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Conserved domains on  [gi|2564918618|ref|WP_306120530|]
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MULTISPECIES: glycosyltransferase [unclassified Roseitalea]

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 ...
76-395 1.75e-32

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 cd03794:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 391  Bit Score: 126.30  E-value: 1.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  76 LIAPAWSLAQMGAGALWSA--RSGKAELIHARS--YLPAAVAWGVWRLTGTPFIFDMRALWPEELITAGRIKRGSVLhRA 151
Cdd:cd03794    74 LIRRLLNYLSFALAALLKLlvREERPDVIIAYSppITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLL-KL 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 152 LQRLERICLRDAAGVVSLTEAAVEHLQAQYPKElagKRTTVIPTCADLDHFKPPAE--------LPQERVYGCVGTvLSG 223
Cdd:cd03794   153 LKKLERKLYRLADAIIVLSPGLKEYLLRKGVPK---EKIIVIPNWADLEEFKPPPKdelrkklgLDDKFVVVYAGN-IGK 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 224 WFRVDWLAALFQQAARRdPDARCEIATR-DNPGRVRAAVQGGALTaeRLAVYARTP-ADMPATVQGHAVSAMLYAGGEIS 301
Cdd:cd03794   229 AQGLETLLEAAERLKRR-PDIRFLFVGDgDEKERLKELAKARGLD--NVTFLGRVPkEEVPELLSAADVGLVPLKDNPAN 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 302 ElGRSPTRMGEVLGCGVPVIANVGvGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPDLSTRCRRAAEEVFSLE 381
Cdd:cd03794   306 R-GSSPSKLFEYMAAGKPILASDD-GGSDLAVEINGCGLVVEPGDPEAL---ADAILELLDDPELRRAMGENGRELAEEK 380
                         330
                  ....*....|....
gi 2564918618 382 RgvaAYRAIYRRIL 395
Cdd:cd03794   381 F---SREKLADRLL 391
 
Name Accession Description Interval E-value
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
76-395 1.75e-32

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: 126.30  E-value: 1.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  76 LIAPAWSLAQMGAGALWSA--RSGKAELIHARS--YLPAAVAWGVWRLTGTPFIFDMRALWPEELITAGRIKRGSVLhRA 151
Cdd:cd03794    74 LIRRLLNYLSFALAALLKLlvREERPDVIIAYSppITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLL-KL 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 152 LQRLERICLRDAAGVVSLTEAAVEHLQAQYPKElagKRTTVIPTCADLDHFKPPAE--------LPQERVYGCVGTvLSG 223
Cdd:cd03794   153 LKKLERKLYRLADAIIVLSPGLKEYLLRKGVPK---EKIIVIPNWADLEEFKPPPKdelrkklgLDDKFVVVYAGN-IGK 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 224 WFRVDWLAALFQQAARRdPDARCEIATR-DNPGRVRAAVQGGALTaeRLAVYARTP-ADMPATVQGHAVSAMLYAGGEIS 301
Cdd:cd03794   229 AQGLETLLEAAERLKRR-PDIRFLFVGDgDEKERLKELAKARGLD--NVTFLGRVPkEEVPELLSAADVGLVPLKDNPAN 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 302 ElGRSPTRMGEVLGCGVPVIANVGvGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPDLSTRCRRAAEEVFSLE 381
Cdd:cd03794   306 R-GSSPSKLFEYMAAGKPILASDD-GGSDLAVEINGCGLVVEPGDPEAL---ADAILELLDDPELRRAMGENGRELAEEK 380
                         330
                  ....*....|....
gi 2564918618 382 RgvaAYRAIYRRIL 395
Cdd:cd03794   381 F---SREKLADRLL 391
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
312-396 5.64e-09

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 53.84  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 312 EVLGCGVPVIAnVGVGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPD----LSTRCRRAAEEVFSLERGVAAY 387
Cdd:COG0438    39 EAMAAGLPVIA-TDVGGLPEVIEDGETGLLVPPGDPEAL---AEAILRLLEDPElrrrLGEAARERAEERFSWEAIAERL 114

