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Conserved domains on  [gi|16080143|ref|NP_390969|]
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spore coat protein [Bacillus subtilis subsp. subtilis str. 168]

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 ...
 2-374 4.92e-77

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: 242.06  E-value: 4.92e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATEKLPVPsvrGGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADREKVDGVHYVHLDEDRYE-------EAVGAE 74
Cdd:cd03801   1 KILLLSPELPPPV---GGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALlrarrllRELRPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  75 LKKSRFDLVHVCNRPSWVP-KLKKQAPDAVFILSVHNEMFAYDKISQ-------AEGEICIDSVAQIVTVSDYIGQTITS 146
Cdd:cd03801  78 LRLRKFDVVHAHGLLAALLaALLALLLGAPLVVTLHGAEPGRLLLLLaaerrllARAEALLRRADAVIAVSEALRDELRA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 147 RFPSARSKTKTVYSGVDLKTYHPRwtnegqrareEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMV 226
Cdd:cd03801 158 LGGIPPEKIVVIPNGVDLERFSPP----------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLV 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 227 FIGSkwfGDNELNNYVKHLHTLGamqkDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNR 306
Cdd:cd03801 228 IVGG---DGPLRAELEELELGLG----DRVRFLGFVPDEELPALYAAADVFVLPSRY-EGFGLVVLEAMAAGLPVVATDV 299

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 307 GGNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYE 374
Cdd:cd03801 300 GGLPEVVEDGEGGLVVPP-DDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-374 4.92e-77

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: 242.06  E-value: 4.92e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATEKLPVPsvrGGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADREKVDGVHYVHLDEDRYE-------EAVGAE 74
Cdd:cd03801   1 KILLLSPELPPPV---GGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALlrarrllRELRPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  75 LKKSRFDLVHVCNRPSWVP-KLKKQAPDAVFILSVHNEMFAYDKISQ-------AEGEICIDSVAQIVTVSDYIGQTITS 146
Cdd:cd03801  78 LRLRKFDVVHAHGLLAALLaALLALLLGAPLVVTLHGAEPGRLLLLLaaerrllARAEALLRRADAVIAVSEALRDELRA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 147 RFPSARSKTKTVYSGVDLKTYHPRwtnegqrareEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMV 226
Cdd:cd03801 158 LGGIPPEKIVVIPNGVDLERFSPP----------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLV 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 227 FIGSkwfGDNELNNYVKHLHTLGamqkDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNR 306
Cdd:cd03801 228 IVGG---DGPLRAELEELELGLG----DRVRFLGFVPDEELPALYAAADVFVLPSRY-EGFGLVVLEAMAAGLPVVATDV 299

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 307 GGNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYE 374
Cdd:cd03801 300 GGLPEVVEDGEGGLVVPP-DDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 190-354 3.76e-51

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: 168.22  E-value: 3.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   190 GKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSKwfgdNELNNYVKHLHTLGAmqKDHVTFIQFVKPKDIPR 269
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG----EEEKRLKKLAEKLGL--GDNVIFLGFVSDEDLPE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   270 LYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERINDLLSSSEKRERLG 349
Cdd:pfam00534  75 LLKIADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLV-KPNNAEALAEAIDKLLEDEELRERLG 152


                  ....*
gi 16080143   350 KYSRR 354
Cdd:pfam00534 153 ENARK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 261-375 1.16e-30

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 113.55  E-value: 1.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 261 FVKPKDIPRL----YTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERIN 336
Cdd:COG0438   4 LVPRKGLDLLlealLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLV-PPGDPEALAEAIL 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16080143 337 DLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYEK 375
Cdd:COG0438  82 RLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEE 120
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
94-367 2.55e-23

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 99.86  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   94 KLKKQAPDAVFILSVHNemfAYdkisQAEGeicIDSVAQIVTVSDYIGQTITSRFPSArsKTKTVYSGVDLKTYHprwtn 173
Cdd:PRK15484 114 QIRERAPQAKLVMHMHN---AF----EPEL---LDKNAKIIVPSQFLKKFYEERLPNA--DISIVPNGFCLETYQ----- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  174 egQRAREEMRSELGL-HGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSKW-FGDNELNNYVKHLHTLGAM 251
Cdd:PRK15484 177 --SNPQPNLRQQLNIsPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTaSSKGEKAAYQKKVLEAAKR 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  252 QKDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWQEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDFENPKQY 331
Cdd:PRK15484 255 IGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLAEPMTSDSI 334

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 16080143  332 AERINDLLSSSEkRERLGKYSRREAESNFGWQRVAE 367
Cdd:PRK15484 335 ISDINRTLADPE-LTQIAEQAKDFVFSKYSWEGVTQ 369
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 130-375 1.42e-17

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


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 83.23  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   130 VAQIVTVSDYIGQTITSRFPSARSKTKTVYSGVDLKTYHPRWTNegqraREEMRSELGLHGKK-IVLFVGRLSKVKGPHI 208
Cdd:TIGR03088 137 IHHYVAVSRDLEDWLRGPVKVPPAKIHQIYNGVDTERFHPSRGD-----RSPILPPDFFADESvVVGTVGRLQAVKDQPT 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   209 LLQALPDIIEEHPD----VMMVFIGskwfgDNELNNYVKHLhtLGAMQKDHVTFIQFVKpKDIPRLYTMSDVFVCSSQwQ 284
Cdd:TIGR03088 212 LVRAFALLVRQLPEgaerLRLVIVG-----DGPARGACEQM--VRAAGLAHLVWLPGER-DDVPALMQALDLFVLPSL-A 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   285 EPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQR 364
Cdd:TIGR03088 283 EGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPP-GDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINA 361

                         250
                  ....*....|.
gi 16080143   365 VAENLLSVYEK 375
Cdd:TIGR03088 362 MVAAYAGLYDQ 372
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-374 4.92e-77

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: 242.06  E-value: 4.92e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATEKLPVPsvrGGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADREKVDGVHYVHLDEDRYE-------EAVGAE 74
Cdd:cd03801   1 KILLLSPELPPPV---GGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALlrarrllRELRPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  75 LKKSRFDLVHVCNRPSWVP-KLKKQAPDAVFILSVHNEMFAYDKISQ-------AEGEICIDSVAQIVTVSDYIGQTITS 146
Cdd:cd03801  78 LRLRKFDVVHAHGLLAALLaALLALLLGAPLVVTLHGAEPGRLLLLLaaerrllARAEALLRRADAVIAVSEALRDELRA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 147 RFPSARSKTKTVYSGVDLKTYHPRwtnegqrareEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMV 226
Cdd:cd03801 158 LGGIPPEKIVVIPNGVDLERFSPP----------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLV 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 227 FIGSkwfGDNELNNYVKHLHTLGamqkDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNR 306
Cdd:cd03801 228 IVGG---DGPLRAELEELELGLG----DRVRFLGFVPDEELPALYAAADVFVLPSRY-EGFGLVVLEAMAAGLPVVATDV 299

