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Conserved domains on  [gi|2788063403|ref|WP_370530626|]
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glycosyltransferase family 4 protein [Pseudoalteromonas tunicata]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 71-342 1.29e-53

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: 180.43  E-value: 1.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  71 VHSHfTYGATAIAFWLKYITNTPYSITLHGADLTFDKVPDLALK---------MQNADKIVSISQFNLDYLNKYFPaVDL 141
Cdd:cd03801    86 VHAH-GLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrllaraealLRRADAVIAVSEALRDELRALGG-IPP 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 142 NCCQVIPLGVPAKLSVSPQTNQV---QQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIG-EGPERQALTQLi 217
Cdd:cd03801   164 EKIVVIPNGVDLERFSPPLRRKLgipPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEEL- 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 218 eQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQ 297
Cdd:cd03801   243 -ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVE 321

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2788063403 298 ALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMFAAIFR 342
Cdd:cd03801   322 ALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 71-342 1.29e-53

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: 180.43  E-value: 1.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  71 VHSHfTYGATAIAFWLKYITNTPYSITLHGADLTFDKVPDLALK---------MQNADKIVSISQFNLDYLNKYFPaVDL 141
Cdd:cd03801    86 VHAH-GLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrllaraealLRRADAVIAVSEALRDELRALGG-IPP 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 142 NCCQVIPLGVPAKLSVSPQTNQV---QQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIG-EGPERQALTQLi 217
Cdd:cd03801   164 EKIVVIPNGVDLERFSPPLRRKLgipPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEEL- 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 218 eQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQ 297
Cdd:cd03801   243 -ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVE 321

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2788063403 298 ALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMFAAIFR 342
Cdd:cd03801   322 ALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 167-310 1.67e-42

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: 144.72  E-value: 1.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 167 PLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFHHEVLASYANADV 246
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788063403 247 FVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDP 310
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDE 145
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 239-344 5.38e-29

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 108.54  E-value: 5.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 239 ASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQ 318
Cdd:COG0438    16 ALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGE 95

                          90       100
                  ....*....|....*....|....*.
gi 2788063403 319 HAIFHIQQHFDLDKNTRMFAAIFRSL 344
Cdd:COG0438    96 AARERAEERFSWEAIAERLLALYEEL 121
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 170-311 6.17e-14

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 72.44  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 170 ILSVGRLSIHKAQHLLIEACSLLQKNNIKFnctiIGEGPERQALtqliEQYSLAEHVQLVGAKFHHEVLASYANADVFVL 249
Cdd:PLN02871  266 IVYVGRLGAEKNLDFLKRVMERLPGARLAF----VGDGPYREEL----EKMFAGTPTVFTGMLQGDELSQAYASGDVFVM 337

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788063403 250 SSITEGMPLVLMEAMQNGVLVIAPDIAGIPELL---DAGKAGILVPVNDVQALSDAIEKAALDPS 311
Cdd:PLN02871  338 PSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPE 402
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 216-345 1.91e-09

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


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 58.79  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 216 LIEQYSLAEHVQLVGAKFHHEVLAsyaNADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDA--------GKA 287
Cdd:NF038011  359 LVASLGLQDKVKFLGFQKIDDLLP---QVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIEGldeedralGAA 435

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788063403 288 GILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDldkNTRMFAAiFRSLF 345
Cdd:NF038011  436 GEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYT---EELMFDR-YRELY 489
Glyco4_Geo_Pelo NF038229
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 93-344 3.78e-09

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 57.30  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  93 PYSITLHGAD----LTFDKVPDLALKMQNADKIVSISQFNLDYLNKYFPAVDlnccqviplgvpAKLSVSPQTnqVQQPL 168
Cdd:NF038229   81 PYLVTLTGTDvneaLDPDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLA------------AKLVVIPQG--VELGG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 169 EILSVGRLSIHKAQHL----------------LIEACSLLQKNNIKFNCTIIG----EGPERQALTQLiEQYSLAEHVQL 228
Cdd:NF038229  147 EPFPLRELGLFDSDEFvfllpaglrpvkgvlfLLEMLAPLHAEDPRLRLAFAGpvldEEYAAAFFAAL-ARRPWARYLGE 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 229 VGakfHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILvpVNDVQALSDAIEKAAL 308
Cdd:NF038229  226 IP---HDAMGALYRRADVVLNNSLFEGMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLL--YRDEAEFLRQARQLLQ 300

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2788063403 309 DPSSTLTMQQHAIFHIQQHFDLDKNTRMFAAIFRSL 344
Cdd:NF038229  301 DPALRRRLGRPGRQLVRERYSPEREAEAYLRLYRAV 336
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 71-342 1.29e-53

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: 180.43  E-value: 1.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  71 VHSHfTYGATAIAFWLKYITNTPYSITLHGADLTFDKVPDLALK---------MQNADKIVSISQFNLDYLNKYFPaVDL 141
Cdd:cd03801    86 VHAH-GLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrllaraealLRRADAVIAVSEALRDELRALGG-IPP 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 142 NCCQVIPLGVPAKLSVSPQTNQV---QQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIG-EGPERQALTQLi 217
Cdd:cd03801   164 EKIVVIPNGVDLERFSPPLRRKLgipPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEEL- 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 218 eQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQ 297
Cdd:cd03801   243 -ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVE 321

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2788063403 298 ALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMFAAIFR 342
Cdd:cd03801   322 ALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 32-344 2.99e-52

