NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1056863543|ref|WP_068280991|]
View 

MULTISPECIES: glycosyltransferase [Loigolactobacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 3-338 4.03e-71

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 cd03812:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 357  Bit Score: 226.40  E-value: 4.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGDFLHGSGVTSFILNAFGNINDQQIQFEALANAGS-SEMKAEIEAKyGWPMTVIPAANQGLHSHLKawhQFLKAN 81
Cdd:cd03812     1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDDkGEYDEELEEL-GGKIFYIPPKKKNIIKYFI---KLLKLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  82 R-GRYDAVHFNYSAMwNFLPLMMAKHYGAKQITLHSHNTyfgtdgSAAKLRVLKLLHNFGKWyVCHFVATDFVAVSKEAA 160
Cdd:cd03812    77 KkEKYDIVHVHGSSS-NGIILLLAAKAGVPVRIAHSHNT------KDSSIKLRKIRKNVLKK-LIERLSTKYLACSEDAG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 161 QWLFtgSIVKRQRYHLIRNGINLAKFNFDPEKRRRLRQAANLDGKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAILY 240
Cdd:cd03812   149 EWLF--GEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 241 LIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTIFPSAEIPLDRYDHE 320
Cdd:cd03812   227 LVGEGELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN 306

                         330
                  ....*....|....*...
gi 1056863543 321 IVFPISLSKSANQWAEVI 338
Cdd:cd03812   307 NVEFLPLNETPSTWAEKI 324
 
Name Accession Description Interval E-value
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 3-338 4.03e-71

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: 226.40  E-value: 4.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGDFLHGSGVTSFILNAFGNINDQQIQFEALANAGS-SEMKAEIEAKyGWPMTVIPAANQGLHSHLKawhQFLKAN 81
Cdd:cd03812     1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDDkGEYDEELEEL-GGKIFYIPPKKKNIIKYFI---KLLKLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  82 R-GRYDAVHFNYSAMwNFLPLMMAKHYGAKQITLHSHNTyfgtdgSAAKLRVLKLLHNFGKWyVCHFVATDFVAVSKEAA 160
Cdd:cd03812    77 KkEKYDIVHVHGSSS-NGIILLLAAKAGVPVRIAHSHNT------KDSSIKLRKIRKNVLKK-LIERLSTKYLACSEDAG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 161 QWLFtgSIVKRQRYHLIRNGINLAKFNFDPEKRRRLRQAANLDGKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAILY 240
Cdd:cd03812   149 EWLF--GEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 241 LIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTIFPSAEIPLDRYDHE 320
Cdd:cd03812   227 LVGEGELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN 306

                         330
                  ....*....|....*...
gi 1056863543 321 IVFPISLSKSANQWAEVI 338
Cdd:cd03812   307 NVEFLPLNETPSTWAEKI 324
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
211-304 2.69e-22

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 91.42  E-value: 2.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 211 VGVF-EKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQqvkAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLH 289
Cdd:pfam13692   7 VGRLhPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEEL---AAGLEDRVIFTGFVEDLAELLAAADVFVLPSLY 83

                          90
                  ....*....|....*
gi 1056863543 290 EGLSMVFVEAQAAGL 304
Cdd:pfam13692  84 EGFGLKLLEAMAAGL 98
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 152-306 1.04e-08

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 56.97  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 152 FVAVSKEAAQ----WLFtgsiVKRQRYHLIRNGINLAKFNFDPEKRRRLRQ--AANLDGKHVYANVGVFEKRKNQQFLIK 225
Cdd:PRK15179  462 LSSNSQFAAHryadWLG----VDERRIPVVYNGLAPLKSVQDDACTAMMAQfdARTSDARFTVGTVMRVDDNKRPFLWVE 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 226 IFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLT 305
Cdd:PRK15179  538 AAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVP 617


                  .
gi 1056863543 306 I 306
Cdd:PRK15179  618 V 618
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 276-373 8.79e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 44.60  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 276 LYQVMDYLIFPSLHEGLSMVFVEAQAAGLTI--FPSAEIP--LDRYDHEIVFPislSKSANQWAEVIGQ-HQNSERRQGH 350
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPViaTDVGGLPevIEDGETGLLVP---PGDPEALAEAILRlLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*.
gi 1056863543 351 IAALRRL---GYDEKQTVKAIHALYQ 373
Cdd:COG0438    94 GEAARERaeeRFSWEAIAERLLALYE 119
 
Name Accession Description Interval E-value
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 3-338 4.03e-71