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 307 GGNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYE 374
Cdd:cd03801 300 GGLPEVVEDGEGGLVVPP-DDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 190-354 3.76e-51

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: 168.22  E-value: 3.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   190 GKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSKwfgdNELNNYVKHLHTLGAmqKDHVTFIQFVKPKDIPR 269
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG----EEEKRLKKLAEKLGL--GDNVIFLGFVSDEDLPE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   270 LYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERINDLLSSSEKRERLG 349
Cdd:pfam00534  75 LLKIADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLV-KPNNAEALAEAIDKLLEDEELRERLG 152


                  ....*
gi 16080143   350 KYSRR 354
Cdd:pfam00534 153 ENARK 157
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 2-370 3.28e-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: 145.82  E-value: 3.28e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATeklpvpsVRGGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADREKVDGVHYVHLDEDRYEEAVGAEL------ 75
Cdd:cd03808   1 KILFIVN-------VDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRRGINPLKDLkalfkl 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  76 ----KKSRFDLVHvCN--RPSWVPKL-KKQAPDAVFILSVHNemFAYDKISQAEGEICIDSV--------AQIVTVSDY- 139
Cdd:cd03808  74 ykllKKEKPDIVH-CHtpKPGILGRLaARLAGVPKVIYTVHG--LGFVFTEGKLLRLLYLLLeklallftDKVIFVNEDd 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 140 IGQTITSRFPSARSKTKTVYSGVDLKTYHPRwtnegqrareemrSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEE 219
Cdd:cd03808 151 RDLAIKKGIIKKKKTVLIPGSGVDLDRFQYS-------------PESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKK 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 220 HPDVMMVFIGskwfgDNELNN-YVKHLHTLGAmqKDHVTFIQFVKpkDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAG 298
Cdd:cd03808 218 GPNVRFLLVG-----DGELENpSEILIEKLGL--EGRIEFLGFRS--DVPELLAESDVFVLPSYR-EGLPRSLLEAMAAG 287

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16080143 299 LPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLL 370
Cdd:cd03808 288 RPVITTDVPGCRELVIDGVNGFLV-PPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 2-354 1.71e-38

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: 140.96  E-value: 1.71e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATEKlpvpsVRGGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADREKVDGVHYVHLDED----------RYEEAV 71
Cdd:cd03811   1 KILFVIPSL-----SGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRvlkliklgllKAILKL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  72 GAELKKSRFDLVHV-CNRPSWVPKLKKqAPDAVFILSVHNEMFAYDKISQAEGEI--CIDSVAQIVTVSDYIGQTITSRF 148
Cdd:cd03811  76 KRILKRAKPDVVISfLGFATYIVAKLA-AARSKVIAWIHSSLSKLYYLKKKLLLKlkLYKKADKIVCVSKGIKEDLIRLG 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 149 PSARSKTKTVYSGVDLktyhprwtnEGQRAREEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFI 228
Cdd:cd03811 155 PSPPEKIEVIYNPIDI---------DRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVIL 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 229 GSkwfGD--NELNNYVKHLHTlgamqKDHVTFIQFVKpkDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNR 306
Cdd:cd03811 226 GD---GPlrEELEKLAKELGL-----AERVIFLGFQS--NPYPYLKKADLFVLSSRY-EGFPNVLLEAMALGTPVVSTDC 294

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 16080143 307 GGNPEVIEEGKNGYIIHDF--ENPKQYAERINDLLSSSEKRERLGKYSRR 354
Cdd:cd03811 295 PGPREILDDGENGLLVPDGdaAALAGILAALLQKKLDAALRERLAKAQEA 344
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 151-371 5.88e-37

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: 137.76  E-value: 5.88e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 151 ARSKTKTVYSGVDLKTYHPrwtneGQRAREEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGS 230
Cdd:cd03800 185 DPSRINVVPPGVDLERFFP-----VDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGG 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 231 KWFGDNELNNYVK----HLHTLGamqkDHVTFIQFVKPKDIPRLYTMSDVFVCSSqWQEPLARVHYEAMAAGLPIITSNR 306
Cdd:cd03800 260 PSDDPLSMDREELaelaEELGLI----DRVRFPGRVSRDDLPELYRAADVFVVPS-LYEPFGLTAIEAMACGTPVVATAV 334

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16080143 307 GGNPEVIEEGKNGYIIHDFEnPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLS 371
Cdd:cd03800 335 GGLQDIVRDGRTGLLVDPHD-PEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT 398
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 76-372 3.24e-33

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: 126.70  E-value: 3.24e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  76 KKSRFDLVHV-CNRPSWVPKLKKQAPDAVFILSVHNEMFAYDKISQAEGEICIDsVAQIVTVSDYIGQTITSRFPSARSK 154
Cdd:cd03819  73 RRERIDLIHAhSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRAR-GDRVIAVSELVRDHLIEALGVDPER 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 155 TKTVYSGVDLKTYHPrwtnegQRAREEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALpDIIEEHPDVMMVFIGskwfg 234
Cdd:cd03819 152 IRVIPNGVDTDRFPP------EAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAA-AELKDEPDFRLLVAG----- 219

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 235 DNELNNYVKHL-HTLGAmqKDHVTFIQFVKpkDIPRLYTMSDVFVCSSQwQEPLARVHYEAMAAGLPIITSNRGGNPEVI 313
Cdd:cd03819 220 DGPERDEIRRLvERLGL--RDRVTFTGFRE--DVPAALAASDVVVLPSL-HEEFGRVALEAMACGTPVVATDVGGAREIV 294

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16080143 314 EEGKNGYIIHDFENPKqYAERINDLLSSSEKRERLGKYSRREAesnfgwqRVAENLLSV 372
Cdd:cd03819 295 VHGRTGLLVPPGDAEA-LADAIRAAKLLPEAREKLQAAAALTE-------AVRELLLRV 345
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 5-373 6.79e-33

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: 126.34  E-value: 6.79e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   5 LIATEKLPVPSVRGGAIQIYlEAVAPLIAKKHEVTVFSIKDPNLADR---EKVDGVHYVHLDEDR--------------Y 67
Cdd:cd03798   2 LILTNIYPNANSPGRGIFVR-RQVRALSRRGVDVEVLAPAPWGPAAArllRKLLGEAVPPRDGRRllplkprlrllaplR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  68 EEAVGAELKKSR---FDLVHVCN-RPS-WVPKLKKQAPDAVFILSVH----NEmFAYDKISQAEGEICIDSVAQIVTVSD 138
Cdd:cd03798  81 APSLAKLLKRRRrgpPDLIHAHFaYPAgFAAALLARLYGVPYVVTEHgsdiNV-FPPRSLLRKLLRWALRRAARVIAVSK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 139 YIGQTITsRFPSARSKTKTVYSGVDLKTYHPrwtnEGQRAREEmrselglHGKKIVLFVGRLSKVKGPHILLQALPDIIE 218
Cdd:cd03798 160 ALAEELV-ALGVPRDRVDVIPNGVDPARFQP----EDRGLGLP-------LDAFVILFVGRLIPRKGIDLLLEAFARLAK 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 219 EHPDVMMVFIgskwfGDNELNNYVKHLHTLGAMQKDhVTFIQFVKPKDIPRLYTMSDVFVCSSqWQEPLARVHYEAMAAG 298
Cdd:cd03798 228 ARPDVVLLIV-----GDGPLREALRALAEDLGLGDR-VTFTGRLPHEQVPAYYRACDVFVLPS-RHEGFGLVLLEAMACG 300

