NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1028513018|gb|OAI91370|]
View 

glycosyl transferase family 1 [Rhizobium sp. GHKF11]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133545)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 74-416 4.58e-53

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: 181.41  E-value: 4.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018  74 LPPSATPLRLRQSLFNNNPLKSSVYWaiRKVVDFRNRRRWATVPDGSAKEVDLSgHVLislgrpkimsDYLAALEARGTN 153
Cdd:cd03809    37 LAVPPLPGELLRLLREYPELSLGVIK--IKLWRELALLRWLQILLPKKDKPDLL-HSP----------HNTAPLLLKGCP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 154 VIFVplLHDMIPlhdFTHRNQFSFPKNFLHDNQV--AIKASSLILTNSEFTAREVLHFSerGVlpPVSKVVAVPLCNE-- 229
Cdd:cd03809   104 QVVT--IHDLIP---LRYPEFFPKRFRLYYRLLLpiSLRRADAIITVSEATRDDIIKFY--GV--PPEKIVVIPLGVDps 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 230 ---LRPTSESIEKRGPSGRYIFCVGIYNGRKNLECVVEAMMSLHERGMDvPNLVLAGARRKRVEKFLKNKRFLPLSTKFH 306
Cdd:cd03809   175 ffpPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGD-LKLVIVGGKGWEDEELLDLVKKLGLGGRVR 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 307 FVHNPNQAELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALREAGGDLARYFDPEKSAELADILGQLLAN 386
Cdd:cd03809   254 FLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLED 333

                         330       340       350
                  ....*....|....*....|....*....|
gi 1028513018 387 KSEYDVLKAKIAdARSSMRTWNDVASDLLQ 416
Cdd:cd03809   334 PSLREELIRKGL-ERAKKFSWEKTAEKTLE 362
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 74-416 4.58e-53

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: 181.41  E-value: 4.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018  74 LPPSATPLRLRQSLFNNNPLKSSVYWaiRKVVDFRNRRRWATVPDGSAKEVDLSgHVLislgrpkimsDYLAALEARGTN 153
Cdd:cd03809    37 LAVPPLPGELLRLLREYPELSLGVIK--IKLWRELALLRWLQILLPKKDKPDLL-HSP----------HNTAPLLLKGCP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 154 VIFVplLHDMIPlhdFTHRNQFSFPKNFLHDNQV--AIKASSLILTNSEFTAREVLHFSerGVlpPVSKVVAVPLCNE-- 229
Cdd:cd03809   104 QVVT--IHDLIP---LRYPEFFPKRFRLYYRLLLpiSLRRADAIITVSEATRDDIIKFY--GV--PPEKIVVIPLGVDps 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 230 ---LRPTSESIEKRGPSGRYIFCVGIYNGRKNLECVVEAMMSLHERGMDvPNLVLAGARRKRVEKFLKNKRFLPLSTKFH 306
Cdd:cd03809   175 ffpPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGD-LKLVIVGGKGWEDEELLDLVKKLGLGGRVR 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 307 FVHNPNQAELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALREAGGDLARYFDPEKSAELADILGQLLAN 386
Cdd:cd03809   254 FLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLED 333

                         330       340       350
                  ....*....|....*....|....*....|
gi 1028513018 387 KSEYDVLKAKIAdARSSMRTWNDVASDLLQ 416
Cdd:cd03809   334 PSLREELIRKGL-ERAKKFSWEKTAEKTLE 362
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 306-420 2.26e-19

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 83.50  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 306 HFVHNPNQAELAE-LYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE--AGGDLARYFDPEKSAELADILGQ 382
Cdd:COG0438     3 RLVPRKGLDLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEviEDGETGLLVPPGDPEALAEAILR 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1028513018 383 LLANKSEYDVLKAKIADARSSMRTWNDVASDLLQALDD 420
Cdd:COG0438    83 LLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEE 120
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 245-394 5.23e-19