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: 176.80  E-value: 2.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  32 VVYFKALLRAFLLEEKLKTSIahltgaLLLKRRYPELtwVHSHFTYGATAIAFWLKYITNTPYSITLHGAD-LTFDKVPd 110
Cdd:cd03798    68 PLKPRLRLLAPLRAPSLAKLL------KRRRRGPPDL--IHAHFAYPAGFAAALLARLYGVPYVVTEHGSDiNVFPPRS- 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 111 lALKMQ------NADKIVSISQFNLDYLNKYFpaVDLNCCQVIPLGVPAKLSvSPQTNQVQQPLE---ILSVGRLSIHKA 181
Cdd:cd03798   139 -LLRKLlrwalrRAARVIAVSKALAEELVALG--VPRDRVDVIPNGVDPARF-QPEDRGLGLPLDafvILFVGRLIPRKG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 182 QHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSITEGMPLVLM 261
Cdd:cd03798   215 IDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLL 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 262 EAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQhAIFHIQQHFDLDKNTRMFAAIF 341
Cdd:cd03798   295 EAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEA-ARARVAERFSWVKAADRIAAAY 373


                  ...
gi 2788063403 342 RSL 344
Cdd:cd03798   374 RDV 376
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 25-325 2.10e-44

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 155.59  E-value: 2.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  25 LFLISSPVVYFKALLRAFLLEEKLKTSIAHLTGALL---------LKRRYPELtwVHSHfTYGATAIAFwLKYITNTPYS 95
Cdd:cd03811    34 LVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLkailklkriLKRAKPDV--VISF-LGFATYIVA-KLAAARSKVI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  96 ITLHGA----DLTFDKVPDLALKMQNADKIVSISQFNLDYLNKYFPaVDLNCCQVIPLGV----PAKLSVSPQTNQVQQP 167
Cdd:cd03811   110 AWIHSSlsklYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGP-SPPEKIEVIYNPIdidrIRALAKEPILNEPEDG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 168 LEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGakFHHEVLASYANADVF 247
Cdd:cd03811   189 PVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLG--FQSNPYPYLKKADLF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 248 VLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVND-------VQALSDAIEKAALdpSSTLTMQQHA 320
Cdd:cd03811   267 VLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDaaalagiLAALLQKKLDAAL--RERLAKAQEA 344


                  ....*
gi 2788063403 321 IFHIQ 325
Cdd:cd03811   345 VFREY 349
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 167-310 1.67e-42

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: 144.72  E-value: 1.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 167 PLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFHHEVLASYANADV 246
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788063403 247 FVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDP 310
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDE 145
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 60-337 9.77e-41

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: 146.31  E-value: 9.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  60 LLKRRYPELtwVHSHFtYGA---TAIAFWLKyiTNTPYSITLHGADLTFDKVPdLALKMQNA-----DKIVSISQFNLD- 130
Cdd:cd03807    74 LIRKRNPDV--VHTWM-YHAdliGGLAAKLA--GGVKVIWSVRSSNIPQRLTR-LVRKLCLLlskfsPATVANSSAVAEf 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 131 YLNKYFPAVDLNccqVIPLGV-PAKLSVSP-QTNQVQQPLE-------ILSVGRLSIHKAQHLLIEACSLLQKNNIKFNC 201
Cdd:cd03807   148 HQEQGYAKNKIV---VIYNGIdLFKLSPDDaSRARARRRLGlaedrrvIGIVGRLHPVKDHSDLLRAAALLVETHPDLRL 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 202 TIIGEGPERQALTQLIEQYSLAEHVQLVGAKfhHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPEL 281
Cdd:cd03807   225 LLVGRGPERPNLERLLLELGLEDRVHLLGER--SDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAEL 302

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2788063403 282 LDaGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMF 337
Cdd:cd03807   303 VD-DGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRY 357
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 60-332 6.02e-40

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: 144.28  E-value: 6.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  60 LLKRRYPELtwVHSHFT----YGAtaIAFWLKYITNTPYsiTLHGADLTFDKVPD----------LALKmqNADKIVSIS 125
Cdd:cd03808    76 LLKKEKPDI--VHCHTPkpgiLGR--LAARLAGVPKVIY--TVHGLGFVFTEGKLlrllylllekLALL--FTDKVIFVN 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 126 QFNLDYLNKYFPAVDLNCCQVIPLGVPAKLSVSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIG 205
Cdd:cd03808   148 EDDRDLAIKKGIIKKKKTVLIPGSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVG 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 206 EGPERQALTQLIEQYSLAEHVQLVGakFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAG 285
Cdd:cd03808   228 DGELENPSEILIEKLGLEGRIEFLG--FRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDG 305

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2788063403 286 KAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDK 332
Cdd:cd03808   306 VNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEK 352
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 20-320 5.44e-39

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: 141.34  E-value: 5.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  20 LLSHWLFLISSPVVYFKALLRAFLLEEKLKtsiahltgaLLLKRRYPELtwVHSHfTYGATAIAFWLKYITNTPYSITLH 99
Cdd:cd03819    40 LLPRLRQIGIGLPGLKVPLLRALLGNVRLA---------RLIRRERIDL--IHAH-SRAPAWLGWLASRLTGVPLVTTVH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 100 GADL-TFDKVPDLALKMQNADKIVSISQFNLDYLNKYFPaVDLNCCQVIPLGVPAKLSVSPQTNQVQQPLE-------IL 171
Cdd:cd03819   108 GSYLaTYHPKDFALAVRARGDRVIAVSELVRDHLIEALG-VDPERIRVIPNGVDTDRFPPEAEAEERAQLGlpegkpvVG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 172 SVGRLSIHKAQHLLIEACSLLQKNnIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGakFHHEVLASYANADVFVLSS 251
Cdd:cd03819   187 YVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTG--FREDVPAALAASDVVVLPS 263

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788063403 252 ITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHA 320
Cdd:cd03819   264 LHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAA 332
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
170-309 1.23e-35

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 126.09  E-value: 1.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 170 ILSVGRLSI-HKAQHLLIEACSLLQKNNIKFNCTIIGEGPERqALTQLIEQysLAEHVQLVGakFHHEVLASYANADVFV 248
Cdd:pfam13692   4 ILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAAG--LEDRVIFTG--FVEDLAELLAAADVFV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788063403 249 LSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDaGKAGILVPVNDVQALSDAIEKAALD 309
Cdd:pfam13692  79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEALAEAILRLLED 138
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 116-332 1.82e-33

