|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-376 |
1.52e-72 |
|
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: 231.66 E-value: 1.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 2 RIYFIGQKGiPASYGGVEHHVEQLASRLAKKGHEVYVYCRPWYQNLVFQNKKVPKTYQKIKLLNNPSINtKNLDAITstf 81
Cdd:cd03801 1 KILLLSPEL-PPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRAR-RLLRELR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 82 tatMNVLTRKADVIHYHGIGPSSLLFIPKLLKtKSRIVATFHC-KDYEHQKWSFLARSYLKFGEHVCVKIpNGTIAVSKT 160
Cdd:cd03801 76 ---PLLRLRKFDVVHAHGLLAALLAALLALLL-GAPLVVTLHGaEPGRLLLLLAAERRLLARAEALLRRA-DAVIAVSEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 161 IQEYVREKYH---KKITYIPNGVPLFTKEKAKNIKDWGLEKDKYILTVARLVKHKNIHTLIKAYQLLFPKPNktNPKLVI 237
Cdd:cd03801 151 LRDELRALGGippEKIVVIPNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP--DVRLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 238 VGGKADgsgQYEDYLKNLAKEDPNIIFTGFQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENLE- 316
Cdd:cd03801 229 VGGDGP---LRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEv 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818302960 317 -PLSDFGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEKTDEFYE 376
Cdd:cd03801 306 vEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4-like |
cd04955 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
3-379 |
2.39e-42 |
|
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 in certain bacteria and Archaea.
Pssm-ID: 340858 [Multi-domain] Cd Length: 379 Bit Score: 152.66 E-value: 2.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 3 IYFIGQKGIPASYGGVEHHVEQLASRLAKKGHEVYVYCRPwyqnlvFQNKKVPKTYQKIKLLNNPSINTKNLDAITSTFt 82
Cdd:cd04955 2 IFIIGSRGLPAKYGGFETFVEKLTERQQSDNIKYHVACLS------ENSKQQHFEYNGADCFYVKVPKIGPARAIAYDI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 83 ATMNVLTR-------KADVIHYHG--IGPSSLLFIPKLLKTKSRIVATFHCKDYEHQKWSFLARSYLKFGEHVCVKIPNG 153
Cdd:cd04955 75 AALNYALKyikeqniKNPIFYILAcrIGPFIAPYIKKIHKLGGKLFVNPDGLEWKRAKWSLPVRKYWKFSESLMVKHADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 154 TIAVSKTIQEYVREKYHK-KITYIPNGVPLF------TKEKAKNI-KDWGLEKDKYILTVARLVKHKNIHTLIKAyqllF 225
Cdd:cd04955 155 LICDSKNIEKYIRKEYGKsNTTFIAYGTDTLksslsdEDEKVREWyKEKGVKPGKYYLIVGRFVPENNYETMIRE----F 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 226 PKPNkTNPKLVIVgGKADGSGQYEDYLKNLA-KEDPNIIFTG-FQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYS 303
Cdd:cd04955 231 MKSS-TKRDLVII-TNVEGNAYYELLLKKTAfDHDERIKFVGtVYDQELLKYIRENAFAYLHGHEVGGTNPSLLEALGST 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818302960 304 NCVLASNIPENLEPLSDFGFSFKVGNVDDLKEKLVNLlhKPKLIKETGEKARLYVRKKYSWDQIVEKtdefYENLY 379
Cdd:cd04955 309 DLNLLLDVGFNREVAEDAALYWKKEPLASLIDEVDNL--NPDEISDLGKKAKQRIEEAYTWEKIVDE----YEELF 378
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
13-362 |
5.27e-39 |
|
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: 143.27 E-value: 5.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 13 ASYGGVEHHVEQLASRLAKKGHEVYVYCRPWYQNLVFQ-NKKVPKTYQKIKLLNnpsINTKNLDAITSTFTAtmNVLTRK 91
Cdd:cd03811 9 LSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQlNGDVKLIRLLIRVLK---LIKLGLLKAILKLKR--ILKRAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 92 ADVIHYHGigPSSLLFIPKLLKTKSRIVATFHC---KDYEHQKWSFLARSYLKFGEHVcvkipngtIAVSKTIQEYVREK 168
Cdd:cd03811 84 PDVVISFL--GFATYIVAKLAAARSKVIAWIHSslsKLYYLKKKLLLKLKLYKKADKI--------VCVSKGIKEDLIRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 169 YH---KKITYIPNGVPlFTKEKAKNIKDWGLEKD--KYILTVARLVKHKNIHTLIKAYQLLfpKPNKTNPKLVIVGGkad 243
Cdd:cd03811 154 GPsppEKIEVIYNPID-IDRIRALAKEPILNEPEdgPVILAVGRLDPQKGHDLLIEAFAKL--RKKYPDVKLVILGD--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 244 gsGQYEDYLKNLAKE---DPNIIFTGFQtgetlaelfSNTY-------LYVHPSAAEGLPIAVLEAMAYSNCVLASNIPE 313
Cdd:cd03811 228 --GPLREELEKLAKElglAERVIFLGFQ---------SNPYpylkkadLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPG 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 818302960 314 NLEPLSD--FGFSFKVGNVDDLKEKLVNLLHKP---KLIKETGEKARLYVRKKY 362
Cdd:cd03811 297 PREILDDgeNGLLVPDGDAAALAGILAALLQKKldaALRERLAKAQEAVFREYT 350
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
16-370 |
8.55e-38 |
|
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: 139.68 E-value: 8.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 16 GGVEHHVEQLASRLAKKGHEVYVYCrpwyqnlVFQNKKVPKtYQKikllnNPSINTKNL-DAITSTFTATMNVLTR---- 90
Cdd:cd03820 13 GGAERVAINLANHLAKKGYDVTIIS-------LDSAEKPPF-YEL-----DDNIKIKNLgDRKYSHFKLLLKYFKKvrrl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 91 -------KADVIHyhGIGPSSLLFIPKLlKTKSRIVATFHckdyeHQKWSFLARSYLKFGEHVCVKIPNGTIAVSKTIQE 163
Cdd:cd03820 80 rkylknnKPDVVI--SFRTSLLTFLALI-GLKSKLIVWEH-----NNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 164 YVREKYHKKITYIPNGVPLFTKEKAKNIKDwglekdKYILTVARLVKHKNIHTLIKAYQLLfpkpNKTNP--KLVIVGgk 241
Cdd:cd03820 152 KKYKQPNSNVVVIPNPLSFPSEEPSTNLKS------KRILAVGRLTYQKGFDLLIEAWALI----AKKHPdwKLRIYG-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 242 adgSGQYEDYLKNLAKE-DPN--IIFTGFQTGetLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIP------ 312