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: 83.48  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 245 RYIFCVGIYNGRKNLECVVEAMMSLHERGMDVpNLVLAG--ARRKRVEKFLKNkrfLPLSTKFHFVHNPNQAELAELYRR 322
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNL-KLVIAGdgEEEKRLKKLAEK---LGLGDNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028513018 323 AFALVLPSRMEGWGLPISEALWCGTPALAADVPALREAGGDL--ARYFDPEKSAELADILGQLLANKSEYDVLK 394
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGetGFLVKPNNAEALAEAIDKLLEDEELRERLG 152
PHA01633 PHA01633
putative glycosyl transferase group 1
 251-359 1.91e-04

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 43.43  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 251 GIYNG---RKNLECVVEAMMSLHERGMDVPnlvlagarrKRVEKF-LKNKRF--LPLSTKFHFV----HNPNQAELAeLY 320
Cdd:PHA01633  152 GIVSGltkRKNMDLMLQVFNELNTKYPDIA---------KKIHFFvISHKQFtqLEVPANVHFVaefgHNSREYIFA-FY 221

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1028513018 321 RRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE 359
Cdd:PHA01633  222 GAMDFTIVPSGTEGFGMPVLESMAMGTPVIHQLMPPLDE 260
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 74-416 4.58e-53

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: 181.41  E-value: 4.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018  74 LPPSATPLRLRQSLFNNNPLKSSVYWaiRKVVDFRNRRRWATVPDGSAKEVDLSgHVLislgrpkimsDYLAALEARGTN 153
Cdd:cd03809    37 LAVPPLPGELLRLLREYPELSLGVIK--IKLWRELALLRWLQILLPKKDKPDLL-HSP----------HNTAPLLLKGCP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 154 VIFVplLHDMIPlhdFTHRNQFSFPKNFLHDNQV--AIKASSLILTNSEFTAREVLHFSerGVlpPVSKVVAVPLCNE-- 229
Cdd:cd03809   104 QVVT--IHDLIP---LRYPEFFPKRFRLYYRLLLpiSLRRADAIITVSEATRDDIIKFY--GV--PPEKIVVIPLGVDps 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 230 ---LRPTSESIEKRGPSGRYIFCVGIYNGRKNLECVVEAMMSLHERGMDvPNLVLAGARRKRVEKFLKNKRFLPLSTKFH 306
Cdd:cd03809   175 ffpPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGD-LKLVIVGGKGWEDEELLDLVKKLGLGGRVR 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 307 FVHNPNQAELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALREAGGDLARYFDPEKSAELADILGQLLAN 386
Cdd:cd03809   254 FLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLED 333

                         330       340       350
                  ....*....|....*....|....*....|
gi 1028513018 387 KSEYDVLKAKIAdARSSMRTWNDVASDLLQ 416
Cdd:cd03809   334 PSLREELIRKGL-ERAKKFSWEKTAEKTLE 362
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 139-418 3.36e-27

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: 111.48  E-value: 3.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 139 IMSDYLAALEARGTNVIFVPLLHDmipLHDFTHRNQFSFPKNFLHDNQVAIKASSLILTNSEFTARevlHFSERGVLPPv 218
Cdd:cd03801    91 LLAALLAALLALLLGAPLVVTLHG---AEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRD---ELRALGGIPP- 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 219 SKVVAVPL---CNELRPTSESIEKRGPSGRYIFCVGIYNGRKNLECVVEAMMSLHERGMDVPnLVLAG---ARRKRVEKF 292
Cdd:cd03801   164 EKIVVIPNgvdLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVR-LVIVGgdgPLRAELEEL 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 293 LKNkrflpLSTKFHFVHNPNQAELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE--AGGDLARYFDP 370
Cdd:cd03801   243 ELG-----LGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEvvEDGEGGLVVPP 317

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1028513018 371 EKSAELADILGQLLANKSEYDVLKAKIADARSSMRTWNDVASDLLQAL 418
Cdd:cd03801   318 DDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 143-420 5.62e-21