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: 126.58  E-value: 1.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 116 QNADKIVSISQFnlDYLNKYfpAVDLNCCQVIPLGVPAKlSVSPQTNQVQQplEILSVGRLSIHKAQHLLIEACSLLQKN 195
Cdd:cd03820   137 KRADKIVVLTEA--DKLKKY--KQPNSNVVVIPNPLSFP-SEEPSTNLKSK--RILAVGRLTYQKGFDLLIEAWALIAKK 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 196 NIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFHHEVLasYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDI 275
Cdd:cd03820   210 HPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEE--YANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDC 287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788063403 276 -AGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIfHIQQHFDLDK 332
Cdd:cd03820   288 pTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNAR-KNAERFSIEK 344
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 116-326 2.44e-30

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: 117.79  E-value: 2.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 116 QNADK----IVSISQFNLDYLNKYFPAVDLnccQVIPLGVPAKLSvSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSL 191
Cdd:cd04949   109 ENLNKydaiIVSTEQQKQDLSERFNKYPPI---FTIPVGYVDQLD-TAESNHERKSNKIITISRLAPEKQLDHLIEAVAK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 192 LQK--NNIKFNctIIGEGPERQALTQLIEQYSLAEHVQLVGakFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVL 269
Cdd:cd04949   185 AVKkvPEITLD--IYGYGEEREKLKKLIEELHLEDNVFLKG--YHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLP 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788063403 270 VIAPDIA-GIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQ 326
Cdd:cd04949   261 VVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEK 318
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 59-320 1.13e-29

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


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 116.61  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  59 LLLKRRYPELTWVHSHFTYGATA--IAFWLK----YITNTPYSITLHGADLTFDKVPDLALKM-----QNADKIVSISQF 127
Cdd:cd03817    78 DRIKELGPDIIHTHTPFSLGKLGlrIARKLKipivHTYHTMYEDYLHYIPKGKLLVKAVVRKLvrrfyNHTDAVIAPSEK 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 128 NLDYLNKYfpAVDlNCCQVIPLGV-PAKLSVSPQTNQVQQ-PLE-----ILSVGRLSIHKAQHLLIEACS-LLQKNNIKF 199
Cdd:cd03817   158 IKDTLREY--GVK-GPIEVIPNGIdLDKFEKPLNTEERRKlGLPpdepiLLYVGRLAKEKNIDFLLRAFAeLKKEPNIKL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 200 ncTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIP 279
Cdd:cd03817   235 --VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAAS 312

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2788063403 280 ELLDAGKAGILVPVNDVqALSDAIEKAALDPSSTLTMQQHA 320
Cdd:cd03817   313 ELVEDGENGFLFEPNDE-TLAEKLLHLRENLELLRKLSKNA 352
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 71-340 1.81e-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: 116.01  E-value: 1.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  71 VHSHFTYGAtAIAFWLKYITNTPYSITLHGADLTFDK-----------VPDL---ALKMQNADkIVSISQFNLD-YLNKY 135
Cdd:cd05844    85 VHAHFGRDG-VYALPLARALGVPLVVTFHGFDITTSRawlaaspgwpsQFQRhrrALQRPAAL-FVAVSGFIRDrLLARG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 136 FPAVDLnccQVIPLGV-PAKLSvsPQTNQVQQPLeILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALT 214
Cdd:cd05844   163 LPAERI---HVHYIGIdPAKFA--PRDPAERAPT-ILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQ 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 215 QLIEQyslAEHVQLVGAKFHHEVLASYANADVFVLSSIT------EGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAG 288
Cdd:cd05844   237 ALAAA---LGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETG 313

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2788063403 289 ILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMFAAI 340
Cdd:cd05844   314 FLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAKLEAI 365
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 60-343 1.82e-29

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: 115.89  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  60 LLKRRYPELtwVHSHFTYGATAIAfwLKYIT--NTPYSITLHGADLTfDKVPDLALKmqNADKIVSISQFNLDYLNKYFP 137
Cdd:cd03823    91 LLEDFRPDV--VHTHNLSGLGASL--LDAARdlGIPVVHTLHDYWLL-CPRQFLFKK--GGDAVLAPSRFTANLHEANGL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 138 AVDLncCQVIPLGVPAKLSVSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFncTIIGEGPERQaltqlI 217
Cdd:cd03823   164 FSAR--ISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIEL--VIAGHGPLSD-----E 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 218 EQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSI-TEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDV 296
Cdd:cd03823   235 RQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDA 314

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2788063403 297 QALSDAIEKAALDPsstlTMQQHAIFHIQQHFDLDKNTRMFAAIFRS 343
Cdd:cd03823   315 EDLAAAMRRLLTDP----ALLERLRAGAEPPRSTESQAEEYLKLYRD 357
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 239-344 5.38e-29

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 108.54  E-value: 5.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 239 ASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQ 318
Cdd:COG0438    16 ALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGE 95

                          90       100
                  ....*....|....*....|....*.
gi 2788063403 319 HAIFHIQQHFDLDKNTRMFAAIFRSL 344
Cdd:COG0438    96 AARERAEERFSWEAIAERLLALYEEL 121
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 55-338 8.76e-29

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: 114.86  E-value: 8.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  55 LTGALLLKRRYPELTWVHSHFTYGATAIAFWLKYitnTPYSITL--------------HGADLTFDKVPDLALKMQNA-- 118
Cdd:cd04946    99 LIASFLSKHRVLALLQFVSIFGQGTVVYSYWLNH---TALGLGLlkdeyyrdvvisraHRYDLYEDQYGSYYLPLREYlv 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 119 ---DKIVSISQFNLDYLNKYFPAVDlNCCQVIPLGVPAKLSVSPQTnqVQQPLEILSVGRLSIHKAQHLLIEACSLL--Q 193
Cdd:cd04946   176 sylDAVFLISKEGKDYLQKCYPAYK-EKIFVSRLGVSDKEQYSKVK--KEGDLRLVSCSSIVPVKRIDLIIETLNSLcvA 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 194 KNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFHHEVLASYAN--ADVFVLSSITEGMPLVLMEAMQNGVLVI 271
Cdd:cd04946   253 HPSICISWTHIGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLYKEndVDVFVNVSESEGIPVSIMEAISFGIPVI 332

