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Conserved domains on  [gi|1806472910|dbj|BBZ62600|]
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glycosyl transferase family 1 [Mycolicibacterium monacense]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 2-363 4.77e-70

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


The actual alignment was detected with superfamily member cd03822:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 370  Bit Score: 223.80  E-value: 4.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910   2 LSTYAPTPCGVAAFSGALCDGLNELGADVGVVRVAADAGAVAAADSIVdstdPRVVGELADGSAQRCAALLN--RYDVAF 79
Cdd:cd03822     5 LGTLPPRKCGIATYTDDLVEGLRKGGPVVIVVIVSPQDEILKDDDFEV----PNEIKSWNSNEYFRLLDHLNfkKPDVVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  80 IQYQYGIYGGAAGEHVLDILDRLDVPSIVVAHTI--PKAPSVQQRAVLEAIIAKADRVVVISDAAHARLRLSYNVDHDKI 157
Cdd:cd03822    81 IQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVldLSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPAVNI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 158 STIPHGVTLPRG---AAPKRA----GRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRISAEEGQAYr 230
Cdd:cd03822   161 EVIPHGVPEVPQdptTALKRLllpeGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGERY- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 231 qsCVERAQRLGVADSVRFDDCYRSQTALTAIARSAAAVVLPYDSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTGAG 310
Cdd:cd03822   240 --RKAAIEELGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRG 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1806472910 311 IIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLAPTMAWPVVSASYLRLAQ 363
Cdd:cd03822   318 VLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
 
Name Accession Description Interval E-value
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 2-363 4.77e-70

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: 223.80  E-value: 4.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910   2 LSTYAPTPCGVAAFSGALCDGLNELGADVGVVRVAADAGAVAAADSIVdstdPRVVGELADGSAQRCAALLN--RYDVAF 79
Cdd:cd03822     5 LGTLPPRKCGIATYTDDLVEGLRKGGPVVIVVIVSPQDEILKDDDFEV----PNEIKSWNSNEYFRLLDHLNfkKPDVVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  80 IQYQYGIYGGAAGEHVLDILDRLDVPSIVVAHTI--PKAPSVQQRAVLEAIIAKADRVVVISDAAHARLRLSYNVDHDKI 157
Cdd:cd03822    81 IQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVldLSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPAVNI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 158 STIPHGVTLPRG---AAPKRA----GRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRISAEEGQAYr 230
Cdd:cd03822   161 EVIPHGVPEVPQdptTALKRLllpeGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGERY- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 231 qsCVERAQRLGVADSVRFDDCYRSQTALTAIARSAAAVVLPYDSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTGAG 310
Cdd:cd03822   240 --RKAAIEELGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRG 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1806472910 311 IIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLAPTMAWPVVSASYLRLAQ 363
Cdd:cd03822   318 VLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 247-366 1.30e-14

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 69.63  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 247 RFDDCYRSQTALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTG-AGIIVDHDDPAALATAL 325
Cdd:COG0438     3 RLVPRKGLDLLLEALLAAADVFVLP--SRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGeTGLLVPPGDPEALAEAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1806472910 326 RRVLTQPRLAGEMAGEGRRLA-PTMAWPVVSASYLRLAQKML 366
Cdd:COG0438    81 LRLLEDPELRRRLGEAARERAeERFSWEAIAERLLALYEELL 122
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
177-330 9.98e-13

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 64.84  E-value: 9.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 177 RPTLLTWGQIGP-GKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRISaeegqayrqscveRAQRLGVADSVRFddcYRSQ 255
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEEL-------------EELAAGLEDRVIF---TGFV 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806472910 256 TALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTGAGIIVDHDDPAALATALRRVLT 330
Cdd:pfam13692  65 EDLAELLAAADVFVLP--SLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLE 137
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
127-346 3.22e-06

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 48.82  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 127 AIIAKADRVVVISDAAHARLRlSYNVDHDKISTIPHGVTLPRGAAPKR-------------AGRPTLLTWGQIGPGKGIE 193
Cdd:PRK10307  167 SLLRRFDNVSTISRSMMNKAR-EKGVAAEKVIFFPNWSEVARFQPVADadvdalraqlglpDGKKIVLYSGNIGEKQGLE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 194 RVIDAMPSLSDvpgRP--QYLVVGQSdprisaeegqAYRQSCVERAQRLGVADsVRFDDC--YRSQTALTAIA------- 262
Cdd:PRK10307  246 LVIDAARRLRD---RPdlIFVICGQG----------GGKARLEKMAQCRGLPN-VHFLPLqpYDRLPALLKMAdchllpq 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 263 -RSAAAVVLPYDSTdqaasGVLAqavaSGRPVVATAFPHAvEL--LGTGAGIIVDHDDPAALATALRRVLTQPRLAGEMA 339
Cdd:PRK10307  312 kAGAADLVLPSKLT-----NMLA----SGRNVVATAEPGT-ELgqLVEGIGVCVEPESVEALVAAIAALARQALLRPKLG 381