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: 93.98  E-value: 5.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 143 YLAALEARGTNVIFVPLLHDmiplhdfTHRNQFSFPKNFLHDNQVAIKASSLILTNSEFTAREVlhfseRGVLPPVSKVV 222
Cdd:cd03798   109 FAAALLARLYGVPYVVTEHG-------SDINVFPPRSLLRKLLRWALRRAARVIAVSKALAEEL-----VALGVPRDRVD 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 223 AVPlcNELRPTSESIEKRG----PSGRYIFCVGIYNGRKNLECVVEAMMSLhERGMDVPNLVLAGA--RRKRVEKFLKNk 296
Cdd:cd03798   177 VIP--NGVDPARFQPEDRGlglpLDAFVILFVGRLIPRKGIDLLLEAFARL-AKARPDVVLLIVGDgpLREALRALAED- 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 297 rfLPLSTKFHFV-HNPNQaELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALREA-GGDLARYFDPEKSA 374
Cdd:cd03798   253 --LGLGDRVTFTgRLPHE-QVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVvGDPETGLLVPPGDA 329

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1028513018 375 E-LADILGQLLAnKSEYDVLKAKIADARSSMRTWNDVASDLLQALDD 420
Cdd:cd03798   330 DaLAAALRRALA-EPYLRELGEAARARVAERFSWVKAADRIAAAYRD 375
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 306-420 2.26e-19

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 83.50  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 306 HFVHNPNQAELAE-LYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE--AGGDLARYFDPEKSAELADILGQ 382
Cdd:COG0438     3 RLVPRKGLDLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEviEDGETGLLVPPGDPEALAEAILR 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1028513018 383 LLANKSEYDVLKAKIADARSSMRTWNDVASDLLQALDD 420
Cdd:COG0438    83 LLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEE 120
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 245-394 5.23e-19

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: 83.48  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 245 RYIFCVGIYNGRKNLECVVEAMMSLHERGMDVpNLVLAG--ARRKRVEKFLKNkrfLPLSTKFHFVHNPNQAELAELYRR 322
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNL-KLVIAGdgEEEKRLKKLAEK---LGLGDNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028513018 323 AFALVLPSRMEGWGLPISEALWCGTPALAADVPALREAGGDL--ARYFDPEKSAELADILGQLLANKSEYDVLK 394
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGetGFLVKPNNAEALAEAIDKLLEDEELRERLG 152
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 125-416 3.06e-18

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: 86.14  E-value: 3.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 125 DLSGHVLISLGRPKI------MSDYLAALEARGTNVifvPLLHDMIPLHDFTHRNQ-----FSFPKNFLHDNQvAIKASS 193
Cdd:cd03800    90 GLLRFIAREGGRYDLihshywDSGLVGALLARRLGV---PLVHTFHSLGRVKYRHLgaqdtYHPSLRITAEEQ-ILEAAD 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 194 LILTNsefTAREVLHFSERGVLPPvSKVVAVPlC----NELRPTSESIEKR-----GPSGRYIFCVGIYNGRKNLECVVE 264
Cdd:cd03800   166 RVIAS---TPQEADELISLYGADP-SRINVVP-PgvdlERFFPVDRAEARRarlllPPDKPVVLALGRLDPRKGIDTLVR 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 265 AMMSLHERGMDVpNLVLAG--------ARRKRVEKFLKNkrfLPLSTKFHFVHNPNQAELAELYRRAFALVLPSRMEGWG 336
Cdd:cd03800   241 AFAQLPELRELA-NLVLVGgpsddplsMDREELAELAEE---LGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFG 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 337 LPISEALWCGTPALAADVPALREAGGDL--ARYFDPEKSAELADILGQLLANKSEYDVLKAKIADARSSMRTWNDVASDL 414
Cdd:cd03800   317 LTAIEAMACGTPVVATAVGGLQDIVRDGrtGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQL 396


                  ..
gi 1028513018 415 LQ 416
Cdd:cd03800   397 LT 398
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
244-386 1.84e-15

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 72.93  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 244 GRYIFCVG-IYNGRKNLECVVEAMMSLHERGMDVpNLVLAGAR-RKRVEKFLKNkrflpLSTKFHFVhnPNQAELAELYR 321
Cdd:pfam13692   1 RPVILFVGrLHPNVKGVDYLLEAVPLLRKRDNDV-RLVIVGDGpEEELEELAAG-----LEDRVIFT--GFVEDLAELLA 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028513018 322 RAFALVLPSRMEGWGLPISEALWCGTPALAADVPALREA-GGDLARYFDPEKSAELADILGQLLAN 386
Cdd:pfam13692  73 AADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELvDGENGLLVPPGDPEALAEAILRLLED 138
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 143-406 1.43e-12