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: 226.40  E-value: 4.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGDFLHGSGVTSFILNAFGNINDQQIQFEALANAGS-SEMKAEIEAKyGWPMTVIPAANQGLHSHLKawhQFLKAN 81
Cdd:cd03812     1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDDkGEYDEELEEL-GGKIFYIPPKKKNIIKYFI---KLLKLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  82 R-GRYDAVHFNYSAMwNFLPLMMAKHYGAKQITLHSHNTyfgtdgSAAKLRVLKLLHNFGKWyVCHFVATDFVAVSKEAA 160
Cdd:cd03812    77 KkEKYDIVHVHGSSS-NGIILLLAAKAGVPVRIAHSHNT------KDSSIKLRKIRKNVLKK-LIERLSTKYLACSEDAG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 161 QWLFtgSIVKRQRYHLIRNGINLAKFNFDPEKRRRLRQAANLDGKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAILY 240
Cdd:cd03812   149 EWLF--GEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 241 LIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTIFPSAEIPLDRYDHE 320
Cdd:cd03812   227 LVGEGELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN 306

                         330
                  ....*....|....*...
gi 1056863543 321 IVFPISLSKSANQWAEVI 338
Cdd:cd03812   307 NVEFLPLNETPSTWAEKI 324
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-373 1.11e-32

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: 125.73  E-value: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGDFL--HGSGVTSFILNAFGNINDQQIQFEALANAGSSEMKAEIEAKYGWPMTVIPAANQGLHSHLKAWHQFLKa 80
Cdd:cd03801     1 KILLLSPELppPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  81 nRGRYDAVHFNYSAMWNFLPLMmAKHYGAKQI-TLHSHNTYFGTDGSAAKLRVLKllhnfgKWYVCHFVATDFVAVSKEA 159
Cdd:cd03801    80 -LRKFDVVHAHGLLAALLAALL-ALLLGAPLVvTLHGAEPGRLLLLLAAERRLLA------RAEALLRRADAVIAVSEAL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 160 AQWLFTGSIVKRQRYHLIRNGINLAKFNFDPEKRRRLRqaanlDGKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAIL 239
Cdd:cd03801   152 RDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLGIP-----PDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 240 YLIG-TGPLETLLKQQvkAAKLTDQVQFLGRRS--DMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTI--FPSAEIP- 313
Cdd:cd03801   227 VIVGgDGPLRAELEEL--ELGLGDRVRFLGFVPdeELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVvaTDVGGLPe 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056863543 314 -LDRYDHEIVFPISLSKS-ANQWAEVIGQHQNSERRQGHIAALRRLGYDEKQTVKAIHALYQ 373
Cdd:cd03801   305 vVEDGEGGLVVPPDDVEAlADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 82-338 9.45e-32

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: 122.81  E-value: 9.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  82 RGRYDAVH-FNYSAMwnFLPLMMAKHYGAKQITLHSHNTYFGTDGSAAKLRVLKLLHNFGKWYVChfvatdfvaVSKEAA 160
Cdd:cd03807    77 KRNPDVVHtWMYHAD--LIGGLAAKLAGGVKVIWSVRSSNIPQRLTRLVRKLCLLLSKFSPATVA---------NSSAVA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 161 QWLFTGSIVKRQRYhLIRNGINLAKFNFDPEKRRRLRQAANLDGK-HVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAIL 239
Cdd:cd03807   146 EFHQEQGYAKNKIV-VIYNGIDLFKLSPDDASRARARRRLGLAEDrRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRL 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 240 YLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTIF-----PSAEIPL 314
Cdd:cd03807   225 LLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVatdvgGAAELVD 304

                         250       260
                  ....*....|....*....|....
gi 1056863543 315 DRydHEIVFPislSKSANQWAEVI 338
Cdd:cd03807   305 DG--TGFLVP---AGDPQALADAI 323
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 3-306 1.19e-31

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: 122.47  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGDFLHGSGVTSFILNAFGNINDQQIQFEALANAGSSEMKAEIEAKYGWPMTVIPAANQgLHSHLKAWHQFLK--A 80
Cdd:cd03811     1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKL-IKLGLLKAILKLKriL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  81 NRGRYDAVH---FNYSAMWNFLPLMMAKHYGakqitlHSHNTYFGTDGSAAKLRVLKLLHNFGKWYVChfvatdfvaVSK 157
Cdd:cd03811    80 KRAKPDVVIsflGFATYIVAKLAAARSKVIA------WIHSSLSKLYYLKKKLLLKLKLYKKADKIVC---------VSK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 158 EAAQWLFTGSIVKRQRYHLIRNGINLAKFNFDPEKRRRLRQAanlDGKHVYAnVGVFEKRKNQQFLIKIFAKIAVQDPQA 237
Cdd:cd03811   145 GIKEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILNEPE---DGPVILA-VGRLDPQKGHDLLIEAFAKLRKKYPDV 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1056863543 238 ILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTI 306
Cdd:cd03811   221 KLVILGDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPV 289
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 55-373 9.53e-25