                  ....*..
gi 1806472910 340 GEGRRLA 346
Cdd:PRK10307  382 TVAREYA 388
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 153-332 1.16e-05

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


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 47.23  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 153 DHDKISTIPHGVTLPRgAAPKRAGRPT-----LLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGqsdpriSAEEGQ 227
Cdd:NF038011  278 PPERTRVIPNGIDLPR-LAPLRAQRPAgippvVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVG------PEEEDP 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 228 AYRQSCVERAQRLGVADSVRFDDCYRSQTALTAIarsaAAVVLpyDSTDQAASGVLAQAVASGRPVVATAFPHAVEL--- 304
Cdd:NF038011  351 AYAAECRSLVASLGLQDKVKFLGFQKIDDLLPQV----GLMVL--SSISEALPLVVLEAFAAGVPVVTTDVGSCRQLieg 424

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1806472910 305 -------LGTgAGIIVDHDDPAALATALRRVLTQP 332
Cdd:NF038011  425 ldeedraLGA-AGEVVAIADPQALARAALDLLRDP 458
 
Name Accession Description Interval E-value
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 2-363 4.77e-70

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: 223.80  E-value: 4.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910   2 LSTYAPTPCGVAAFSGALCDGLNELGADVGVVRVAADAGAVAAADSIVdstdPRVVGELADGSAQRCAALLN--RYDVAF 79
Cdd:cd03822     5 LGTLPPRKCGIATYTDDLVEGLRKGGPVVIVVIVSPQDEILKDDDFEV----PNEIKSWNSNEYFRLLDHLNfkKPDVVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  80 IQYQYGIYGGAAGEHVLDILDRLDVPSIVVAHTI--PKAPSVQQRAVLEAIIAKADRVVVISDAAHARLRLSYNVDHDKI 157
Cdd:cd03822    81 IQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVldLSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPAVNI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 158 STIPHGVTLPRG---AAPKRA----GRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRISAEEGQAYr 230
Cdd:cd03822   161 EVIPHGVPEVPQdptTALKRLllpeGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGERY- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 231 qsCVERAQRLGVADSVRFDDCYRSQTALTAIARSAAAVVLPYDSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTGAG 310
Cdd:cd03822   240 --RKAAIEELGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRG 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1806472910 311 IIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLAPTMAWPVVSASYLRLAQ 363
Cdd:cd03822   318 VLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 5-361 6.09e-33

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: 126.11  E-value: 6.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910   5 YAPTPCGVAAFSGALCDGLNELGADV----------GVVRVAADAGAVAAADSIVDSTDPRVVGELadgsaqRCAALLNR 74
Cdd:cd03801     9 LPPPVGGAERHVRELARALAARGHDVtvltpadpgePPEELEDGVIVPLLPSLAALLRARRLLREL------RPLLRLRK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  75 YDVAFIQYQYGIYGGAAGEHvldildRLDVPSIVVAHTIPKAPSVQQRAVLEAIIAK-------ADRVVVISDAAHARLR 147
Cdd:cd03801    83 FDVVHAHGLLAALLAALLAL------LLGAPLVVTLHGAEPGRLLLLLAAERRLLARaeallrrADAVIAVSEALRDELR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 148 LSYNVDHDKISTIPHGVTLPRGAAPKRA------GRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRI 221
Cdd:cd03801   157 ALGGIPPEKIVVIPNGVDLERFSPPLRRklgippDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 222 SAEEgqayrqscverAQRLGVADSVRFDDcYRSQTALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHA 301
Cdd:cd03801   237 AELE-----------ELELGLGDRVRFLG-FVPDEELPALYAAADVFVLP--SRYEGFGLVVLEAMAAGLPVVATDVGGL 302

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806472910 302 VELLGTG-AGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGR-RLAPTMAWPVVSASYLRL 361
Cdd:cd03801   303 PEVVEDGeGGLVVPPDDVEALADALLRLLADPELRARLGRAAReRVAERFSWERVAERLLDL 364
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 54-360 4.52e-21