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: 68.54  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 143 YLAALEARGTNVIFVplLHDMIPLHDFthrnqfsfPKNFLHDNQVAIKASSLILTNSEFTAREvlhFSERGVLPPvSKVV 222
Cdd:cd03811    97 IVAKLAAARSKVIAW--IHSSLSKLYY--------LKKKLLLKLKLYKKADKIVCVSKGIKED---LIRLGPSPP-EKIE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 223 AVP---LCNELRPTS-ESIEKRGPSGRYIFCVGIYNGRKNLECVVEAMMSLHERGMDVpNLVLAG--ARRKRVEKFLKNk 296
Cdd:cd03811   163 VIYnpiDIDRIRALAkEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDV-KLVILGdgPLREELEKLAKE- 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 297 rfLPLSTKFHF---VHNPnqaelAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE--AGGDLARYFDPE 371
Cdd:cd03811   241 --LGLAERVIFlgfQSNP-----YPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREilDDGENGLLVPDG 313

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1028513018 372 KSAELADILGQLLANKSEYDvLKAKIADARSSMRT 406
Cdd:cd03811   314 DAAALAGILAALLQKKLDAA-LRERLAKAQEAVFR 347
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 149-416 5.66e-12

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: 67.01  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 149 ARGTNVIFVPLLHDMIPLHDFTHRNQFSFPKNFLHDNQVAIKASSLILTNSEFtAREVLHFserGVLPPVSKV---VAVP 225
Cdd:cd03821   111 ARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIERRNLNNAALVHFTSEQE-ADELRRF---GLEPPIAVIpngVDIP 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 226 lcnELRPTSESIEKRG--PSGRYIFCVGIYNGRKNLECVVEAMMSLHERGMDVpNLVLAGARRKRVEKFLKNKRFLPLST 303
Cdd:cd03821   187 ---EFDPGLRDRRKHNglEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDW-HLVIAGPDDGAYPAFLQLQSSLGLGD 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 304 KFHFVHNPNQAELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALREAG-GDLARYFDPEKSaELADILGQ 382
Cdd:cd03821   263 RVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVeAGCGVVVDPNVS-SLAEALAE 341

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1028513018 383 LLANKSEYDVLKAKI--ADARSSMRTWNDVASDLLQ 416
Cdd:cd03821   342 ALRDPADRKRLGEMArrARQVEENFSWEAVAGQLGE 377
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 254-396 9.35e-12

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: 66.20  E-value: 9.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 254 NGRKNLECVVEAMMSLHergmDVPN--LVLAGARRKRVEKFLKNKRFLPLSTkfhfvhnpNQAELAELYRRAFALVLPSR 331
Cdd:cd03825   205 KPRKGFDELIEALKLLA----TKDDllLVVFGKNDPQIVILPFDIISLGYID--------DDEQLVDIYSAADLFVHPSL 272

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 332 MEGWGLPISEALWCGTPALAADVPALREA-----GGDLARYFDPEksaELADILGQLLANKSEYDVLKAK 396
Cdd:cd03825   273 ADNLPNTLLEAMACGTPVVAFDTGGSPEIvqhgvTGYLVPPGDVQ---ALAEAIEWLLANPKERESLGER 339
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 190-394 2.33e-11

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: 65.03  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 190 KASSLILTNSEFTAREVLhfsERGVLPPVSKVV---------AVPLCNELRPTSESIEKRgpSGRYIFCVGIYNGRKNLE 260
Cdd:cd03807   132 KFSPATVANSSAVAEFHQ---EQGYAKNKIVVIyngidlfklSPDDASRARARRRLGLAE--DRRVIGIVGRLHPVKDHS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 261 CVVEAMMSLHERGMDVpNLVLAG--ARRKRVEKFLKNkrfLPLSTKFHFVHNpnQAELAELYRRAFALVLPSRMEGWGLP 338
Cdd:cd03807   207 DLLRAAALLVETHPDL-RLLLVGrgPERPNLERLLLE---LGLEDRVHLLGE--RSDVPALLPAMDIFVLSSRTEGFPNA 280