                  ....*....
gi 2564918618 388 RAIYRRILE 396
Cdd:COG0438   115 LALYEELLA 123
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
21-200 1.18e-07

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 51.38  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  21 VMNYLRGLA-RDHTIILVTFEKPEDMADSAAMVRAredcaahGIDWRPRRFRRRPRLIAPAWSLAQMgagalwsARSGKA 99
Cdd:pfam13439   7 VLELARALArRGHEVTVVTPGGPGPLAEEVVRVVR-------VPRVPLPLPPRLLRSLAFLRRLRRL-------LRRERP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 100 ELIHARSYLPA-AVAWGVWRLTGTPFIFDMRALWPEELITAGRIKRgsvLHRALQRLERICLRDAAGVVSLTEAAVEHLQ 178
Cdd:pfam13439  73 DVVHAHSPFPLgLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSP---LRRLLRRLERRLLRRADRVIAVSEAVADELR 149
                         170       180
                  ....*....|....*....|..
gi 2564918618 179 AQYPkeLAGKRTTVIPTCADLD 200
Cdd:pfam13439 150 RLYG--VPPEKIRVIPNGVDLE 169
 
Name Accession Description Interval E-value
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
76-395 1.75e-32

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: 126.30  E-value: 1.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  76 LIAPAWSLAQMGAGALWSA--RSGKAELIHARS--YLPAAVAWGVWRLTGTPFIFDMRALWPEELITAGRIKRGSVLhRA 151
Cdd:cd03794    74 LIRRLLNYLSFALAALLKLlvREERPDVIIAYSppITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLL-KL 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 152 LQRLERICLRDAAGVVSLTEAAVEHLQAQYPKElagKRTTVIPTCADLDHFKPPAE--------LPQERVYGCVGTvLSG 223
Cdd:cd03794   153 LKKLERKLYRLADAIIVLSPGLKEYLLRKGVPK---EKIIVIPNWADLEEFKPPPKdelrkklgLDDKFVVVYAGN-IGK 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 224 WFRVDWLAALFQQAARRdPDARCEIATR-DNPGRVRAAVQGGALTaeRLAVYARTP-ADMPATVQGHAVSAMLYAGGEIS 301
Cdd:cd03794   229 AQGLETLLEAAERLKRR-PDIRFLFVGDgDEKERLKELAKARGLD--NVTFLGRVPkEEVPELLSAADVGLVPLKDNPAN 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 302 ElGRSPTRMGEVLGCGVPVIANVGvGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPDLSTRCRRAAEEVFSLE 381
Cdd:cd03794   306 R-GSSPSKLFEYMAAGKPILASDD-GGSDLAVEINGCGLVVEPGDPEAL---ADAILELLDDPELRRAMGENGRELAEEK 380
                         330
                  ....*....|....
gi 2564918618 382 RgvaAYRAIYRRIL 395
Cdd:cd03794   381 F---SREKLADRLL 391
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
17-392 1.56e-19