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: 93.46  E-value: 4.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  54 PRVVGELADGSAQRCAALLNRYDVAFIQYQYGIYGGAAGEHvldildRLDVPSIVVAHTIPK----------APSVQQRA 123
Cdd:cd03800    81 WPYLEEFADGLLRFIAREGGRYDLIHSHYWDSGLVGALLAR------RLGVPLVHTFHSLGRvkyrhlgaqdTYHPSLRI 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 124 VLE-AIIAKADRVVVISDAAHARLRLSYNVDHDKISTIPHGVTLPR-----GAAPKRAG------RPTLLTWGQIGPGKG 191
Cdd:cd03800   155 TAEeQILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDLERffpvdRAEARRARlllppdKPVVLALGRLDPRKG 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 192 IERVIDAMPSLSDVPGRPQYLVVGQSDPRISAEEGQAYRqscvERAQRLGVADSVRFDDcYRSQTALTAIARSAAAVVLP 271
Cdd:cd03800   235 IDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELA----ELAEELGLIDRVRFPG-RVSRDDLPELYRAADVFVVP 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 272 ydSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTG-AGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLAP-TM 349
Cdd:cd03800   310 --SLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGrTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARaHY 387

                         330
                  ....*....|.
gi 1806472910 350 AWPVVSASYLR 360
Cdd:cd03800   388 TWESVADQLLT 398
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 99-351 5.11e-21

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: 92.81  E-value: 5.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  99 LDRLDVPSIVVAHTI---------PKAPSVQQRAVLEAIIAKADRVVVISDAAHARLRLSYNVDHDKISTIPHGV----- 164
Cdd:cd03809    97 LLLKGCPQVVTIHDLiplrypeffPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVdpsff 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 165 ---TLPRGAAPKRAGRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRISAEegqayrqscVERAQRLG 241
Cdd:cd03809   177 ppeSAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEEL---------LDLVKKLG 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 242 VADSVRF----DDCYrsqtaLTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVA---TAFPhavELLGtGAGIIVD 314
Cdd:cd03809   248 LGGRVRFlgyvSDED-----LPALYRGARAFVFP--SLYEGFGLPVLEAMACGTPVIAsniSVLP---EVAG-DAALYFD 316

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1806472910 315 HDDPAALATALRRVLTQPRLAGEMAGEGRRLAPTMAW 351
Cdd:cd03809   317 PLDPESIADAILRLLEDPSLREELIRKGLERAKKFSW 353
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 67-351 1.74e-20

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: 91.26  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  67 RCAALLNRYDVAFIQYQYGIYGGAAgehvLDILDRLDVPSIVVAHTIPkAPSVQQRAVLEAIIAKADRVVVISDAAHARL 146
Cdd:cd03819    67 RLARLIRRERIDLIHAHSRAPAWLG----WLASRLTGVPLVTTVHGSY-LATYHPKDFALAVRARGDRVIAVSELVRDHL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 147 RLSYNVDHDKISTIPHGVTL----PRGAAPKRA------GRPTLLTWGQIGPGKGIERVIDAMPSLSDvpGRPQYLVVGQ 216
Cdd:cd03819   142 IEALGVDPERIRVIPNGVDTdrfpPEAEAEERAqlglpeGKPVVGYVGRLSPEKGWLLLVDAAAELKD--EPDFRLLVAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 217 SDPRisaeegqayRQSCVERAQRLGVADSVRFDDcYRSQtaLTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVAT 296
Cdd:cd03819   220 DGPE---------RDEIRRLVERLGLRDRVTFTG-FRED--VPAALAASDVVVLP--SLHEEFGRVALEAMACGTPVVAT 285

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806472910 297 AFPHAVELLGTGA-GIIVDHDDPAALATALRRVLTQPRLAGEmagEGRRLAPTMAW 351
Cdd:cd03819   286 DVGGAREIVVHGRtGLLVPPGDAEALADAIRAAKLLPEAREK---LQAAAALTEAV 338
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 73-351 7.26e-15

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: 75.11  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  73 NRYDVAFIQYQYGiYGGAAGEHVLdildRLDVPSIVVAHT-----IPKAPSVqqRAVLEAIIAKADRVVVISdAAHARLR 147
Cdd:cd03798    94 GPPDLIHAHFAYP-AGFAAALLAR----LYGVPYVVTEHGsdinvFPPRSLL--RKLLRWALRRAARVIAVS-KALAEEL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 148 LSYNVDHDKISTIPHGVTL----PRGAAP-KRAGRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGqsdpriS 222
Cdd:cd03798   166 VALGVPRDRVDVIPNGVDParfqPEDRGLgLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVG------D 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 223 AEEGQAYRQScverAQRLGVADSVRFDDcYRSQTALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAV 302
Cdd:cd03798   240 GPLREALRAL----AEDLGLGDRVTFTG-RLPHEQVPAYYRACDVFVLP--SRHEGFGLVLLEAMACGLPVVATDVGGIP 312

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1806472910 303 ELLGTG-AGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLAPTMAW 351
Cdd:cd03798   313 EVVGDPeTGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSW 362
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 130-346 1.10e-14