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1028513018 339 ISEALWCGTPALAADVPALREAGGDLARY-FDPEKSAELADILGQLLANKSEYDVLK 394
Cdd:cd03807   281 LLEAMACGLPVVATDVGGAAELVDDGTGFlVPAGDPQALADAIRALLEDPEKRARLG 337
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 157-387 3.76e-11

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: 64.40  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 157 VPLLhdmIPLHDF---THRNQFSF----PKNF-LHDNQVAIKASsLILTNSEFTAREVLhfsERGVlpPVSKVVAVPL-- 226
Cdd:cd05844   105 VPLV---VTFHGFditTSRAWLAAspgwPSQFqRHRRALQRPAA-LFVAVSGFIRDRLL---ARGL--PAERIHVHYIgi 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 227 -CNELRPTSesiekRGPSGRYIFCVGIYNGRKNLECVVEAMMSLHERGMDVPnLVLA--GARRKRVEKF---LKNKRFLP 300
Cdd:cd05844   176 dPAKFAPRD-----PAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTAR-LVIAgdGPLRPALQALaaaLGRVRFLG 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 301 LSTkfhfvhnpnQAELAELYRRAFALVLPSRM------EGWGLPISEALWCGTPALAADVPALREAGGD----LAryFDP 370
Cdd:cd05844   250 ALP---------HAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDgetgFL--VPE 318

                         250
                  ....*....|....*..
gi 1028513018 371 EKSAELADILGQLLANK 387
Cdd:cd05844   319 GDVDALADALQALLADR 335
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 241-419 2.14e-10

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: 61.93  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 241 GPSGRYIFcvgIYNGR----KNLECVVEAMMSLHERgmDVPNLVLAG--ARRKRVEKFLknkrflplsTKFHFVHNPNQA 314
Cdd:cd03814   194 GPPGRPLL---LYVGRlapeKNLEALLDADLPLAAS--PPVRLVVVGdgPARAELEARG---------PDVIFTGFLTGE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 315 ELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE--AGGDLARYFDPEKSAELADILGQLLANKSEYDV 392
Cdd:cd03814   260 ELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDivRPGGTGALVEPGDAAAFAAALRALLEDPELRRR 339

                         170       180
                  ....*....|....*....|....*..
gi 1028513018 393 LkAKIADARSSMRTWNDVASDLLQALD 419
Cdd:cd03814   340 M-AARARAEAERYSWEAFLDNLLDYYA 365
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 143-396 4.44e-10

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: 61.14  E-value: 4.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 143 YLAALEARGTNVIFVPLLHDMipLHDFTHRnqfsFPKNFLHDNQVAIKASS-------LILTNSEFTAREVLhfsERGVL 215
Cdd:cd03817    98 KLGLRIARKLKIPIVHTYHTM--YEDYLHY----IPKGKLLVKAVVRKLVRrfynhtdAVIAPSEKIKDTLR---EYGVK 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 216 ppvSKVVAVPLCNELR-----PTSESIEKRGPS--GRYIFCVGIYNGRKNLECVVEAMMSLHERgmdvPN--LVLAGA-- 284
Cdd:cd03817   169 ---GPIEVIPNGIDLDkfekpLNTEERRKLGLPpdEPILLYVGRLAKEKNIDFLLRAFAELKKE----PNikLVIVGDgp 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 285 RRKRVEKFLKNKRfLPLSTKFHFVHNPNqaELAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE--AGG 362
Cdd:cd03817   242 EREELKELARELG-LADKVIFTGFVPRE--ELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASElvEDG 318

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1028513018 363 DlARYFDPEKSAELADILGQLLANKSEYDVLKAK 396
Cdd:cd03817   319 E-NGFLFEPNDETLAEKLLHLRENLELLRKLSKN 351
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 249-360 1.40e-09

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: 58.18  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 249 CVGIYNGRKNLECVVEAMMSLHERGMDVPNLVLAGARRKRVEKFLKNKRFLpLSTKFHFVHNPNQAELAELYRRAFALVL 328
Cdd:cd01635   115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGL-LERVVIIGGLVDDEVLELLLAAADVFVL 193

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1028513018 329 PSRMEGWGLPISEALWCGTPALAADVPALREA 360
Cdd:cd01635   194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEF 225
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 166-403 5.39e-08