Cdd:cd03820 220 ---DGPEREELEKLIDKlGLEdrVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPtgpsei 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818302960 313 ----ENleplsdfGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARlYVRKKYSWDQIVEK 370
Cdd:cd03820 295 iedgEN-------GLLVPNGDVDALAEALLRLMEDEELRKKMGKNAR-KNAERFSIEKIIKQ 348
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
12-378 |
9.34e-38 |
|
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: 140.21 E-value: 9.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 12 PASYGGVEHHVEQLASRLAKKGHEVYVYC-RPWYQNLVFQNKKVPKTYQKIKLLNNPSINTKNLDAITSTFTATMN---- 86
Cdd:cd03798 10 NANSPGRGIFVRRQVRALSRRGVDVEVLApAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAkllk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 87 -VLTRKADVIHYHGIGPSSLLFIPKLLKTKSRIVATFHCKDY-EHQKWSFLARSYLKFGEHvcvkiPNGTIAVSKTIQEY 164
Cdd:cd03798 90 rRRRGPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHGSDInVFPPRSLLRKLLRWALRR-----AARVIAVSKALAEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 165 VRE--KYHKKITYIPNGVPLFTKEKAknIKDWGLEKD-KYILTVARLVKHKNIHTLIKAYQLLFPKPNktNPKLVIVGGk 241
Cdd:cd03798 165 LVAlgVPRDRVDVIPNGVDPARFQPE--DRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARP--DVVLLIVGD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 242 adgsGQYEDYLKNLAKE---DPNIIFTGFQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASN---IPENL 315
Cdd:cd03798 240 ----GPLREALRALAEDlglGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDvggIPEVV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818302960 316 EPLSDfGFSFKVGNVDDLKEKLVNLLHKPKLiKETGEKARLYVRKKYSWDQIVEKTDEFYENL 378
Cdd:cd03798 316 GDPET-GLLVPPGDADALAAALRRALAEPYL-RELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
15-373 |
3.82e-36 |
|
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: 135.57 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 15 YGGVEHHVEQLASRLAK-KGHEVYVYCRPWYQNLVFQNKKVPKTYQKIkllnnpSINTKNLDAITSTFTATMNVLTRKAD 93
Cdd:cd03809 13 LTGIGRYTRELLKALAKnDPDESVLAVPPLPGELLRLLREYPELSLGV------IKIKLWRELALLRWLQILLPKKDKPD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 94 VIH-YHGIGPssllfipkLLKTKSRIVATFHckD---YEHQKW-SFLARSYLKFGEHVCVKIPNGTIAVSKTIQEYVREK 168
Cdd:cd03809 87 LLHsPHNTAP--------LLLKGCPQVVTIH--DlipLRYPEFfPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 169 YH---KKITYIPNGVP--LFTKEKAKNIKDWGLEKDKYILTVARLVKHKNIHTLIKAYQLLfpKPNKTNPKLVIVGGKAD 243
Cdd:cd03809 157 YGvppEKIVVIPLGVDpsFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALL--KKQGGDLKLVIVGGKGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 244 GSGQYEDYLKNLaKEDPNIIFTGFQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAySNC-VLASNIPENLEPLSDFG 322
Cdd:cd03809 235 EDEELLDLVKKL-GLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMA-CGTpVIASNISVLPEVAGDAA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 818302960 323 FSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVrKKYSWDQIVEKTDE 373
Cdd:cd03809 313 LYFDPLDPESIADAILRLLEDPSLREELIRKGLERA-KKFSWEKTAEKTLE 362
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
16-376 |
4.68e-35 |
|
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: 132.83 E-value: 4.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 16 GGVEHHVEQLASRLAKKGHEVYVYCrpwyqnlvFQNkkvPKTYQKiKLLNNP----SINTKNLDAITSTFTATMNVLTRK 91
Cdd:cd03807 12 GGAETMLLRLLEHMDKSRFEHVVIS--------LTG---DGVLGE-ELLAAGvpvvCLGLSSGKDPGVLLRLAKLIRKRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 92 ADVIHYHGIGPSSLLFIPKLLKTKSRIVATFHCKDYEHQKWSFLARSYLKFGehvcvKIPNGTIAVSKTIQEYVREKY-- 169
Cdd:cd03807 80 PDVVHTWMYHADLIGGLAAKLAGGVKVIWSVRSSNIPQRLTRLVRKLCLLLS-----KFSPATVANSSAVAEFHQEQGya 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 170 HKKITYIPNGVPLFT-----KEKAKNIKDWGLEKDKYIL-TVARLVKHKNIHTLIKAYQLLfpkpNKTNPKLVIVG-GKA 242
Cdd:cd03807 155 KNKIVVIYNGIDLFKlspddASRARARRRLGLAEDRRVIgIVGRLHPVKDHSDLLRAAALL----VETHPDLRLLLvGRG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 243 DGSGQYEDYLKNLAKEDpNIIFTGfqTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENLEPLSDF- 321
Cdd:cd03807 231 PERPNLERLLLELGLED-RVHLLG--ERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGt 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 818302960 322 GFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEKTDEFYE 376
Cdd:cd03807 308 GFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
198-355 |
7.56e-35 |
|
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: 126.23 E-value: 7.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 198 KDKYILTVARLVKHKNIHTLIKAYQLLfpKPNKTNPKLVIVGGkadgsGQYEDYLKNLAKE---DPNIIFTGFQTGETLA 274
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALL--KEKNPNLKLVIAGD-----GEEEKRLKKLAEKlglGDNVIFLGFVSDEDLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 275 ELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENLEPLSDF--GFSFKVGNVDDLKEKLVNLLHKPKLIKETGE 352
Cdd:pfam00534 74 ELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGetGFLVKPNNAEALAEAIDKLLEDEELRERLGE 153
|
...
