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Conserved domains on  [gi|1538964748|gb|AZP39043|]
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glycosyltransferase [Acidipropionibacterium acidipropionici]

Protein Classification

glycosyltransferase( domain architecture ID 11660203)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

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
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 170-388 7.07e-28

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 cd03808:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 358  Bit Score: 113.46  E-value: 7.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 170 IRQVRELCRTIEPTVVHAHSSFAGLYVRVAS---GRVPVVYTPHCFGFERTDLPHSARGALWaIERVLALRTAEVAACSP 246
Cdd:cd03808    70 LFKLYKLLKKEKPDIVHCHTPKPGILGRLAArlaGVPKVIYTVHGLGFVFTEGKLLRLLYLL-LEKLALLFTDKVIFVNE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 247 REAQLARRM----VRNVTSVPNVGRfeGLDL-KHSTRGSAGRVPKVTFMGRISAQKDPKFAAETVREFRELHVgQVDFEW 321
Cdd:cd03808   149 DDRDLAIKKgiikKKKTVLIPGSGV--DLDRfQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGP-NVRFLL 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538964748 322 IGDGPQE--ACAALKRAG----IRVTGWLSgeQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIP 388
Cdd:cd03808   226 VGDGELEnpSEILIEKLGlegrIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVP 296
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 353-449 5.63e-06

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


:

Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 45.37  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 353 LSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPALNQMPRDYLGG------DPETVAAIIARAIASTGELNRCAAR- 425
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGllvppgDPEALAEAILRLLEDPELRRRLGEAa 97

                          90       100
                  ....*....|....*....|....
gi 1538964748 426 WSDALAANTRDNQRDALLAVYARA 449
Cdd:COG0438    98 RERAEERFSWEAIAERLLALYEEL 121
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 170-388 7.07e-28

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: 113.46  E-value: 7.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 170 IRQVRELCRTIEPTVVHAHSSFAGLYVRVAS---GRVPVVYTPHCFGFERTDLPHSARGALWaIERVLALRTAEVAACSP 246
Cdd:cd03808    70 LFKLYKLLKKEKPDIVHCHTPKPGILGRLAArlaGVPKVIYTVHGLGFVFTEGKLLRLLYLL-LEKLALLFTDKVIFVNE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 247 REAQLARRM----VRNVTSVPNVGRfeGLDL-KHSTRGSAGRVPKVTFMGRISAQKDPKFAAETVREFRELHVgQVDFEW 321
Cdd:cd03808   149 DDRDLAIKKgiikKKKTVLIPGSGV--DLDRfQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGP-NVRFLL 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538964748 322 IGDGPQE--ACAALKRAG----IRVTGWLSgeQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIP 388
Cdd:cd03808   226 VGDGELEnpSEILIEKLGlegrIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVP 296
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 285-399 3.28e-14

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: 70.00  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 285 PKVTFMGRISAQKDPKFAAETVREFRELHVGQVdFEWIGDGPQEAC------AALKRAGIRVTGWLSGEQVTEELSGSSV 358
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLK-LVIAGDGEEEKRlkklaeKLGLGDNVIFLGFVSDEDLPELLKIADV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1538964748 359 YVHAAAWEGFPMAVLEASQLGLPIVARAIPalnqMPRDYLG 399
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVG----GPPEVVK 118
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 353-449 5.63e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 45.37  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 353 LSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPALNQMPRDYLGG------DPETVAAIIARAIASTGELNRCAAR- 425
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGllvppgDPEALAEAILRLLEDPELRRRLGEAa 97

                          90       100
                  ....*....|....*....|....
gi 1538964748 426 WSDALAANTRDNQRDALLAVYARA 449
Cdd:COG0438    98 RERAEERFSWEAIAERLLALYEEL 121
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 170-388 7.07e-28