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: 54.26  E-value: 5.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 166 LHDFThrnqfsfpknFLHDNQV-AIKASSLILTNSEFTARevLHfseRGVLPPVSKVVAVPlcNELRPTSESIEKRGPSG 244
Cdd:cd03823   127 LHDYW----------LLCPRQFlFKKGGDAVLAPSRFTAN--LH---EANGLFSARISVIP--NAVEPDLAPPPRRRPGT 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 245 RYIFCvgIYNGR----KNLECVVEAMMSLHERGmdvPNLVLAGARRKRVEKFLKNKRFLplstkfHFVHNPNQAELAELY 320
Cdd:cd03823   190 ERLRF--GYIGRlteeKGIDLLVEAFKRLPRED---IELVIAGHGPLSDERQIEGGRRI------AFLGRVPTDDIKDFY 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 321 RRAFALVLPSR-MEGWGLPISEALWCGTPALAADVPALREAGGDLA--RYFDPEKSAELADILgQLLANKSEYDVLKAKI 397
Cdd:cd03823   259 EKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVngLLFAPGDAEDLAAAM-RRLLTDPALLERLRAG 337


                  ....*.
gi 1028513018 398 ADARSS 403
Cdd:cd03823   338 AEPPRS 343
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 144-386 1.19e-07

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: 53.13  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 144 LAALEARGTNVIFVPLLHDMIPLHDFTHRNQFSFPKNFlhDNQVAIkassliltnSEFTARevlHFSERGVLPPVsKVVA 223
Cdd:cd03819    90 LGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARG--DRVIAV---------SELVRD---HLIEALGVDPE-RIRV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 224 VPL---CNELRPTSESIEKRG---PSGRYIFcvgIYNGR----KNLECVVEAMMSLHERgMDVPNLVL-AGARRKRVEKf 292
Cdd:cd03819   155 IPNgvdTDRFPPEAEAEERAQlglPEGKPVV---GYVGRlspeKGWLLLVDAAAELKDE-PDFRLLVAgDGPERDEIRR- 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 293 LKNKRFLplSTKFHFVHNPNQaeLAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE-----AGGDLARY 367
Cdd:cd03819   230 LVERLGL--RDRVTFTGFRED--VPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREivvhgRTGLLVPP 305

                         250
                  ....*....|....*....
gi 1028513018 368 FDPEksaELADILGQLLAN 386
Cdd:cd03819   306 GDAE---ALADAIRAAKLL 321
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 247-404 4.78e-07

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: 51.68  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 247 IFCVGIYNGRKNLECVVEAMMSLHERGMDVpNLVLAG--ARRKRVEKFLKNkrfLPLSTKFHFVHNpnQAELAELYRRAF 324
Cdd:cd04951   191 ILNVGRLTEAKDYPNLLLAISELILSKNDF-KLLIAGdgPLRNELERLICN---LNLVDRVILLGQ--ISNISEYYNAAD 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 325 ALVLPSRMEGWGLPISEALWCGTPALAADVPALREAGGDlARYFDP-EKSAELADILGQLLANKSEYDVLKAKIADARSS 403
Cdd:cd04951   265 LFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD-HNYVVPvSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAK 343


                  .
gi 1028513018 404 M 404
Cdd:cd04951   344 N 344
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 188-353 5.07e-07

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 51.44  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 188 AIKASSLILTNSEFTAREV------LHFSERGVL-PPV--SKVVAVPLCNELRptsesiEKRGPSGRYIFcVGI--YNGR 256
Cdd:cd03805   151 TTGMADQIVVNSNFTAGVFkktfpsLAKNPPEVLyPCVdtDSFDSTSEDPDPG------DLIAKSNKKFF-LSInrFERK 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 257 KNLECVVEAMMSLHERGMDVPN--LVLAGARRKRVE------KFLKN--KRFLPLSTKFHFVHNPNQAELAELYRRAFAL 326
Cdd:cd03805   224 KNIALAIEAFAKLKQKLPEFENvrLVIAGGYDPRVAenveylEELQRlaEELLNVEDQVLFLRSISDSQKEQLLSSALAL 303

                         170       180
                  ....*....|....*....|....*....
gi 1028513018 327 VL-PSRmEGWGL-PIsEALWCGTPALAAD 353
Cdd:cd03805   304 LYtPSN-EHFGIvPL-EAMYAGKPVIACN 330
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 23-355 1.10e-06