gi 818302960 353 KAR 355
Cdd:pfam00534 154 NAR 156
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-370 |
4.30e-34 |
|
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: 130.93 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 2 RIYFIGQKGIPASyGGVEHHVEQLASRLAKKGHEVYVYCRPWYQNLVFQNKKVPKTYQKIKLL-------NNPSINTKNL 74
Cdd:cd03794 1 KILLISQYYPPPK-GAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDGIRVIrvklgpiKKNGLIRRLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 75 DAITSTFTATMNVL--TRKADVIHYHGIgPSSLLFIPKLLKTKSRIVATFHCKDYEHQ--------KWSFLARsYLKFGE 144
Cdd:cd03794 80 NYLSFALAALLKLLvrEERPDVIIAYSP-PITLGLAALLLKKLRGAPFILDVRDLWPEslialgvlKKGSLLK-LLKKLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 145 HVCVKIPNGTIAVSKTIQEYVREKYH--KKITYIPNGVPL--FTKEKAKNIKDWGLEKDKYILTVARLVKHK-NIHTLIK 219
Cdd:cd03794 158 RKLYRLADAIIVLSPGLKEYLLRKGVpkEKIIVIPNWADLeeFKPPPKDELRKKLGLDDKFVVVYAGNIGKAqGLETLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 220 AYQLLfpkPNKTNPKLVIVGgkadgSGQYEDYLKNLAKED--PNIIFTGFQTGETLAELFSN---TYLYVHPSAAEG--L 292
Cdd:cd03794 238 AAERL---KRRPDIRFLFVG-----DGDEKERLKELAKARglDNVTFLGRVPKEEVPELLSAadvGLVPLKDNPANRgsS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 293 PIAVLEAMAYSNCVLASNIPEN--LEPLSDFGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEK 370
Cdd:cd03794 310 PSKLFEYMAAGKPILASDDGGSdlAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADR 389
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
16-378 |
2.84e-33 |
|
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: 128.17 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 16 GGVEHHVEQLASRLAKKGHEVYVYCrPWYQNLVFQNKKV--------PKTYQKIKLLnnpsinTKNLDAITSTFTAtmnv 87
Cdd:cd03817 14 NGVATSVRNLARALEKRGHEVYVIT-PSDPGAEDEEEVVryrsfsipIRKYHRQHIP------FPFKKAVIDRIKE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 88 ltRKADVIHYHGigPSSLLFIPKLLKTKSRI--VATFHCK--DYEHQKWSF----------LARSYLKFGEHVcvkipng 153
Cdd:cd03817 83 --LGPDIIHTHT--PFSLGKLGLRIARKLKIpiVHTYHTMyeDYLHYIPKGkllvkavvrkLVRRFYNHTDAV------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 154 tIAVSKTIQEYVRE-KYHKKITYIPNGVPLFTKEKAKN---IKDWGLEKDKY-ILTVARLVKHKNIHTLIKAYQLLfpkP 228
Cdd:cd03817 152 -IAPSEKIKDTLREyGVKGPIEVIPNGIDLDKFEKPLNteeRRKLGLPPDEPiLLYVGRLAKEKNIDFLLRAFAEL---K 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 229 NKTNPKLVIVggkadGSGQYEDYLKNLAKED---PNIIFTGFQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNC 305
Cdd:cd03817 228 KEPNIKLVIV-----GDGPEREELKELARELglaDKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818302960 306 VLA---SNIPENLEpLSDFGFSFKVGNVdDLKEKLVNLLHKPKLIKETGEKARLYVRKKyswdQIVEKTDEFYENL 378
Cdd:cd03817 303 VVAakdPAASELVE-DGENGFLFEPNDE-TLAEKLLHLRENLELLRKLSKNAEISAREF----AFAKSVEKLYEEV 372
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
14-371 |
9.31e-32 |
|
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: 123.47 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 14 SYGGVEHHVEQLASRLAKKGHEVYVYCRPWyqnlvfqnkkvPKTYQKIKLLNNPSINTKNLDAITSTFT--ATMNVLTR- 90
Cdd:cd03808 8 VDGGFQSFRLPLIKALVKKGYEVHVIAPDG-----------DKLSDELKELGVKVIDIPILRRGINPLKdlKALFKLYKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 91 ----KADVIHYHGIGPSSLLFIPKLLKTKSRIVATFH----CKDYEHQKWSFLARSY---LKFGEHVcvkipngtIAVSK 159
Cdd:cd03808 77 lkkeKPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHglgfVFTEGKLLRLLYLLLEklaLLFTDKV--------IFVNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 160 TIQEYVREKYH----KKITYIPNGVPLFTKEKAKNIkdwgLEKDKYILT-VARLVKHKNIHTLIKAYQLLfpKPNKTNPK 234
Cdd:cd03808 149 DDRDLAIKKGIikkkKTVLIPGSGVDLDRFQYSPES----LPSEKVVFLfVARLLKDKGIDELIEAAKIL--KKKGPNVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 235 LVIVGGKADGsGQYEDYLKNLAKEDpNIIFTGFQtgETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPEN 314
Cdd:cd03808 223 FLLVGDGELE-NPSEILIEKLGLEG-RIEFLGFR--SDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGC 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 818302960 315 LEPLSD--FGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEKT 371
Cdd:cd03808 299 RELVIDgvNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
15-373 |
4.53e-28 |
|
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: 114.00 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 15 YGGVEHHVEQLASRLAKKGHEVYVY-CRPWYQNLV----FQNKKVPKTYQKIKLLNNPSINTKNLDAITSTFTAtmnvLT 89
Cdd:cd03821 13 AGGPVKVVLRLAAALAALGHEVTIVsTGDGYESLVveenGRYIPPQDGFASIPLLRQGAGRTDFSPGLPNWLRR----NL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 90 RKADVIHYHGI-GPSSLLFIPKLLKTKSRIVATFH------CKDYEHQKWsFLARsylkfgeHVCVKIPNGTIAVSKTIQ 162
Cdd:cd03821 89 REYDVVHIHGVwTYTSLAACKLARRRGIPYVVSPHgmldpwALQQKHWKK-RIAL-------HLIERRNLNNAALVHFTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 163 EYVREKYHK-----KITYIPNGV--PLFTKEKAKNIKDWGLEKDKYILTVARLVKHKNIHTLIKAYQLLFPKPNKTnpKL 235