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: 113.46  E-value: 7.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 170 IRQVRELCRTIEPTVVHAHSSFAGLYVRVAS---GRVPVVYTPHCFGFERTDLPHSARGALWaIERVLALRTAEVAACSP 246
Cdd:cd03808    70 LFKLYKLLKKEKPDIVHCHTPKPGILGRLAArlaGVPKVIYTVHGLGFVFTEGKLLRLLYLL-LEKLALLFTDKVIFVNE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 247 REAQLARRM----VRNVTSVPNVGRfeGLDL-KHSTRGSAGRVPKVTFMGRISAQKDPKFAAETVREFRELHVgQVDFEW 321
Cdd:cd03808   149 DDRDLAIKKgiikKKKTVLIPGSGV--DLDRfQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGP-NVRFLL 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538964748 322 IGDGPQE--ACAALKRAG----IRVTGWLSgeQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIP 388
Cdd:cd03808   226 VGDGELEnpSEILIEKLGlegrIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVP 296
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 139-390 4.57e-21

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: 94.14  E-value: 4.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 139 HIVVGAYRGEPLPENPDGYRFIAMVDGQLAR-----IRQVRELCRTIEPTVVHAHSSFAGLYVRVA--SGRVPVVYTPHC 211
Cdd:cd03801    35 TVLTPADPGEPPEELEDGVIVPLLPSLAALLrarrlLRELRPLLRLRKFDVVHAHGLLAALLAALLalLLGAPLVVTLHG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 212 FGFERTDLPHSARgaLWAIERVLAL--RTAEVAACSPREAQLARRM----VRNVTSVPNvgrfeGLDLKH------STRG 279
Cdd:cd03801   115 AEPGRLLLLLAAE--RRLLARAEALlrRADAVIAVSEALRDELRALggipPEKIVVIPN-----GVDLERfspplrRKLG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 280 SAGRVPKVTFMGRISAQKDPKFAAETVREFRELHVgqvDFEWI---GDGPQEACAALKRAG----IRVTGWLSGEQVTEE 352
Cdd:cd03801   188 IPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP---DVRLVivgGDGPLRAELEELELGlgdrVRFLGFVPDEELPAL 264

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1538964748 353 LSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPAL 390
Cdd:cd03801   265 YAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGL 302
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 167-400 5.51e-16

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: 78.94  E-value: 5.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 167 LARIRQVRELCRTIEPTVVHAHSSFAGLYVR-VASGRVPVVYTPHCFGFERTDLPhsargALWAIERVLALRTAEVAACS 245
Cdd:cd03811    69 LKAILKLKRILKRAKPDVVISFLGFATYIVAkLAAARSKVIAWIHSSLSKLYYLK-----KKLLLKLKLYKKADKIVCVS 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 246 PREAQLARR----MVRNVTSVPN---VGRFEGLDLKHSTRGSAGRvPKVTFMGRISAQKDPKFAAETVREFRElHVGQVD 318
Cdd:cd03811   144 KGIKEDLIRlgpsPPEKIEVIYNpidIDRIRALAKEPILNEPEDG-PVILAVGRLDPQKGHDLLIEAFAKLRK-KYPDVK 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 319 FEWIGDGPQ-EACAAL-KRAGI--RV--TGWLSgeQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPALNQ 392
Cdd:cd03811   222 LVILGDGPLrEELEKLaKELGLaeRVifLGFQS--NPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPRE 299


                  ....*...
gi 1538964748 393 MPRDYLGG 400
Cdd:cd03811   300 ILDDGENG 307
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 167-456 2.50e-14