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: 103.61  E-value: 9.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  55 WPMTVIPAANQGLHSHLKAWHQFLK-ANRGRYDAVHFNYsAMWNflPLMMAKHYGAKQ----ITLHshntyfGTDgsAAK 129
Cdd:cd03798    65 RLLPLKPRLRLLAPLRAPSLAKLLKrRRRGPPDLIHAHF-AYPA--GFAAALLARLYGvpyvVTEH------GSD--INV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 130 LRVLKLLHNFGKWYVCHFVATdfVAVSKEAAQwLFTGSIVKRQRYHLIRNGINLAKFNFDPekrRRLRqaANLDGKhVYA 209
Cdd:cd03798   134 FPPRSLLRKLLRWALRRAARV--IAVSKALAE-ELVALGVPRDRVDVIPNGVDPARFQPED---RGLG--LPLDAF-VIL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 210 NVGVFEKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRS--DMADLYQVMDYLIFPS 287
Cdd:cd03798   205 FVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPheQVPAYYRACDVFVLPS 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 288 LHEGLSMVFVEAQAAGLTIFPSA-----EIPLDRYDHEIVFPislsKSANQWAEVIGQHQNSERRQGHIAALRRLG---Y 359
Cdd:cd03798   285 RHEGFGLVLLEAMACGLPVVATDvggipEVVGDPETGLLVPP----GDADALAAALRRALAEPYLRELGEAARARVaerF 360

                         330
                  ....*....|....
gi 1056863543 360 DEKQTVKAIHALYQ 373
Cdd:cd03798   361 SWVKAADRIAAAYR 374
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 54-303 3.90e-24

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: 101.66  E-value: 3.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  54 GWPMTVIPAANQGLHsHLKAW---HQFLKANRGRY----------------DAVHFNYSAMwNFLPLMMAKHYGAKqITL 114
Cdd:cd03819    28 GHRVLVVTAGGPLLP-RLRQIgigLPGLKVPLLRAllgnvrlarlirreriDLIHAHSRAP-AWLGWLASRLTGVP-LVT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 115 HSHNtyfgtdgsaakLRVLKLLHNFGKWYVChfVATDFV-AVSKEAAQWLFTGSIVKRQRYHLIRNGINLAKFNFDPEKR 193
Cdd:cd03819   105 TVHG-----------SYLATYHPKDFALAVR--ARGDRViAVSELVRDHLIEALGVDPERIRVIPNGVDTDRFPPEAEAE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 194 RRLRQAANLDGKHVyANVGVFEKRKNQQFLIKIFAKIAVQDPQAILyLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDM 273
Cdd:cd03819   172 ERAQLGLPEGKPVV-GYVGRLSPEKGWLLLVDAAAELKDEPDFRLL-VAGDGPERDEIRRLVERLGLRDRVTFTGFREDV 249

                         250       260       270
                  ....*....|....*....|....*....|
gi 1056863543 274 ADLYQVMDYLIFPSLHEGLSMVFVEAQAAG 303
Cdd:cd03819   250 PAALAASDVVVLPSLHEEFGRVALEAMACG 279
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 3-304 6.19e-23

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: 98.44  E-value: 6.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGdfLHGSGVTSFILNAFGNINDQQIQFEALANaGSSEMKAEIEaKYGWPMTVIPAANQGLHS-----HLKAWHQF 77
Cdd:cd03808     1 KILFIV--NVDGGFQSFRLPLIKALVKKGYEVHVIAP-DGDKLSDELK-ELGVKVIDIPILRRGINPlkdlkALFKLYKL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  78 LKanRGRYDAVHfNYSAMWNFLPLMMAKHYGAKQI--TLHSHNTYFGTDGSAAKL--RVLKLLHNFgkwyvchfvATDFV 153
Cdd:cd03808    77 LK--KEKPDIVH-CHTPKPGILGRLAARLAGVPKViyTVHGLGFVFTEGKLLRLLylLLEKLALLF---------TDKVI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 154 AVSKEAAQWLFTGSIVKRQRYHLIR-NGINLAKFNFDPEkrrrlrqaANLDGKHVYANVGVFEKRKNQQFLIKIFAKIAV 232
Cdd:cd03808   145 FVNEDDRDLAIKKGIIKKKKTVLIPgSGVDLDRFQYSPE--------SLPSEKVVFLFVARLLKDKGIDELIEAAKILKK 216

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056863543 233 QDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGL 304
Cdd:cd03808   217 KGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGR 288
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 48-306 8.57e-23

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: 98.12  E-value: 8.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  48 EIEAKYGWPMTVIPAanqglhshlkawHQFLKANRGrYDAVHFN--YSAMwnFLPLMMAKHYGAKQI-TLH---SHNTYF 121
Cdd:cd03817    61 RKYHRQHIPFPFKKA------------VIDRIKELG-PDIIHTHtpFSLG--KLGLRIARKLKIPIVhTYHtmyEDYLHY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 122 GTDGsaaKLRVLKLLHNFGKWYVCHFVAtdFVAVSKEAAQwLFTGSIVKRqRYHLIRNGINLAKFNFDPEKRRRlRQAAN 201
Cdd:cd03817   126 IPKG---KLLVKAVVRKLVRRFYNHTDA--VIAPSEKIKD-TLREYGVKG-PIEVIPNGIDLDKFEKPLNTEER-RKLGL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 202 LDGKHVYANVGVFEKRKNQQFLIKIFAKIaVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGR--RSDMADLYQV 279
Cdd:cd03817   198 PPDEPILLYVGRLAKEKNIDFLLRAFAEL-KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFvpREELPEYYKA 276

                         250       260
                  ....*....|....*....|....*..
gi 1056863543 280 MDYLIFPSLHEGLSMVFVEAQAAGLTI 306
Cdd:cd03817   277 ADLFVFASTTETQGLVYLEAMAAGLPV 303
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
211-304 2.69e-22

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 91.42  E-value: 2.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 211 VGVF-EKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQqvkAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLH 289
Cdd:pfam13692   7 VGRLhPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEEL---AAGLEDRVIFTGFVEDLAELLAAADVFVLPSLY 83

                          90
                  ....*....|....*
gi 1056863543 290 EGLSMVFVEAQAAGL 304
Cdd:pfam13692  84 EGFGLKLLEAMAAGL 98
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 150-338 2.01e-21

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: 94.05  E-value: 2.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 150 TDFVA-----VSKEAAQWLFTGSIVKRQRYHLIRNGINLAKFNFDPEKRRRLRQAANL-DGKHVYANVGVFEKRKNQQFL 223
Cdd:cd04951   127 TDFLCdittnVSREALDEFIAKKAFSKNKSVPVYNGIDLNKFKKDINVRLKIRNKLNLkNDEFVILNVGRLTEAKDYPNL 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 224 IKIFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAG 303
Cdd:cd04951   207 LLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACE 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1056863543 304 LTIFPS-----AEIpLDryDHEIVFPIS-LSKSANQWAEVI 338
Cdd:cd04951   287 RPVVATdaggvAEV-VG--DHNYVVPVSdPQLLAEKIKEIF 324
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 76-310 9.74e-20

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: 89.61  E-value: 9.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  76 QFLKANRGRYDAVHFNYsAMWNFLPLMMAKHYGAKQI-TLHS----HNTYFGT-DGSAAKLRV---LKLLHNfgkwyvch 146
Cdd:cd03800    93 RFIAREGGRYDLIHSHY-WDSGLVGALLARRLGVPLVhTFHSlgrvKYRHLGAqDTYHPSLRItaeEQILEA-------- 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 147 fvaTDFVAVS-KEAAQWLFTGSIVKRQRYHLIRNGINLAKFNFDPEKRRRLRQAANLDGKHVYANVGVFEKRKNQQFLIK 225
Cdd:cd03800   164 ---ADRVIAStPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVR 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 226 IFAKIAVQDPQAILYLIG---TGPLET---LLKQQVKAAKLTDQVQFLGR--RSDMADLYQVMDYLIFPSLHEGLSMVFV 297
Cdd:cd03800   241 AFAQLPELRELANLVLVGgpsDDPLSMdreELAELAEELGLIDRVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAI 320

                         250
                  ....*....|...
gi 1056863543 298 EAQAAGLTIFPSA 310
Cdd:cd03800   321 EAMACGTPVVATA 333
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 204-338 3.71e-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: 3.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 204 GKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRS--DMADLYQVMD 281
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056863543 282 YLIFPSLHEGLSMVFVEAQAAGLTIFPS-----AEIPLDRYDHEIVFPislsKSANQWAEVI 338
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASdvggpPEVVKDGETGFLVKP----NNAEALAEAI 138
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 197-306 9.87e-18

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: 83.44  E-value: 9.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 197 RQAANLDGKHVYAnVGVFEKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADL 276
Cdd:cd03820   174 EPSTNLKSKRILA-VGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEE 252

                          90       100       110
                  ....*....|....*....|....*....|
gi 1056863543 277 YQVMDYLIFPSLHEGLSMVFVEAQAAGLTI 306
Cdd:cd03820   253 YANSSIFVLSSRYEGFPMVLLEAMAYGLPI 282
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 3-306 5.41e-17

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: 81.26  E-value: 5.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGDFL--HGSGV---TSFILNAFGNINDQQIQFEAlanagsSEMKAEIEAKYGWPMTVIPAANQGLHSHLKAWHQF 77
Cdd:cd03809     1 KILIDGRSLaqRLTGIgryTRELLKALAKNDPDESVLAV------PPLPGELLRLLREYPELSLGVIKIKLWRELALLRW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  78 LKANRGR--YDAVHFNYSamwNFLPLmmaKHYGAKQI-TLH-----SHNTYFGTDGSAA-KLRVLKLLHNfgkwyvchfv 148
Cdd:cd03809    75 LQILLPKkdKPDLLHSPH---NTAPL---LLKGCPQVvTIHdliplRYPEFFPKRFRLYyRLLLPISLRR---------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 149 ATDFVAVSKEAAQWLFTGSIVKRQRYHLIRNGINlaKFNFDPEKRRRLRQAANLDGKHVYAnVGVFEKRKNQQFLIKIFA 228
Cdd:cd03809   139 ADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVD--PSFFPPESAAVLIAKYLLPEPYFLY-VGTLEPRKNHERLLKAFA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 229 KIAVQDPQAILYLIGTGPLETL-LKQQVKAAKLTDQVQFLGRRSDM--ADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLT 305
Cdd:cd03809   216 LLKKQGGDLKLVIVGGKGWEDEeLLDLVKKLGLGGRVRFLGYVSDEdlPALYRGARAFVFPSLYEGFGLPVLEAMACGTP 295


                  .
gi 1056863543 306 I 306
Cdd:cd03809   296 V 296
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 177-303 3.30e-13

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: 70.07  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 177 IRNGINLAKFNFDPeKRRRLRQAANLDGKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPqAILYLIGTGPLETLLKQQVK 256
Cdd:cd04962   169 IHNFIDEDVFKRKP-AGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIP-AKLLLVGDGPERVPAEELAR 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1056863543 257 AAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAG 303
Cdd:cd04962   247 ELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACG 293
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 149-310 1.20e-12

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: 68.25  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 149 ATDFVAVS---KEAAqwLFTGSIVKRQRYHLIrnGINLAKFNFDPEKRRrlrqaanldgKHVYANVGVFEKRKNQQFLIK 225
Cdd:cd05844   144 AALFVAVSgfiRDRL--LARGLPAERIHVHYI--GIDPAKFAPRDPAER----------APTILFVGRLVEKKGCDVLIE 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 226 IFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAkltDQVQFLGR--RSDMADLYQVMDYLIFPSL------HEGLSMVFV 297
Cdd:cd05844   210 AFRRLAARHPTARLVIAGDGPLRPALQALAAAL---GRVRFLGAlpHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLL 286

                         170
                  ....*....|...
gi 1056863543 298 EAQAAGLTIFPSA 310
Cdd:cd05844   287 EAAACGVPVVSSR 299
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 211-304 6.61e-11

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: 61.65  E-value: 6.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 211 VGVFEKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLG---RRSDMADLYQVMDYLIFPS 287
Cdd:cd01635   116 VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGglvDDEVLELLLAAADVFVLPS 195

                          90
                  ....*....|....*..
gi 1056863543 288 LHEGLSMVFVEAQAAGL 304
Cdd:cd01635   196 RSEGFGLVLLEAMAAGK 212
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 71-306 8.11e-11

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: 62.74  E-value: 8.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  71 LKAWHqFLKANRGRYDAVH-FNYSAMWNFLPLMMAKHYGAKQItLHSHNTYF--GTDGSAAKLRVLKLLHNFGKWYVCHF 147
Cdd:cd03794    86 LAALL-KLLVREERPDVIIaYSPPITLGLAALLLKKLRGAPFI-LDVRDLWPesLIALGVLKKGSLLKLLKKLERKLYRL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 148 VATdFVAVSKEAAQWLFTGSIvKRQRYHLIRNGINLAkfNFDPEKRRRLRQAANLDGKHVYANVGVFEKRKNQQFLIKIF 227
Cdd:cd03794   164 ADA-IIVLSPGLKEYLLRKGV-PKEKIIVIPNWADLE--EFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAA 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 228 AKIAvQDPQAILYLIGTGPLETLLKQQVKAAKLTDqVQFLGR--RSDMADLYQVMDYLIFPsLHEGLSMV------FVEA 299
Cdd:cd03794   240 ERLK-RRPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRvpKEEVPELLSAADVGLVP-LKDNPANRgsspskLFEY 316


                  ....*..
gi 1056863543 300 QAAGLTI 306
Cdd:cd03794   317 MAAGKPI 323
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 176-340 1.07e-10

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: 62.39  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 176 LIRNGINLAkfNFDPEKRRRlRQAANLDGKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQQV 255
Cdd:cd03821   178 VIPNGVDIP--EFDPGLRDR-RKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAYPAFLQL 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 256 KAAK-LTDQVQFLGRRSDMA--DLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTIFPSAEIPL-DRYDHEIVFPISLSKSA 331
Cdd:cd03821   255 QSSLgLGDRVTFTGPLYGEAkwALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLsELVEAGCGVVVDPNVSS 334


                  ....*....
gi 1056863543 332 nqWAEVIGQ 340
Cdd:cd03821   335 --LAEALAE 341
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 171-313 1.65e-09

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: 58.82  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 171 RQRYHLIRNGINLAKFNFDPEKRRRLRQaaNLDGKHVYANVGVFEKRKNQQFLIKifakiAVQDPQAILYLIGTGPLETL 250
Cdd:cd03795   159 KNKVRVIPLGIDKNVYNIPRVDFENIKR--EKKGKKIFLFIGRLVYYKGLDYLIE-----AAQYLNYPIVIGGEGPLKPD 231

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056863543 251 LKQQVKAAKLtDQVQFLGRRSD--MADLYQVMDYLIFPSL--HEGLSMVFVEAQAAGLTIFpSAEIP 313
Cdd:cd03795   232 LEAQIELNLL-DNVKFLGRVDDeeKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVI-STNIG 296
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 147-368 3.54e-09

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 57.69  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 147 FVATdfVAVSKEAAQWLFtgsivkrQRYHLIRNGINLAKFNfdPEKRRR-LRQAANLDGKHVYANVGVFEKRKNQQFLIK 225
Cdd:cd03814   150 LVPS--PSIARELEGHGF-------ERVRLWPRGVDTELFH--PSRRDAaLRRRLGPPGRPLLLYVGRLAPEKNLEALLD 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 226 IFAKIAVQDPQAILyLIGTGPLETLLKQQvkaaklTDQVQFLG--RRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAG 303
Cdd:cd03814   219 ADLPLAASPPVRLV-VVGDGPARAELEAR------GPDVIFTGflTGEELARAYASADVFVFPSRTETFGLVVLEAMASG 291

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056863543 304 L-TIFPSAEIPLDRYDHEIVFPISLSKSANQWAEVIGQ-HQNSERRQGhiAALRRLGYDEKQTVKAI 368
Cdd:cd03814   292 LpVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRAlLEDPELRRR--MAARARAEAERYSWEAF 356
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 3-372 5.03e-09

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: 57.34  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543   3 RVLIVGDF---LHGSGVTSFILNAFGNINDQQIQFEALA--NAGSSEMKAEIEAKYGWPMTVIPAANQGLHSHLKAWHQF 77
Cdd:cd03823     1 KILLVNSLyppQRVGGAEISVHDLAEALVAEGHEVAVLTagVGPPGQATVARSVVRYRRAPDETLPLALKRRGYELFETY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  78 LKANRGRY---------DAVHFNYSAMWNFLPLMMAKHYGAKQI-TLHShntYFGTDGSAAKLRVLKLLhnfgkwyvchf 147
Cdd:cd03823    81 NPGLRRLLarlledfrpDVVHTHNLSGLGASLLDAARDLGIPVVhTLHD---YWLLCPRQFLFKKGGDA----------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 148 vatdFVAVSKEAAQwLFTGSIVKRQRYHLIRNGINlakfnfdPEKRRRLRQAANlDGKHVYANVGVFEKRKNQQFLIKIF 227
Cdd:cd03823   147 ----VLAPSRFTAN-LHEANGLFSARISVIPNAVE-------PDLAPPPRRRPG-TERLRFGYIGRLTEEKGIDLLVEAF 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 228 AKIAvqDPQAILYLIGTGPLEtllkqQVKAAKLTDQVQFLGR--RSDMADLYQVMDYLIFPSL-HEGLSMVFVEAQAAGL 304
Cdd:cd03823   214 KRLP--REDIELVIAGHGPLS-----DERQIEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGL 286