Cdd:cd03821 161 EQEADELRRfglepPIAVIPNGVdiPEFDPGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDW--HL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 236 VIVGgKADGSGQYEDYLKNLAKEDPNIIFTGFQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLAS---NIP 312
Cdd:cd03821 239 VIAG-PDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITdkcGLS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818302960 313 ENLEPlsDFGFSFKVgNVDDLKEKLVNLL---HKPKLIKETGEKARLyVRKKYSWDQIVEKTDE 373
Cdd:cd03821 318 ELVEA--GCGVVVDP-NVSSLAEALAEALrdpADRKRLGEMARRARQ-VEENFSWEAVAGQLGE 377
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
12-379 |
4.44e-24 |
|
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: 102.41 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 12 PASYGGVEHHVEQLASRLAKKGHEVYVYCrPWYQNLVfqnKKVPKTYQKIKLLNNPSINTKNLDAITS----TFTATM-- 85
Cdd:cd03823 11 PQRVGGAEISVHDLAEALVAEGHEVAVLT-AGVGPPG---QATVARSVVRYRRAPDETLPLALKRRGYelfeTYNPGLrr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 86 ---NVLTR-KADVIHYHGIGPSSLLFIPKLLKTKSRIVATFHckDYehqkWSFLARSYLkfgehvCVKIPNGTIAVSKTI 161
Cdd:cd03823 87 llaRLLEDfRPDVVHTHNLSGLGASLLDAARDLGIPVVHTLH--DY----WLLCPRQFL------FKKGGDAVLAPSRFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 162 QEYVREK--YHKKITYIPNGVPlftKEKAKNIKDWGLEKDKYILTVARLVKHKNIHTLIKAYQLLFPKpnktNPKLVIVG 239
Cdd:cd03823 155 ANLHEANglFSARISVIPNAVE---PDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPRE----DIELVIAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 240 GKADgsgqyEDYLKNLAkeDPNIIFTGFQTGETLAELFSNTYLYVHPSA-AEGLPIAVLEAMAYSNCVLASN---IPENL 315
Cdd:cd03823 228 HGPL-----SDERQIEG--GRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDlggIAELI 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818302960 316 EPLSDfGFSFKVGNVDDLKEKLVNLLHKPKLIKEtgEKARLYVRkkyswdQIVEKTDEFYENLY 379
Cdd:cd03823 301 QPGVN-GLLFAPGDAEDLAAAMRRLLTDPALLER--LRAGAEPP------RSTESQAEEYLKLY 355
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
91-378 |
1.86e-23 |
|
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: 100.48 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 91 KADVIHYHGI--GPSSLLFIPKLLKTKsRIVATFH----------------------------------CKDYEHQKWS- 133
Cdd:cd03825 51 EADIIHLHWIhgGYLSLKALFKLLRRK-PVVWTLHdmwpftggchypmecegwktgcgncpnlnsyppaKKDLSRQLFRr 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 134 ---FLARSYLKFgehvcvkipngtIAVSKTIQEYVREKY---HKKITYIPNGVPL---FTKEKAKNIKDWGLEKDKY-IL 203
Cdd:cd03825 130 kreALAKKRLTI------------VAPSRWLADMVRRSPllkGLPVVVIPNGIDTeifAPVDKAKARKRLGIPQDKKvIL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 204 TVARLV--KHKNIHTLIKAYQLLFPKPNKtnpKLVIVGGKAdgsgqyedylKNLAKEDPNIIFTGFQT-GETLAELFSNT 280
Cdd:cd03825 198 FGAESVtkPRKGFDELIEALKLLATKDDL---LLVVFGKND----------PQIVILPFDIISLGYIDdDEQLVDIYSAA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 281 YLYVHPSAAEGLPIAVLEAMAYSNCVLASN---IPENLEPLSDfGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLY 357
Cdd:cd03825 265 DLFVHPSLADNLPNTLLEAMACGTPVVAFDtggSPEIVQHGVT-GYLVPPGDVQALAEAIEWLLANPKERESLGERARAL 343
|
330 340
....*....|....*....|.
gi 818302960 358 VRKKYSWDQIVEKTDEFYENL 378
Cdd:cd03825 344 AENHFDQRVQAQRYLELYKDL 364
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
200-342 |
1.95e-23 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 94.89 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 200 KYILTVARLVK-HKNIHTLIKAYQLLFPKPNKTnpKLVIVGgkaDGSgqyEDYLKNLAKE-DPNIIFTGFQtgETLAELF 277
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDV--RLVIVG---DGP---EEELEELAAGlEDRVIFTGFV--EDLAELL 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818302960 278 SNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENLEPLS-DFGFSFKVGNVDDLKEKLVNLLH 342
Cdd:pfam13692 72 AAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDgENGLLVPPGDPEALAEAILRLLE 137
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
194-376 |
8.44e-23 |
|
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: 98.52 E-value: 8.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 194 WGLEKDKYILTVARLVKHKNIHTLIKAYQLLfpkPNKTNPKLVIVGgkaDGSGQYEdylknLAKEDPNIIFTGFQTGETL 273
Cdd:cd03814 193 LGPPGRPLLLYVGRLAPEKNLEALLDADLPL---AASPPVRLVVVG---DGPARAE-----LEARGPDVIFTGFLTGEEL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 274 AELFSNTYLYVHPSAAEGLPIAVLEAMAySN----CVLASNIPENLEPLSDfGFSFKVGNVDDLKEKLVNLLHKPKLIKE 349
Cdd:cd03814 262 ARAYASADVFVFPSRTETFGLVVLEAMA-SGlpvvAADAGGPRDIVRPGGT-GALVEPGDAAAFAAALRALLEDPELRRR 339
|
170 180
....*....|....*....|....*..
gi 818302960 350 TGEKARLYVrKKYSWDQIVEKTDEFYE 376
Cdd:cd03814 340 MAARARAEA-ERYSWEAFLDNLLDYYA 365
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
271-378 |
9.39e-23 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 92.75 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 271 ETLAE-LFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENLEPLSD--FGFSFKVGNVDDLKEKLVNLLHKPKLI 347
Cdd:COG0438 11 DLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDgeTGLLVPPGDPEALAEAILRLLEDPELR 90
|
90 100 110
....*....|....*....|....*....|.