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: 50.31  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018  23 GISRTVMEVAYELTKLDSRVryVIYSPYHGR---FYEVFPRVgdasptgvldhnlppsatplrLRQSLFNNNPLKSSVYW 99
Cdd:cd03820    14 GAERVAINLANHLAKKGYDV--TIISLDSAEkppFYELDDNI---------------------KIKNLGDRKYSHFKLLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 100 A-IRKVVDFRNRRRwATVPDgsakevdlsghVLISlgrpkIMSDYLAALEARGTNVIFVPLLHdmiplhdFTHRNQFSFP 178
Cdd:cd03820    71 KyFKKVRRLRKYLK-NNKPD-----------VVIS-----FRTSLLTFLALIGLKSKLIVWEH-------NNYEAYNKGL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 179 KNFLHDNQVAIKASSLILTnsefTAREVLHFSErgvlPPVSKVVAVPlcNELRPTSESIEKRgPSGRYIFCVGIYNGRKN 258
Cdd:cd03820   127 RRLLLRRLLYKRADKIVVL----TEADKLKKYK----QPNSNVVVIP--NPLSFPSEEPSTN-LKSKRILAVGRLTYQKG 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 259 LECVVEAMMSLHERgmdVPN--LVLAGA--RRKRVEKFLKNKRflpLSTKFHFVhnPNQAELAELYRRAFALVLPSRMEG 334
Cdd:cd03820   196 FDLLIEAWALIAKK---HPDwkLRIYGDgpEREELEKLIDKLG---LEDRVKLL--GPTKNIAEEYANSSIFVLSSRYEG 267

                         330       340
                  ....*....|....*....|.
gi 1028513018 335 WGLPISEALWCGTPALAADVP 355
Cdd:cd03820   268 FPMVLLEAMAYGLPIISFDCP 288
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 177-355 1.27e-05

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: 46.88  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 177 FPKNFLHDNQVAIKASSLILTNSEFtareVLHFSErgvlppvsKVVAVPL-CNELRPTS-----ESIEKRGPSGRYIFCV 250
Cdd:cd03795   130 LMTRFLRRADRIIATSPNYVETSPT----LREFKN--------KVRVIPLgIDKNVYNIprvdfENIKREKKGKKIFLFI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 251 GIYNGRKNLECVVEAMmslheRGMDVPnLVLAGARRKRVEkfLKNKRFLPLSTKFHFVHNPNQAELAELYRRAFALVLPS 330
Cdd:cd03795   198 GRLVYYKGLDYLIEAA-----QYLNYP-IVIGGEGPLKPD--LEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPS 269

                         170       180
                  ....*....|....*....|....*..
gi 1028513018 331 --RMEGWGLPISEALWCGTPALAADVP 355
Cdd:cd03795   270 vlRSEAFGIVLLEAMMCGKPVISTNIG 296
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 242-388 1.46e-05

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: 46.82  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 242 PSGRYIF-CVGIYNGRKNLECVVEAMMSLHERGMDVpNLVLAGARRKRVEKFLKNKRfLPLSTKFHFVHNPNqaELAELY 320
Cdd:cd03808   186 PSEKVVFlFVARLLKDKGIDELIEAAKILKKKGPNV-RFLLVGDGELENPSEILIEK-LGLEGRIEFLGFRS--DVPELL 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028513018 321 RRAFALVLPSRMEGwgLPIS--EALWCGTPALAADVPALREA-----GGDLaryFDPEKSAELADILGQLLANKS 388
Cdd:cd03808   262 AESDVFVLPSYREG--LPRSllEAMAAGRPVITTDVPGCRELvidgvNGFL---VPPGDVEALADAIEKLIEDPE 331
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 238-375 1.89e-04

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 43.43  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 238 EKRGPSGRYIFC-VGIYNGRKNLECVVEAMMSLHERGMDVpNLVLAGARRKRVEKflKNK-RFLPLSTKFHFVHNPNqaE 315
Cdd:cd03812   184 KLLILEDKLVLGhVGRFNEQKNHSFLIDIFEELKKKNPNV-KLVLVGEGELKEKI--KEKvKELGLEDKVIFLGFRN--D 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 316 LAELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALREAGGDLARYFDPEKSAE 375
Cdd:cd03812   259 VSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPS 318
PHA01633 PHA01633
putative glycosyl transferase group 1
 251-359 1.91e-04