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056863543 305 TIFPS-----AEIPLDRYDhEIVFPISlskSANQWAEVIgqhqnsERRQGHIAALRRL--GYDEKQTVKAIHALY 372
Cdd:cd03823   287 PVIASdlggiAELIQPGVN-GLLFAPG---DAEDLAAAM------RRLLTDPALLERLraGAEPPRSTESQAEEY 351
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 152-306 1.04e-08

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 56.97  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 152 FVAVSKEAAQ----WLFtgsiVKRQRYHLIRNGINLAKFNFDPEKRRRLRQ--AANLDGKHVYANVGVFEKRKNQQFLIK 225
Cdd:PRK15179  462 LSSNSQFAAHryadWLG----VDERRIPVVYNGLAPLKSVQDDACTAMMAQfdARTSDARFTVGTVMRVDDNKRPFLWVE 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 226 IFAKIAVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLT 305
Cdd:PRK15179  538 AAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVP 617


                  .
gi 1056863543 306 I 306
Cdd:PRK15179  618 V 618
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 177-304 9.92e-08

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: 53.49  E-value: 9.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 177 IRNGINLAKFNfDPEKRRRLRqaanlDGKHVyANVGVFEKRKNQQFLIKIFAKIAVQDPQAILYLIGtGPLETLL----- 251
Cdd:cd03813   272 IPNGIDIQRFA-PAREERPEK-----EPPVV-GLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIG-PEDEDPEyaqec 343

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1056863543 252 KQQVKAAKLTDQVQFLGRRsDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGL 304
Cdd:cd03813   344 KRLVASLGLENKVKFLGFQ-NIKEYYPKLGLLVLTSISEGQPLVILEAMASGV 395
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 178-306 3.88e-07

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 51.30  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 178 RNGINLAKFNFDPekrRRLrqaaNLDGKHVYANVGVFEKRKNQQFLIKIFAKIAVQDPQAILYLIGTGPLETLLKQQVKA 257
Cdd:cd03799   154 RSGIDCNKFRFKP---RYL----PLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQE 226

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1056863543 258 AKLTDQVQFLGRRSDmADLYQVMDY---LIFPSL------HEGLSMVFVEAQAAGLTI 306
Cdd:cd03799   227 LNIGDCVKLLGWKPQ-EEIIEILDEadiFIAPSVtaadgdQDGPPNTLKEAMAMGLPV 283
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 146-304 7.36e-07

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 50.41  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 146 HFVATDFVAVSkeAAQWL---FTGS-IVKRQRYHLIRNGINLAKFNFDPekRRRLRQAANLDGKH---VYANVGVFEKRK 218
Cdd:cd03825   133 ALAKKRLTIVA--PSRWLadmVRRSpLLKGLPVVVIPNGIDTEIFAPVD--KAKARKRLGIPQDKkviLFGAESVTKPRK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 219 NQQFLIKIFAKIAvQDPQAILYLIGTGPLETLLK--QQVKAAKLTDQVQflgrrsdMADLYQVMDYLIFPSLHEGLSMVF 296
Cdd:cd03825   209 GFDELIEALKLLA-TKDDLLLVVFGKNDPQIVILpfDIISLGYIDDDEQ-------LVDIYSAADLFVHPSLADNLPNTL 280


                  ....*...
gi 1056863543 297 VEAQAAGL 304
Cdd:cd03825   281 LEAMACGT 288
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 151-304 1.28e-06

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 49.61  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 151 DFVAVSKEAAQWLFTGSIVKRQRYHLIRNGInlakfnFDPEKRRRLRQAANldgKHVYANVGVFEKRKNQQFLIKIFAKI 230
Cdd:cd04949   115 DAIIVSTEQQKQDLSERFNKYPPIFTIPVGY------VDQLDTAESNHERK---SNKIITISRLAPEKQLDHLIEAVAKA 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1056863543 231 AVQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGL 304
Cdd:cd04949   186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGL 259
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 81-348 2.04e-06