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: 89.13  E-value: 1.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  17 GQSQVMNYLRGLARD-HTIILVTFEKPEDMADsaamvraredcaAHGIDWRPRRFRRRPRLIAPAWSLAQMGAGALWsar 95
Cdd:cd03801    16 AERHVRELARALAARgHDVTVLTPADPGEPPE------------ELEDGVIVPLLPSLAALLRARRLLRELRPLLRL--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  96 sGKAELIHARSYLPAAVAWGVWRLTGTPFIFDMRALWPEELITAGRIKRgsvlhRALQRLERIcLRDAAGVVSLTEAAVE 175
Cdd:cd03801    81 -RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAER-----RLLARAEAL-LRRADAVIAVSEALRD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 176 HLQAQYPKELAgkRTTVIPTCADLDHFKPPAE-----LPQERVYGCVGTvLSGWFRVDWLAALFQQAARRDPDARCEIAT 250
Cdd:cd03801   154 ELRALGGIPPE--KIVVIPNGVDLERFSPPLRrklgiPPDRPVLLFVGR-LSPRKGVDLLLEALAKLLRRGPDVRLVIVG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 251 RDNPGRVRAAVQGGALtAERLAVY-ARTPADMPATVQGH--AVSAMLYAGGeiselgrsPTRMGEVLGCGVPVIANvGVG 327
Cdd:cd03801   231 GDGPLRAELEELELGL-GDRVRFLgFVPDEELPALYAAAdvFVLPSRYEGF--------GLVVLEAMAAGLPVVAT-DVG 300
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2564918618 328 DVARIVERYNVGILATDGSAAAMdatLDALDSLLADPDLSTRCRRAA----EEVFSLERGVAAYRAIYR 392
Cdd:cd03801   301 GLPEVVEDGEGGLVVPPDDVEAL---ADALLRLLADPELRARLGRAArervAERFSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
13-394 4.71e-10

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: 60.86  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  13 LEPLGQSQVMNYLRGLA-RDHTIILVTFEKPEDMADSAAMVRAREDCAAHGIDWRPRRFRRRPRLIAP-AWSLAQMgaga 90
Cdd:cd03798    12 NSPGRGIFVRRQVRALSrRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLrAPSLAKL---- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  91 LWSARSGKAELIHARSYLPA-AVAWGVWRLTGTPFIFDMRAlwpeelitaGRIKRGSVlHRALQRLERICLRDAAGVVSL 169
Cdd:cd03798    88 LKRRRRGPPDLIHAHFAYPAgFAAALLARLYGVPYVVTEHG---------SDINVFPP-RSLLRKLLRWALRRAARVIAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 170 TEAAVEHLQAQYPkelAGKRTTVIPTCADLDHFKPPAELPQE----RVYGCVGTvLSGWFRVDWLAALFQQAARRDPDAR 245
Cdd:cd03798   158 SKALAEELVALGV---PRDRVDVIPNGVDPARFQPEDRGLGLpldaFVILFVGR-LIPRKGIDLLLEAFARLAKARPDVV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 246 CEIATRD-NPGRVRAAVQGGALTAERLAVYARTPADMPAtvqghavsamLYAGGEISELgrsPTRMG-------EVLGCG 317
Cdd:cd03798   234 LLIVGDGpLREALRALAEDLGLGDRVTFTGRLPHEQVPA----------YYRACDVFVL---PSRHEgfglvllEAMACG 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 318 VPVIANvGVGDVARIVERYNVGILATDGSAaamDATLDALDSLLADPDLSTRCRRAAEEV---FSLERGVAAYRAIYRRI 394
Cdd:cd03798   301 LPVVAT-DVGGIPEVVGDPETGLLVPPGDA---DALAAALRRALAEPYLRELGEAARARVaerFSWVKAADRIAAAYRDV 376
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
98-382 2.60e-09

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: 58.14  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  98 KAELIHARSYLPAAVAWGVWRLTGTPFIFdmralwpeelitagrIKRGSVLHRALQRLERICLR-DAAGVVSLTEAAVEH 176
Cdd:cd03819    76 RIDLIHAHSRAPAWLGWLASRLTGVPLVT---------------TVHGSYLATYHPKDFALAVRaRGDRVIAVSELVRDH 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 177 LQAQYPkeLAGKRTTVIPTCADLDHFKPPAELPQERVYGCVGTV--------LSGWFRVDwlaaLFQQAARRDPDARCei 248
Cdd:cd03819   141 LIEALG--VDPERIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKpvvgyvgrLSPEKGWL----LLVDAAAELKDEPD-- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 249 atrdnpgrVRAAVQGGALTAERLAVYARTPA------------DMPATvqgHAVSAMLYAGGEISELGRSptrMGEVLGC 316
Cdd:cd03819   213 --------FRLLVAGDGPERDEIRRLVERLGlrdrvtftgfreDVPAA---LAASDVVVLPSLHEEFGRV---ALEAMAC 278
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564918618 317 GVPVIAnVGVGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPDLSTRCRRAAEEVFSLER 382
Cdd:cd03819   279 GTPVVA-TDVGGAREIVVHGRTGLLVPPGDAEAL---ADAIRAAKLLPEAREKLQAAAALTEAVRE 340
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
312-396 5.64e-09

