLIEDDNlRINMGKTGRRFVEDNFNIE 345
Cdd:PRK15484  320 ITGYhLAEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWE 365
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
49-349 2.26e-12

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: 67.49  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  49 DLDKIRKGSSFNK--------ISYIKYFSDIKKIIEKIKPDVVHAH--YATSYGL-LGALSGFHPYIIS-VWGSDVYDFP 116
Cdd:cd04946    83 IKDKPRSGSFLLLyyfliasfLSKHRVLALLQFVSIFGQGTVVYSYwlNHTALGLgLLKDEYYRDVVISrAHRYDLYEDQ 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 117 KGSYI---KRKMVEYnLSKADIIMSTSKVMAEETNQYTTKNIEITPFGVNIDTFKpcaDKYEKKENLVIGTVKTLEPKYG 193
Cdd:cd04946   163 YGSYYlplREYLVSY-LDAVFLISKEGKDYLQKCYPAYKEKIFVSRLGVSDKEQY---SKVKKEGDLRLVSCSSIVPVKR 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 194 IEYLVRAFAKVKQKHNNIKLE---IAGVGDQKDFLLNLCNELNIKDhVKFLGFINQEKVIEAFNRFDVAVFPSTLDSESF 270
Cdd:cd04946   239 IDLIIETLNSLCVAHPSICISwthIGGGPLKERLEKLAENKLENVK-VNFTGEVSNKEVKQLYKENDVDVFVNVSESEGI 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 271 GVAAVEAQACGTPVIVSNVGGLPEATS-PNNSSLLVNKKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFNIEDNFN 349
Cdd:cd04946   318 PVSIMEAISFGIPVIATNVGGTREIVEnETNGLLLDKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYS 397
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
129-338 4.20e-10

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 59.94  E-value: 4.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 129 NLSKADIIMSTSKVMAEETNQYTTKNIEITPFGVNIDTFKPCADKYEKKENLV-IGTvktlepkyGIEYLVRAFAKVKQK 207
Cdd:COG4641    89 LLPLYDLVFTFDGDCVEEYRALGARRVFYLPFAADPELHRPVPPEARFRYDVAfVGN--------YYPDRRARLEELLLA 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 208 HNNIKLEIAGVGDQKDFLLnlcnelnikDHVKFLGFINQEKVIEAFNRFDVAV-FPSTLDSE-SFGVAAVEAQACGTPVI 285
Cdd:COG4641   161 PAGLRLKIYGPGWPKLALP---------ANVRRGGHLPGEEHPAAYASSKITLnVNRMAASPdSPTRRTFEAAACGAFLL 231
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1816124943 286 VSNVGGLPEATSPNNSSLLVNkkSVDELEEAIERLIEDDNLRINMGKTGRRFV 338
Cdd:COG4641   232 SDPWEGLEELFEPGEEVLVFR--DGEELAEKLRYLLADPEERRAIAEAGRRRV 282
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
154-327 1.38e-09

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: 58.94  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 154 NIEITPFGVNIDTFKPcaDKYEKKENL-----VIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAG--VGDQKD--- 223
Cdd:cd03822   159 NIEVIPHGVPEVPQDP--TTALKRLLLpegkkVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelHPSLARyeg 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 224 --FLLNLCNELNIKDHVKF-LGFINQEKVIEAFNRFDVAVFP--STLDSESfGVAAVeAQACGTPVIVSNVGGLpEATSP 298
Cdd:cd03822   237 erYRKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPylNTEQSSS-GTLSY-AIACGKPVISTPLRHA-EELLA 313
                         170       180
                  ....*....|....*....|....*....
gi 1816124943 299 NNSSLLVNKKSVDELEEAIERLIEDDNLR 327
Cdd:cd03822   314 DGRGVLVPFDDPSAIAEAILRLLEDDERR 342
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
264-343 2.13e-08

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 51.07  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 264 TLDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVnkKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDNFN 343
Cdd:pfam13524   6 SRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLY--RDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHT 83
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
176-346 6.55e-08

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: 53.91  E-value: 6.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 176 KKENLVIGTV-KTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGvGDQ-------------KDFLLNlcnELNIKDH-VKF 240
Cdd:cd03818   210 KAGDPVITYVaRNLEPYRGFHVFMRALPRIQARRPDARVVVVG-GDGvsygspppdggswKQKMLA---ELGVDLErVHF 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 241 LGFINQEKVIEAFNRFDVAVFPSTLDSESFGVaaVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERL 320
Cdd:cd03818   286 VGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLEL 363
                         170       180
                  ....*....|....*....|....*.
gi 1816124943 321 IEDDNLRINMGKTGRRFVEDNFNIED 346
Cdd:cd03818   364 LEDPDRAAALRRAARRTVERSDSLDV 389
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
198-342 1.30e-07

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 53.00  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 198 VRAFAKVKQKH-----NNIKLEIAG----VGDQK--DFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVfpSTLD 266
Cdd:cd03806   256 LRAFAELLKRLpesirSNPKLVLIGscrnEEDKErvEALKLLAKELILEDSVEFVVDAPYEELKELLSTASIGL--HTMW 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 267 SESFGVAAVEAQACGTPVIVSNVGGlPE-----ATSPNNSSLLVnkKSVDELEEAIERLIEDDNLRINMGKTGRRFVEDN 341
Cdd:cd03806   334 NEHFGIGVVEYMAAGLIPLAHASAG-PLldivvPWDGGPTGFLA--STPEEYAEAIEKILTLSEEERLQRREAARSSAER 410

                  .
gi 1816124943 342 F 342
Cdd:cd03806   411 F 411
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
182-331 6.54e-06

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 48.11  E-value: 6.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 182 IGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINqeKVIEAFNRFDVAVF 261
Cdd:PRK15179  520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSR--RVGYWLTQFNAFLL 597
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816124943 262 PSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKSVD--ELEEAIERLIedDNLRINMG 331
Cdd:PRK15179  598 LSRF--EGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIH--DMCAADPG 665
PLN02949 PLN02949
transferase, transferring glycosyl groups
198-343 6.41e-05

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 44.73  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 198 VRAFAKVKQKHN----NIKLEIAGV----GDQK--DFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRfDVAVFPSTLDs 267
Cdd:PLN02949  287 LEAFALALEKLDadvpRPKLQFVGScrnkEDEErlQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGG-AVAGLHSMID- 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 268 ESFGVAAVEAQACGTPVIVSNVGG------LPEATSPnnSSLLVNkkSVDELEEAIERLIE-DDNLRINMGKTGR----R 336
Cdd:PLN02949  365 EHFGISVVEYMAAGAVPIAHNSAGpkmdivLDEDGQQ--TGFLAT--TVEEYADAILEVLRmRETERLEIAAAARkranR 440

                  ....*..
gi 1816124943 337 FVEDNFN 343
Cdd:PLN02949  441 FSEQRFN 447
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
11-165 2.59e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 41.36  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  11 STHTKKWCRFFKNKGYDIDVISLNDG------EIDGVTVHSFNKDLDKIRKGSSFNKISYIKYFSDIKkiiekikPDVVH 84
Cdd:pfam13439   4 ERYVLELARALARRGHEVTVVTPGGPgplaeeVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRER-------PDVVH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  85 AHYATS--YGLLGALSGFH-PYIISV-----WGSDVYDFPKGSYIKRKMVEYNL-SKADIIMSTSKVMAEETNQY---TT 152
Cdd:pfam13439  77 AHSPFPlgLAALAARLRLGiPLVVTYhglfpDYKRLGARLSPLRRLLRRLERRLlRRADRVIAVSEAVADELRRLygvPP 156
                         170
                  ....*....|...
gi 1816124943 153 KNIEITPFGVNID 165
Cdd:pfam13439 157 EKIRVIPNGVDLE 169
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
25-146 6.48e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 39.69  E-value: 6.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943  25 GYDIDVISLNDGEI------DGVTVHSfnkdLDKIRKGSSFNKISYIKYFSDIKKIIEkikPDVVHAHYATS--YGLLGA 96
Cdd:pfam13579  18 GHEVRVVTPGGPPGrpelvgDGVRVHR----LPVPPRPSPLADLAALRRLRRLLRAER---PDVVHAHSPTAglAARLAR 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1816124943  97 LSGFHPYIISVWGSDV--YDFPKGSYIkRKMVEYNLSKADIIMSTSKVMAEE 146
Cdd:pfam13579  91 RRRGVPLVVTVHGLALdyGSGWKRRLA-RALERRLLRRADAVVVVSEAEAEL 141
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
169-351 4.17e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 38.92  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 169 PCADKYEKKENLVIGTVKtLEPKYGIEYLVRAFAKVkqkHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEK 248
Cdd:PRK09922  173 PPPERDKPAVFLYVGRLK-FEGQKNVKELFDGLSQT---TGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPW 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816124943 249 VIEAFNRFDVAVFPSTLDSESFGVAAVEAQACGTPVIVSN-VGGLPEATSPNNSSLLVNKKSVDELEEAIERLIEDDNLR 327
Cdd:PRK09922  249 EVVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVISGEVKY 328
                         170       180
                  ....*....|....*....|....*...
gi 1816124943 328 ----INMgkTGRRFVEDNFniEDNFNNV 351
Cdd:PRK09922  329 qhdaIPN--SIERFYEVLY--FKNLNNA 352
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
227-290 7.93e-03

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


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 37.99  E-value: 7.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816124943 227 NLCNELNIKDHVKFLGFinqEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVG 290
Cdd:NF038011  358 SLVASLGLQDKVKFLGF---QKIDDLLPQVGLMVLSSI--SEALPLVVLEAFAAGVPVVTTDVG 416
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
281-323 9.01e-03

Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an operon of fourteen genes (phnC-to-phnP) related to the cleavage of carbon-phosphorus (C-P) bonds in unactivated alkylphosphonates, supporting bacterial growth on alkylphosphonates as the sole phosphorus source. It was originally considered part of that operon. PhnB appears to play no direct catalytic role in the usage of alkylphosphonate. Although many of the proteins in this family have been annotated as 3-demethylubiquinone-9 3-methyltransferase enzymes by automatic annotation programs, the experimental evidence for this assignment is lacking. In Escherichia coli, the gene coding 3-demethylubiquinone-9 3-methyltransferase enzyme is ubiG, which belongs to the AdoMet-MTase protein family. PhnB-like proteins adopt a structural fold similar to bleomycin resistance proteins, glyoxalase I, and type I extradiol dioxygenases.


Pssm-ID: 319899  Cd Length: 129  Bit Score: 36.10  E-value: 9.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1816124943 281 GTPVIVSNVGGLPEATSPNNSSLLVNKKSVDELEEAIERLIED 323
Cdd:cd06588    57 GQTLMASDDGPGFPFTFGNAISLSVDCDSQEEADRLFEKLSEG 99
 
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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