gi 818302960 348 KETGEKARLYVRKKYSWDQIVEKTDEFYENL 378
Cdd:COG0438 91 RRLGEAARERAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
16-356 |
2.44e-22 |
|
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: 97.04 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 16 GGVEHHVEQLASRLAKKGHEVYVYC--RPWYQNLVFQNKKVPK-TYQKIKLLNNPsintKNLDAITstftatmnvLTRKA 92
Cdd:cd03819 11 GGAETYILDLARALAERGHRVLVVTagGPLLPRLRQIGIGLPGlKVPLLRALLGN----VRLARLI---------RRERI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 93 DVIHYHGIGPSSLLFI-PKLLKTKsrIVATFHCKDYEHQKWSFLARSYLKFGEHVcvkipngtIAVSKTIQEYVREKY-- 169
Cdd:cd03819 78 DLIHAHSRAPAWLGWLaSRLTGVP--LVTTVHGSYLATYHPKDFALAVRARGDRV--------IAVSELVRDHLIEALgv 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 170 -HKKITYIPNGV--PLFTKE-KAKNIKDWGLEKDKY-ILTVARLVKHKNIHTLIKAYQLLfpkPNKTNPKLVIVGgkaDG 244
Cdd:cd03819 148 dPERIRVIPNGVdtDRFPPEaEAEERAQLGLPEGKPvVGYVGRLSPEKGWLLLVDAAAEL---KDEPDFRLLVAG---DG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 245 SGqyEDYLKNLAKE---DPNIIFTGFQtgETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASN---IPENLEP- 317
Cdd:cd03819 222 PE--RDEIRRLVERlglRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDvggAREIVVHg 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 818302960 318 ----LSDFgfsfkvGNVDDLKEKLVNLLHKPKLIKETGEKARL 356
Cdd:cd03819 298 rtglLVPP------GDAEALADAIRAAKLLPEAREKLQAAAAL 334
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
12-363 |
1.06e-21 |
|
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: 95.42 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 12 PASYGGVEHHVEQLASRLAKKGHEVYVycrpwyqnLVFQNKKVPKTYQkikLLNNPSINTK---NLDAITSTFTA--TMN 86
Cdd:cd03795 10 YPDIGGIEQVIYDLAEGLKKKGIEVDV--------LCFSKEKETPEKE---ENGIRIHRVKsflNVASTPFSPSYikRFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 87 VLTRKADVIHYHGIGP-SSLLFIPKLLKTKSriVATFHcKDYEHQK-----WSFLARSYLKFGEHVCVKIPNgTIAVSKT 160
Cdd:cd03795 79 KLAKEYDIIHYHFPNPlADLLLFFSGAKKPV--VVHWH-SDIVKQKkllklYKPLMTRFLRRADRIIATSPN-YVETSPT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 161 IQEYvREKYHkkitYIPNGVPLFTKEK-AKNIKDWGLEKD--KYILTVARLVKHKNIHTLIKAYQLLfpkpnktNPKLVI 237
Cdd:cd03795 155 LREF-KNKVR----VIPLGIDKNVYNIpRVDFENIKREKKgkKIFLFIGRLVYYKGLDYLIEAAQYL-------NYPIVI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 238 VggkadGSGQYEDYLKNLAKED--PNIIFTGFQTGETLAELFSNTYLYVHPS--AAEGLPIAVLEAMAYSNCVLASNIPE 313
Cdd:cd03795 223 G-----GEGPLKPDLEAQIELNllDNVKFLGRVDDEEKVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIGT 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 818302960 314 NLEPLSDFGFS---FKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYS 363
Cdd:cd03795 298 GVPYVNNNGETglvVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFT 350
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
3-320 |
2.09e-21 |
|
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: 92.08 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 3 IYFIGQkGIPASYGGVEHHVEQLASRLAKKGHEVYVYCRPWYQNLVFQNKkvpktyqkikllnnpsintknldaitstft 82
Cdd:cd01635 1 ILLVTG-EYPPLRGGLELHVRALARALAALGHEVTVLALLLLALRRILKK------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 83 atmnVLTRKADVIHYHGIGPSSLLFIPKLLKTKSRIVATFHCKDY-EHQKWSFLARSYLKFGEHVCVKipngtiavskti 161
Cdd:cd01635 50 ----LLELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSlESTRSELLALARLLVSLPLADK------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 162 qeyvrekyhkkityipngvplftkekaknikdwglekdkyiLTVARLVKHKNIHTLIKAYQLLfpKPNKTNPKLVIVGGk 241
Cdd:cd01635 114 -----------------------------------------VSVGRLVPEKGIDLLLEALALL--KARLPDLVLVLVGG- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 242 aDGSGQYEDYLKNLAKEDPNIIFTGFQTGETLAELFSNTY-LYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENLEPLSD 320
Cdd:cd01635 150 -GGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAAdVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
16-182 |
9.34e-21 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 88.74 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 16 GGVEHHVEQLASRLAKKGHEVYVYCRPWYQNLVFQNKKVPKTYQKikllnNPSINTKNLDAITSTFTATMNVLTRKADVI 95
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRV-----PLPLPPRLLRSLAFLRRLRRLLRRERPDVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 96 HYHGIGPSSLLFIPKLLKTKSRIVATFHCKDYEHQKWSF---LARSYLKFGEHVCVKIPNGTIAVSKTIQEYVREKYH-- 170
Cdd:pfam13439 76 HAHSPFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGArlsPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGvp 155
|
170
....*....|...
gi 818302960 171 -KKITYIPNGVPL 182
Cdd:pfam13439 156 pEKIRVIPNGVDL 168
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
14-378 |
1.89e-18 |
|
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: 86.25 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 14 SYGGVEHHVEQLASRLAKKGHEVYV--YCRPWYQNLVFQNKKvpktYQKIKLLNNPSINTKNLDAITSTFTATMnVLTRK 91
Cdd:cd04962 10 SYGGSGVVATELGLELAERGHEVHFisSAIPFRLNLYSGNIF----FHEVEVPNYPLFEYPPYTLALASKIVEV-AKEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 92 ADVIHYHGIGP--SSLLFIPKLLKTKSRIVATFHCKD-----YEHqkwSFlaRSYLKFGehvcVKIPNGTIAVSKTIQEY 164
Cdd:cd04962 85 LDVLHAHYAIPhaSCAYLAREILGEKIPIVTTLHGTDitlvgYDP---SL--QPAVRFS----INKSDRVTAVSSSLRQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 165 VRE--KYHKKITYIPNGVPL--FTKEKAKNIKD--WGLEKDKYILTVARLVKHKNIHTLIKAYQLLfpkPNKTNPKLVIV 238
Cdd:cd04962 156 TYElfDVDKDIEVIHNFIDEdvFKRKPAGALKRrlLAPPDEKVVIHVSNFRPVKRIDDVVRVFARV---RRKIPAKLLLV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 239 GgkadgSGQYEDYLKNLAKE---DPNIIFTGFQtgETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASN---IP 312
Cdd:cd04962 233 G-----DGPERVPAEELARElgvEDRVLFLGKQ--DDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNaggIP 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818302960 313 E-NLEPLSdfGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEKTDEFYENL 378
Cdd:cd04962 306 EvVKHGET--GFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
3-375 |
5.92e-18 |
|
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: 84.42 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 3 IYFIGQKGIpasyGGVEHHVEQLASRLAKKGHEVYVYCrpwyqnLVFQNKKVPKtyQKIKLLNNPSINTKNLDAITSTFT 82
Cdd:cd04951 3 LYVITGLGL----GGAEKQTVLLADQMFIRGHDVNIVY------LTGEVEVKPL--NNNIIIYNLGMDKNPRSLLKALLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 83 ATMNVLTRKADVIHYHGIGPSSLLFIPKLLKTKSRIVATFHCKDYEHQKWSFLARsylkFGEHVCVKIPNgtiaVSK-TI 161
Cdd:cd04951 71 LKKIISAFKPDVVHSHMFHANIFARFLRMLYPIPLLICTAHNKNEGGRIRMFIYR----LTDFLCDITTN----VSReAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 162 QEYVREKY--HKKITYIPNGVPL----FTKEKAKNIKD-WGLEKD-KYILTVARLVKHKNIHTLIKAYQLLFPKPNKTnp 233
Cdd:cd04951 143 DEFIAKKAfsKNKSVPVYNGIDLnkfkKDINVRLKIRNkLNLKNDeFVILNVGRLTEAKDYPNLLLAISELILSKNDF-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 234 KLVIVGgkaDGS--GQYEDYLKNLAKEDpNIIFTGFQTgeTLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNI 311
Cdd:cd04951 221 KLLIAG---DGPlrNELERLICNLNLVD-RVILLGQIS--NISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDA 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818302960 312 PENLEPLSDFGFSFKVGNVDDLKEKLVN-LLHKPKLIKETGEKaRLYVRKKYSWDQIVEKTDEFY 375
Cdd:cd04951 295 GGVAEVVGDHNYVVPVSDPQLLAEKIKEiFDMSDEERDILGNK-NEYIAKNFSINTIVNEWERLY 358
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
171-379 |
5.94e-15 |
|
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: 76.22 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 171 KKITYIPNGVPLftkEKAKNIKDWGLEKDKYILT-VARLVKHKNIHTLIKAYQLLfpKPNKTNPKLVIVGGKADGsgqyE 249
Cdd:cd03813 267 DKTRVIPNGIDI---QRFAPAREERPEKEPPVVGlVGRVVPIKDVKTFIRAFKLV--RRAMPDAEGWLIGPEDED----P 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 250 DYL---KNLAKE---DPNIIFTGFQTgetLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASN-------IPENLE 316
Cdd:cd03813 338 EYAqecKRLVASlglENKVKFLGFQN---IKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDvgscrelIYGADD 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818302960 317 PLSDFGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEKtdefYENLY 379
Cdd:cd03813 415 ALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDS----YRKLY 473
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
91-373 |
1.48e-14 |
|
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: 74.25 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 91 KADVIHYHG-IGPSSLLFIPKLLKTKSRIvATFHCKDYEHQKwsfLARSYLKFGEHVCVKIPNGTIAVSKTIQEYV-REK 168
Cdd:cd03812 80 KYDIVHVHGsSSNGIILLLAAKAGVPVRI-AHSHNTKDSSIK---LRKIRKNVLKKLIERLSTKYLACSEDAGEWLfGEV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 169 YHKKITYIPNGVPL----FTKEKAKNIKDWGLEKDKYIL-TVARLVKHKNIHTLIKAYQLLfpKPNKTNPKLVIVGgkad 243
Cdd:cd03812 156 ENGKFKVIPNGIDIekykFNKEKRRKRRKLLILEDKLVLgHVGRFNEQKNHSFLIDIFEEL--KKKNPNVKLVLVG---- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 244 gSGQYEDYLKNLAKE---DPNIIFTGFQtgETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENLEPLSD 320
Cdd:cd03812 230 -EGELKEKIKEKVKElglEDKVIFLGFR--NDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 818302960 321 FGFSFKVGNVDDL-KEKLVNLLHKPKLIKEtgEKARLYVRKKYsWDQIVEKTDE 373
Cdd:cd03812 307 NVEFLPLNETPSTwAEKILKLIKRKRRINK--EINKEKKELGY-DDESLELTLL 357
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
169-371 |
2.06e-13 |
|
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: 71.12 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 169 YHKKITYIPNGV------PLFTKEKAKNIKDWGLEKdKYILTVARLVKHKNIHTLIKAYQLLFPKPNKTNpkLVIVGGKA 242
Cdd:cd03800 185 DPSRINVVPPGVdlerffPVDRAEARRARLLLPPDK-PVVLALGRLDPRKGIDTLVRAFAQLPELRELAN--LVLVGGPS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 243 DGSGQYEDYLKNLAKEDPNII----FTGFQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASN---IPENL 315
Cdd:cd03800 262 DDPLSMDREELAELAEELGLIdrvrFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAvggLQDIV 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818302960 316 EPLSDfGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEKT 371
Cdd:cd03800 342 RDGRT-GLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQL 396
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
118-362 |
2.66e-13 |
|
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: 70.56 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 118 IVATFHCKD-YEHQKW---SFLARSYLKFGEHVCVKIPNGTIAVSKTIQEYVREK--YHKKITYIPNGVplftkEKAKNI 191
Cdd:cd05844 107 LVVTFHGFDiTTSRAWlaaSPGWPSQFQRHRRALQRPAALFVAVSGFIRDRLLARglPAERIHVHYIGI-----DPAKFA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 192 KDWGLEKDKYILTVARLVKHKNIHTLIKAYQLLfpKPNKTNPKLVIVggkadGSGQYEDYLKNLAKEDPNIIFTGFQTGE 271
Cdd:cd05844 182 PRDPAERAPTILFVGRLVEKKGCDVLIEAFRRL--AARHPTARLVIA-----GDGPLRPALQALAAALGRVRFLGALPHA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 272 TLAELFSNTYLYVHPSA------AEGLPIAVLEAMAYSNCVLAS---NIPENLEPlSDFGFSFKVGNVDDLKEKLVNLLH 342
Cdd:cd05844 255 EVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSrhgGIPEAILD-GETGFLVPEGDVDALADALQALLA 333
|
250 260
....*....|....*....|
gi 818302960 343 KPKLIKETGEKARLYVRKKY 362
Cdd:cd05844 334 DRALADRMGGAARAFVCEQF 353
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
133-335 |
3.47e-13 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 70.39 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 133 SFLAR---SYLKFGEHVCVKIPNGTIAVSKTIQEYVREKYHKK--ITYIPNGVPLFTkekaknIKDwglEKDKYILTVAR 207
Cdd:cd03804 137 SLLASlflHYLRLWDVRTAQRVDLFIANSQFVARRIKKFYGREstVIYPPVDTDAFA------PAA---DKEDYYLTASR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 208 LVKHKNIHTLIKAYqllfpkpNKTNPKLVIVGGkadgsGQYEDYLKNLAKedPNIIFTGFQTGETLAELFSNTYLYVHPs 287