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 53.84  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 312 EVLGCGVPVIAnVGVGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPD----LSTRCRRAAEEVFSLERGVAAY 387
Cdd:COG0438    39 EAMAAGLPVIA-TDVGGLPEVIEDGETGLLVPPGDPEAL---AEAILRLLEDPElrrrLGEAARERAEERFSWEAIAERL 114

                  ....*....
gi 2564918618 388 RAIYRRILE 396
Cdd:COG0438   115 LALYEELLA 123
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
21-200 1.18e-07

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 51.38  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  21 VMNYLRGLA-RDHTIILVTFEKPEDMADSAAMVRAredcaahGIDWRPRRFRRRPRLIAPAWSLAQMgagalwsARSGKA 99
Cdd:pfam13439   7 VLELARALArRGHEVTVVTPGGPGPLAEEVVRVVR-------VPRVPLPLPPRLLRSLAFLRRLRRL-------LRRERP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 100 ELIHARSYLPA-AVAWGVWRLTGTPFIFDMRALWPEELITAGRIKRgsvLHRALQRLERICLRDAAGVVSLTEAAVEHLQ 178
Cdd:pfam13439  73 DVVHAHSPFPLgLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSP---LRRLLRRLERRLLRRADRVIAVSEAVADELR 149
                         170       180
                  ....*....|....*....|..
gi 2564918618 179 AQYPkeLAGKRTTVIPTCADLD 200
Cdd:pfam13439 150 RLYG--VPPEKIRVIPNGVDLE 169
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
152-376 4.09e-07

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: 51.68  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 152 LQRLERICLRDAAGVVSLTEAAVEHLQAQ-YPKElagkRTTVIPTCADLDHFKPPAELPQERVYGCVGTvLSGWFRVDWL 230
Cdd:cd05844   133 FQRHRRALQRPAALFVAVSGFIRDRLLARgLPAE----RIHVHYIGIDPAKFAPRDPAERAPTILFVGR-LVEKKGCDVL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 231 AALFQQAARRDPDARCEIAtrdNPGRVRAAVQGGALTAERLAVYARtpadmpatvQGHAVSAMLYAGGEI----SELGRS 306
Cdd:cd05844   208 IEAFRRLAARHPTARLVIA---GDGPLRPALQALAAALGRVRFLGA---------LPHAEVQDWMRRAEIfclpSVTAAS 275
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564918618 307 PTRMG------EVLGCGVPVIANvGVGDVARIVERYNVGILATDGSAAAMDatlDALDSLLADPDLSTRCRRAAEE 376
Cdd:cd05844   276 GDSEGlgivllEAAACGVPVVSS-RHGGIPEAILDGETGFLVPEGDVDALA---DALQALLADRALADRMGGAARA 347
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
310-394 5.75e-07

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: 51.13  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 310 MGEVLGCGVPVIANvGVGDVARIVERYNVGILAtdGSAAAMDATLDALDSLlaDPdlsTRCRRAAEEVFSLERGVAAYRA 389
Cdd:cd03802   257 MIEAMACGTPVIAY-RRGGLPEVIQHGETGFLV--DSVEEMAEAIANIDRI--DR---AACRRYAEDRFSAARMADRYEA 328

                  ....*
gi 2564918618 390 IYRRI 394
Cdd:cd03802   329 LYRKV 333
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
95-194 1.41e-06