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788063403 272 APDIAGIPELLDAGKAGILvPVND--VQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMFA 338
Cdd:cd04946   333 ATNVGGTREIVENETNGLL-LDKDptPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYSKFA 400
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 152-332 2.61e-28

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: 112.54  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 152 PAKLSVSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGA 231
Cdd:cd03799   159 CNKFRFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGW 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 232 KFHHEVLASYANADVFVLSSIT------EGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEK 305
Cdd:cd03799   239 KPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTY 318

                         170       180
                  ....*....|....*....|....*..
gi 2788063403 306 AALDPSSTLTMQQHAIFHIQQHFDLDK 332
Cdd:cd03799   319 LIEHPAIWPEMGKAGRARVEEEYDINK 345
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 58-291 5.81e-27

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: 106.33  E-value: 5.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  58 ALLLKRRYPELTWVHSHFTYGATAIAFWLKYITNTPYSITLHGADLTFDKVPDLALKmqnadkivsisqFNLDYLNKYFP 137
Cdd:cd01635    45 RILKKLLELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLAL------------ARLLVSLPLAD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 138 AVdlnccqviplgvpaklsvspqtnqvqqpleilSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLI 217
Cdd:cd01635   113 KV--------------------------------SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788063403 218 EQYSLAEHVQLVGAKFHHEVLASY-ANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILV 291
Cdd:cd01635   161 AALGLLERVVIIGGLVDDEVLELLlAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 5-336 3.93e-26

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: 106.68  E-value: 3.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403   5 QNEVSYLCEARWGELLLSHWLFLISSPVVYFKALLRAFLLEeklktsiaHLTGALLLKRRYPELTWVHSHFTYgataiaf 84
Cdd:cd03809    32 PDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALL--------RWLQILLPKKDKPDLLHSPHNTAP------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  85 wlKYITNTPYSITLHgaDLTFDKVPDLALK-------------MQNADKIVSISQFNLDYLNKYFPaVDLNCCQVIPLGV 151
Cdd:cd03809    97 --LLLKGCPQVVTIH--DLIPLRYPEFFPKrfrlyyrlllpisLRRADAIITVSEATRDDIIKFYG-VPPEKIVVIPLGV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 152 -----PAKLSVSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGE-GPERQALTQLIEQYSLAEH 225
Cdd:cd03809   172 dpsffPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGkGWEDEELLDLVKKLGLGGR 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 226 VQLVGaKFHHEVLAS-YANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELldAGKAGILVPVNDVQALSDAIE 304
Cdd:cd03809   252 VRFLG-YVSDEDLPAlYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEV--AGDAALYFDPLDPESIADAIL 328

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2788063403 305 KAALDPSSTLTMQQHAIFHIQQhFDLDKNTRM 336
Cdd:cd03809   329 RLLEDPSLREELIRKGLERAKK-FSWEKTAEK 359
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 61-345 1.10e-23

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


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 101.26  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  61 LKRRYPELTWVHSHFTYGATAIAFWLKYITNTPYSITLHG----------ADLTFDKvPDL------------ALKMQNA 118
Cdd:cd03813   167 AADDLPEADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGiytrerkieiLQSTWIM-GYIkklwirfferlgKLAYQQA 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 119 DKIVSISQFNLDYLNKYfpAVDLNCCQVIPLGV------PAKLSVSPQTnqvqqPLEILSVGRLSIHKAQHLLIEACSLL 192
Cdd:cd03813   246 DKIISLYEGNRRRQIRL--GADPDKTRVIPNGIdiqrfaPAREERPEKE-----PPVVGLVGRVVPIKDVKTFIRAFKLV 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 193 QKNNIKFNCTIIG---EGPE-RQALTQLIEQYSLAEHVQLVGAKfhhEVLASYANADVFVLSSITEGMPLVLMEAMQNGV 268
Cdd:cd03813   319 RRAMPDAEGWLIGpedEDPEyAQECKRLVASLGLENKVKFLGFQ---NIKEYYPKLGLLVLTSISEGQPLVILEAMASGV 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 269 LVIAPDIAGIPELL-----DAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDkntRMFAAiFRS 343
Cdd:cd03813   396 PVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLE---GMIDS-YRK 471


                  ..
gi 2788063403 344 LF 345
Cdd:cd03813   472 LY 473
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 61-332 7.06e-23

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: 97.73  E-value: 7.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  61 LKRRYPELTWVHSHFTYG-ATAIAFWLKYitNTPYSITLHgADLTFDKV------PDLALKMQNADKIV-------SISQ 126
Cdd:cd03795    77 FKKLAKEYDIIHYHFPNPlADLLLFFSGA--KKPVVVHWH-SDIVKQKKllklykPLMTRFLRRADRIIatspnyvETSP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 127 FNLDYLNKyfpavdlncCQVIPLGVPAKLSVSPQTNQVQQPLE------ILSVGRLSIHKAQHLLIEACSLlqknnIKFN 200
Cdd:cd03795   154 TLREFKNK---------VRVIPLGIDKNVYNIPRVDFENIKREkkgkkiFLFIGRLVYYKGLDYLIEAAQY-----LNYP 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 201 CTIIGEGPERQALTQLIEqYSLAEHVQLVGAKFHHEVLASYANADVFVLSSI--TEGMPLVLMEAMQNGVLVIAPDIA-G 277
Cdd:cd03795   220 IVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGtG 298