Cdd:cd03804 208 LVPYKRIDLAVEAF-------NELPKRLVVIGD-----GPDLDRLRAMAS--PNVEFLGYQPDEVLKELLSKARAFVFA- 272
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818302960 288 AAEGLPIAVLEAMAYSNCVLASNIPENLEPLSDF--GFSFKVGNVDDLKE 335
Cdd:cd03804 273 AEEDFGIVPVEAQACGTPVIAFGKGGALETVRPGptGILFGEQTVESLKA 322
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
2-376 |
9.63e-13 |
|
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: 68.95 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 2 RIYFIGQkgIPASYGGVEHHVEQLASRLAKKGHEVYVycrpwyqNLVFQNKKVPKTYQKIKLLNNPSINTKNLDaitSTF 81
Cdd:cd03822 1 KIAVLGT--LPPRKCGIATYTDDLVEGLRKGGPVVIV-------VIVSPQDEILKDDDFEVPNEIKSWNSNEYF---RLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 82 TAtmnVLTRKADVIH--YH---GIGPSSLLFIPKLLKTKSRIVATFHCKDYE----HQKWSFLARSyLKFGEHVCVKIPN 152
Cdd:cd03822 69 DH---LNFKKPDVVHiqHEfgiFGGKYGLYALGLLLHLRIPVITTLHTVLDLsdpgKQALKVLFRI-ATLSERVVVMAPI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 153 GtIAVSKTIQEYVREKYHKkityIPNGVPLFTKEKAKNIKDWGLEKDKY-ILTVARLVKHKNIHTLIKAYQLLFPKPnkT 231
Cdd:cd03822 145 S-RFLLVRIKLIPAVNIEV----IPHGVPEVPQDPTTALKRLLLPEGKKvILTFGFIGPGKGLEILLEALPELKAEF--P 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 232 NPKLVIVGGKADGS--GQYEDYLKNLAKE---DPNIIF-TGFQTGETLAELFSNTYLYVHP--SAAEGLPIAVLEAMAYS 303
Cdd:cd03822 218 DVRLVIAGELHPSLarYEGERYRKAAIEElglQDHVDFhNNFLPEEEVPRYISAADVVVLPylNTEQSSSGTLSYAIACG 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818302960 304 NCVLASNIPENLEPL-SDFGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYvRKKYSWDQIVEKTDEFYE 376
Cdd:cd03822 298 KPVISTPLRHAEELLaDGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAY-ARAMTWESIADRYLRLFN 370
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
195-364 |
2.79e-12 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 68.20 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 195 GLEKDKYILTVARLVKHKNIHTLIKAYQLLfpkpnkTNPKLVIVGgkadgSGQYEDYLKNLAKeDPNIIFTGFQTGETLA 274
Cdd:PLN02871 259 GEPEKPLIVYVGRLGAEKNLDFLKRVMERL------PGARLAFVG-----DGPYREELEKMFA-GTPTVFTGMLQGDELS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 275 ELFSNTYLYVHPSAAEGLPIAVLEAMAySN----CVLASNIPENLEPLS--DFGFSFKVGNVDDLKEKLVNLLHKPKLIK 348
Cdd:PLN02871 327 QAYASGDVFVMPSESETLGFVVLEAMA-SGvpvvAARAGGIPDIIPPDQegKTGFLYTPGDVDDCVEKLETLLADPELRE 405
|
170
....*....|....*.
gi 818302960 349 ETGEKARLYVrKKYSW 364
Cdd:PLN02871 406 RMGAAAREEV-EKWDW 420
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
166-370 |
3.42e-12 |
|
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: 66.94 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 166 REKYHKKITYIPNGV--PLFTKEKAKNIKDwglekdKYILTVARLVKHKNIHTLIKAYQLLFPKPNKTnpKLVIVGgKAD 243
Cdd:cd04949 131 RFNKYPPIFTIPVGYvdQLDTAESNHERKS------NKIITISRLAPEKQLDHLIEAVAKAVKKVPEI--TLDIYG-YGE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 244 GSGQYEDYLKNLAKEDpNIIFTGFQTgeTLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNIPENlepLSDF-- 321
Cdd:cd04949 202 EREKLKKLIEELHLED-NVFLKGYHS--NLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYG---PSELie 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818302960 322 ----GFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLyVRKKYSWDQIVEK 370
Cdd:cd04949 276 dgenGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK-IAEKYSTENVMEK 327
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
160-362 |
4.88e-11 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 63.88 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 160 TIQEYVREKYHKKITYIPNGV-PLftKEKAKNIKDWGLEK-----------DKYILTVARLVKHKNIHTLIKAYQLLfpK 227
Cdd:cd03792 148 HPPEFVPPQVPPPKFYIPPSIdPL--SGKNKDLSPADIRYylekpfvidpeRPYILQVARFDPSKDPLGVIDAYKLF--K 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 228 PNKTNPKLVIVGGKA----DGSGQYEDYLKnLAKEDPNIIFTGFQTG-ETLAELFSNTYLYVHPSAAEGLPIAVLEAMAY 302
Cdd:cd03792 224 RRAEEPQLVICGHGAvddpEGSVVYEEVME-YAGDDHDIHVLRLPPSdQEINALQRAATVVLQLSTREGFGLTVSEALWK 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818302960 303 SNCVLASN---IPENLEplsDFGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKY 362
Cdd:cd03792 303 GKPVIATPaggIPLQVI---DGETGFLVNSVEGAAVRILRLLTDPELRRKMGLAAREHVRDNF 362
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
202-362 |
2.24e-08 |
|
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: 55.53 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 202 ILTVARLVKHKNIHTLIKAYQLLFPKpnKTNPKLVIVggkadGSGQYEDYLKNLAKE---DPNIIFTGFQTGETLAELFS 278
Cdd:cd03799 177 ILTVGRLTEKKGLEYAIEAVAKLAQK--YPNIEYQII-----GDGDLKEQLQQLIQElniGDCVKLLGWKPQEEIIEILD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 279 NTYLYVHPSAA------EGLPIAVLEAMAYSNCVLA---SNIPENLEP-LSdfGFSFKVGNVDDLKEKLVNLLHKPKLIK 348
Cdd:cd03799 250 EADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVIStehGGIPELVEDgVS--GFLVPERDAEAIAEKLTYLIEHPAIWP 327
|
170
....*....|....
gi 818302960 349 ETGEKARLYVRKKY 362
Cdd:cd03799 328 EMGKAGRARVEEEY 341
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
155-379 |
3.25e-08 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 55.18 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 155 IAVSKTIQEYVREKY-HKKITYIPNGVPLFT--KEKAKNIK-DWGLEKDKYILTVA-RLVKHKNIHTLIKAYQLLFPKpn 229
Cdd:PRK15484 144 IVPSQFLKKFYEERLpNADISIVPNGFCLETyqSNPQPNLRqQLNISPDETVLLYAgRISPDKGILLLMQAFEKLATA-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 230 KTNPKLVIVGGKADGS----GQYEDYLKNLAKE-DPNIIFTGFQTGETLAELFSNTYLYVHPSA-AEGLPIAVLEAMAYS 303
Cdd:PRK15484 222 HSNLKLVVVGDPTASSkgekAAYQKKVLEAAKRiGDRCIMLGGQPPEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 304 NCVLASN-------IPENL------EPLSDFGFSFKVGNVDDLKEKLvnllhkpklikETGEKARLYVRKKYSWDQIVEK 370
Cdd:PRK15484 302 KPVLASTkggitefVLEGItgyhlaEPMTSDSIISDINRTLADPELT-----------QIAEQAKDFVFSKYSWEGVTQR 370
|
....*....