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 47.78  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  95 RSGKAELIHARSYLPAAVAWGVWRLTGTPFIFDMRALWPEELITAgrikrgsvLHRALQRLERICLRDAAGVVSLTEAAV 174
Cdd:pfam13579  68 RAERPDVVHAHSPTAGLAARLARRRRGVPLVVTVHGLALDYGSGW--------KRRLARALERRLLRRADAVVVVSEAEA 139
                          90       100
                  ....*....|....*....|
gi 2564918618 175 EHLQAQYPKElagKRTTVIP 194
Cdd:pfam13579 140 ELLRALGVPA---ARVVVVP 156
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
83-387 1.60e-05

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: 46.85  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  83 LAQMGAGAL--WSARSGKAELIHARSYLPAAVAWGVWRLTGTPFIFDMRALwpeelitaGRIKRGSVL-----HRALQ-R 154
Cdd:cd03800    84 LEEFADGLLrfIAREGGRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHSL--------GRVKYRHLGaqdtyHPSLRiT 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 155 LERICLRDAAGVVSLTEAAVEHLQAQYpkELAGKRTTVIPTCADLDHFKPPAELPQERVYgcvgtvlsgwFRVDWLAALF 234
Cdd:cd03800   156 AEEQILEAADRVIASTPQEADELISLY--GADPSRINVVPPGVDLERFFPVDRAEARRAR----------LLLPPDKPVV 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 235 QQAARRDPdarceiatRDNP-GRVRAAVQGGALTAE-RLAVYA--RTPADMPATVQGHAVSAMLYAGGEISELGR-SPTR 309
Cdd:cd03800   224 LALGRLDP--------RKGIdTLVRAFAQLPELRELaNLVLVGgpSDDPLSMDREELAELAEELGLIDRVRFPGRvSRDD 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 310 MGEVL-----------------------GCGVPVIANvGVGDVARIVERYNVGIL--ATDGSAAAmdatlDALDSLLADP 364
Cdd:cd03800   296 LPELYraadvfvvpslyepfgltaieamACGTPVVAT-AVGGLQDIVRDGRTGLLvdPHDPEALA-----AALRRLLDDP 369
                         330       340
                  ....*....|....*....|...
gi 2564918618 365 DLSTRCRRAAeevfsLERGVAAY 387
Cdd:cd03800   370 ALWQRLSRAG-----LERARAHY 387
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
95-392 4.01e-05

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: 45.39  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  95 RSGKAELIHarSYLPAAVAWG---VWRLTGTPFIFDMRALWPEELITAGRIKrgsvLHRALQRLERICLRDAAGVvslte 171
Cdd:cd03807    76 RKRNPDVVH--TWMYHADLIGglaAKLAGGVKVIWSVRSSNIPQRLTRLVRK----LCLLLSKFSPATVANSSAV----- 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 172 aAVEHLQAQYPKElagkRTTVIPTCADLDHFKPPAE----------LPQE-RVYGCVGTvLSGWFRVDWLAALFQQAARR 240
Cdd:cd03807   145 -AEFHQEQGYAKN----KIVVIYNGIDLFKLSPDDAsrararrrlgLAEDrRVIGIVGR-LHPVKDHSDLLRAAALLVET 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 241 DPDARCEIA----TRDNPGRVRAAVQGGA---LTAERlavyartpADMPAtvqghAVSAM-LYAGGEISElgRSPTRMGE 312
Cdd:cd03807   219 HPDLRLLLVgrgpERPNLERLLLELGLEDrvhLLGER--------SDVPA-----LLPAMdIFVLSSRTE--GFPNALLE 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 313 VLGCGVPVIANvGVGDVARIVeRYNVGILATDGSAAAMdatLDALDSLLADPDLSTRCRRAA----EEVFSLERGVAAYR 388
Cdd:cd03807   284 AMACGLPVVAT-DVGGAAELV-DDGTGFLVPAGDPQAL---ADAIRALLEDPEKRARLGRAAreriANEFSIDAMVRRYE 358