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2788063403 278 IPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDK 332
Cdd:cd03795   299 VPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEK 353
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 121-332 1.11e-22

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: 97.40  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 121 IVSISQFNLDYLNKYFPAVDLNCcQVIPLGV------PAKLSVSPQTNQVQQPLEILSVGRLSIH---KAQHLLIEACSL 191
Cdd:cd03825   141 IVAPSRWLADMVRRSPLLKGLPV-VVIPNGIdteifaPVDKAKARKRLGIPQDKKVILFGAESVTkprKGFDELIEALKL 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 192 LQKNnIKFNCTIIGEGPERQALT--QLIEQYSLAEHVQLVGAkfhhevlasYANADVFVLSSITEGMPLVLMEAMQNGVL 269
Cdd:cd03825   220 LATK-DDLLLVVFGKNDPQIVILpfDIISLGYIDDDEQLVDI---------YSAADLFVHPSLADNLPNTLLEAMACGTP 289

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788063403 270 VIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDK 332
Cdd:cd03825   290 VVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRV 352
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 53-328 2.12e-22

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: 96.93  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  53 AHLTGALLLKRRYPELtwVHSHFTYGATAiAFWLKYITNTPYSITLH----------GADLTFDkvPDLALK-----MQN 117
Cdd:cd03800    89 DGLLRFIAREGGRYDL--IHSHYWDSGLV-GALLARRLGVPLVHTFHslgrvkyrhlGAQDTYH--PSLRITaeeqiLEA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 118 ADKIVSISQFNLDYL----NKYFPAVDlnccqVIPLGVPAKL--SVSPQTNQV------QQPLEILSVGRLSIHKAQHLL 185
Cdd:cd03800   164 ADRVIASTPQEADELislyGADPSRIN-----VVPPGVDLERffPVDRAEARRarlllpPDKPVVLALGRLDPRKGIDTL 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 186 IEACSLLQKNNIKFNCTIIGeGPE-------RQALTQLIEQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSITEGMPL 258
Cdd:cd03800   239 VRAFAQLPELRELANLVLVG-GPSddplsmdREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGL 317

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 259 VLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHF 328
Cdd:cd03800   318 TAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHY 387
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 170-311 1.56e-21

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 93.90  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 170 ILSVGRLSIHKAQHLLIEACSLLQKNnIKFNCTIIGEGPERQALtqliEQYSLaeHVQLVGAKFHHEVLASYANADVFVL 249
Cdd:cd03814   201 LLYVGRLAPEKNLEALLDADLPLAAS-PPVRLVVVGDGPARAEL----EARGP--DVIFTGFLTGEELARAYASADVFVF 273

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788063403 250 SSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPS 311
Cdd:cd03814   274 PSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPE 335
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 71-344 6.89e-21

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


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 92.41  E-value: 6.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  71 VHSHFTYGATAIAFWLKYIT--NTPYSITLHGADLTF---DKV--PDLALKMQNADKIVSISQFNLDYLNKYFPaVDlNC 143
Cdd:cd04962    88 LHAHYAIPHASCAYLAREILgeKIPIVTTLHGTDITLvgyDPSlqPAVRFSINKSDRVTAVSSSLRQETYELFD-VD-KD 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 144 CQVIPLGVPAKLSVSPQTNQVQQPLEILSVGRLSIH-------KAQHLLIEACSLLQkNNIKFNCTIIGEGPERQALTQL 216
Cdd:cd04962   166 IEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHvsnfrpvKRIDDVVRVFARVR-RKIPAKLLLVGDGPERVPAEEL 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 217 IEQYSLAEHVQLVGAKFHHEVLasYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDV 296
Cdd:cd04962   245 ARELGVEDRVLFLGKQDDVEEL--LSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDV 322

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2788063403 297 QALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMFAAIFRSL 344
Cdd:cd04962   323 DAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 170-331 1.68e-20

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: 90.97  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 170 ILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGakFHHEVLASYANADVFVL 249
Cdd:cd04951   191 ILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLG--QISNISEYYNAADLFVL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 250 SSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLdaGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFD 329
Cdd:cd04951   269 SSEWEGFGLVVAEAMACERPVVATDAGGVAEVV--GDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFS 346


                  ..
gi 2788063403 330 LD 331
Cdd:cd04951   347 IN 348
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 54-332 2.62e-20

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: 90.51  E-value: 2.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  54 HLTGALLLKRRYPELTWVHSHFTYGATAIAFWLKYiTNTPYSITLHGA----DLTFDKVPDLALKM-------QNADKIV 122
Cdd:cd03821    79 GLPNWLRRNLREYDVVHIHGVWTYTSLAACKLARR-RGIPYVVSPHGMldpwALQQKHWKKRIALHlierrnlNNAALVH 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 123 SISQFNLDYLNKYFPAVDLnccQVIPLGV-----PAKLSVSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSLLQKNNI 197
Cdd:cd03821   158 FTSEQEADELRRFGLEPPI---AVIPNGVdipefDPGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGR 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 198 KFNCTIIGEGP-ERQALTQLIEQYSLAEHVQLVGAKFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIA 276
Cdd:cd03821   235 DWHLVIAGPDDgAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKC 314

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788063403 277 GIPELLDAGkAGILVPVNDvQALSDAIEKAALDPSSTLTMQQ--HAIFHIQQHFDLDK 332
Cdd:cd03821   315 GLSELVEAG-CGVVVDPNV-SSLAEALAEALRDPADRKRLGEmaRRARQVEENFSWEA 370
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 51-338 7.74e-16