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: 74.34  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 167 LARIRQVRELCRTIEPTVVHAHSSFAGLYVRVASGR---VPVVYTPHCfgferTD-LPHSARGALWAIERVLALRTAEVA 242
Cdd:cd03798    81 APSLAKLLKRRRRGPPDLIHAHFAYPAGFAAALLARlygVPYVVTEHG-----SDiNVFPPRSLLRKLLRWALRRAARVI 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 243 ACSPReaqLARRMVR------NVTSVPN---VGRFEGLDlkhSTRGSAGRVPKVTFMGRISAQKDPKFAAETV-REFREL 312
Cdd:cd03798   156 AVSKA---LAEELVAlgvprdRVDVIPNgvdPARFQPED---RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFaRLAKAR 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 313 HVgqVDFEWIGDGPQ-EACAAL-----KRAGIRVTGWLSGEQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARA 386
Cdd:cd03798   230 PD--VVLLIVGDGPLrEALRALaedlgLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATD 307

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 387 IpalnqmprdylGGDPETVAAIIaraiasTGELnrCAARWSDALAANTRDNQRDALLAVYARAAGRNAQE 456
Cdd:cd03798   308 V-----------GGIPEVVGDPE------TGLL--VPPGDADALAAALRRALAEPYLRELGEAARARVAE 358
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 285-399 3.28e-14

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: 70.00  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 285 PKVTFMGRISAQKDPKFAAETVREFRELHVGQVdFEWIGDGPQEAC------AALKRAGIRVTGWLSGEQVTEELSGSSV 358
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLK-LVIAGDGEEEKRlkklaeKLGLGDNVIFLGFVSDEDLPELLKIADV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1538964748 359 YVHAAAWEGFPMAVLEASQLGLPIVARAIPalnqMPRDYLG 399
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVG----GPPEVVK 118
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
285-390 1.66e-13

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 67.54  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 285 PKVTFMGRISA-QKDPKFAAETVREFRElHVGQVDFEWIGDGPQEACAALKRA---GIRVTGWLsgEQVTEELSGSSVYV 360
Cdd:pfam13692   2 PVILFVGRLHPnVKGVDYLLEAVPLLRK-RDNDVRLVIVGDGPEEELEELAAGledRVIFTGFV--EDLAELLAAADVFV 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1538964748 361 HAAAWEGFPMAVLEASQLGLPIVARAIPAL 390
Cdd:pfam13692  79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGI 108
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 167-400 2.02e-13

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: 69.74  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 167 LARIRQVRELCRTIEPTVVHAHSSFAGLYVRV---ASGRVPVVYTPHCFGFERTDLPHSARgalWAIERVLALRTAEVaa 243
Cdd:cd01635    40 LLALRRILKKLLELKPDVVHAHSPHAAALAALlaaRLLGIPIVVTVHGPDSLESTRSELLA---LARLLVSLPLADKV-- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 244 cspreaqlarrmvrnvtsvpnvgrfegldlkhstrgsagrvpkvtFMGRISAQKDPKFAAETVREFRELHVGQVdFEWIG 323
Cdd:cd01635   115 ---------------------------------------------SVGRLVPEKGIDLLLEALALLKARLPDLV-LVLVG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 324 DGP----QEACAALKRAGIRV--TGWLSGEQVTEELS-GSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPALNQMPRD 396
Cdd:cd01635   149 GGGereeEEALAAALGLLERVviIGGLVDDEVLELLLaAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228


                  ....
gi 1538964748 397 YLGG 400
Cdd:cd01635   229 GENG 232
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 170-390 7.46e-13

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: 69.31  E-value: 7.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 170 IRQVRELCRTIEPTVVHAHSSFAGLYVRVASG--RVPVVYTPHCFGFERTDLPHSARGALWAIERVLAL------RTAEV 241
Cdd:cd03819    65 NVRLARLIRRERIDLIHAHSRAPAWLGWLASRltGVPLVTTVHGSYLATYHPKDFALAVRARGDRVIAVselvrdHLIEA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 242 AACSPREAQLARRMVrnvtsvpNVGRF--EGLDLKHSTRGSAGRVPKVTFMGRISAQKDPKFAAETVREFRElhvgQVDF 319
Cdd:cd03819   145 LGVDPERIRVIPNGV-------DTDRFppEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKD----EPDF 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1538964748 320 EW--IGDGPQE------ACAALKRAGIRVTGWLsgEQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPAL 390
Cdd:cd03819   214 RLlvAGDGPERdeirrlVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA 290
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 139-385 1.99e-12