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16080143 299 LPIITSNRGGNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKReRLGKYSRREAESNFGWQRVAENLLSVY 373
Cdd:cd03798 301 LPVVATDVGGIPEVVGDPETGLLVPP-GDADALAAALRRALAEPYLR-ELGEAARARVAERFSWVKAADRIAAAY 373
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
191-340 1.22e-32

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 119.15  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   191 KKIVLFVGRLSK-VKGPHILLQALPDIIEEHPDVMMVFIGSKWfgDNELNNYVKHLhtlgamqKDHVTFIQFVKpkDIPR 269
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGP--EEELEELAAGL-------EDRVIFTGFVE--DLAE 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16080143   270 LYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPEVIeEGKNGYIIhDFENPKQYAERINDLLS 340
Cdd:pfam13692  70 LLAAADVFVLPSLY-EGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLV-PPGDPEALAEAILRLLE 137
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 2-371 8.33e-31

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: 120.55  E-value: 8.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATeklPVPSVRGGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADREKVDGVHYVHLD---------EDRYEEAVG 72
Cdd:cd03821   1 KILHVTP---SISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDgfasipllrQGAGRTDFS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  73 AELK------KSRFDLVH---VCNRPSW-VPKLKKQA--PdavFILSVHNEMFAYDKIS-----QAEGEICIDsvaQIVT 135
Cdd:cd03821  78 PGLPnwlrrnLREYDVVHihgVWTYTSLaACKLARRRgiP---YVVSPHGMLDPWALQQkhwkkRIALHLIER---RNLN 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 136 VSDYIGQTIT-----SRFPSARSKTKTVYSGVDLKTYHPRwtneGQRAREEMrselGLHGKKIVLFVGRLSKVKGPHILL 210
Cdd:cd03821 152 NAALVHFTSEqeadeLRRFGLEPPIAVIPNGVDIPEFDPG----LRDRRKHN----GLEDRRIILFLGRIHPKKGLDLLI 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 211 QALPDIIEEHPDVMMVFIGSkwfGDNElnnyvkHLHTLGAMQK----DHVTFIQFVKPKDIPRLYTMSDVFVCSSQwQEP 286
Cdd:cd03821 224 RAARKLAEQGRDWHLVIAGP---DDGA------YPAFLQLQSSlglgDRVTFTGPLYGEAKWALYASADLFVLPSY-SEN 293

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 287 LARVHYEAMAAGLPIITSNRGGNPEVIEEGkNGYIIHDfeNPKQYAERINDLLSSSEKRERLGKYSRR--EAESNFGWQR 364
Cdd:cd03821 294 FGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP--NVSSLAEALAEALRDPADRKRLGEMARRarQVEENFSWEA 370


                ....*..
gi 16080143 365 VAENLLS 371
Cdd:cd03821 371 VAGQLGE 377
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 261-375 1.16e-30

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 113.55  E-value: 1.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 261 FVKPKDIPRL----YTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERIN 336
Cdd:COG0438   4 LVPRKGLDLLlealLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLV-PPGDPEALAEAIL 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16080143 337 DLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYEK 375
Cdd:COG0438  82 RLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEE 120
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 151-374 3.16e-28

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: 113.18  E-value: 3.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 151 ARSKTKTVYSGVDLKTYHPrwtneGQRAREEMRSELGLHGKKIVL-FVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIG 229
Cdd:cd03807 154 AKNKIVVIYNGIDLFKLSP-----DDASRARARRRLGLAEDRRVIgIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVG 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 230 SkwfGDNElNNYVKHLHTLGAmqKDHVTFiqFVKPKDIPRLYTMSDVFVCSSQwQEPLARVHYEAMAAGLPIITSNRGGN 309
Cdd:cd03807 229 R---GPER-PNLERLLLELGL--EDRVHL--LGERSDVPALLPAMDIFVLSSR-TEGFPNALLEAMACGLPVVATDVGGA 299

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16080143 310 PEVIEEGKngYIIHDFENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYE 374
Cdd:cd03807 300 AELVDDGT--GFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 161-374 1.05e-27

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: 112.00  E-value: 1.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 161 GVDLKTYHPRwtnegqRAREEMRSELGLHGKKIVLFVGRLSKVKGphilLQALPDIIEE---HPDVMMVFIGskwfgDNE 237
Cdd:cd03814 174 GVDTELFHPS------RRDAALRRRLGPPGRPLLLYVGRLAPEKN----LEALLDADLPlaaSPPVRLVVVG-----DGP 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 238 LnnyvkhlhtLGAMQK--DHVTFIQFVKPKDIPRLYTMSDVFVCSSQwQEPLARVHYEAMAAGLPIITSNRGGNPEVIEE 315
Cdd:cd03814 239 A---------RAELEArgPDVIFTGFLTGEELARAYASADVFVFPSR-TETFGLVVLEAMASGLPVVAADAGGPRDIVRP 308

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16080143 316 GKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESnFGWQRVAENLLSVYE 374
Cdd:cd03814 309 GGTGALVEP-GDAAAFAAALRALLEDPELRRRMAARARAEAER-YSWEAFLDNLLDYYA 365
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 2-374 2.03e-27

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: 110.88  E-value: 2.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATekLPVPSVRGGAiQIYLEAVA-PLIAKKHEVTVFSIKD-PNLADREKVDGVHYV-HLDEDRYEEA-------- 70
Cdd:cd03823   1 KILLVNS--LYPPQRVGGA-EISVHDLAeALVAEGHEVAVLTAGVgPPGQATVARSVVRYRrAPDETLPLALkrrgyelf 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  71 ----------VGAELKKSRFDLVHVCN----RPSWVPKLKKQAPDAVFILsvHNemfaYDKISqAEGEICIDSVAQIVTV 136
Cdd:cd03823  78 etynpglrrlLARLLEDFRPDVVHTHNlsglGASLLDAARDLGIPVVHTL--HD----YWLLC-PRQFLFKKGGDAVLAP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 137 SDYIGQTITSRFPsARSKTKTVYSGVdlkTYHPRWTNEGQRAREEMRselglhgkkiVLFVGRLSKVKGPHILLQALPDI 216
Cdd:cd03823 151 SRFTANLHEANGL-FSARISVIPNAV---EPDLAPPPRRRPGTERLR----------FGYIGRLTEEKGIDLLVEAFKRL 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 217 IEEHPDVMMVfigskwfgDNELNNYVKHLHTLGAmqkdhVTFIQFVKPKDIPRLYTMSDVFVCSSQWQEPLARVHYEAMA 296
Cdd:cd03823 217 PREDIELVIA--------GHGPLSDERQIEGGRR-----IAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIA 283