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 43.43  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 251 GIYNG---RKNLECVVEAMMSLHERGMDVPnlvlagarrKRVEKF-LKNKRF--LPLSTKFHFV----HNPNQAELAeLY 320
Cdd:PHA01633  152 GIVSGltkRKNMDLMLQVFNELNTKYPDIA---------KKIHFFvISHKQFtqLEVPANVHFVaefgHNSREYIFA-FY 221

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1028513018 321 RRAFALVLPSRMEGWGLPISEALWCGTPALAADVPALRE 359
Cdd:PHA01633  222 GAMDFTIVPSGTEGFGMPVLESMAMGTPVIHQLMPPLDE 260
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 137-415 3.41e-04

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: 42.71  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 137 PKIMSDYLAALEARGTNVIFVPLLHDMIPLHDFT--HRNQFSFPKNFLHDNQVAIKASSLILTNSEfTAREvlHFSERGV 214
Cdd:cd03794   107 PPITLGLAALLLKKLRGAPFILDVRDLWPESLIAlgVLKKGSLLKLLKKLERKLYRLADAIIVLSP-GLKE--YLLRKGV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 215 LPpvSKVVAVPLCNEL-----RPTSESIEKRGPSGRYIFcvgIYNG----RKNLECVVEAMMSLHERgMDVpNLVLAG-- 283
Cdd:cd03794   184 PK--EKIIVIPNWADLeefkpPPKDELRKKLGLDDKFVV---VYAGnigkAQGLETLLEAAERLKRR-PDI-RFLFVGdg 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 284 ARRKRVEKFLKNKrflpLSTKFHFVHNPNQAELAELYRRAFALVLP---SRMEGWGLP--ISEALWCGTPALAADVPALR 358
Cdd:cd03794   257 DEKERLKELAKAR----GLDNVTFLGRVPKEEVPELLSAADVGLVPlkdNPANRGSSPskLFEYMAAGKPILASDDGGSD 332

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1028513018 359 EA--GGDLARYFDPEKSAELADILGQLLANKSEYDVLKAKIADARSSMRTWNDVASDLL 415
Cdd:cd03794   333 LAveINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 242-407 5.76e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 42.01  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 242 PSGRYIFCVGIYNGRKNLECVVEAMmslhERgmdVPNLVLA----GARRKRVEKFLKNkrflplsTKFHFVHNPNQAELA 317
Cdd:PLN02871  261 PEKPLIVYVGRLGAEKNLDFLKRVM----ER---LPGARLAfvgdGPYREELEKMFAG-------TPTVFTGMLQGDELS 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 318 ELYRRAFALVLPSRMEGWGLPISEALWCGTPALAADVPAL-----REAGGDLARYFDPEKSAELADILGQLLANKSeydv 392
Cdd:PLN02871  327 QAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIpdiipPDQEGKTGFLYTPGDVDDCVEKLETLLADPE---- 402

                         170
                  ....*....|....*.
gi 1028513018 393 LKAKIAD-ARSSMRTW 407
Cdd:PLN02871  403 LRERMGAaAREEVEKW 418
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
285-420 5.22e-03

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 38.76  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513018 285 RRKRVEKFLKNKRFLPL------------STKFHFVHNPNQAELAELYRRA-FALVLPSRM-EGWGLPIS--EALWCGTP 348
Cdd:COG4641   150 RRARLEELLLAPAGLRLkiygpgwpklalPANVRRGGHLPGEEHPAAYASSkITLNVNRMAaSPDSPTRRtfEAAACGAF 229

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028513018 349 ALAADVPALR---EAGGDLARYFDPEksaELADILGQLLANKSEYDvlkaKIADA--RSSMR--TWNDVASDLLQALDD 420
Cdd:COG4641   230 LLSDPWEGLEelfEPGEEVLVFRDGE---ELAEKLRYLLADPEERR----AIAEAgrRRVLAehTYAHRARELLAILEE 301
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH