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Conserved domains on  [gi|924281479|ref|WP_053469087|]
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glycosyltransferase [Clostridium sp. L74]

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 7.70e-60

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: 197.22  E-value: 7.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEETSQYTT--KD 154
Cdd:cd03798   96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEELVALGVprDR 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIDTFKPFADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELN 233
Cdd:cd03798  175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 234 IRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDEL 313
Cdd:cd03798  255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 924281479 314 AEAIEKLIEDDNLRINMGKTGRRFVEdNFNIEDNFNNVDTIYKSI 358
Cdd:cd03798  333 AAALRRALAEPYLRELGEAARARVAE-RFSWVKAADRIAAAYRDV 376
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
2-140 6.89e-39

Glycosyl transferase 4-like;


:

Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 135.14  E-value: 6.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479    2 KICYLADANSTHTKKWCRFFNNKGYDIDVISLNDGEID-----GVAVHSFNKDldkiRKGssfnKISYIKYFSdIKKIIE 76
Cdd:pfam13477   1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479   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 7.70e-60

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: 197.22  E-value: 7.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEETSQYTT--KD 154
Cdd:cd03798   96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEELVALGVprDR 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIDTFKPFADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELN 233
Cdd:cd03798  175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 234 IRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDEL 313
Cdd:cd03798  255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 924281479 314 AEAIEKLIEDDNLRINMGKTGRRFVEdNFNIEDNFNNVDTIYKSI 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 4.35e-47

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: 157.44  E-value: 4.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  177 KENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRF 256
Cdd:pfam00534   1 KKKIIL-FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  257 DIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRR 336
Cdd:pfam00534  80 DVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157

                  .
gi 924281479  337 F 337
Cdd:pfam00534 158 R 158
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
2-140 6.89e-39

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 135.14  E-value: 6.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479    2 KICYLADANSTHTKKWCRFFNNKGYDIDVISLNDGEID-----GVAVHSFNKDldkiRKGssfnKISYIKYFSdIKKIIE 76
Cdd:pfam13477   1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479   77 KIKPDVVHAHYATSYGLLGAL----SGFHPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTS 140
Cdd:pfam13477  72 KIKPDVVHVHYAKPYGLLAGLaarlSGFPPVVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
245-359 1.86e-30

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 112.78  E-value: 1.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 245 NQEKVIEAF-NRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIED 323
Cdd:COG0438    9 GLDLLLEALlAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED 86
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 924281479 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 1.90e-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: 117.15  E-value: 1.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  133 ADI-IMSTSKVMAEETSQY--TTKDIEITPFGVNIDTFKPfADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFA 202
Cdd:TIGR03449 164 ADRlIANTDEEARDLVRHYdaDPDRIDVVAPGADLERFRP-GDRATERARLglpldtkVVAFVGRIQPLKAPDVLLRAVA 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  203 KVKQKHSNIKLEIAGVG-------EQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAV 275
Cdd:TIGR03449 243 ELLDRDPDRNLRVIVVGgpsgsglATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVPSY--NESFGLVAM 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 924281479  276 EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMG 331
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMG 376
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
131-339 6.42e-17

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 81.68  E-value: 6.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 131 SKADIIMSTSKVMAEE--TSQYTT-KDIEITPFGVNIDTFKPFADKYEKKENL--------VIGTVKTLepkyGIEYLVR 199
Cdd:PLN02871 204 RAADLTLVTSPALGKEleAAGVTAaNRIRVWNKGVDSESFHPRFRSEEMRARLsggepekpLIVYVGRL----GAEKNLD 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 200 AFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNirdhVKFLGFINQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQA 279
Cdd:PLN02871 280 FLKRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPS--ESETLGFVVLEAMA 353
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924281479 280 CGTPVIVSNVGGLPE---ATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVE 339
Cdd:PLN02871 354 SGVPVVAARAGGIPDiipPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVE 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 7.70e-60

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: 197.22  E-value: 7.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEETSQYTT--KD 154
Cdd:cd03798   96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEELVALGVprDR 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIDTFKPFADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELN 233
Cdd:cd03798  175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 234 IRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDEL 313
Cdd:cd03798  255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 924281479 314 AEAIEKLIEDDNLRINMGKTGRRFVEdNFNIEDNFNNVDTIYKSI 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 7.90e-59

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: 194.29  E-value: 7.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  11 STHTKKWCRFFNNKGYDIDVISLNDGEIDGVAVHSFNKDLDKIRKGSSFNKISYIKYFSdikKIIEKIKPDVVHAHYATS 90
Cdd:cd03801   17 ERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR---PLLRLRKFDVVHAHGLLA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  91 --YGLLGALSGFHPYIISVWGSDVYDFPKGSYIKRKMV---EYNLSKADIIMSTSKVMAEETSQY---TTKDIEITPFGV 162
Cdd:cd03801   94 alLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLaraEALLRRADAVIAVSEALRDELRALggiPPEKIVVIPNGV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 163 NIDTFKPF--ADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGV-GEQKDFLLSLcnELNIRDHVK 239
Cdd:cd03801  174 DLERFSPPlrRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGdGPLRAELEEL--ELGLGDRVR 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 240 FLGFINQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEK 319
Cdd:cd03801  252 FLGFVPDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLR 329
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 924281479 320 LIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03801  330 LLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
2-345 3.52e-48

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: 166.23  E-value: 3.52e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479   2 KICYLADANS---THTKKWCRFFNNKGYDIDVISLNDGEID------GVAVHSFNkdldkiRKGSSFNKISYIKYFSDIK 72
Cdd:cd03808    1 KILFIVNVDGgfqSFRLPLIKALVKKGYEVHVIAPDGDKLSdelkelGVKVIDIP------ILRRGINPLKDLKALFKLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  73 KIIEKIKPDVVHAHyaTS----YGLLGALSGFHPYIISV---WGsdvYDFPKGSYIKR--KMVE-YNLSKADIIMSTSKV 142
Cdd:cd03808   75 KLLKKEKPDIVHCH--TPkpgiLGRLAARLAGVPKVIYTvhgLG---FVFTEGKLLRLlyLLLEkLALLFTDKVIFVNED 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 143 MAEETSQYTTKDIEITPF----GVNIDTFKPfADKYEKKENLVIGTV-KTLEPKyGIEYLVRAFAKVKQKHSNIKLEIAG 217
Cdd:cd03808  150 DRDLAIKKGIIKKKKTVLipgsGVDLDRFQY-SPESLPSEKVVFLFVaRLLKDK-GIDELIEAAKILKKKGPNVRFLLVG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 218 VGEQKDFLLSLCNELNIRDHVKFLGFInqEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATS 297
Cdd:cd03808  228 DGELENPSEILIEKLGLEGRIEFLGFR--SDVPELLAESDVFVLPS--YREGLPRSLLEAMAAGRPVITTDVPGCRELVI 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 924281479 298 PNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 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 4.35e-47

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: 157.44  E-value: 4.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  177 KENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRF 256
Cdd:pfam00534   1 KKKIIL-FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  257 DIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRR 336
Cdd:pfam00534  80 DVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157

                  .
gi 924281479  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 3.06e-45

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: 158.63  E-value: 3.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  18 CRFFNNKGYDIDVISL-NDGEI------DGVAVHSFNKDLDKirkgSSFNKISYIKYFSDIKkiiekikPDVVHAH--YA 88
Cdd:cd03807   22 LEHMDKSRFEHVVISLtGDGVLgeellaAGVPVVCLGLSSGK----DPGVLLRLAKLIRKRN-------PDVVHTWmyHA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  89 TSYGLLGA-LSGFHPYIISVWGSDvyDFPKGSYIKRKMvEYNLSKADI-IMSTSKVMAEETSQ--YTTKDIEITPFGVNI 164
Cdd:cd03807   91 DLIGGLAAkLAGGVKVIWSVRSSN--IPQRLTRLVRKL-CLLLSKFSPaTVANSSAVAEFHQEqgYAKNKIVVIYNGIDL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 165 DTFKP-FADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRD 236
Cdd:cd03807  168 FKLSPdDASRARARRRLglaedrrVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLED 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 237 HVKFLGfiNQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEaTSPNNSSLLVNKKNVDELAEA 316
Cdd:cd03807  248 RVHLLG--ERSDVPALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVGGAAE-LVDDGTGFLVPAGDPQALADA 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 924281479 317 IEKLIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03807  323 IRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
2-140 6.89e-39

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 135.14  E-value: 6.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479    2 KICYLADANSTHTKKWCRFFNNKGYDIDVISLNDGEID-----GVAVHSFNKDldkiRKGssfnKISYIKYFSdIKKIIE 76
Cdd:pfam13477   1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479   77 KIKPDVVHAHYATSYGLLGAL----SGFHPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTS 140
Cdd:pfam13477  72 KIKPDVVHVHYAKPYGLLAGLaarlSGFPPVVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
80-343 3.57e-38

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: 140.84  E-value: 3.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  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 924281479 141 KVMAEETSQYTTKD--IEITPFGVNIDTFKPFADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNI 211
Cdd:cd03800  173 QEADELISLYGADPsrINVVPPGVDLERFFPVDRAEARRARLllppdkpVVLALGRLDPRKGIDTLVRAFAQLPELRELA 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 212 KLEIAGvGEQKD-------FLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd03800  253 NLVLVG-GPSDDplsmdreELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSL--YEPFGLTAIEAMACGTPV 329
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 924281479 285 IVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFN 343
Cdd:cd03800  330 VATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYT 388
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
17-344 9.85e-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: 135.95  E-value: 9.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  17 WCRFFNNKGYDIDVISLNDG----EIDGVAVHSFNKDLDKIRKGSSFNKISYIKYFSdikkIIEKIKPDVVHAHYATSYG 92
Cdd:cd03811   21 LANALDKRGYDVTLVLLRDEgdldKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR----ILKRAKPDVVISFLGFATY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  93 LLGALSGFHPYIISVWGSDvYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEE---TSQYTTKDIEITPFGVNIDTFKP 169
Cdd:cd03811   97 IVAKLAAARSKVIAWIHSS-LSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDlirLGPSPPEKIEVIYNPIDIDRIRA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 170 FADK---YEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFinQ 246
Cdd:cd03811  176 LAKEpilNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGF--Q 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 247 EKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAE---AIEKLIED 323
Cdd:cd03811  254 SNPYPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGilaALLQKKLD 331
                        330       340
                 ....*....|....*....|.
gi 924281479 324 DNLRINMGKtGRRFVEDNFNI 344
Cdd:cd03811  332 AALRERLAK-AQEAVFREYTI 351
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
21-344 1.29e-36

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: 135.66  E-value: 1.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  21 FNNKGYDIDVISLNDGeiDGVAVHSfnkDLDKIRKgSSFNKISYIKYFSDIKKIiekikpDVVHAHYatsyGLLGALSGF 100
Cdd:cd03799   24 LIDRGHEVDIYAVNPG--DLVKRHP---DVEKYNV-PSLNLLYAIVGLNKKGAY------DIIHCQF----GPLGALGAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 101 HPYIISVWGSDVYDFpKGSYIKRKMVEYN-------LSKADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFK-PFAD 172
Cdd:cd03799   88 LRRLKVLKGKLVTSF-RGYDISMYVILEGnkvypqlFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKfRFKP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 173 KYEKKENLV-IGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIE 251
Cdd:cd03799  167 RYLPLDGKIrILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 252 AFNRFDIAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLR 327
Cdd:cd03799  247 ILDEADIFIAPSVTaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIW 326
                        330
                 ....*....|....*..
gi 924281479 328 INMGKTGRRFVEDNFNI 344
Cdd:cd03799  327 PEMGKAGRARVEEEYDI 343
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
23-345 2.53e-36

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: 134.67  E-value: 2.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  23 NKGYDIDVISLNDG------EIDGVAVHsfnKDLDKIRKGSSFNKISYIKYFSDIKKIIEKIKPDVVhahYATSYGLLGA 96
Cdd:cd03820   28 KKGYDVTIISLDSAekppfyELDDNIKI---KNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVV---ISFRTSLLTF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  97 LSGF-HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEETSQYTTKDIEITPfgvNIDTFKPFADKYE 175
Cdd:cd03820  102 LALIgLKSKLIVWEHNNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKKYKQPNSNVVVIP---NPLSFPSEEPSTN 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 176 KKENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFinQEKVIEAFNR 255
Cdd:cd03820  179 LKSKRIL-AVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGP--TKNIAEEYAN 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 256 FDIAVFPStlDSESFGVAAVEAQACGTPVIVSN-VGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTG 334
Cdd:cd03820  256 SSIFVLSS--RYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNA 333
                        330
                 ....*....|.
gi 924281479 335 RRFVEDnFNIE 345
Cdd:cd03820  334 RKNAER-FSIE 343
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
23-345 3.41e-36

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: 135.19  E-value: 3.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  23 NKGYDIDVISLNDGEIDGVAVhsfnKDLDKIRKGSSFNKISYIK---------YFSDIKKIIEKIKPDVVHAHYATSYGL 93
Cdd:cd03821   29 ALGHEVTIVSTGDGYESLVVE----ENGRYIPPQDGFASIPLLRqgagrtdfsPGLPNWLRRNLREYDVVHIHGVWTYTS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  94 LGAL---SGFH-PYIISVWGS-DVYDFPKgSYIKRKMVEY-----NLSKADIIMSTSKVMAEETS--QYTTKdIEITPFG 161
Cdd:cd03821  105 LAACklaRRRGiPYVVSPHGMlDPWALQQ-KHWKKRIALHlierrNLNNAALVHFTSEQEADELRrfGLEPP-IAVIPNG 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 162 VNIDTFKPfADKYEKKENL-----VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQK-DFLLSLCNELNIR 235
Cdd:cd03821  183 VDIPEFDP-GLRDRRKHNGledrrIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAyPAFLQLQSSLGLG 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 236 DHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSslLVNKKNVDELAE 315
Cdd:cd03821  262 DRVTFTGPLYGEAKWALYASADLFVLPSY--SENFGNVVAEALACGLPVVITDKCGLSELVEAGCG--VVVDPNVSSLAE 337
                        330       340       350
                 ....*....|....*....|....*....|..
gi 924281479 316 AIEKLIEDDNLRINMGKTGRRFV--EDNFNIE 345
Cdd:cd03821  338 ALAEALRDPADRKRLGEMARRARqvEENFSWE 369
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
81-345 3.72e-36

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: 134.79  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  81 DVVHAHYATSYgllgALSGFH---------PYIISVWGSDV----YDFPKGSYIKrkmveYNLSKADIIMSTSKVMAEET 147
Cdd:cd04962   86 DVLHAHYAIPH----ASCAYLareilgekiPIVTTLHGTDItlvgYDPSLQPAVR-----FSINKSDRVTAVSSSLRQET 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 148 SQY--TTKDIEITPFGVNIDTFKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVkQKHSNIKLEIAGVG 219
Cdd:cd04962  157 YELfdVDKDIEVIHNFIDEDVFKRKPAGALKRRLLappdekVVIHVSNFRPVKRIDDVVRVFARV-RRKIPAKLLLVGDG 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 220 EQKDFLLSLCNELNIRDHVKFLGfiNQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPN 299
Cdd:cd04962  236 PERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPS--EKESFGLAALEAMACGVPVVSSNAGGIPEVVKHG 311
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 924281479 300 NSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd04962  312 ETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPE 357
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-345 7.27e-36

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: 134.39  E-value: 7.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479   2 KICYLAD-------ANSTHTKKWCRFFNNKGYDIDVI------------SLNDGEIDGVAVHSF-------NKDLDKIRK 55
Cdd:cd03794    1 KILLISQyypppkgAAAARVYELAKELVRRGHEVTVLtpspnyplgrifAGATETKDGIRVIRVklgpikkNGLIRRLLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  56 GSSFNKISYIKYFsdikkiIEKIKPDVVHAH--YATSYGLLGALSGFH--PYIISV------WGSDVYDFPKGSYIK--R 123
Cdd:cd03794   81 YLSFALAALLKLL------VREERPDVIIAYspPITLGLAALLLKKLRgaPFILDVrdlwpeSLIALGVLKKGSLLKllK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 124 KMVEYNLSKADIIMSTSKVMAEETSQYTTKD--IEITPFGVNIDTFKPFADKYEKKEN-----LVIGTVKTLEPKYGIEY 196
Cdd:cd03794  155 KLERKLYRLADAIIVLSPGLKEYLLRKGVPKekIIVIPNWADLEEFKPPPKDELRKKLglddkFVVVYAGNIGKAQGLET 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 197 LVRAFAKVKQkHSNIKLEIAGVGEQKDFLLSLCNELNIrDHVKFLGFINQEKVIEAFNRFDIAVFPstLDSESFGVAAV- 275
Cdd:cd03794  235 LLEAAERLKR-RPDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLVP--LKDNPANRGSSp 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924281479 276 ----EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03794  311 sklfEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSRE 384
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
18-345 1.66e-35

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: 132.78  E-value: 1.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  18 CRFFNNKGYDIDVISLN------DGEIDGVAVHSFNKDLDKIRKGSSFnkiSYIKYFsdikkIIEKIKPDVVHAHYATSY 91
Cdd:cd03795   24 AEGLKKKGIEVDVLCFSkeketpEKEENGIRIHRVKSFLNVASTPFSP---SYIKRF-----KKLAKEYDIIHYHFPNPL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  92 G-LLGALSGFH-PYIISvWGSDVydfpkgsyIKRKMVE--YN------LSKADIIMSTSKVMAEET---SQYTTKdIEIT 158
Cdd:cd03795   96 AdLLLFFSGAKkPVVVH-WHSDI--------VKQKKLLklYKplmtrfLRRADRIIATSPNYVETSptlREFKNK-VRVI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 159 PFGVNIDTFKPFADKYEKKENLVIGT-----VKTLEPKYGIEYLVRAfakvkQKHSNIKLEIAGVGEQKDFLLSLCnELN 233
Cdd:cd03795  166 PLGIDKNVYNIPRVDFENIKREKKGKkiflfIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPLKPDLEAQI-ELN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 234 IRDHVKFLGFINQEKVIEAFNRFDIAVFPSTLDSESFGVAAVEAQACGTPVIVSNVGGlpeATSPNN----SSLLVNKKN 309
Cdd:cd03795  240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGT---GVPYVNnngeTGLVVPPKD 316
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 924281479 310 VDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03795  317 PDALAEAIDKLLSDEELRESYGENAKKRFEELFTAE 352
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
121-345 3.68e-35

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: 132.10  E-value: 3.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 121 IKRKMVEYNLSKADIIMSTSKVMAEETSQYT---TKDIEITPFGVNIDTFKPFADKYEKKEN-------LVIGTvktLEP 190
Cdd:cd03809  127 YYRLLLPISLRRADAIITVSEATRDDIIKFYgvpPEKIVVIPLGVDPSFFPPESAAVLIAKYllpepyfLYVGT---LEP 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 191 KYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDF-LLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSES 269
Cdd:cd03809  204 RKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEeLLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSL--YEG 281
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924281479 270 FGVAAVEAQACGTPVIVSNVGGLPEATSPnnSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEdNFNIE 345
Cdd:cd03809  282 FGLPVLEAMACGTPVIASNISVLPEVAGD--AALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWE 354
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
181-323 4.07e-35

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 125.32  E-value: 4.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  181 VIGTVKTLEPKY-GIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDfLLSLCNELNirDHVKFLGFINQekVIEAFNRFDIA 259
Cdd:pfam13692   3 VILFVGRLHPNVkGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLE--DRVIFTGFVED--LAELLAAADVF 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924281479  260 VFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNsSLLVNKKNVDELAEAIEKLIED 323
Cdd:pfam13692  78 VLPSL--YEGFGLKLLEAMAAGLPVVATDVGGIPELVDGEN-GLLVPPGDPEALAEAILRLLED 138
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
4-358 3.01e-34

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: 129.71  E-value: 3.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479   4 CYLADAN--STHTKKWCRFFNNKGYDIDVISLNDGEidgvavHSFNKDLDKIRKGSSFNKISY-----IKYFSDIKKIIE 76
Cdd:cd03817    8 TYLPQVNgvATSVRNLARALEKRGHEVYVITPSDPG------AEDEEEVVRYRSFSIPIRKYHrqhipFPFKKAVIDRIK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  77 KIKPDVVHAHYATSYGLLGALSG----------FHpyiiSVWGSDVYDFPKGSYIKRKMVE------YNlsKADIIMSTS 140
Cdd:cd03817   82 ELGPDIIHTHTPFSLGKLGLRIArklkipivhtYH----TMYEDYLHYIPKGKLLVKAVVRklvrrfYN--HTDAVIAPS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 141 KVMAEETSQY-TTKDIEITPFGVNIDTFKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKQKhSNIKL 213
Cdd:cd03817  156 EKIKDTLREYgVKGPIEVIPNGIDLDKFEKPLNTEERRKLGlppdepILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 214 EIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLP 293
Cdd:cd03817  235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFAST--TETQGLVYLEAMAAGLPVVAAKDPAAS 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924281479 294 EATSPNNSSLLVnKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIEDnfnnVDTIYKSI 358
Cdd:cd03817  313 ELVEDGENGFLF-EPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKS----VEKLYEEV 372
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
80-339 2.66e-31

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: 120.92  E-value: 2.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  80 PDVVHAHyATSYGLLGAL---SGFHPYIISVWGSD-VYDFPKGSYI-KRKMVEYnlskaDIIMSTSKVMAEETSQYTTKD 154
Cdd:cd03819   77 IDLIHAH-SRAPAWLGWLasrLTGVPLVTTVHGSYlATYHPKDFALaVRARGDR-----VIAVSELVRDHLIEALGVDPE 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 -IEITPFGVNIDTFKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKqKHSNIKLEIAGVGEQKDFLLS 227
Cdd:cd03819  151 rIRVIPNGVDTDRFPPEAEAEERAQLGlpegkpVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLLVAGDGPERDEIRR 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 228 LCNELNIRDHVKFLGFInqEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNK 307
Cdd:cd03819  230 LVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSL--HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPP 305
                        250       260       270
                 ....*....|....*....|....*....|..
gi 924281479 308 KNVDELAEAIEKLIEDDNLRinmGKTGRRFVE 339
Cdd:cd03819  306 GDAEALADAIRAAKLLPEAR---EKLQAAAAL 334
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
245-359 1.86e-30

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 112.78  E-value: 1.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 245 NQEKVIEAF-NRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIED 323
Cdd:COG0438    9 GLDLLLEALlAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED 86
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 924281479 324 DNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYKSII 359
Cdd:COG0438   87 PELRRRLGEAARERAEERFSWEAIAERLLALYEELL 122
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
81-356 1.26e-29

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: 118.59  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  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 924281479 140 SkvmaEETSQYTTKD------IEITPFGVNIDTFKPFADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKL 213
Cdd:cd03813  252 Y----EGNRRRQIRLgadpdkTRVIPNGIDIQRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEG 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 214 EIAG-VGEQKDFL---LSLCNELNIRDHVKFLGFINqekVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNV 289
Cdd:cd03813  328 WLIGpEDEDPEYAqecKRLVASLGLENKVKFLGFQN---IKEYYPKLGLLVLTSI--SEGQPLVILEAMASGVPVVATDV 402
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 924281479 290 GGLPEA-----TSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03813  403 GSCRELiygadDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
mycothiol_MshA TIGR03449
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ...
133-331 1.90e-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: 117.15  E-value: 1.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  133 ADI-IMSTSKVMAEETSQY--TTKDIEITPFGVNIDTFKPfADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFA 202
Cdd:TIGR03449 164 ADRlIANTDEEARDLVRHYdaDPDRIDVVAPGADLERFRP-GDRATERARLglpldtkVVAFVGRIQPLKAPDVLLRAVA 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  203 KVKQKHSNIKLEIAGVG-------EQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAV 275
Cdd:TIGR03449 243 ELLDRDPDRNLRVIVVGgpsgsglATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVPSY--NESFGLVAM 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 924281479  276 EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMG 331
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMG 376
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
155-344 6.22e-29

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: 115.24  E-value: 6.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIDtfkPFADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELni 234
Cdd:cd05844  168 IHVHYIGIDPA---KFAPRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL-- 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 235 rDHVKFLGFINQEKVIEAFNRFDIAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNV 310
Cdd:cd05844  243 -GRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDV 321
                        170       180       190
                 ....*....|....*....|....*....|....
gi 924281479 311 DELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNI 344
Cdd:cd05844  322 DALADALQALLADRALADRMGGAARAFVCEQFDI 355
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
130-358 2.70e-26

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: 107.80  E-value: 2.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 130 LSKADI-IMSTSKVMAEETSQ---YTTKDIEITPFGVNIDTFKPFADKY-------EKKENLVI-GTVKTLEPKYGIEYL 197
Cdd:cd03825  134 LAKKRLtIVAPSRWLADMVRRsplLKGLPVVVIPNGIDTEIFAPVDKAKarkrlgiPQDKKVILfGAESVTKPRKGFDEL 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 198 VRAfakVKQKHSNIKLEIAGVGEQKDFLLSLcnELNIRDhvkfLGFI-NQEKVIEAFNRFDIAVFPSTLDSesFGVAAVE 276
Cdd:cd03825  214 IEA---LKLLATKDDLLLVVFGKNDPQIVIL--PFDIIS----LGYIdDDEQLVDIYSAADLFVHPSLADN--LPNTLLE 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 277 AQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFN----IEDNFNnvd 352
Cdd:cd03825  283 AMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDqrvqAQRYLE--- 359

                 ....*.
gi 924281479 353 tIYKSI 358
Cdd:cd03825  360 -LYKDL 364
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
133-340 5.18e-25

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: 104.30  E-value: 5.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 133 ADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFKP------FADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQ 206
Cdd:cd03814  146 FDTTLVPSPSIARELEGHGFERVRLWPRGVDTELFHPsrrdaaLRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAA 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 207 kHSNIKLEIAGVGEQKDfllslcnELNIRD-HVKFLGFINQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVI 285
Cdd:cd03814  226 -SPPVRLVVVGDGPARA-------ELEARGpDVIFTGFLTGEELARAYASADVFVFPS--RTETFGLVVLEAMASGLPVV 295
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 924281479 286 VSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVED 340
Cdd:cd03814  296 AADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER 350
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
178-357 4.83e-24

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


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 101.25  E-value: 4.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 178 ENLVIGTVKTLEPKYGIEYLVRAFAKVKQKhsNIKLEIAGvgeqkDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFD 257
Cdd:cd03823  190 ERLRFGYIGRLTEEKGIDLLVEAFKRLPRE--DIELVIAG-----HGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKID 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 258 IAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTgrrf 337
Cdd:cd03823  263 VLVVPSIWP-EPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAG---- 337
                        170       180
                 ....*....|....*....|
gi 924281479 338 VEDNFNIEDNFNNVDTIYKS 357
Cdd:cd03823  338 AEPPRSTESQAEEYLKLYRD 357
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
19-328 3.02e-23

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: 98.90  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  19 RFFNNKGYDIDVISLNDGEIDgvavhsfnKDLDKIRKGS-----SFNKISYIKYFSDIKKIIEKIKPDVVHAHYATSYG- 92
Cdd:cd03812   23 RKLDKSKIEFDFLATSDDKGE--------YDEELEELGGkifyiPPKKKNIIKYFIKLLKLIKKEKYDIVHVHGSSSNGi 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  93 -LLGALSGFHPYIISVWGSDVYDfpkgSYIKRKMVEYNLSKADIIMST-----SKVMAEET-SQYTTKDIEITPFGVNID 165
Cdd:cd03812   95 iLLLAAKAGVPVRIAHSHNTKDS----SIKLRKIRKNVLKKLIERLSTkylacSEDAGEWLfGEVENGKFKVIPNGIDIE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 166 TF---KPFADKYEKKEN----LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHV 238
Cdd:cd03812  171 KYkfnKEKRRKRRKLLIledkLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKV 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 239 KFLGFINQekVIEAFNRFDIAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGlPEATSPNNSSLLVNKKNVDELAEAIE 318
Cdd:cd03812  251 IFLGFRND--VSEILSAMDVFLFPSLY--EGLPLVAVEAQASGLPCLLSDTIT-KECDITNNVEFLPLNETPSTWAEKIL 325
                        330
                 ....*....|
gi 924281479 319 KLIEDDNLRI 328
Cdd:cd03812  326 KLIKRKRRIN 335
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
80-305 1.47e-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: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMstskvmaeetsqyttkdie 156
Cdd:cd01635   55 PDVVHAHSPHAAALAALLAARllgIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVS------------------- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 157 itpfgvnidtfkpfadkyekkenlvigtVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRD 236
Cdd:cd01635  116 ----------------------------VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLE 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 237 HVKFLGFINQEKVIEAFNR-FDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLV 305
Cdd:cd01635  168 RVVIIGGLVDDEVLELLLAaADVFVLPSR--SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
129-332 5.87e-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: 89.28  E-value: 5.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 129 NLSKAD-IIMSTSK---VMAEETSQYTTkdIEITPFGVnIDTFKPFADKYEKKENLVIgTVKTLEPKYGIEYLVRAFAKV 204
Cdd:cd04949  110 NLNKYDaIIVSTEQqkqDLSERFNKYPP--IFTIPVGY-VDQLDTAESNHERKSNKII-TISRLAPEKQLDHLIEAVAKA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 205 KQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIeaFNRFDIAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd04949  186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQE--YQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPV 261
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 924281479 285 IVSNVG-GLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGK 332
Cdd:cd04949  262 VSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSE 310
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
81-322 1.45e-18

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: 86.14  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  81 DVVHAHYATSY----GLLGA-LSGFHPYII--SVWG-SDVydfpkGSYIKRKMVEYNLSKADIIMSTSKVMAEET---SQ 149
Cdd:cd03796   90 QIVHGHQAFSSlaheALFHArTLGLKTVFTdhSLFGfADA-----SSILTNKLLRFSLADIDHVICVSHTSKENTvlrAS 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 150 YTTKDIEITPFGVNIDTFKPfADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLC 229
Cdd:cd03796  165 LDPRIVSVIPNAVDSSDFTP-DPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMR 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 230 NELNIRDHVKFLGFINQEKVIEAFNRFDIavFPSTLDSESFGVAAVEAQACGTPVIVSNVGGLPEATsPNNSSLLVNKKN 309
Cdd:cd03796  244 EKYQLQDRVELLGAVPHEEVRDVLVQGHI--FLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVL-PPDMILLAEPDP 320
                        250
                 ....*....|....*.
gi 924281479 310 VD---ELAEAIEKLIE 322
Cdd:cd03796  321 EDivrKLEEAISILRT 336
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
80-355 5.38e-18

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: 84.03  E-value: 5.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  80 PDVVHAHYatsygllgalsgFHPYIISVWGSDVYDFPK----------GSYIKRKMVEYNLSKADIIMSTSKVMAEE-TS 148
Cdd:cd04951   80 PDVVHSHM------------FHANIFARFLRMLYPIPLlictahnkneGGRIRMFIYRLTDFLCDITTNVSREALDEfIA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 149 QYTTKDIEITPF--GVNIDTFKPFADKYEKKEN--------LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGV 218
Cdd:cd04951  148 KKAFSKNKSVPVynGIDLNKFKKDINVRLKIRNklnlkndeFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGD 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 219 GEQKDFLLSLCNELNIRDHVKFLGFINQekVIEAFNRFDIAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATSP 298
Cdd:cd04951  228 GPLRNELERLICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSEW--EGFGLVVAEAMACERPVVATDAGGVAEVVGD 303
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479 299 NNssLLVNKKNVDELAEAI-EKLIEDDNLRINMGKTgRRFVEDNFNIEDNFNNVDTIY 355
Cdd:cd04951  304 HN--YVVPVSDPQLLAEKIkEIFDMSDEERDILGNK-NEYIAKNFSINTIVNEWERLY 358
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
80-344 1.56e-17

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: 82.85  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479   80 PDVVHAH--YATSYGLLGALSGFHPYIISVWGSDVYDfPKGSYIKrkmveYNLSKADI--IMSTSKVMAEETSQYTTKDI 155
Cdd:TIGR03088  82 PDIVHTRnlAALEAQLPAALAGVPARIHGEHGRDVFD-LDGSNWK-----YRWLRRLYrpLIHHYVAVSRDLEDWLRGPV 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  156 EITPF-------GVNIDTFKP--------FADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHS----NIKLEIA 216
Cdd:TIGR03088 156 KVPPAkihqiynGVDTERFHPsrgdrspiLPPDFFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPegaeRLRLVIV 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  217 GVGEQKDFLLSLCNELNIRDHVKFLGfiNQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEAT 296
Cdd:TIGR03088 236 GDGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQALDLFVLPSL--AEGISNTILEAMASGLPVIATAVGGNPELV 311
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 924281479  297 SPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNI 344
Cdd:TIGR03088 312 QHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSI 359
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
159-345 1.85e-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: 82.34  E-value: 1.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 159 PFGVNIDTFkPFADKyeKKENLV-IGTVKtlePKYGIEYLVRAFAKvkqkhSNIKLEIAGVGEQKDFLLSLcNELNIRDH 237
Cdd:cd03802  154 HNGLDPADY-RFQPD--PEDYLAfLGRIA---PEKGLEDAIRVARR-----AGLPLKIAGKVRDEDYFYYL-QEPLPGPR 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 238 VKFLGFINQEKVIEAFNRFDIAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNkkNVDELAEAI 317
Cdd:cd03802  222 IEFIGEVGHDEKQELLGGARALLFPINWD-EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD--SVEEMAEAI 298
                        170       180
                 ....*....|....*....|....*...
gi 924281479 318 EKLIEDDNLRInmgktgRRFVEDNFNIE 345
Cdd:cd03802  299 ANIDRIDRAAC------RRYAEDRFSAA 320
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
131-339 6.42e-17

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 81.68  E-value: 6.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 131 SKADIIMSTSKVMAEE--TSQYTT-KDIEITPFGVNIDTFKPFADKYEKKENL--------VIGTVKTLepkyGIEYLVR 199
Cdd:PLN02871 204 RAADLTLVTSPALGKEleAAGVTAaNRIRVWNKGVDSESFHPRFRSEEMRARLsggepekpLIVYVGRL----GAEKNLD 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 200 AFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNirdhVKFLGFINQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQA 279
Cdd:PLN02871 280 FLKRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPS--ESETLGFVVLEAMA 353
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924281479 280 CGTPVIVSNVGGLPE---ATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVE 339
Cdd:PLN02871 354 SGVPVVAARAGGIPDiipPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVE 416
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
116-345 7.98e-16

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: 78.01  E-value: 7.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 116 PKGSYIKR-------KMVEYNLSKADIIMSTSKVMAEETSQyTTKDIEITPFGV-----NIDTFKPFADKYEKKENLVIG 183
Cdd:cd03805  131 QRKSLLKRlyrkpfdWLEEFTTGMADQIVVNSNFTAGVFKK-TFPSLAKNPPEVlypcvDTDSFDSTSEDPDPGDLIAKS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 184 TVKTL------EPKYGIEYLVRAFAKVKQKH---SNIKLEIAG-----VGEQKDF---LLSLCNEL-NIRDHVKFLGFIN 245
Cdd:cd03805  210 NKKFFlsinrfERKKNIALAIEAFAKLKQKLpefENVRLVIAGgydprVAENVEYleeLQRLAEELlNVEDQVLFLRSIS 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 246 QEKVIEAFNRFDIAVFpsTLDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNkKNVDELAEAIEKLIEDDN 325
Cdd:cd03805  290 DSQKEQLLSSALALLY--TPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PTPEAFAEAMLKLANDPD 366
                        250       260
                 ....*....|....*....|
gi 924281479 326 LRINMGKTGRRFVEDNFNIE 345
Cdd:cd03805  367 LADRMGAAGRKRVKEKFSRE 386
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
162-318 9.82e-16

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: 77.33  E-value: 9.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 162 VNIDTFKPfadKYEKKENLVigTVKTLEPKYGIEYLVRAFAKvkqkhSNIKLEIAGVGEQKDFLLSLCnelniRDHVKFL 241
Cdd:cd03804  187 VDTDAFAP---AADKEDYYL--TASRLVPYKRIDLAVEAFNE-----LPKRLVVIGDGPDLDRLRAMA-----SPNVEFL 251
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924281479 242 GFINQEKVIEAFNRFDIAVFPSTldsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIE 318
Cdd:cd03804  252 GYQPDEVLKELLSKARAFVFAAE---EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVE 325
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
190-344 1.22e-13

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: 71.20  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 190 PKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKD----FLLS--LCNELNIRD-HVKFLGFINQEkvIEAFNRF-DIAVF 261
Cdd:cd03792  208 PSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDpegsVVYEevMEYAGDDHDiHVLRLPPSDQE--INALQRAaTVVLQ 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 262 PSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKknVDELAEAIEKLIEDDNLRINMGKTGRRFVEDN 341
Cdd:cd03792  286 LST--REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAVRILRLLTDPELRRKMGLAAREHVRDN 361

                 ...
gi 924281479 342 FNI 344
Cdd:cd03792  362 FLI 364
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
154-345 2.02e-13

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 70.59  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 154 DIEITPFGVNIDTFKPFADKyEKKENLVIGTVKT-------LEPKYGIEYLVRAFAKVKQKHSNIKLEIAG------VGE 220
Cdd:PRK15484 162 DISIVPNGFCLETYQSNPQP-NLRQQLNISPDETvllyagrISPDKGILLLMQAFEKLATAHSNLKLVVVGdptassKGE 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 221 QKDF---LLSLCNElnIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATS 297
Cdd:PRK15484 241 KAAYqkkVLEAAKR--IGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVE-EAFCMVAVEAMAAGKPVLASTKGGITEFVL 317
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 924281479 298 PNNSSL-LVNKKNVDELAEAIEKLIEDDNlRINMGKTGRRFVEDNFNIE 345
Cdd:PRK15484 318 EGITGYhLAEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWE 365
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
49-349 4.58e-13

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: 69.80  E-value: 4.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  49 DLDKIRKGSSFNK--------ISYIKYFSDIKKIIEKIKPDVVHAH--YATSYGL-LGALSGFHPYIIS-VWGSDVYDFP 116
Cdd:cd04946   83 IKDKPRSGSFLLLyyfliasfLSKHRVLALLQFVSIFGQGTVVYSYwlNHTALGLgLLKDEYYRDVVISrAHRYDLYEDQ 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 117 KGSYI---KRKMVEYnLSKADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFKpfaDKYEKKENLVIGTVKTLEPKYG 193
Cdd:cd04946  163 YGSYYlplREYLVSY-LDAVFLISKEGKDYLQKCYPAYKEKIFVSRLGVSDKEQY---SKVKKEGDLRLVSCSSIVPVKR 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 194 IEYLVRAFAKVKQKHSNIKLEIA--GVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTLDSESFG 271
Cdd:cd04946  239 IDLIIETLNSLCVAHPSICISWThiGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIP 318
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 924281479 272 VAAVEAQACGTPVIVSNVGGLPEATS-PNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIEDNFN 349
Cdd:cd04946  319 VSIMEAISFGIPVIATNVGGTREIVEnETNGLLLDKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYS 397
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
129-338 1.24e-09

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 58.79  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 129 NLSKADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFKPFADKYEKKENLV-IGTvktlepkyGIEYLVRAFAKVKQK 207
Cdd:COG4641   89 LLPLYDLVFTFDGDCVEEYRALGARRVFYLPFAADPELHRPVPPEARFRYDVAfVGN--------YYPDRRARLEELLLA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 208 HSNIKLEIAGVGeqkdFllslcNELNIRDHVKFLGFINQEKVIEAFNRFDIAV-FPSTLDSE-SFGVAAVEAQACGTPVI 285
Cdd:COG4641  161 PAGLRLKIYGPG----W-----PKLALPANVRRGGHLPGEEHPAAYASSKITLnVNRMAASPdSPTRRTFEAAACGAFLL 231
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 924281479 286 VSNVGGLPEATSPNNSSLLVNkkNVDELAEAIEKLIEDDNLRINMGKTGRRFV 338
Cdd:COG4641  232 SDPWEGLEELFEPGEEVLVFR--DGEELAEKLRYLLADPEERRAIAEAGRRRV 282
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
155-327 1.69e-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: 58.55  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIdtfKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAG--VGEQKD--- 223
Cdd:cd03822  160 IEVIPHGVPE---VPQDPTTALKRLLlpegkkVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelHPSLARyeg 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 224 --FLLSLCNELNIRDHVKF-LGFINQEKVIEAFNRFDIAVFP--STLDSESfGVAAVeAQACGTPVIVSNVGGLpEATSP 298
Cdd:cd03822  237 erYRKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPylNTEQSSS-GTLSY-AIACGKPVISTPLRHA-EELLA 313
                        170       180
                 ....*....|....*....|....*....
gi 924281479 299 NNSSLLVNKKNVDELAEAIEKLIEDDNLR 327
Cdd:cd03822  314 DGRGVLVPFDDPSAIAEAILRLLEDDERR 342
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
176-346 2.12e-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: 55.45  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 176 KKENLVIGTV-KTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAG------------VGEQKDFLLSlcnELNI-RDHVKFL 241
Cdd:cd03818  210 KAGDPVITYVaRNLEPYRGFHVFMRALPRIQARRPDARVVVVGgdgvsygspppdGGSWKQKMLA---ELGVdLERVHFV 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 242 GFINQEKVIEAFNRFDIAVFPSTLDSESFGVaaVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLI 321
Cdd:cd03818  287 GKVPYDQYVRLLQLSDAHVYLTYPFVLSWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELL 364
                        170       180
                 ....*....|....*....|....*
gi 924281479 322 EDDNLRINMGKTGRRFVEDNFNIED 346
Cdd:cd03818  365 EDPDRAAALRRAARRTVERSDSLDV 389
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
162-342 4.20e-08

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: 54.54  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 162 VNIDTFKPFADKYEKKENLVIgTVKTLEPKYGIEYLVRAFAKVKQKH-----SNIKLEIAG-VGEQKD-----FLLSLCN 230
Cdd:cd03806  221 CDTEELTKLPIDEKTRENQIL-SIAQFRPEKNHPLQLRAFAELLKRLpesirSNPKLVLIGsCRNEEDkerveALKLLAK 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 231 ELNIRDHVKFLGFINQEKVIEAFNRFDIAVfpSTLDSESFGVAAVEAQACGTPVIVSNVGGlPE-----ATSPNNSSLLV 305
Cdd:cd03806  300 ELILEDSVEFVVDAPYEELKELLSTASIGL--HTMWNEHFGIGVVEYMAAGLIPLAHASAG-PLldivvPWDGGPTGFLA 376
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 924281479 306 nkKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNF 342
Cdd:cd03806  377 --STPEEYAEAIEKILTLSEEERLQRREAARSSAERF 411
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
258-343 4.34e-08