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: 77.77  E-value: 7.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  51 SIAHLTGALLLKRRYPELtwVHSHFTYGATAIAFWLKYITNTPYSITLHgaDLTFDKVPDLALKM--------------- 115
Cdd:cd03794    85 ALAALLKLLVREERPDVI--IAYSPPITLGLAALLLKKLRGAPFILDVR--DLWPESLIALGVLKkgsllkllkklerkl 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 116 -QNADKIVSISQFNLDYLNKyfPAVDLNCCQVIPLGV------PAKLSVSPQTNQVQQPLEILSVGrlSIHKAQHL--LI 186
Cdd:cd03794   161 yRLADAIIVLSPGLKEYLLR--KGVPKEKIIVIPNWAdleefkPPPKDELRKKLGLDDKFVVVYAG--NIGKAQGLetLL 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 187 EACSLLQKN-NIKFncTIIGEGPERQALTQLIEQYSLaEHVQLVGAKFHHEVLASYANADVFVLS-----SITEGMPLVL 260
Cdd:cd03794   237 EAAERLKRRpDIRF--LFVGDGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLVPlkdnpANRGSSPSKL 313

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788063403 261 MEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLDKNTRMFA 338
Cdd:cd03794   314 FEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 146-312 1.06e-14

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


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 74.58  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 146 VIPLGVPAKLSVSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEH 225
Cdd:cd03796   172 VIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDR 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 226 VQLVGAKFHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKagILVPVNDVQALSDAIEK 305
Cdd:cd03796   252 VELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDM--ILLAEPDPEDIVRKLEE 329

                         170
                  ....*....|....
gi 2788063403 306 AA-------LDPSS 312
Cdd:cd03796   330 AIsilrtgkHDPWS 343
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 170-311 6.17e-14

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 72.44  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 170 ILSVGRLSIHKAQHLLIEACSLLQKNNIKFnctiIGEGPERQALtqliEQYSLAEHVQLVGAKFHHEVLASYANADVFVL 249
Cdd:PLN02871  266 IVYVGRLGAEKNLDFLKRVMERLPGARLAF----VGDGPYREEL----EKMFAGTPTVFTGMLQGDELSQAYASGDVFVM 337

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788063403 250 SSITEGMPLVLMEAMQNGVLVIAPDIAGIPELL---DAGKAGILVPVNDVQALSDAIEKAALDPS 311
Cdd:PLN02871  338 PSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPE 402
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 29-275 2.41e-13

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: 70.01  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  29 SSPVVYFKALLRaflLEEKLKTSIAH-----LTGALLL---KRRYPELTwVHSHftygataiafwlkyitNTPYSITLhg 100
Cdd:cd03812    63 KNIIKYFIKLLK---LIKKEKYDIVHvhgssSNGIILLlaaKAGVPVRI-AHSH----------------NTKDSSIK-- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 101 adltFDKVPDLALK---MQNADKIVSISQFNLDYLnkyFPAVDLNCCQVIPLGVPAKLSV-SPQTNQVQQPLEILS---- 172
Cdd:cd03812   121 ----LRKIRKNVLKkliERLSTKYLACSEDAGEWL---FGEVENGKFKVIPNGIDIEKYKfNKEKRRKRRKLLILEdklv 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 173 ---VGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGakFHHEVLASYANADVFVL 249
Cdd:cd03812   194 lghVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLG--FRNDVSEILSAMDVFLF 271

                         250       260
                  ....*....|....*....|....*.
gi 2788063403 250 SSITEGMPLVLMEAMQNGVLVIAPDI 275
Cdd:cd03812   272 PSLYEGLPLVAVEAQASGLPCLLSDT 297
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 172-342 2.84e-10

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 61.59  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 172 SVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFHheVLASYANADVFVLSS 251
Cdd:PRK15179  522 TVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRR--VGYWLTQFNAFLLLS 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 252 ITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDV------QALSDAIEKAALDPSstltMQQHAIFHIQ 325
Cdd:PRK15179  600 RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVtapdvaEALARIHDMCAADPG----IARKAADWAS 675

                         170
                  ....*....|....*..
gi 2788063403 326 QHFDLDKntrMFAAIFR 342
Cdd:PRK15179  676 ARFSLNQ---MIASTVR 689
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 216-345 1.91e-09

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


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 58.79  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 216 LIEQYSLAEHVQLVGAKFHHEVLAsyaNADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDA--------GKA 287
Cdd:NF038011  359 LVASLGLQDKVKFLGFQKIDDLLP---QVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIEGldeedralGAA 435

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788063403 288 GILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDldkNTRMFAAiFRSLF 345
Cdd:NF038011  436 GEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYT---EELMFDR-YRELY 489
Glyco4_Geo_Pelo NF038229
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 93-344 3.78e-09

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 57.30  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  93 PYSITLHGAD----LTFDKVPDLALKMQNADKIVSISQFNLDYLNKYFPAVDlnccqviplgvpAKLSVSPQTnqVQQPL 168
Cdd:NF038229   81 PYLVTLTGTDvneaLDPDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLA------------AKLVVIPQG--VELGG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 169 EILSVGRLSIHKAQHL----------------LIEACSLLQKNNIKFNCTIIG----EGPERQALTQLiEQYSLAEHVQL 228
Cdd:NF038229  147 EPFPLRELGLFDSDEFvfllpaglrpvkgvlfLLEMLAPLHAEDPRLRLAFAGpvldEEYAAAFFAAL-ARRPWARYLGE 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 229 VGakfHHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILvpVNDVQALSDAIEKAAL 308
Cdd:NF038229  226 IP---HDAMGALYRRADVVLNNSLFEGMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLL--YRDEAEFLRQARQLLQ 300

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2788063403 309 DPSSTLTMQQHAIFHIQQHFDLDKNTRMFAAIFRSL 344
Cdd:NF038229  301 DPALRRRLGRPGRQLVRERYSPEREAEAYLRLYRAV 336
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 256-332 4.02e-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: 54.29  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 256 MPLV----LMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFHIQQHFDLD 331
Cdd:cd03818   309 YPFVlswsLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLD 388


                  .
gi 2788063403 332 K 332
Cdd:cd03818   389 V 389
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 146-303 3.63e-07