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 297 AGLPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERINDLLSSSE--KRERLGKYSRREAESnfgwqrVAENLLSVYE 374
Cdd:cd03823 284 AGLPVIASDLGGIAELIQPGVNGLLF-APGDAEDLAAAMRRLLTDPAllERLRAGAEPPRSTES------QAEEYLKLYR 356
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 2-375 1.12e-24

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: 102.75  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATEKLPVPSVRGGAIQIYLEAVAP-LIAKKHEVTVFSIKD-PNLADREKVDGVHY----VHLDEDRYE--EAVGA 73
Cdd:cd03802   1 RIAQVSPPRGPVPPGKYGGTELVVSALTEgLVRRGHEVTLFAPGDsHTSAPLVAVIPRALrldpIPQESKLAEllEALEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  74 ELKKSRFDLVHVcNRPSWVPKLKkQAPDAVFILSVHNEMFAYDKISQAEgeiciDSVAQIVTVSDyigqtiTSR--FPSA 151
Cdd:cd03802  81 QLRASDFDVIHN-HSYDWLPPFA-PLIGTPFVTTLHGPSIPPSLAIYAA-----EPPVNYVSISD------AQRaaTPPI 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 152 RSKTkTVYSGVDLKTYHPRwtnegqrareemrselgLHGKKIVLFVGRLSKVKGPHILLQA-----LPdiieehpdvmmV 226
Cdd:cd03802 148 DYLT-VVHNGLDPADYRFQ-----------------PDPEDYLAFLGRIAPEKGLEDAIRVarragLP-----------L 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 227 FIgskwFGDNELNNYVKHLH--TLGamqkDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWQEPLARVHYEAMAAGLPIITS 304
Cdd:cd03802 199 KI----AGKVRDEDYFYYLQepLPG----PRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAY 270

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16080143 305 NRGGNPEVIEEGKNGYIIHDFENPKQYAERINDLlssseKRerlgKYSRREAESNFGWQRVAENLLSVYEK 375
Cdd:cd03802 271 RRGGLPEVIQHGETGFLVDSVEEMAEAIANIDRI-----DR----AACRRYAEDRFSAARMADRYEALYRK 332
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 2-370 1.24e-24

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: 103.58  E-value: 1.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   2 KIALIATEKLPVPsvrGGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADR------EKVDGVHYVHLD---------EDR 66
Cdd:cd03794   1 KILLISQYYPPPK---GAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRifagatETKDGIRVIRVKlgpikknglIRR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  67 YEEAVG--------AELKKSRFDLVHVCNRP---SWVPKLKKQAPDAVFILSVH----NEMFAYDKISQ---------AE 122
Cdd:cd03794  78 LLNYLSfalaallkLLVREERPDVIIAYSPPitlGLAALLLKKLRGAPFILDVRdlwpESLIALGVLKKgsllkllkkLE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 123 gEICIDSVAQIVTVSDYIGQTITSRFPSARsKTKTVYSGVDLKTYHPRwtnegqrAREEMRSELGLHGKKIVLFVGRLSK 202
Cdd:cd03794 158 -RKLYRLADAIIVLSPGLKEYLLRKGVPKE-KIIVIPNWADLEEFKPP-------PKDELRKKLGLDDKFVVVYAGNIGK 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 203 VKGPHILLQALpDIIEEHPDVMMVFIGS--------KWFGDNELNNyvkhlhtlgamqkdhVTFIQFVKPKDIPRLYTMS 274
Cdd:cd03794 229 AQGLETLLEAA-ERLKRRPDIRFLFVGDgdekerlkELAKARGLDN---------------VTFLGRVPKEEVPELLSAA 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 275 DV-FVcssqwqePLARVH----------YEAMAAGLPIITSNRGGNPEVIEEGKNGyIIHDFENPKQYAERINDLLSSSE 343
Cdd:cd03794 293 DVgLV-------PLKDNPanrgsspsklFEYMAAGKPILASDDGGSDLAVEINGCG-LVVEPGDPEALADAILELLDDPE 364

                       410       420
                ....*....|....*....|....*..
gi 16080143 344 KRERLGKYSRREAESNFGWQRVAENLL 370
Cdd:cd03794 365 LRRAMGENGRELAEEKFSREKLADRLL 391
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 75-370 2.81e-24

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: 102.44  E-value: 2.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  75 LKKSRFDLVHV-CNRPSWVPKLKKQA---PDAVFILSVHNEMFAYDKISQAEGEICIDSVAQIVTVSDYIGQTITSRFPS 150
Cdd:cd03809  80 PKKDKPDLLHSpHNTAPLLLKGCPQVvtiHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFYGV 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 151 ARSKTKTVYSGVDLktyHPRWtnegqRAREEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGS 230
Cdd:cd03809 160 PPEKIVVIPLGVDP---SFFP-----PESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGG 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 231 KWFGDNELNNYVKHLHtlgamQKDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWqE----PLArvhyEAMAAGLPIITSNR 306
Cdd:cd03809 232 KGWEDEELLDLVKKLG-----LGGRVRFLGYVSDEDLPALYRGARAFVFPSLY-EgfglPVL----EAMACGTPVIASNI 301

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16080143 307 GGNPEVIeeGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAeSNFGWQRVAENLL 370
Cdd:cd03809 302 SVLPEVA--GDAALYFDP-LDPESIADAILRLLEDPSLREELIRKGLERA-KKFSWEKTAEKTL 361
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 158-375 4.01e-24

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: 101.97  E-value: 4.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 158 VYSGVDLKtyhpRWTNEGQrarEEMRSELGL-HGKKIVLFVGRLSKVKGPHILLQALPDIIEEhPDVMMVFIGSkwfGdN 236
Cdd:cd03817 174 IPNGIDLD----KFEKPLN---TEERRKLGLpPDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGD---G-P 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 237 ELNNYVKHLHTLGAmqKDHVTFIQFVKPKDIPRLYTMSDVFVCSSQwQEPLARVHYEAMAAGLPIITSNRGGNPEVIEEG 316
Cdd:cd03817 242 EREELKELARELGL--ADKVIFTGFVPREELPEYYKAADLFVFAST-TETQGLVYLEAMAAGLPVVAAKDPAASELVEDG 318

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16080143 317 KNGYIIHdfENPKQYAERINDLLSSSEKRERLGKYSRREAESNfgwqRVAENLLSVYEK 375
Cdd:cd03817 319 ENGFLFE--PNDETLAEKLLHLRENLELLRKLSKNAEISAREF----AFAKSVEKLYEE 371
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
94-367 2.55e-23