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 49.31  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  81 NRGRYDAVHFNY-------SAMWNFLPLMmaKHYGAKQITLhSHNTYFGTDGSAAKLRVLKLLHNFGKWYVCHFVATDFV 153
Cdd:cd03822    72 NFKKPDVVHIQHefgifggKYGLYALGLL--LHLRIPVITT-LHTVLDLSDPGKQALKVLFRIATLSERVVVMAPISRFL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 154 AVSKeaaqwlftgSIVKRQRYHLIRNGINLAKFNfdpeKRRRLRQAANLDGKHVYANVGVFEKRKNQQFLIKIFAKIaVQ 233
Cdd:cd03822   149 LVRI---------KLIPAVNIEVIPHGVPEVPQD----PTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPEL-KA 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 234 DPQAILYLIGTGPLETLLKQQVKAAK--------LTDQVQFLGRRSDMADLY---QVMDYLIFP--SLHEGLSMVFVEAQ 300
Cdd:cd03822   215 EFPDVRLVIAGELHPSLARYEGERYRkaaieelgLQDHVDFHNNFLPEEEVPryiSAADVVVLPylNTEQSSSGTLSYAI 294

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1056863543 301 AAGLTI----FPSAEIPLDRyDHEIVFPIslsKSANQWAEVIGQHQNSERRQ 348
Cdd:cd03822   295 ACGKPVistpLRHAEELLAD-GRGVLVPF---DDPSAIAEAILRLLEDDERR 342
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
15-184 5.40e-06

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 46.37  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  15 GVTSFILNAFGNINDQQIQFEALANAGSSEMKAEIEAKYGWPMTVIPAANQGLHSHLKAWHQFLKANRGRYDAVHFNYSA 94
Cdd:pfam13439   2 GVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543  95 MWNFLPLMMAKHYGAKQITlHSHNTYFGTDGSAAKLRVLK-LLHNFGKWYVCHFVAtdFVAVSKEAAQWLFTGSIVKRQR 173
Cdd:pfam13439  82 PLGLAALAARLRLGIPLVV-TYHGLFPDYKRLGARLSPLRrLLRRLERRLLRRADR--VIAVSEAVADELRRLYGVPPEK 158

                         170
                  ....*....|.
gi 1056863543 174 YHLIRNGINLA 184
Cdd:pfam13439 159 IRVIPNGVDLE 169
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 276-373 8.79e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 44.60  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 276 LYQVMDYLIFPSLHEGLSMVFVEAQAAGLTI--FPSAEIP--LDRYDHEIVFPislSKSANQWAEVIGQ-HQNSERRQGH 350
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPViaTDVGGLPevIEDGETGLLVP---PGDPEALAEAILRlLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*.
gi 1056863543 351 IAALRRL---GYDEKQTVKAIHALYQ 373
Cdd:COG0438    94 GEAARERaeeRFSWEAIAERLLALYE 119
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
155-309 1.05e-03

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 40.84  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 155 VSKEAAQWLftgsIVKRQRYHLIRNGINLAKFNFDPEKRRRLRQA---ANLDGKHVYANVGVFEKRKNQQFLIKIFAKIA 231
Cdd:PRK15490  349 VTRHYADWL----KLEAKHFQVVYNGVLPPSTEPSSEVPHKIWQQftqKTQDADTTIGGVFRFVGDKNPFAWIDFAARYL 424

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1056863543 232 VQDPQAILYLIGTGPLETLLKQQVKAAKLTDQVQFLGRRSDMADLYQVMDYLIFPSLHEGLSMVFVEAQAAGLTIFPS 309
Cdd:PRK15490  425 QHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVIST 502
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
169-309 3.96e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 38.92  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056863543 169 VKRQRYHLIRNGINLAKFNFDPEKRRrlrQAANLdgkhVYANVGVFEKRKNQQFLIKIFAKIavqDPQAILYLIGTGPLE 248
Cdd:PRK09922  153 ISAQRISVIYNPVEIKTIIIPPPERD---KPAVF----LYVGRLKFEGQKNVKELFDGLSQT---TGEWQLHIIGDGSDF 222

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056863543 249 TLLKQQVKAAKLTDQVQFLGRRSD-----MADLYQVmDYLIFPSLHEGLSMVFVEAQAAGLTIFPS 309
Cdd:PRK09922  223 EKCKAYSRELGIEQRIIWHGWQSQpwevvQQKIKNV-SALLLTSKFEGFPMTLLEAMSYGIPCISS 287
 
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