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: 51.23  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 146 VIPLGVP----AKLSVSPQTNQVQQPLEILSVGRLSIHKAQHLLIEACSLLQKNNIKFNCTIIGE-GPE------RQALT 214
Cdd:cd03822   162 VIPHGVPevpqDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGElHPSlaryegERYRK 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 215 QLIEQYSLAEHVQLVGAKFHHEVLASYANA-DVFVLS--SITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGkAGILV 291
Cdd:cd03822   242 AAIEELGLQDHVDFHNNFLPEEEVPRYISAaDVVVLPylNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADG-RGVLV 320

                         170
                  ....*....|..
gi 2788063403 292 PVNDVQALSDAI 303
Cdd:cd03822   321 PFDDPSAIAEAI 332
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 71-331 2.29e-06

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: 48.82  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  71 VHSHFTYgataiafWLKYIT---NTPYSITLHGadltFDKVPDLALKMQNADK-IVSISQFNLDYLNkyfpavDLNCCQV 146
Cdd:cd03802    90 IHNHSYD-------WLPPFApliGTPFVTTLHG----PSIPPSLAIYAAEPPVnYVSISDAQRAATP------PIDYLTV 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 147 IPLGVPakLSVSPQTNQVQQPLeiLSVGRLSIHKAQHLLIEACsllQKNNIKFncTIIGeGPERQALTQLIEQYSLAEHV 226
Cdd:cd03802   153 VHNGLD--PADYRFQPDPEDYL--AFLGRIAPEKGLEDAIRVA---RRAGLPL--KIAG-KVRDEDYFYYLQEPLPGPRI 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 227 QLVGAKFHHEVLASYANADVfVLSSIT--EGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPvnDVQALSDAIE 304
Cdd:cd03802   223 EFIGEVGHDEKQELLGGARA-LLFPINwdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD--SVEEMAEAIA 299

                         250       260
                  ....*....|....*....|....*...
gi 2788063403 305 K-AALDPsstltMQQHAifHIQQHFDLD 331
Cdd:cd03802   300 NiDRIDR-----AACRR--YAEDRFSAA 320
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 234-335 2.37e-06

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: 48.86  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 234 HHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSdaIEKAALDPSST 313
Cdd:cd03792   270 DQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVR--ILRLLTDPELR 347

                          90       100
                  ....*....|....*....|..
gi 2788063403 314 LTMQQHAIFHIQQHFDLDKNTR 335
Cdd:cd03792   348 RKMGLAAREHVRDNFLITGNLR 369
GT20_TPS cd03788
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ...
 235-316 2.73e-06

trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.


Pssm-ID: 340820 [Multi-domain]  Cd Length: 463  Bit Score: 48.74  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 235 HEVLASYANADVFVLSSITEGMPLVLME--AMQ---NGVLVIAPDIAGIPELLDAgkagILVPVNDVQALSDAIEKAald 309
Cdd:cd03788   355 EELLALYRAADVALVTSLRDGMNLVAKEyvACQrdnPGVLILSEFAGAASELDGA----ILVNPWDIEEVAEAINRA--- 427


                  ....*..
gi 2788063403 310 psstLTM 316
Cdd:cd03788   428 ----LTM 430
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
120-274 5.34e-06

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 47.78  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 120 KIVSISQFNLDYlNKYFPAVDLNCC------------QVIPLGVPA-KLS-----VSPQTNQVQQP-----LEILSVGRL 176
Cdd:PRK09922  111 KIFSWPHFSLDH-KKHAECKKITCAdyhlaissgikeQMMARGISAqRISviynpVEIKTIIIPPPerdkpAVFLYVGRL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 177 SIHKAQHL--LIEACSLLQKNnikFNCTIIGEGPERQALTQLIEQYSLAEHVQLVGAKFH--HEVLASYANADVFVLSSI 252
Cdd:PRK09922  190 KFEGQKNVkeLFDGLSQTTGE---WQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQpwEVVQQKIKNVSALLLTSK 266

                         170       180
                  ....*....|....*....|..
gi 2788063403 253 TEGMPLVLMEAMQNGVLVIAPD 274
Cdd:PRK09922  267 FEGFPMTLLEAMSYGIPCISSD 288
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
116-346 3.96e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 45.17  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 116 QNAdKIVSISQFNLDYLNKYFPAVDLnccQVIPLGVPAKLSVSPQTNQVQQPLEI-------LSVGRLSIHKAQHLLIEA 188
Cdd:PRK15484  139 KNA-KIIVPSQFLKKFYEERLPNADI---SIVPNGFCLETYQSNPQPNLRQQLNIspdetvlLYAGRISPDKGILLLMQA 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 189 CSLLQK--NNIKFncTIIGE---------GPERQALTQLIEQysLAEHVQLVGAKFHHEVLASYANAD-VFVLSSITEGM 256
Cdd:PRK15484  215 FEKLATahSNLKL--VVVGDptasskgekAAYQKKVLEAAKR--IGDRCIMLGGQPPEKMHNYYPLADlVVVPSQVEEAF 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 257 PLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGI-LVPVNDVQALSDAIEKAALDPSSTLTMQQHAIFhIQQHFDLDKNTR 335
Cdd:PRK15484  291 CMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADPELTQIAEQAKDF-VFSKYSWEGVTQ 369

                         250
                  ....*....|.
gi 2788063403 336 MFAAIFRSLFS 346
Cdd:PRK15484  370 RFEEQIHNWFD 380
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 171-304 8.22e-05

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: 43.81  E-value: 8.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 171 LSVGRLSIHKAQHLLIEACSLLQKNNIkfnctIIGEGPERQALtqlieQYSLAEHVQLVGAKFHHEVLASYANADVFVLS 250
Cdd:cd03804   203 LTASRLVPYKRIDLAVEAFNELPKRLV-----VIGDGPDLDRL-----RAMASPNVEFLGYQPDEVLKELLSKARAFVFA 272

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2788063403 251 SiTEGMPLVLMEAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVQALSDAIE 304
Cdd:cd03804   273 A-EEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVE 325
Glyco_transf_20 pfam00982
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ...
 235-316 9.32e-05

Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,.


Pssm-ID: 425972 [Multi-domain]  Cd Length: 471  Bit Score: 44.19  E-value: 9.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 235 HEVLASYANADVFVLSSITEGMPLVLMEAM-----QNGVLVIAPDIAGIPELLDagkAGILVPVNDVQALSDAIEKAald 309
Cdd:pfam00982 361 DELIALYAVADVCLVTSLRDGMNLVAYEYVacqqgRKGVLILSEFAGAAQSLND---GAILVNPWDIDEVAEAINEA--- 434


                  ....*..
gi 2788063403 310 psstLTM 316
Cdd:pfam00982 435 ----LTM 437
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
1-151 1.52e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 41.75  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403   1 MKAMQNEVSYLCEARWGELLLSHWLFLISSPVVYFKALLRAFLLeeklktsIAHLTGALLLKRRYPELtwVHSHFTYGAT 80
Cdd:pfam13439  14 LARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSL-------AFLRRLRRLLRRERPDV--VHAHSPFPLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403  81 AIAFWLKYITNTPYSITLHGADLTFDKVPDLALK------------MQNADKIVSISQFNLDYLNKYFPaVDLNCCQVIP 148
Cdd:pfam13439  85 LAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPlrrllrrlerrlLRRADRVIAVSEAVADELRRLYG-VPPEKIRVIP 163


                  ...
gi 2788063403 149 LGV 151
Cdd:pfam13439 164 NGV 166
PLN03063 PLN03063
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
 235-306 1.70e-04

alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional


Pssm-ID: 215555 [Multi-domain]  Cd Length: 797  Bit Score: 43.32  E-value: 1.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788063403 235 HEVLASYANADVFVLSSITEGMPLVLME--AMQN---GVLVIApDIAGIPELLDAGkaGILVPVNDVQALSDAIEKA 306
Cdd:PLN03063  367 NYLCALYAITDVMLVTSLRDGMNLVSYEfvACQKakkGVLVLS-EFAGAGQSLGAG--ALLVNPWNITEVSSAIKEA 440
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
203-343 1.95e-04

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 43.15  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 203 IIGEGPERQALTQLIEQYSLAEHVQLVGAKfhHEVLASYANADVFVLSSITEGMPLVLMEAMQNGVLVIAPDIAGIPELL 282
Cdd:PRK15490  434 LVGDGDLRAEAQKRAEQLGILERILFVGAS--RDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECF 511

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788063403 283 DAGKAGILV----PVNDVQALSDAIEKAALDPSSTLTMQQHAIFhIQQHFDLDKNTRMFAAIFRS 343
Cdd:PRK15490  512 IEGVSGFILddaqTVNLDQACRYAEKLVNLWRSRTGICQQTQSF-LQERFTVEHMVGTFVKTIAS 575
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 173-320 2.22e-04

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


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 42.94  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 173 VGRLSIHKAQHLLIEACSLLQKNNIKFncTIIGEGPER--QALTQLIEQYSlaEHVQLVgAKFhHEVLAS--YANADVFV 248
Cdd:cd03791   300 VGRLTEQKGVDLILDALPELLEEGGQL--VVLGSGDPEyeQAFRELAERYP--GKVAVV-IGF-DEALAHriYAGADFFL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 249 LSSITEgmP--LVLMEAMQNGVLVIAPDIAG-----IPELLDAGKA-GILVPVNDVQALSDAIEKAAL---DPSSTLTMQ 317
Cdd:cd03791   374 MPSRFE--PcgLVQMYAMRYGTLPIVRRTGGladtvFDYDPETGEGtGFVFEDYDAEALLAALRRALAlyrNPELWRKLQ 451


                  ...
gi 2788063403 318 QHA 320
Cdd:cd03791   452 KNA 454
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
 235-316 4.80e-04

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 41.83  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 235 HEVLASYANADVFVLSSITEGMPLVLMEAM-----QNGVLVIApDIAGIP-ELLDAgkagILVPVNDVQALSDAIEKAal 308
Cdd:PRK14501  353 EELVALYRAADVALVTPLRDGMNLVAKEYVasrtdGDGVLILS-EMAGAAaELAEA----LLVNPNDIEGIAAAIKRA-- 425


                  ....*...
gi 2788063403 309 dpsstLTM 316
Cdd:PRK14501  426 -----LEM 428
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 105-331 2.52e-03

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: 39.49  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 105 FDKVPDLALKMqnADKIVSISQFNLDYLNKYFPAVdlnccQVIPLGV---PAKLSVSPQTNQVQQPLEILSVGR----LS 177
Cdd:cd03805   144 FDWLEEFTTGM--ADQIVVNSNFTAGVFKKTFPSL-----AKNPPEVlypCVDTDSFDSTSEDPDPGDLIAKSNkkffLS 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 178 IH-----KAQHLLIEACSLLQKNNIKFNCT--IIGEG-PERqaltqlieqysLAEHVQlvgakfHHEVLASYA------N 243
Cdd:cd03805   217 INrferkKNIALAIEAFAKLKQKLPEFENVrlVIAGGyDPR-----------VAENVE------YLEELQRLAeellnvE 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788063403 244 ADVFVLSSITEGMPLVLM--------------------EAMQNGVLVIAPDIAGIPELLDAGKAGILVPVNDVqALSDAI 303
Cdd:cd03805   280 DQVLFLRSISDSQKEQLLssalallytpsnehfgivplEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPE-AFAEAM 358

                         250       260
                  ....*....|....*....|....*...
gi 2788063403 304 EKAALDPSSTLTMQQHAIFHIQQHFDLD 331
Cdd:cd03805   359 LKLANDPDLADRMGAAGRKRVKEKFSRE 386
 
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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