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: 74.69  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 130 AKADRVVVISDAAHARLRLSYnVDHDKISTIPHGVTLPRGAAPKRAGRPTLLTW---------GQIGPGKGIERVIDAMP 200
Cdd:cd03794   162 RLADAIIVLSPGLKEYLLRKG-VPKEKIIVIPNWADLEEFKPPPKDELRKKLGLddkfvvvyaGNIGKAQGLETLLEAAE 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 201 SLSDVPGRpQYLVVGQSDPRisaEEgqayrqscVERAQRLGVADSVRFDDcYRSQTALTAIARSAAAVVLPYDSTDQAAS 280
Cdd:cd03794   241 RLKRRPDI-RFLFVGDGDEK---ER--------LKELAKARGLDNVTFLG-RVPKEEVPELLSAADVGLVPLKDNPANRG 307

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 281 GV---LAQAVASGRPVVATAFPHAVEL-LGTGAGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLA 346
Cdd:cd03794   308 SSpskLFEYMAAGKPILASDDGGSDLAvEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELA 377
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 95-332 1.17e-14

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: 74.32  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  95 VLDILDRLDVPSIVVAHTIPKA--PSVQQRAVLEAIIAKADRVVVISDAAHARLRLSYNVDHDKISTIPHGVTLPR---- 168
Cdd:cd03811    97 IVAKLAAARSKVIAWIHSSLSKlyYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPEKIEVIYNPIDIDRiral 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 169 ---GAAPKRAGRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGqsdprisaeEGQaYRQSCVERAQRLGVADS 245
Cdd:cd03811   177 akePILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG---------DGP-LREELEKLAKELGLAER 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 246 VRF----DDCYRsqtaltaIARSAAAVVLPYDSTdqaasG---VLAQAVASGRPVVATAFPHAVELLGTG-AGIIVDHDD 317
Cdd:cd03811   247 VIFlgfqSNPYP-------YLKKADLFVLSSRYE-----GfpnVLLEAMALGTPVVSTDCPGPREILDDGeNGLLVPDGD 314

                         250
                  ....*....|....*
gi 1806472910 318 PAALATALRRVLTQP 332
Cdd:cd03811   315 AAALAGILAALLQKK 329
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 247-366 1.30e-14

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 69.63  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 247 RFDDCYRSQTALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTG-AGIIVDHDDPAALATAL 325
Cdd:COG0438     3 RLVPRKGLDLLLEALLAAADVFVLP--SRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGeTGLLVPPGDPEALAEAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1806472910 326 RRVLTQPRLAGEMAGEGRRLA-PTMAWPVVSASYLRLAQKML 366
Cdd:COG0438    81 LRLLEDPELRRRLGEAARERAeERFSWEAIAERLLALYEELL 122
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 69-343 4.17e-13

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: 70.06  E-value: 4.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  69 AALLNRYDVAFIQYQYGIYggaAGEHVLDILD-RLDVPS-----IVVAHTIPKApSVQQravleaiiakADRVVVISDaa 142
Cdd:cd03813   190 ALARHRRGIPFLLTEHGIY---TRERKIEILQsTWIMGYikklwIRFFERLGKL-AYQQ----------ADKIISLYE-- 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 143 HARLR-LSYNVDHDKISTIPHGVTLPR-GAAPKRAGRPTLLTWGQIG---PGKGIERVIDAMPSLSDVPGRPQYLVVGQS 217
Cdd:cd03813   254 GNRRRqIRLGADPDKTRVIPNGIDIQRfAPAREERPEKEPPVVGLVGrvvPIKDVKTFIRAFKLVRRAMPDAEGWLIGPE 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 218 DprisaeEGQAYRQSCVERAQRLGVADSVRFD------DCYRSQ--TALTAIARSaaavvLPYdstdqaasgVLAQAVAS 289
Cdd:cd03813   334 D------EDPEYAQECKRLVASLGLENKVKFLgfqnikEYYPKLglLVLTSISEG-----QPL---------VILEAMAS 393

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 290 GRPVVATAFPHAVELLGTG------AGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGR 343
Cdd:cd03813   394 GVPVVATDVGSCRELIYGAddalgqAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGR 453
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
177-330 9.98e-13

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 64.84  E-value: 9.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 177 RPTLLTWGQIGP-GKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRISaeegqayrqscveRAQRLGVADSVRFddcYRSQ 255
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEEL-------------EELAAGLEDRVIF---TGFV 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806472910 256 TALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTGAGIIVDHDDPAALATALRRVLT 330
Cdd:pfam13692  65 EDLAELLAAADVFVLP--SLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLE 137
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 95-339 1.57e-12