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 50.30  E-value: 4.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479  258 IAVFPStLDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVnkKNVDELAEAIEKLIEDDNLRINMGKTGRRF 337
Cdd:pfam13524   1 IVLNPS-RRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLY--RDPEELAEKIRYLLEHPEERRAIAAAGRER 77

                  ....*.
gi 924281479  338 VEDNFN 343
Cdd:pfam13524  78 VLAEHT 83
PLN02949 PLN02949
transferase, transferring glycosyl groups
198-343 1.43e-06

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 49.74  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 198 VRAFAKVKQKHS----NIKLEIAGVGEQK------DFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRfDIAVFPSTLDs 267
Cdd:PLN02949 287 LEAFALALEKLDadvpRPKLQFVGSCRNKedeerlQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGG-AVAGLHSMID- 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 268 ESFGVAAVEAQACGTPVIVSNVGG------LPEATSPnnSSLLVNkkNVDELAEAIEKLIE-DDNLRINMGKTGR----R 336
Cdd:PLN02949 365 EHFGISVVEYMAAGAVPIAHNSAGpkmdivLDEDGQQ--TGFLAT--TVEEYADAILEVLRmRETERLEIAAAARkranR 440

                 ....*..
gi 924281479 337 FVEDNFN 343
Cdd:PLN02949 441 FSEQRFN 447
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
182-331 3.33e-06

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 48.88  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 182 IGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINqeKVIEAFNRFDIAVF 261
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSR--RVGYWLTQFNAFLL 597
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 924281479 262 PSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVD--ELAEAIEKLIedDNLRINMG 331
Cdd:PRK15179 598 LSRF--EGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIH--DMCAADPG 665
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
11-165 3.44e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 40.98  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479   11 STHTKKWCRFFNNKGYDIDVISLNDG------EIDGVAVHSFNKDLDKIRKGSSFNKISYIKYFSDIKkiiekikPDVVH 84
Cdd:pfam13439   4 ERYVLELARALARRGHEVTVVTPGGPgplaeeVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRER-------PDVVH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479   85 AHYATS--YGLLGALSGFH-PYIISV-----WGSDVYDFPKGSYIKRKMVEYNL-SKADIIMSTSKVMAEETSQY---TT 152
Cdd:pfam13439  77 AHSPFPlgLAALAARLRLGiPLVVTYhglfpDYKRLGARLSPLRRLLRRLERRLlRRADRVIAVSEAVADELRRLygvPP 156
                         170
                  ....*....|...
gi 924281479  153 KDIEITPFGVNID 165
Cdd:pfam13439 157 EKIRVIPNGVDLE 169
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
25-146 1.10e-03

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 39.31  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479   25 GYDIDVISLNDGEI------DGVAVHSfnkdLDKIRKGSSFNKISYIKYFSDIKKIIEkikPDVVHAHYATS--YGLLGA 96
Cdd:pfam13579  18 GHEVRVVTPGGPPGrpelvgDGVRVHR----LPVPPRPSPLADLAALRRLRRLLRAER---PDVVHAHSPTAglAARLAR 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 924281479   97 LSGFHPYIISVWGSDV--YDFPKGSYIkRKMVEYNLSKADIIMSTSKVMAEE 146
Cdd:pfam13579  91 RRRGVPLVVTVHGLALdyGSGWKRRLA-RALERRLLRRADAVVVVSEAEAEL 141
PRK05749 PRK05749
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed
276-341 1.12e-03

3-deoxy-D-manno-octulosonic-acid transferase; Reviewed


Pssm-ID: 235589 [Multi-domain]  Cd Length: 425  Bit Score: 40.59  E-value: 1.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479 276 EAQACGTPVIvsnvgglpeaTSP---NNSSL---------LVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDN 341
Cdd:PRK05749 339 EPAAFGVPVI----------SGPhtfNFKEIferllqagaAIQVEDAEDLAKAVTYLLTDPDARQAYGEAGVAFLKQN 406
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
268-329 2.96e-03

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


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 39.76  E-value: 2.96e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924281479   268 ESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNL----RIN 329
Cdd:TIGR02468  582 EPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLwaecRQN 647
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
167-358 4.24e-03

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 38.91  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 167 FKPFADKYEKKENLVIGTVKTLEPKYGIEYLVRAfAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLG---- 242
Cdd:PRK15490 387 WQQFTQKTQDADTTIGGVFRFVGDKNPFAWIDFA-ARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGasrd 465
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 243 ---FINQEKVIEAFNRFDiaVFPSTLdsesfgvaaVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKK---NVDELAEA 316
Cdd:PRK15490 466 vgyWLQKMNVFILFSRYE--GLPNVL---------IEAQMVGVPVISTPAGGSAECFIEGVSGFILDDAqtvNLDQACRY 534
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 924281479 317 IEKLIEDDNLRINMGKTGRRFVEDNFNIEdnfNNVDTIYKSI 358
Cdd:PRK15490 535 AEKLVNLWRSRTGICQQTQSFLQERFTVE---HMVGTFVKTI 573
PHA01633 PHA01633
putative glycosyl transferase group 1
183-315 6.98e-03

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 38.04  E-value: 6.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 183 GTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAG-VGEQKDFllslcNELNIRDHVKFL---GFINQEKVIEAFNRFDI 258
Cdd:PHA01633 152 GIVSGLTKRKNMDLMLQVFNELNTKYPDIAKKIHFfVISHKQF-----TQLEVPANVHFVaefGHNSREYIFAFYGAMDF 226
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 924281479 259 AVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPnNSSLLVNKKNVDELAE 315
Cdd:PHA01633 227 TIVPS--GTEGFGMPVLESMAMGTPVIHQLMPPLDEFTSW-QWNLLIKSSKVEEYYD 280
 
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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