                  ....
gi 2564918618 389 AIYR 392
Cdd:cd03807   359 TLYY 362
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
93-392 1.31e-04

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: 43.86  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618  93 SARSGKAELIHARS-----YLPAAVAWgvwrLTGTPFIFDMRALWP----EELITAGRIKRG--SVLHRALQRLERICLR 161
Cdd:cd03813   168 ADDLPEADLYHSVStgyagLLGALARH----RRGIPFLLTEHGIYTrerkIEILQSTWIMGYikKLWIRFFERLGKLAYQ 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 162 DAAGVVSLTEAAvehlqAQYPKELA--GKRTTVIPTCADLDHFKPPAELPQERVYGCVGTVLsgwfRVDWLAAL------ 233
Cdd:cd03813   244 QADKIISLYEGN-----RRRQIRLGadPDKTRVIPNGIDIQRFAPAREERPEKEPPVVGLVG----RVVPIKDVktfira 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 234 FQQAARRDPDARCEI--ATRDNPGRVraavqggaltAERLAVYARTPADMPATVQGHAVSAMLYAGGE------ISElgR 305
Cdd:cd03813   315 FKLVRRAMPDAEGWLigPEDEDPEYA----------QECKRLVASLGLENKVKFLGFQNIKEYYPKLGllvltsISE--G 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 306 SPTRMGEVLGCGVPVIANvGVGDVARIVErynvGILATDGSA----AAMD--ATLDALDSLLADPDLSTRCRRAA----E 375
Cdd:cd03813   383 QPLVILEAMASGVPVVAT-DVGSCRELIY----GADDALGQAglvvPPADpeALAEALIKLLRDPELRQAFGEAGrkrvE 457
                         330
                  ....*....|....*..
gi 2564918618 376 EVFSLERGVAAYRAIYR 392
Cdd:cd03813   458 KYYTLEGMIDSYRKLYL 474
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
312-394 1.64e-04

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: 43.47  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 312 EVLGCGVPVIAnVGVGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPD----LSTRCRRAAEEVFSLERGVAAY 387
Cdd:cd03825   282 EAMACGTPVVA-FDTGGSPEIVQHGVTGYLVPPGDVQAL---AEAIEWLLANPKeresLGERARALAENHFDQRVQAQRY 357

                  ....*..
gi 2564918618 388 RAIYRRI 394
Cdd:cd03825   358 LELYKDL 364
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
312-394 2.29e-04

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


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 43.11  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 312 EVLGCGVPVIANvGVGDVARIVERYNVGILATDGSAAAMdaTLDALdSLLADPDLSTRCRRAA----EEVFSLERGVAAY 387
Cdd:cd04962   288 EAMACGVPVVSS-NAGGIPEVVKHGETGFLSDVGDVDAM--AKSAL-SILEDDELYNRMGRAArkraAERFDPERIVPQY 363

                  ....*..
gi 2564918618 388 RAIYRRI 394
Cdd:cd04962   364 EAYYRRL 370
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
312-377 2.01e-03

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: 38.41  E-value: 2.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564918618 312 EVLGCGVPVIANVgVGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPDLSTRCRRAAEEV 377
Cdd:pfam00534  97 EAMACGLPVIASD-VGGPPEVVKDGETGFLVKPNNAEAL---AEAIDKLLEDEELRERLGENARKR 158
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
310-396 8.27e-03

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: 38.04  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564918618 310 MGEVLGCGVPVIAnVGVGDVARIVERYNVGILATDGSAAAMdatLDALDSLLADPDlstRCRRAAEEvFSLERGVAAYRA 389
Cdd:cd03814   284 VLEAMASGLPVVA-ADAGGPRDIVRPGGTGALVEPGDAAAF---AAALRALLEDPE---LRRRMAAR-ARAEAERYSWEA 355

                  ....*..
gi 2564918618 390 IYRRILE 396
Cdd:cd03814   356 FLDNLLD 362
 
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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