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: 68.12  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  95 VLDILDRLDVPsivVAHTIPKAPSVQQRAVLEaiIAKADRVVVISdAAHARLRLSYNVDHDKISTIPHGVTLPRGAAPKR 174
Cdd:cd03823   112 LLDAARDLGIP---VVHTLHDYWLLCPRQFLF--KKGGDAVLAPS-RFTANLHEANGLFSARISVIPNAVEPDLAPPPRR 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 175 AGRPTLLTWGQIG---PGKGIERVIDAMPSLSdvPGRPQYLVVGqsdpriSAEEGQAYRQSCVERAQRLGVADSVRFDDC 251
Cdd:cd03823   186 RPGTERLRFGYIGrltEEKGIDLLVEAFKRLP--REDIELVIAG------HGPLSDERQIEGGRRIAFLGRVPTDDIKDF 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 252 YRSqtaltaiarsAAAVVLPydSTDQAASG-VLAQAVASGRPVVATAFPHAVELLGTGA-GIIVDHDDPAALATALRRVL 329
Cdd:cd03823   258 YEK----------IDVLVVP--SIWPEPFGlVVREAIAAGLPVIASDLGGIAELIQPGVnGLLFAPGDAEDLAAAMRRLL 325

                         250
                  ....*....|
gi 1806472910 330 TQPRLAGEMA 339
Cdd:cd03823   326 TDPALLERLR 335
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 122-329 2.57e-12

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: 67.34  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 122 RAVLEAIIAKADRVVVISDAAHARLRLSYNVDHDKISTIPHGVTLPRGAAPKRAGRPTLLTWGQ------IG------PG 189
Cdd:cd03807   123 VRKLCLLLSKFSPATVANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSPDDASRARARRRLGLaedrrvIGivgrlhPV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 190 KGIERVIDAMPSLsdVPGRPQY--LVVGQSDPRISAEEgqayrqscveRAQRLGVADSVRFDDcYRSQTAltAIARSAAA 267
Cdd:cd03807   203 KDHSDLLRAAALL--VETHPDLrlLLVGRGPERPNLER----------LLLELGLEDRVHLLG-ERSDVP--ALLPAMDI 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806472910 268 VVLPydSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTGAGIIVDHDDPAALATALRRVL 329
Cdd:cd03807   268 FVLS--SRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGTGFLVPAGDPQALADAIRALL 327
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 176-344 9.65e-12

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: 62.68  E-value: 9.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 176 GRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGqsdprisaeeGQAYRQSCVERAQRLGVADSVRFDDcYRSQ 255
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG----------DGEEEKRLKKLAEKLGLGDNVIFLG-FVSD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 256 TALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTG-AGIIVDHDDPAALATALRRVLTQPRL 334
Cdd:pfam00534  70 EDLPELLKIADVFVLP--SRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGeTGFLVKPNNAEALAEAIDKLLEDEEL 147

                         170
                  ....*....|
gi 1806472910 335 AGEMAGEGRR 344
Cdd:pfam00534 148 RERLGENARK 157
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 156-359 1.32e-09

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: 59.30  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 156 KISTIPHGVTLP--------RGAAPKRAGRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDPrisaeEGQ 227
Cdd:cd03821   175 PIAVIPNGVDIPefdpglrdRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDG-----AYP 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 228 AYRQScverAQRLGVADSVRFDD-CYrsQTALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAVELLG 306
Cdd:cd03821   250 AFLQL----QSSLGLGDRVTFTGpLY--GEAKWALYASADLFVLP--SYSENFGNVVAEALACGLPVVITDKCGLSELVE 321

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806472910 307 TGAGIIVDhDDPAALATALRRVL---TQPRLAGEMAGEGRRLAPTMAWPVVSASYL 359
Cdd:cd03821   322 AGCGVVVD-PNVSSLAEALAEALrdpADRKRLGEMARRARQVEENFSWEAVAGQLG 376
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 4-343 1.67e-09

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: 58.83  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910   4 TYAPTPCGVAAFSGALCDGLNELGADV------GVVRVAADAGAVAAADSIVDSTDPRVVGELADGSAQRCAALLNRYDV 77
Cdd:cd03817     8 TYLPQVNGVATSVRNLARALEKRGHEVyvitpsDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRIKELGPDI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  78 AFIQYQYGIyGGAAgehvLDILDRLDVPSIVVAHT--------IPKAPSVqQRAVLEAIIAK----ADRVVVISDAAHAR 145
Cdd:cd03817    88 IHTHTPFSL-GKLG----LRIARKLKIPIVHTYHTmyedylhyIPKGKLL-VKAVVRKLVRRfynhTDAVIAPSEKIKDT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 146 LRlSYNVDhDKISTIPHGVTL----------PRGAAPKRAGRPTLLTWGQIGPGKGIERVIDAMPSLSDVPGrPQYLVVG 215
Cdd:cd03817   162 LR-EYGVK-GPIEVIPNGIDLdkfekplnteERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN-IKLVIVG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 216 qsdprisaeEGqAYRQSCVERAQRLGVADSVRFDDcYRSQTALTAIARSAAAVVLPYDSTDQAAsgVLAQAVASGRPVVA 295
Cdd:cd03817   239 ---------DG-PEREELKELARELGLADKVIFTG-FVPREELPEYYKAADLFVFASTTETQGL--VYLEAMAAGLPVVA 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1806472910 296 TAFPHAVELLGTG-AGIIVDhDDPAALATALRRVLTQPRLAGEMAGEGR 343
Cdd:cd03817   306 AKDPAASELVEDGeNGFLFE-PNDETLAEKLLHLRENLELLRKLSKNAE 353
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 3-354 1.67e-09

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: 58.84  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910   3 STYAPTPCGVAAFSGALCDGLNELGADVGVVRVAADAGAVAAADSIVDSTDPRVVG----ELADGSAQRCAALLNRYDVA 78
Cdd:cd03814     7 DTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFPLPFypeyRLALPLPRRVRRLIKEFQPD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  79 FIQYQY-GIYGGAAgehvLDILDRLDVPSIVVAHT-IPKAPSVQQRAVLEAIIAK--------ADRVVVISDAAHARLRl 148
Cdd:cd03814    87 IIHIATpGPLGLAA----LRAARRLGLPVVTSYHTdFPEYLSYYTLGPLSWLAWAylrwfhnpFDTTLVPSPSIARELE- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 149 synvDHD--KISTIPHGVTL------PRGAAPKRA----GRPTLLTWGQIGPGKGIERVIDAMPSLSDVPgRPQYLVVGq 216
Cdd:cd03814   162 ----GHGfeRVRLWPRGVDTelfhpsRRDAALRRRlgppGRPLLLYVGRLAPEKNLEALLDADLPLAASP-PVRLVVVG- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 217 sDPRISAEEGQAYRQscverAQRLGvadsvrfddcYRSQTALTAIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVAT 296
Cdd:cd03814   236 -DGPARAELEARGPD-----VIFTG----------FLTGEELARAYASADVFVFP--SRTETFGLVVLEAMASGLPVVAA 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1806472910 297 AFPHAVELLG-TGAGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLAPTMAWPVV 354
Cdd:cd03814   298 DAGGPRDIVRpGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAF 356
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 89-346 1.98e-09

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: 58.62  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  89 GAAGEHVLDILDRLDVPSIVVAH------------TIPKAPSVQQRaVLEAIIAKADRVVVISDAAHARLrLSYNVDHDK 156
Cdd:cd05844    90 GRDGVYALPLARALGVPLVVTFHgfdittsrawlaASPGWPSQFQR-HRRALQRPAALFVAVSGFIRDRL-LARGLPAER 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 157 ISTIPHGVTLPRGAAPKRAGR-PTLLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSdPRISAEEGQAYRqscve 235
Cdd:cd05844   168 IHVHYIGIDPAKFAPRDPAERaPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDG-PLRPALQALAAA----- 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 236 raqrlgvADSVRFDDCYrSQTALTAIARSAAAVVLPydsTDQAASG-------VLAQAVASGRPVVATAFPHAVELLGTG 308
Cdd:cd05844   242 -------LGRVRFLGAL-PHAEVQDWMRRAEIFCLP---SVTAASGdseglgiVLLEAAACGVPVVSSRHGGIPEAILDG 310

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1806472910 309 -AGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLA 346
Cdd:cd05844   311 eTGFLVPEGDVDALADALQALLADRALADRMGGAARAFV 349
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 102-346 4.10e-08

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: 54.55  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 102 LDVPSIVVAHTIPKA--PSVQQRAVLEAIIAKADRVVVISdaaHARLRLSYNVDHDKISTIPHGVTLPRGAAPKRAGRPT 179
Cdd:cd03820   107 LKSKLIVWEHNNYEAynKGLRRLLLRRLLYKRADKIVVLT---EADKLKKYKQPNSNVVVIPNPLSFPSEEPSTNLKSKR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 180 LLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGqsdpriSAEEGQAYRQscveRAQRLGVADSVRFddcYRSQTALT 259
Cdd:cd03820   184 ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG------DGPEREELEK----LIDKLGLEDRVKL---LGPTKNIA 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 260 AIARSAAAVVLPydSTDQAASGVLAQAVASGRPVVATAFPHAV-ELLGTGA-GIIVDHDDPAALATALRRVLTQPRLAGE 337
Cdd:cd03820   251 EEYANSSIFVLS--SRYEGFPMVLLEAMAYGLPIISFDCPTGPsEIIEDGEnGLLVPNGDVDALAEALLRLMEDEELRKK 328


                  ....*....
gi 1806472910 338 MAGEGRRLA 346
Cdd:cd03820   329 MGKNARKNA 337
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 77-305 1.03e-07

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: 52.41  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  77 VAFIQYQYGIYGGAAGEHVLDILDRLDVPSIVVaHTIPKAPSVQQRAVLEAIIAKADRVVVIS--DAAHARLRLSYNVDH 154
Cdd:cd01635     1 ILLVTGEYPPLRGGLELHVRALARALAALGHEV-TVLALLLLALRRILKKLLELKPDVVHAHSphAAALAALLAARLLGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 155 dKISTIPHG---VTLPRGAAPKRAGRPTLLTW------GQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDPRiSAEE 225
Cdd:cd01635    80 -PIVVTVHGpdsLESTRSELLALARLLVSLPLadkvsvGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGER-EEEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 226 GQAYRQSCVERAQRLGVADSVRFDDCYRsqtaltaiaRSAAAVVLPYDSTDQaaSGVLAQAVASGRPVVATAFPHAVELL 305
Cdd:cd01635   158 ALAAALGLLERVVIIGGLVDDEVLELLL---------AAADVFVLPSRSEGF--GLVLLEAMAAGKPVIATDVGGIPEFV 226
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
11-164 3.45e-07

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 49.84  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  11 GVAAFSGALCDGLNELGADV------GVVRVAADAGAVAAADSIVDSTDPRVVGELADGSAQRCAALLNRYDVafIQYQY 84
Cdd:pfam13439   2 GVERYVLELARALARRGHEVtvvtpgGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDV--VHAHS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910  85 GIYGGAAGehvLDILDRLDVPSIVVAHT----------IPKAPSVQQRAVLEAIIAKADRVVVISDAAHARLRLSYNVDH 154
Cdd:pfam13439  80 PFPLGLAA---LAARLRLGIPLVVTYHGlfpdykrlgaRLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPP 156

                         170
                  ....*....|
gi 1806472910 155 DKISTIPHGV 164
Cdd:pfam13439 157 EKIRVIPNGV 166
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 135-346 4.03e-07

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: 51.56  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 135 VVVISDAAHARLRLSYNVDHDKISTIPHGV------TLPRGAAPKRAGRPT---LLTWGQIG---PGKGIERVIDAMPSL 202
Cdd:cd03825   141 IVAPSRWLADMVRRSPLLKGLPVVVIPNGIdteifaPVDKAKARKRLGIPQdkkVILFGAESvtkPRKGFDELIEALKLL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 203 SDVPgRPQYLVVGQSDPRISAEEGQAYRqscveraqrLGVADSVRfddcyrsqtaLTAIARSAAAV-VLPydSTDQAASG 281
Cdd:cd03825   221 ATKD-DLLLVVFGKNDPQIVILPFDIIS---------LGYIDDDE----------QLVDIYSAADLfVHP--SLADNLPN 278

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806472910 282 VLAQAVASGRPVVATAFPHAVELLGTG-AGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLA 346
Cdd:cd03825   279 TLLEAMACGTPVVAFDTGGSPEIVQHGvTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALA 344
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
127-346 3.22e-06

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 48.82  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 127 AIIAKADRVVVISDAAHARLRlSYNVDHDKISTIPHGVTLPRGAAPKR-------------AGRPTLLTWGQIGPGKGIE 193
Cdd:PRK10307  167 SLLRRFDNVSTISRSMMNKAR-EKGVAAEKVIFFPNWSEVARFQPVADadvdalraqlglpDGKKIVLYSGNIGEKQGLE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 194 RVIDAMPSLSDvpgRP--QYLVVGQSdprisaeegqAYRQSCVERAQRLGVADsVRFDDC--YRSQTALTAIA------- 262
Cdd:PRK10307  246 LVIDAARRLRD---RPdlIFVICGQG----------GGKARLEKMAQCRGLPN-VHFLPLqpYDRLPALLKMAdchllpq 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 263 -RSAAAVVLPYDSTdqaasGVLAqavaSGRPVVATAFPHAvEL--LGTGAGIIVDHDDPAALATALRRVLTQPRLAGEMA 339
Cdd:PRK10307  312 kAGAADLVLPSKLT-----NMLA----SGRNVVATAEPGT-ELgqLVEGIGVCVEPESVEALVAAIAALARQALLRPKLG 381


                  ....*..
gi 1806472910 340 GEGRRLA 346
Cdd:PRK10307  382 TVAREYA 388
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 153-332 1.16e-05

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


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 47.23  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 153 DHDKISTIPHGVTLPRgAAPKRAGRPT-----LLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGqsdpriSAEEGQ 227
Cdd:NF038011  278 PPERTRVIPNGIDLPR-LAPLRAQRPAgippvVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVG------PEEEDP 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 228 AYRQSCVERAQRLGVADSVRFDDCYRSQTALTAIarsaAAVVLpyDSTDQAASGVLAQAVASGRPVVATAFPHAVEL--- 304
Cdd:NF038011  351 AYAAECRSLVASLGLQDKVKFLGFQKIDDLLPQV----GLMVL--SSISEALPLVVLEAFAAGVPVVTTDVGSCRQLieg 424

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1806472910 305 -------LGTgAGIIVDHDDPAALATALRRVLTQP 332
Cdd:NF038011  425 ldeedraLGA-AGEVVAIADPQALARAALDLLRDP 458
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 154-344 2.81e-05

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: 45.82  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 154 HDKISTIPHGVTLPRgAAPKRAGRPTLLTWGQIGPG--------------KGIERVIDAMPSLSDVpgRPQYLVV----- 214
Cdd:cd03818   178 RDRISVIHDGVDTDR-LAPDPAARLRLLNGTELKAGdpvityvarnlepyRGFHVFMRALPRIQAR--RPDARVVvvggd 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 215 ----GQSDPRISAEEGQAYRQSCVERaQRLGVADSVRFDdcyrsqTALTAIARSAAAVVLPYDStdqAASGVLAQAVASG 290
Cdd:cd03818   255 gvsyGSPPPDGGSWKQKMLAELGVDL-ERVHFVGKVPYD------QYVRLLQLSDAHVYLTYPF---VLSWSLLEAMACG 324

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1806472910 291 RPVVATAFPHAVELLGTGA-GIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRR 344
Cdd:cd03818   325 CPVIGSDTAPVREVIRDGRnGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARR 379
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 173-344 5.18e-04

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: 41.49  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 173 KRAGRPTLLTWGQIGPGKGIERVIDAMPSLsdvpgRPQYLVVGqsdprisaeEG--QAYRQSCVEraqrLGVADSVRF-- 248
Cdd:cd03795   187 EKKGKKIFLFIGRLVYYKGLDYLIEAAQYL-----NYPIVIGG---------EGplKPDLEAQIE----LNLLDNVKFlg 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 249 --DDCYRSqTALTAiarsAAAVVLPYDSTDQAASGVLAQAVASGRPVVATAfphavelLGTG---------AGIIVDHDD 317
Cdd:cd03795   249 rvDDEEKV-IYLHL----CDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTN-------IGTGvpyvnnngeTGLVVPPKD 316

                         170       180
                  ....*....|....*....|....*..
gi 1806472910 318 PAALATALRRVLTQPRLAGEMAGEGRR 344
Cdd:cd03795   317 PDALAEAIDKLLSDEELRESYGENAKK 343
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
 288-368 7.60e-04

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 41.20  E-value: 7.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 288 ASGRPVVATAFPHAVELLGtgaGIIVDHDDPAALATALRRVLTQPRlagemAGEGRRLAPTMAwpvVSASYLRLAQKMLT 367
Cdd:cd04950   299 AAGKPVVATSIPSVVRFYG---EAVLCGDDPDEFSAAIEKALALKG-----DARDKRLARALA---RQESWDERARAMEE 367


                  .
gi 1806472910 368 G 368
Cdd:cd04950   368 A 368
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 282-346 1.16e-03

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: 40.66  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806472910 282 VLAQAVASGRPVVATAFPHAVELL--GTGaGIIVDHDDPAALATALRRVLTQPRLAGEMAGEGRRLA 346
Cdd:cd03808   279 SLLEAMAAGRPVITTDVPGCRELVidGVN-GFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRV 344
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 180-343 4.30e-03

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: 38.59  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 180 LLTWGQIGPGKGIERVIDAMPSLSDVPGRPQYLVVGQSDprisaeegqaYRQSCVERAQRLGVADSVRFDDcYRSQTALT 259
Cdd:cd03799   177 ILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGD----------LKEQLQQLIQELNIGDCVKLLG-WKPQEEII 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806472910 260 AIARSAAAVVLPY----DSTDQAASGVLAQAVASGRPVVATAFPHAVELLGTG-AGIIVDHDDPAALATALRRVLTQPRL 334
Cdd:cd03799   246 EILDEADIFIAPSvtaaDGDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGvSGFLVPERDAEAIAEKLTYLIEHPAI 325


                  ....*....
gi 1806472910 335 AGEMAGEGR 343
Cdd:cd03799   326 WPEMGKAGR 334
 
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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