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 99.86  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   94 KLKKQAPDAVFILSVHNemfAYdkisQAEGeicIDSVAQIVTVSDYIGQTITSRFPSArsKTKTVYSGVDLKTYHprwtn 173
Cdd:PRK15484 114 QIRERAPQAKLVMHMHN---AF----EPEL---LDKNAKIIVPSQFLKKFYEERLPNA--DISIVPNGFCLETYQ----- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  174 egQRAREEMRSELGL-HGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSKW-FGDNELNNYVKHLHTLGAM 251
Cdd:PRK15484 177 --SNPQPNLRQQLNIsPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTaSSKGEKAAYQKKVLEAAKR 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  252 QKDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWQEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDFENPKQY 331
Cdd:PRK15484 255 IGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLAEPMTSDSI 334

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 16080143  332 AERINDLLSSSEkRERLGKYSRREAESNFGWQRVAE 367
Cdd:PRK15484 335 ISDINRTLADPE-LTQIAEQAKDFVFSKYSWEGVTQ 369
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 18-367 1.09e-22

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: 97.69  E-value: 1.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  18 GGAiqiylEAVAPLIA-----KKHEVTVFSIKDPNLADREKVD-GVHYVHLDEDRYEEAVGAE------------LKKSR 79
Cdd:cd03820  13 GGA-----ERVAINLAnhlakKGYDVTIISLDSAEKPPFYELDdNIKIKNLGDRKYSHFKLLLkyfkkvrrlrkyLKNNK 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  80 FDLV--HVCNRPSWVPKLKKQAPdavFILSVHNEMFAYDKIS--QAEGEICIDSVAQIVTVSDyigQTITSRFPSARSKT 155
Cdd:cd03820  88 PDVVisFRTSLLTFLALIGLKSK---LIVWEHNNYEAYNKGLrrLLLRRLLYKRADKIVVLTE---ADKLKKYKQPNSNV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 156 KTVYSGVDLKTYHPRWTNEGqrareemrselglhgkKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSkwfGD 235
Cdd:cd03820 162 VVIPNPLSFPSEEPSTNLKS----------------KRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGD---GP 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 236 --NELNNYVKHLHTlgamqKDHVTFIQFVkpKDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNR-GGNPEV 312
Cdd:cd03820 223 erEELEKLIDKLGL-----EDRVKLLGPT--KNIAEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFDCpTGPSEI 294

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16080143 313 IEEGKNGYIIhDFENPKQYAERINDLLSSSEKRERLGKYSRREAEsNFGWQRVAE 367
Cdd:cd03820 295 IEDGENGLLV-PNGDVDALAEALLRLMEDEELRKKMGKNARKNAE-RFSIEKIIK 347
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 127-360 1.47e-22

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: 97.34  E-value: 1.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 127 IDSVAQIVTVSDYIGQT--ITSRFpsaRSKTKTVYSGVDLKTYhprwtNEGQRAREEMRSELGlhGKKIVLFVGRLSKVK 204
Cdd:cd03795 135 LRRADRIIATSPNYVETspTLREF---KNKVRVIPLGIDKNVY-----NIPRVDFENIKREKK--GKKIFLFIGRLVYYK 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 205 GPHILLQALPDIIEEhpdvmmVFIGskwfGDNELNNYVKHLHTLGAMQKdhVTFIQFVKPKDIPRLYTMSDVFVCSSQWQ 284
Cdd:cd03795 205 GLDYLIEAAQYLNYP------IVIG----GEGPLKPDLEAQIELNLLDN--VKFLGRVDDEEKVIYLHLCDVFVFPSVLR 272

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 285 -EPLARVHYEAMAAGLPIITSNRG-GNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESNF 360
Cdd:cd03795 273 sEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPP-KDPDALAEAIDKLLSDEELRESYGENAKKRFEELF 349
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 166-322 2.76e-20

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: 88.62  E-value: 2.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 166 TYHPRWTNEGQRAREEMRS-ELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVmmVFIgskWFGDNELNNYVKH 244
Cdd:cd01635  84 TVHGPDSLESTRSELLALArLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDL--VLV---LVGGGGEREEEEA 158

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 245 LHTLGAMQKDHVTFIQFVKPKDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYII 322
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRS-EGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 132-375 4.97e-20

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: 90.08  E-value: 4.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 132 QIVTVSDYIGQTITSRFPSARSKTKTVYSGVDLKTYHPRwtnegqrAREEMRSELGLHG-KKIVLFVGR--LSKVKGPHI 208
Cdd:cd03825 140 TIVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPV-------DKAKARKRLGIPQdKKVILFGAEsvTKPRKGFDE 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 209 LLQALpDIIEEHPDVMMVFIGSkwFGDNELNNYVKHLHtLGAMQKDHvtfiQFVkpkdipRLYTMSDVFVCSSQwQEPLA 288
Cdd:cd03825 213 LIEAL-KLLATKDDLLLVVFGK--NDPQIVILPFDIIS-LGYIDDDE----QLV------DIYSAADLFVHPSL-ADNLP 277

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 289 RVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDFEnPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAEN 368
Cdd:cd03825 278 NTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGD-VQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQR 356


                ....*..
gi 16080143 369 LLSVYEK 375
Cdd:cd03825 357 YLELYKD 363
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 161-363 6.92e-20

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 90.54  E-value: 6.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  161 GVDLKTYHPRWTNEgqrareEMRSEL--GLHGKKIVLFVGRLSKVKGphilLQALPDIIEEHPDVMMVFIGSKWFgDNEL 238
Cdd:PLN02871 237 GVDSESFHPRFRSE------EMRARLsgGEPEKPLIVYVGRLGAEKN----LDFLKRVMERLPGARLAFVGDGPY-REEL 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  239 NNYVKHLHT--LGAMQKDhvtfiqfvkpkDIPRLYTMSDVFVCSSQwQEPLARVHYEAMAAGLPIITSNRGGNPEVI--- 313
Cdd:PLN02871 306 EKMFAGTPTvfTGMLQGD-----------ELSQAYASGDVFVMPSE-SETLGFVVLEAMASGVPVVAARAGGIPDIIppd 373

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16080143  314 EEGKNGYIIH--DFEnpkQYAERINDLLSSSEKRERLGKYSRREAESnFGWQ 363
Cdd:PLN02871 374 QEGKTGFLYTpgDVD---DCVEKLETLLADPELRERMGAAAREEVEK-WDWR 421
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 152-375 4.11e-19

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: 87.50  E-value: 4.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 152 RSKTKTVYSGVDLKTYHPRWTNegqraREEMRSELGLHGKKIVLF-VGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGS 230
Cdd:cd04951 153 KNKSVPVYNGIDLNKFKKDINV-----RLKIRNKLNLKNDEFVILnVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGD 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 231 kwfGD--NELNNYVKHLHTlgamqKDHVTFIQFVKpkDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGG 308
Cdd:cd04951 228 ---GPlrNELERLICNLNL-----VDRVILLGQIS--NISEYYNAADLFVLSSEW-EGFGLVVAEAMACERPVVATDAGG 296

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 309 NPEVIEEGKngYIIhDFENPKQYAERIND-LLSSSEKRERLGKySRREAESNFGWQRVAENLLSVYEK 375
Cdd:cd04951 297 VAEVVGDHN--YVV-PVSDPQLLAEKIKEiFDMSDEERDILGN-KNEYIAKNFSINTIVNEWERLYSG 360
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 185-374 2.89e-18