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: 68.46  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 139 HIVVGAYRGEPLPENPDGYRFIAMVDGQLARIR----QVRELCRTI---EPTVVHAHSSFA--GLYVRVASG-RVPVVYT 208
Cdd:cd03817    35 YVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHipfpFKKAVIDRIkelGPDIIHTHTPFSlgKLGLRIARKlKIPIVHT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 209 PHcfgferT----DLPHSARGALWA------IERVLALRTAEVAACSPREAQLARR--MVRNVTSVPNvgrfeGLDLKH- 275
Cdd:cd03817   115 YH------TmyedYLHYIPKGKLLVkavvrkLVRRFYNHTDAVIAPSEKIKDTLREygVKGPIEVIPN-----GIDLDKf 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 276 ---------STRGSAGRVPKVTFMGRISAQKDPKFAAETVREFRELHVGQVDFewIGDGPQ----EACAALKRAGIRV-- 340
Cdd:cd03817   184 ekplnteerRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPNIKLVI--VGDGPEreelKELARELGLADKVif 261

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1538964748 341 TGWLSGEQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVAR 385
Cdd:cd03817   262 TGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAA 306
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 132-452 5.43e-10

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: 60.79  E-value: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 132 RSTPMIEHIVVGAY-----RGEPLPENPDGYRFIAMVDGQ-LARIRQVRELCRTIEPTVVHAHSSFAGLYVRVAS---GR 202
Cdd:cd03807    24 HMDKSRFEHVVISLtgdgvLGEELLAAGVPVVCLGLSSGKdPGVLLRLAKLIRKRNPDVVHTWMYHADLIGGLAAklaGG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 203 VPVVYTPHCfgfeRTDLPHSARGALWaIERVLALRTAEVAACSPREAQLARRM---VRNVTSVPN---VGRF----EGLD 272
Cdd:cd03807   104 VKVIWSVRS----SNIPQRLTRLVRK-LCLLLSKFSPATVANSSAVAEFHQEQgyaKNKIVVIYNgidLFKLspddASRA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 273 LKHSTRGSAGRVPKVTFMGRISAQKDpkfAAETVREFREL--HVGQVDFEWIGDGPQEACAA--LKRAGIRVTGWLSGEQ 348
Cdd:cd03807   179 RARRRLGLAEDRRVIGIVGRLHPVKD---HSDLLRAAALLveTHPDLRLLLVGRGPERPNLErlLLELGLEDRVHLLGER 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 349 --VTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIpalnqmprdylGGDPETVAAIiaraiasTGELnrCAARW 426
Cdd:cd03807   256 sdVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDV-----------GGAAELVDDG-------TGFL--VPAGD 315

                         330       340
                  ....*....|....*....|....*.
gi 1538964748 427 SDALAantrdnqrDALLAVYARAAGR 452
Cdd:cd03807   316 PQALA--------DAIRALLEDPEKR 333
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
139-264 1.68e-09

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 56.64  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 139 HIVVGAYRGEPLPENPDGYRFIA-------MVDGQLARIRQVRELCRTIEPTVVHAHSSFAGLYVRVASGR--VPVVYTP 209
Cdd:pfam13579  22 RVVTPGGPPGRPELVGDGVRVHRlpvpprpSPLADLAALRRLRRLLRAERPDVVHAHSPTAGLAARLARRRrgVPLVVTV 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1538964748 210 HCFGFERTDlpHSARGALWAIERVLALRTAEVAACSPREAQLARRMV---RNVTSVPN 264
Cdd:pfam13579 102 HGLALDYGS--GWKRRLARALERRLLRRADAVVVVSEAEAELLRALGvpaARVVVVPN 157
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 181-383 5.28e-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: 57.76  E-value: 5.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 181 EPTVVHAHSSFAGLYVRVA----SGRVPVVYTPHcfgferTDLPHSARG---ALWAIERVLALRTA-EVAACSPREAQLA 252
Cdd:cd03821    90 EYDVVHIHGVWTYTSLAACklarRRGIPYVVSPH------GMLDPWALQqkhWKKRIALHLIERRNlNNAALVHFTSEQE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 253 RRMVR--NVTS----VPN---VGRFEGLDLKHSTRGSAGRVPKVTFMGRISAQKDPKFAAETVREFRELHVGqVDFEWIG 323
Cdd:cd03821   164 ADELRrfGLEPpiavIPNgvdIPEFDPGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRD-WHLVIAG 242

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538964748 324 DGPQEACAALK---RAGI--RVT--GWLSGEQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIV 383
Cdd:cd03821   243 PDDGAYPAFLQlqsSLGLgdRVTftGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVV 309
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 146-450 5.71e-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: 57.69  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 146 RGEPLPENPdGYRFIamvdgqLARIRQVRELCRTIEPTVVHAHSSF-AGLYVRVASGR--VPVVYTPHcfgferTDLPH- 221
Cdd:cd03814    56 PSFPLPFYP-EYRLA------LPLPRRVRRLIKEFQPDIIHIATPGpLGLAALRAARRlgLPVVTSYH------TDFPEy 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 222 -SARGALWAIERVLA-LRT------AEVAACSPREAQLARRMVRNVTSVP---NVGRF-----EGLDLKHstRGSAGRvP 285
Cdd:cd03814   123 lSYYTLGPLSWLAWAyLRWfhnpfdTTLVPSPSIARELEGHGFERVRLWPrgvDTELFhpsrrDAALRRR--LGPPGR-P 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 286 KVTFMGRISAQKDPKFAAETVREFRELHvgQVDFEWIGDGPQEAcaALKRAGIRV--TGWLSGEQVTEELSGSSVYVHAA 363
Cdd:cd03814   200 LLLYVGRLAPEKNLEALLDADLPLAASP--PVRLVVVGDGPARA--ELEARGPDVifTGFLTGEELARAYASADVFVFPS 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 364 AWEGFPMAVLEASQLGLPIVARAIPAlnqmPRDYLGGDPetvaaiiaraiasTGEL--NRCAARWSDALAANTRDNQRDA 441
Cdd:cd03814   276 RTETFGLVVLEAMASGLPVVAADAGG----PRDIVRPGG-------------TGALvePGDAAAFAAALRALLEDPELRR 338


                  ....*....
gi 1538964748 442 LLAVYARAA 450
Cdd:cd03814   339 RMAARARAE 347
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
99-264 6.93e-09

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 54.85  E-value: 6.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748  99 GGAEMTdsqrrprVLHVAECFAA-GVRTAMLEYIRSTPMIEHIVVGAYRGEPLPENPDGYRFIamvdgqLARIRQVRELC 177
Cdd:pfam13439   1 GGVERY-------VLELARALARrGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRS------LAFLRRLRRLL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 178 RTIEPTVVHAHSSFAGLYVRVA---SGRVPVVYTPHCFGFERTDLPHS---ARGALWAIERVLALRTAEVAACSPREAQL 251
Cdd:pfam13439  68 RRERPDVVHAHSPFPLGLAALAarlRLGIPLVVTYHGLFPDYKRLGARlspLRRLLRRLERRLLRRADRVIAVSEAVADE 147

                         170
                  ....*....|....*..
gi 1538964748 252 ARRMV----RNVTSVPN 264
Cdd:pfam13439 148 LRRLYgvppEKIRVIPN 164
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 286-396 1.51e-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: 56.09  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 286 KVTFMGRISAQKDPKFAAETVREFRELHVgqvDFEW--IGDGPQEAC--AALKRAGI--RVTgwLSG--EQVTEELSGSS 357
Cdd:cd03820   183 RILAVGRLTYQKGFDLLIEAWALIAKKHP---DWKLriYGDGPEREEleKLIDKLGLedRVK--LLGptKNIAEEYANSS 257

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1538964748 358 VYVHAAAWEGFPMAVLEASQLGLPIVARAIPAlnqMPRD 396
Cdd:cd03820   258 IFVLSSRYEGFPMVLLEAMAYGLPIISFDCPT---GPSE 293
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 166-386 9.33e-08

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: 54.00  E-value: 9.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 166 QLARIRQVRELCRTIEPTVVHAHSSFAGLYVRVASGR--VPVVYTPHcfGFERTDLPH--SARGALWAI----ERVLALR 237
Cdd:cd05844    66 LLGWSAPRLGGAAGLAPALVHAHFGRDGVYALPLARAlgVPLVVTFH--GFDITTSRAwlAASPGWPSQfqrhRRALQRP 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 238 TAEVAACSP--REAQLARRMVRNVTSVpnvgRFEGLDL-KHSTRGSAGRVPKVTFMGRISAQKDPKFAAETVREFRELHv 314
Cdd:cd05844   144 AALFVAVSGfiRDRLLARGLPAERIHV----HYIGIDPaKFAPRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARH- 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 315 GQVDFEWIGDGP-QEACAALKRAGIRVT--GWLSGEQVTEELSGS------SVYVHAAAWEGFPMAVLEASQLGLPIVAR 385
Cdd:cd05844   219 PTARLVIAGDGPlRPALQALAAALGRVRflGALPHAEVQDWMRRAeifclpSVTAASGDSEGLGIVLLEAAACGVPVVSS 298


                  .
gi 1538964748 386 A 386
Cdd:cd05844   299 R 299
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 353-449 5.63e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 45.37  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 353 LSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPALNQMPRDYLGG------DPETVAAIIARAIASTGELNRCAAR- 425
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGllvppgDPEALAEAILRLLEDPELRRRLGEAa 97

                          90       100
                  ....*....|....*....|....
gi 1538964748 426 WSDALAANTRDNQRDALLAVYARA 449
Cdd:COG0438    98 RERAEERFSWEAIAERLLALYEEL 121
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 304-384 1.71e-04

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: 43.60  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 304 ETVREFRELHvGQVDFEW--IGDGPQE------ACAALKRAGIRVTGWLSGEQVTE--ELSGSSVYVHAAAWEGFPMAVL 373
Cdd:cd04946   244 ETLNSLCVAH-PSICISWthIGGGPLKerleklAENKLENVKVNFTGEVSNKEVKQlyKENDVDVFVNVSESEGIPVSIM 322

                          90
                  ....*....|.
gi 1538964748 374 EASQLGLPIVA 384
Cdd:cd04946   323 EAISFGIPVIA 333
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 172-384 9.90e-04

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: 41.28  E-value: 9.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 172 QVRELCRTIEPTVVHAHSSFAGLYVRVAS---GRVPVVYTPHcfgfeRTDLPHSARGALWAIERVLALRTAEVAacspRE 248
Cdd:cd04951    70 KLKKIISAFKPDVVHSHMFHANIFARFLRmlyPIPLLICTAH-----NKNEGGRIRMFIYRLTDFLCDITTNVS----RE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 249 AQ---LARRMVRNVTSVP-----NVGRFE-GLDLKHSTRGSAGrVPKVTFM----GRISAQKDpkfAAETVREFRELHVG 315
Cdd:cd04951   141 ALdefIAKKAFSKNKSVPvyngiDLNKFKkDINVRLKIRNKLN-LKNDEFVilnvGRLTEAKD---YPNLLLAISELILS 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1538964748 316 QVDFEWI--GDGP--QEACAALKRAGIRVTGWLSG--EQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVA 384
Cdd:cd04951   217 KNDFKLLiaGDGPlrNELERLICNLNLVDRVILLGqiSNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVA 291
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 291-405 1.33e-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: 40.90  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 291 GRISAQKDPKFAAETVREFRELHvGQVDFEWIGDGP-----QEACAALKRAG-IRVTGWLSGEQVTEELSGS------SV 358
Cdd:cd03799   181 GRLTEKKGLEYAIEAVAKLAQKY-PNIEYQIIGDGDlkeqlQQLIQELNIGDcVKLLGWKPQEEIIEILDEAdifiapSV 259

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1538964748 359 YVHAAAWEGFPMAVLEASQLGLPIVAraipalnqmprDYLGGDPETV 405
Cdd:cd03799   260 TAADGDQDGPPNTLKEAMAMGLPVIS-----------TEHGGIPELV 295
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 184-405 2.70e-03

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: 39.58  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 184 VVHAHSSFAGLYVrVASGRVPVVYTPHCfgfeRTDLPHSARGALWAIERVLALRTAEVAACSPreaqlarrmVRNVTSVP 263
Cdd:cd03802    89 VIHNHSYDWLPPF-APLIGTPFVTTLHG----PSIPPSLAIYAAEPPVNYVSISDAQRAATPP---------IDYLTVVH 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 264 NvgrfeGLDLKHSTRGSAGRvPKVTFMGRISAQKDPKFAAETVREF-RELHV-GQVDFEwigDGPQEACAALKRAGIRVT 341
Cdd:cd03802   155 N-----GLDPADYRFQPDPE-DYLAFLGRIAPEKGLEDAIRVARRAgLPLKIaGKVRDE---DYFYYLQEPLPGPRIEFI 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1538964748 342 GWLSGEQVTEELSGSSVYVHAAAW-EGFPMAVLEASQLGLPIVARAipalnqmprdyLGGDPETV 405
Cdd:cd03802   226 GEVGHDEKQELLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYR-----------RGGLPEVI 279
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 161-405 3.96e-03

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: 39.53  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 161 AMVDGQLARIRQvrelcRTIEPTVVHAH---SSFAGLYVRVASGrVPVVYTPHCFGfeRTDLPHSARGALWAIERVL--- 234
Cdd:cd03800    86 EFADGLLRFIAR-----EGGRYDLIHSHywdSGLVGALLARRLG-VPLVHTFHSLG--RVKYRHLGAQDTYHPSLRItae 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 235 --ALRTAE-VAACSPREAQLARRMVRN----VTSVPNvgrfeGLDLKH---STRGSAGRV--------PKVTFMGRISAQ 296
Cdd:cd03800   158 eqILEAADrVIASTPQEADELISLYGAdpsrINVVPP-----GVDLERffpVDRAEARRArlllppdkPVVLALGRLDPR 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538964748 297 KDPKFAAETV---REFRELH----VGQVDFEwIGDGPQEACAAL-KRAGI----RVTGWLSGEQVTEELSGSSVYVHAAA 364
Cdd:cd03800   233 KGIDTLVRAFaqlPELRELAnlvlVGGPSDD-PLSMDREELAELaEELGLidrvRFPGRVSRDDLPELYRAADVFVVPSL 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1538964748 365 WEGFPMAVLEASQLGLPIVARAIpalnqmprdylGGDPETV 405
Cdd:cd03800   312 YEPFGLTAIEAMACGTPVVATAV-----------GGLQDIV 341
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 338-390 4.10e-03

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: 39.27  E-value: 4.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1538964748 338 IRVTGWLSGEQVTEELSGSSVYVHAAAWEGFPMAVLEASQLGLPIVARAIPAL 390
Cdd:cd03809   252 VRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVL 304
 
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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