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: 85.13  E-value: 2.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 185 ELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSKWFG--DNELNNYVKHLHTLGAMQkDHVTFI-QF 261
Cdd:cd03822 181 LLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSlaRYEGERYRKAAIEELGLQ-DHVDFHnNF 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 262 VKPKDIPRLYTMSDVFVCSSQWQEPLAR--VHYeAMAAGLPIITSNRGGNPEVIEEGkNGYIIhDFENPKQYAERINDLL 339
Cdd:cd03822 260 LPEEEVPRYISAADVVVLPYLNTEQSSSgtLSY-AIACGKPVISTPLRHAEELLADG-RGVLV-PFDDPSAIAEAILRLL 336

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 16080143 340 SSSEKR----ERLGKYSRreaesNFGWQRVAENLLSVYE 374
Cdd:cd03822 337 EDDERRqaiaERAYAYAR-----AMTWESIADRYLRLFN 370
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 131-369 7.62e-18

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: 84.04  E-value: 7.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 131 AQIVTVSDYIGQTITSR-FPSARskTKTVYSGVDLKTYHPRwtNEGQRAReemrselglhgkkIVLFVGRLSKVKGPHIL 209
Cdd:cd05844 145 ALFVAVSGFIRDRLLARgLPAER--IHVHYIGIDPAKFAPR--DPAERAP-------------TILFVGRLVEKKGCDVL 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 210 LQALPDIIEEHPDVMMVFIGskwfgDNELNNyvkHLHTLGAmQKDHVTFIQFVKPKDIPRLYTMSDVFVCSSQW-----Q 284
Cdd:cd05844 208 IEAFRRLAARHPTARLVIAG-----DGPLRP---ALQALAA-ALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdS 278

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 285 EPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQR 364
Cdd:cd05844 279 EGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPE-GDVDALADALQALLADRALADRMGGAARAFVCEQFDIRV 357


                ....*
gi 16080143 365 VAENL 369
Cdd:cd05844 358 QTAKL 362
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 130-375 1.42e-17

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


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 83.23  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   130 VAQIVTVSDYIGQTITSRFPSARSKTKTVYSGVDLKTYHPRWTNegqraREEMRSELGLHGKK-IVLFVGRLSKVKGPHI 208
Cdd:TIGR03088 137 IHHYVAVSRDLEDWLRGPVKVPPAKIHQIYNGVDTERFHPSRGD-----RSPILPPDFFADESvVVGTVGRLQAVKDQPT 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   209 LLQALPDIIEEHPD----VMMVFIGskwfgDNELNNYVKHLhtLGAMQKDHVTFIQFVKpKDIPRLYTMSDVFVCSSQwQ 284
Cdd:TIGR03088 212 LVRAFALLVRQLPEgaerLRLVIVG-----DGPARGACEQM--VRAAGLAHLVWLPGER-DDVPALMQALDLFVLPSL-A 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   285 EPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQR 364
Cdd:TIGR03088 283 EGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPP-GDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINA 361

                         250
                  ....*....|.
gi 16080143   365 VAENLLSVYEK 375
Cdd:TIGR03088 362 MVAAYAGLYDQ 372
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 146-366 6.09e-17

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: 81.64  E-value: 6.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 146 SRFP-SARSKTKTVYSGVDLKTYHPrwtnEGQRAREEMRSELGLHGKKIVLFVGR-LSKVKGPHILLQALPDIIEEHPDV 223
Cdd:cd03818 171 SLFPaAYRDRISVIHDGVDTDRLAP----DPAARLRLLNGTELKAGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDA 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 224 MMVFIGskwfgdNELNNYVKHLHTLG----------AMQKDHVTFIQFVKPKDIPRLYTMSDV-------FVCSsqWQEp 286
Cdd:cd03818 247 RVVVVG------GDGVSYGSPPPDGGswkqkmlaelGVDLERVHFVGKVPYDQYVRLLQLSDAhvyltypFVLS--WSL- 317

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 287 larvhYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVA 366
Cdd:cd03818 318 -----LEAMACGCPVIGSDTAPVREVIRDGRNGLLV-DFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCL 391
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 127-375 1.71e-15

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: 77.01  E-value: 1.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 127 IDSVAQIVTVSDYIGQTITSRFPSARsKTKTVYSGVDLKTYHPrwtnegQRAREEMRSELGLHGKKIVLFVGRLSKVKGP 206
Cdd:cd04962 139 INKSDRVTAVSSSLRQETYELFDVDK-DIEVIHNFIDEDVFKR------KPAGALKRRLLAPPDEKVVIHVSNFRPVKRI 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 207 HILLQALPDIIEEHP-DVMMVfigskwfGDN-ELNNYVKHLHTLGAmqKDHVTFiqFVKPKDIPRLYTMSDVFVCSSQwQ 284
Cdd:cd04962 212 DDVVRVFARVRRKIPaKLLLV-------GDGpERVPAEELARELGV--EDRVLF--LGKQDDVEELLSIADLFLLPSE-K 279

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 285 EPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYiIHDFENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQR 364
Cdd:cd04962 280 ESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGF-LSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPER 358

                       250
                ....*....|.
gi 16080143 365 VAENLLSVYEK 375
Cdd:cd04962 359 IVPQYEAYYRR 369
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 154-346 3.66e-14

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: 72.71  E-value: 3.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 154 KTKTVYSGVDLKTYhprwtNEGQRAREEMRSELGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSkwf 233
Cdd:cd03812 159 KFKVIPNGIDIEKY-----KFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGE--- 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 234 G--DNELNNYVKHLHTLgamqkDHVTFIQFVkpKDIPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPE 311
Cdd:cd03812 231 GelKEKIKEKVKELGLE-----DKVIFLGFR--NDVSEILSAMDVFLFPSLY-EGLPLVAVEAQASGLPCLLSDTITKEC 302

                       170       180       190
                ....*....|....*....|....*....|....*
gi 16080143 312 VIEEGKNGYIIHdfENPKQYAERINDLLSSSEKRE 346
Cdd:cd03812 303 DITNNVEFLPLN--ETPSTWAEKILKLIKRKRRIN 335
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 186-360 1.01e-13

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: 71.33  E-value: 1.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 186 LGLHGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGskwfgDNELNNYVKHLHTLGAMQkDHVTFIQFVKPK 265
Cdd:cd03799 169 LPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG-----DGDLKEQLQQLIQELNIG-DCVKLLGWKPQE 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 266 DIPRLYTMSDVFVCSSQW-----QEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDfENPKQYAERINDLLS 340
Cdd:cd03799 243 EIIEILDEADIFIAPSVTaadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPE-RDAEAIAEKLTYLIE 321

                       170       180
                ....*....|....*....|
gi 16080143 341 SSEKRERLGKYSRREAESNF 360
Cdd:cd03799 322 HPAIWPEMGKAGRARVEEEY 341
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 152-374 1.06e-12

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: 68.90  E-value: 1.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 152 RSKTKTVYSGVDLKTYHPrwtnegqrAREEMRSELGLHgkkiVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGsk 231
Cdd:cd03813 266 PDKTRVIPNGIDIQRFAP--------AREERPEKEPPV----VGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIG-- 331

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 232 wfGDNELNNYVKHLHTL--GAMQKDHVTFIQFVKPKDIprlYTMSDVFVCSSQWQ-EPLARVhyEAMAAGLPIITSNRGG 308
Cdd:cd03813 332 --PEDEDPEYAQECKRLvaSLGLENKVKFLGFQNIKEY---YPKLGLLVLTSISEgQPLVIL--EAMASGVPVVATDVGS 404

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 309 NPEVIEEGKNGY----IIHDFENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYE 374
Cdd:cd03813 405 CRELIYGADDALgqagLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 191-359 1.48e-11

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: 64.63  E-value: 1.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 191 KKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGSkwfgDNELNNYVKHLHTLGAmqKDHVTFIQFVKpkDIPRL 270
Cdd:cd04949 160 SNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGY----GEEREKLKKLIEELHL--EDNVFLKGYHS--NLDQE 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 271 YTMSDVFVCSSQWQE-PLARVhyEAMAAGLPIITSN-RGGNPEVIEEGKNGYIIhDFENPKQYAERINDLLSSSEKRERL 348
Cdd:cd04949 232 YQDAYLSLLTSQMEGfGLTLM--EAIGHGLPVVSYDvKYGPSELIEDGENGYLI-EKNNIDALADKIIELLNDPEKLQQF 308

                       170
                ....*....|.
gi 16080143 349 GKYSRREAESN 359
Cdd:cd04949 309 SEESYKIAEKY 319
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 165-375 2.16e-10

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: 61.81  E-value: 2.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 165 KTYHPRWTNEGQRAREEMRSELGL-HGKKIVL--FVGRLSKVKGPHILLQALPDIIEEhpDVMMVFIGSkwfGDNELNNY 241
Cdd:cd03791 265 ANYSANDLEGKAENKAALQKELGLpVDPDAPLfgFVGRLTEQKGVDLILDALPELLEE--GGQLVVLGS---GDPEYEQA 339

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 242 VKHlhtLGAMQKDHVTF-IQFVKPKDiPRLYTMSDVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGG--------NPEv 312
Cdd:cd03791 340 FRE---LAERYPGKVAVvIGFDEALA-HRIYAGADFFLMPSRF-EPCGLVQMYAMRYGTLPIVRRTGGladtvfdyDPE- 413

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16080143 313 iEEGKNGYIIHDFeNPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYEK 375
Cdd:cd03791 414 -TGEGTGFVFEDY-DAEALLAALRRALALYRNPELWRKLQKNAMKQDFSWDKSAKEYLELYRS 474
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 200-360 6.49e-10

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: 60.17  E-value: 6.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 200 LSKVKGPHILLQALPDIIEEHPDvmmvfIGSKW--FGDNELNNYVKHLHTlGAMQKDHVTFIQFVKPKDIPRLYTMS--D 275
Cdd:cd04946 233 IVPVKRIDLIIETLNSLCVAHPS-----ICISWthIGGGPLKERLEKLAE-NKLENVKVNFTGEVSNKEVKQLYKENdvD 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 276 VFVCSSQwQEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHDFENPKQYAERINDLLSSSEKRERLGKYSRRE 355
Cdd:cd04946 307 VFVNVSE-SEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLDKDPTPNEIVSSIMKFYLDGGDYKTMKISAREC 385


                ....*
gi 16080143 356 AESNF 360
Cdd:cd04946 386 WEERF 390
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
292-371 1.46e-08

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 51.84  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   292 YEAMAAGLPIITSNRGGNPEVIEEGKNGYIihdFENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLS 371
Cdd:pfam13524  17 FEAAACGAPLLTDRTPGLEELFEPGEEILL---YRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAEQLLD 93
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
18-164 3.72e-08

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 52.53  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143    18 GGAiQIYLEAVAP-LIAKKHEVTVFSIKDPNLADREKVDGVHYVHLDEDRYEE---------AVGAELKKSRFDLVHVCN 87
Cdd:pfam13439   1 GGV-ERYVLELARaLARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRllrslaflrRLRRLLRRERPDVVHAHS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143    88 RPSWVPKL--KKQAPDAVFILSVHNEMFAYDKISQAEG----------EICIDSVAQIVTVSDYIGQTITSRFPSARSKT 155
Cdd:pfam13439  80 PFPLGLAAlaARLRLGIPLVVTYHGLFPDYKRLGARLSplrrllrrleRRLLRRADRVIAVSEAVADELRRLYGVPPEKI 159


                  ....*....
gi 16080143   156 KTVYSGVDL 164
Cdd:pfam13439 160 RVIPNGVDL 168
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 293-369 3.02e-07

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: 51.82  E-value: 3.02e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16080143 293 EAMAAGLPIITSNRGGNPEVIEEGKNGYIIHdfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENL 369
Cdd:cd03805 318 EAMYAGKPVIACNSGGPLETVVEGVTGFLCE--PTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
glgA PRK00654
glycogen synthase GlgA;
161-375 2.20e-06

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 49.35  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  161 GVDLKTYHPR----------WTN-EGQRA-REEMRSELGLHGKKIVLF--VGRLSKVKGPHILLQALPDIIEEhpDVMMV 226
Cdd:PRK00654 238 GIDYDIWNPEtdpllaanysADDlEGKAEnKRALQERFGLPDDDAPLFamVSRLTEQKGLDLVLEALPELLEQ--GGQLV 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  227 FIGSkwfGDNELNNYVKHLHtlgAMQKDHV-TFIQFvkpkDIP---RLYTMSDVFVCSSqwqeplarvHYE--------A 294
Cdd:PRK00654 316 LLGT---GDPELEEAFRALA---ARYPGKVgVQIGY----DEAlahRIYAGADMFLMPS---------RFEpcgltqlyA 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  295 MAAG-LPIItSNRGG--------NPEviEEGKNGYIIHDFENpkqyaeriNDLLSSSE------KRERLGKYSRREA-ES 358
Cdd:PRK00654 377 LRYGtLPIV-RRTGGladtvidyNPE--DGEATGFVFDDFNA--------EDLLRALRralelyRQPPLWRALQRQAmAQ 445

                        250
                 ....*....|....*..
gi 16080143  359 NFGWQRVAENLLSVYEK 375
Cdd:PRK00654 446 DFSWDKSAEEYLELYRR 462
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
176-375 3.29e-06

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 48.93  E-value: 3.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 176 QRAREEMRSELGLHGKK---IVLFVGRLSKVKGPHILLQALPDIIEEhpDVMMVFIGSkwfGDNELNNYvkhlhtLGAMQ 252
Cdd:COG0297 277 AANKAALQEELGLPVDPdapLIGMVSRLTEQKGLDLLLEALDELLEE--DVQLVVLGS---GDPEYEEA------FRELA 345

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 253 KDH----VTFIQFvkpkDIP---RLYTMSDVFVCSSQWqEP-----LarvhYeAMAAG-LPIITSNrGG--------NPE 311
Cdd:COG0297 346 ARYpgrvAVYIGY----DEAlahRIYAGADFFLMPSRF-EPcglnqM----Y-ALRYGtVPIVRRT-GGladtvidyNEA 414

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16080143 312 viEEGKNGYIIHDFeNPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYEK 375
Cdd:COG0297 415 --TGEGTGFVFDEY-TAEALLAAIRRALALYRDPEAWRKLQRNAMKQDFSWEKSAKEYLELYRE 475
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
1-377 3.96e-06

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 48.00  E-value: 3.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143   1 MKIALIateklpvpsvrgGAIQIYLEAVAPLIAKKHEVTVFsikDPNLADREkvdgvhyvHLDEDRYEEAVGAelkksrf 80
Cdd:COG4641   1 MKILWN------------GHATYYRGLLRALAALGHEVTFL---EPDDPWHD--------PLYAAELLDAFRP------- 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  81 DLVHVCNRPSWVPKLKKQAPDAVFilsvhnemfaYDKisqaEGEICIDSVAQIVTVSDYIgqTITSRFPSAR------SK 154
Cdd:COG4641  51 DLVLVISGVELVAALRARGIPTVF----------WDT----DDPVTLDRFRELLPLYDLV--FTFDGDCVEEyralgaRR 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 155 TKTVYSGVDLKTYHPRwtnegqRAREEMRSELGlhgkkivlFVGRLSKVKGPhillqALPDIIEEHPDVMMVFIGSKWFG 234
Cdd:COG4641 115 VFYLPFAADPELHRPV------PPEARFRYDVA--------FVGNYYPDRRA-----RLEELLLAPAGLRLKIYGPGWPK 175

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 235 DNELNNYVKHlhtlgamqkdhvtfiQFVKPKDIPRLYTMSDVFVC-----SSQWQePLARVhYEAMAAGLPIITSNRGGN 309
Cdd:COG4641 176 LALPANVRRG---------------GHLPGEEHPAAYASSKITLNvnrmaASPDS-PTRRT-FEAAACGAFLLSDPWEGL 238

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 310 PEVIEEGKngyIIHDFENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLLSVYEKNR 377
Cdd:COG4641 239 EELFEPGE---EVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVLAEHTYAHRARELLAILEELG 303
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 293-370 8.49e-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: 47.32  E-value: 8.49e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080143 293 EAMAAGLPIITSNRGGNPEVIEEGKNGYIIhdfENPKQYAERINDLLSSSEKRERLGKYSRREAESNFGWQRVAENLL 370
Cdd:cd03792 298 EALWKGKPVIATPAGGIPLQVIDGETGFLV---NSVEGAAVRILRLLTDPELRRKMGLAAREHVRDNFLITGNLRAWL 372
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
18-152 6.04e-05

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 42.77  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143    18 GGAIQIYLEAVAPLIAKKHEVTVFSIKDPNLADREKVDGVHYVHLDEDRYEE---------AVGAELKKSRFDLVHV-CN 87
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPSpladlaalrRLRRLLRAERPDVVHAhSP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16080143    88 RPSWVPKLKKQAPDAVFILSVHNEMFAYDkiSQAEGEI-------CIDSVAQIVTVSDYIGQTITSRFPSAR 152
Cdd:pfam13579  81 TAGLAARLARRRRGVPLVVTVHGLALDYG--SGWKRRLaralerrLLRRADAVVVVSEAEAELLRALGVPAA 150
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
197-341 2.75e-04

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 42.76  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143  197 VGRLSKVKGPHILLQALPDIIEEHPDVMMVFIGskwfgDNELNNYV-KHLHTLGAMQKdhvtfIQFVK-PKDIPRLYTMS 274
Cdd:PRK15490 404 VFRFVGDKNPFAWIDFAARYLQHHPATRFVLVG-----DGDLRAEAqKRAEQLGILER-----ILFVGaSRDVGYWLQKM 473

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16080143  275 DVFVCSSQWqEPLARVHYEAMAAGLPIITSNRGGNPEVIEEGKNGYIIHD-----FENPKQYAERINDLLSS 341
Cdd:PRK15490 474 NVFILFSRY-EGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVSGFILDDaqtvnLDQACRYAEKLVNLWRS 544
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 189-375 7.02e-04

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: 41.45  E-value: 7.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 189 HGKKIVLFVGRLSKVKGPHILLQALPDIIEEHPDVMMVfIGskwfGD-------------NELNNYVKHLHTlgamqkdh 255
Cdd:cd03796 191 PNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFI-IG----GDgpkrieleemrekYQLQDRVELLGA-------- 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 256 vtfiqfVKPKDIPRLYTMSDVFVCSSQwQEPLARVHYEAMAAGLPIITSNRGGNPEVIeegKNGYIIHDFENPKQYAERI 335
Cdd:cd03796 258 ------VPHEEVRDVLVQGHIFLNTSL-TEAFCIAIVEAASCGLLVVSTRVGGIPEVL---PPDMILLAEPDPEDIVRKL 327

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16080143 336 NDLLSSSeKRERLGKYSRREAESNF-GWQRVAENLLSVYEK 375
Cdd:cd03796 328 EEAISIL-RTGKHDPWSFHNRVKKMySWEDVARRTEKVYDR 367
PLN00142 PLN00142
sucrose synthase
 293-337 7.36e-04

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 41.50  E-value: 7.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 16080143  293 EAMAAGLPIITSNRGGNPEVIEEGKNGYIIhDFENPKQYAERIND 337
Cdd:PLN00142 685 EAMTCGLPTFATCQGGPAEIIVDGVSGFHI-DPYHGDEAANKIAD 728
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 176-372 1.75e-03

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 40.11  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 176 QRAREEMRSELGL-HGKKIVLFVG------RLSKVkgphiLLQALPDIIEEHPDVmmVFIGskwfGDNELNNYVKHlhtL 248
Cdd:COG0707 170 ELDRPEARAKLGLdPDKPTLLVFGgsqgarALNEA-----VPAALAALLEARLQV--VHQT----GKGDYEEVRAA---Y 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080143 249 GAMQKDHVTFIQFVkpKDIPRLYTMSDVFVC----SSqwqepLArvhyEAMAAGLP---IITSNRGG-----NPEVIEEG 316
Cdd:COG0707 236 AAAIRPNAEVFPFI--DDMADAYAAADLVISragaST-----VA----ELAALGKPailVPLPHAADdhqtkNARALVEA 304

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16080143 317 KNGYIIHDFE-NPKQYAERINDLLSSSEKRERLGKYSRREAESNfGWQRVAENLLSV 372
Cdd:COG0707 305 GAAVLIPQSElTPEKLAEALEELLEDPERLAKMAEAARALARPD-AAERIADLILEL 360
 
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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