gi 818302960 371 TDEFYENLY 379
Cdd:PRK15484 371 FEEQIHNWF 379
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
1-389 |
7.30e-08 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 53.95 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 1 MRIYFIGQKgiPASYGGVEHHVEQLASRLAKKGH--EVYVYCRpwyqnlvfqNKKVPKTY-QKIKLLNNPSINTKNLDAI 77
Cdd:PRK09922 1 MKIAFIGEA--VSGFGGMETVISNVINTFEESKIncEMFFFCR---------NDKMDKAWlKEIKYAQSFSNIKLSFLRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 78 TSTFTATMNVLTRKADVIhYHGIGPSSLLFIPKLLKTKSRIVATFhckdyehqKWSFLARSYLKFGEHVCVKIPNGTIAV 157
Cdd:PRK09922 70 AKHVYNFSKWLKETQPDI-VICIDVISCLYANKARKKSGKQFKIF--------SWPHFSLDHKKHAECKKITCADYHLAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 158 SKTIQEYVREKYHK--KITYIPNGVplftKEKAKNIKDWGLEKDKYILTVARLV--KHKNIHTLIKAYQLLfpkpnKTNP 233
Cdd:PRK09922 141 SSGIKEQMMARGISaqRISVIYNPV----EIKTIIIPPPERDKPAVFLYVGRLKfeGQKNVKELFDGLSQT-----TGEW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 234 KLVIVGgkadgSGQYEDYLKNLAKE---DPNIIFTGFQTG--ETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLA 308
Cdd:PRK09922 212 QLHIIG-----DGSDFEKCKAYSRElgiEQRIIWHGWQSQpwEVVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCIS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 309 SNIPEnleplsdfgfsfkvGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKK--YSWDQIVEKTDEFYENLYHHNPKNL 386
Cdd:PRK09922 287 SDCMS--------------GPRDIIKPGLNGELYTPGNIDEFVGKLNKVISGEvkYQHDAIPNSIERFYEVLYFKNLNNA 352
|
...
gi 818302960 387 HPK 389
Cdd:PRK09922 353 LFS 355
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
157-366 |
2.94e-07 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 52.08 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 157 VSKTIQEYVREKY---HKKITYIPNGVPlfTKEKAKNIKdwgLEKDKYILTVARLVKHKNIHTLIKAYQLLFPKPNKTNP 233
Cdd:cd04946 184 ISKEGKDYLQKCYpayKEKIFVSRLGVS--DKEQYSKVK---KEGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSICI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 234 KLVIVGGkadgsGQYEDYLKNLAKEDP---NIIFTGFQTGETLAELF--SNTYLYVHPSAAEGLPIAVLEAMAYSNCVLA 308
Cdd:cd04946 259 SWTHIGG-----GPLKERLEKLAENKLenvKVNFTGEVSNKEVKQLYkeNDVDVFVNVSESEGIPVSIMEAISFGIPVIA 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818302960 309 SNIPENLEPLSDFGFSFKVGN---VDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQ 366
Cdd:cd04946 334 TNVGGTREIVENETNGLLLDKdptPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEV 394
|
|
| DUF1972 |
pfam09314 |
Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized ... |
3-179 |
8.12e-07 |
|
Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized domains are found in bacterial glycosyltransferases and rhamnosyltransferases.
Pssm-ID: 430520 Cd Length: 186 Bit Score: 49.02 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 3 IYFIGQKGIPASYGGVEHHVEQLASRLAKKGHEVYVYCRP---------WYQNLVFQNKKVPKT-YQKIKLLNNPSINtK 72
Cdd:pfam09314 4 VFIIGSRGLPAKYGGFETFVEKLTEYQKNKSIKYHVACLSensaksehfEYNGADCFTIKVPKIgPARVIAYDIMAIN-Y 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 73 NLDAItstftATMNVltrKADVIHYHG--IGPSSLLFIPKLLKTKSRIVATFHCKDYEHQKWSFLARSYLKFGEHVCVKI 150
Cdd:pfam09314 83 ALKYI-----KDHNI---KEPIFYILGntIGPFIAHFARKIHKLGGKLYVNPDGLEWKRAKWSAPVRQYLKFSEKLMTKY 154
|
170 180 190
....*....|....*....|....*....|
gi 818302960 151 PNGTIAVSKTIQEYVREKY-HKKITYIPNG 179
Cdd:pfam09314 155 ADLLISDNKGIEKYIHDEYgNPKTTYIAYG 184
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
16-377 |
1.61e-06 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 49.93 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 16 GGVEHHVEQLASRLAKKGHEVYVYCRPwYQNLV----FQNK-KVpkTYQKIKLLNNPSIntknLDAITSTFTATMNVLTR 90
Cdd:cd03796 14 GGVETHIYQLSQCLIKRGHKVIVITHA-YGNRVgvryLTNGlKV--YYLPFKVFYNQST----LPTLFSTFPLLRNILIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 91 -KADVIHYHGiGPSSL----LFIPKLLKTKSriVATFHC----KDYEhqkwSFLARSYLKFGEHvCVkipNGTIAVSKTI 161
Cdd:cd03796 87 eRIQIVHGHQ-AFSSLaheaLFHARTLGLKT--VFTDHSlfgfADAS----SILTNKLLRFSLA-DI---DHVICVSHTS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 162 QE--YVREKYH-KKITYIPNGV--PLFTKEKAKNIKDWglekdKYILTVARLVKHKNIHTLIKAyqllFPKPNKTNPKL- 235
Cdd:cd03796 156 KEntVLRASLDpRIVSVIPNAVdsSDFTPDPSKPDPNK-----ITIVVISRLVYRKGIDLLVGI----IPRICKKHPNVr 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 236 VIVGGkaDG-----------SGQYEDYLKNLAKEDPNIIFTGFQTGEtlaelfsntyLYVHPSAAEGLPIAVLEAMAYSN 304
Cdd:cd03796 227 FIIGG--DGpkrieleemreKYQLQDRVELLGAVPHEEVRDVLVQGH----------IFLNTSLTEAFCIAIVEAASCGL 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818302960 305 CVLASN---IPENLEPlsDFgFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEKTDEFYEN 377
Cdd:cd03796 295 LVVSTRvggIPEVLPP--DM-ILLAEPDPEDIVRKLEEAISILRTGKHDPWSFHNRVKKMYSWEDVARRTEKVYDR 367
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
169-370 |
2.75e-04 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 42.74 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 169 YHKKITYIPNGV---PLFTKEKAKNIKDWG--LEKDKYILT-VAR-LVKHKNIHTLIKAyqllFPKPNKTNPKL--VIVG 239
Cdd:cd03818 177 YRDRISVIHDGVdtdRLAPDPAARLRLLNGteLKAGDPVITyVARnLEPYRGFHVFMRA----LPRIQARRPDArvVVVG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302960 240 GK--------ADGSGQYEDYLKNLAKEDPNIIFTGFQTGETLAELFSNTYLYVHPSAAEGLPIAVLEAMAYSNCVLASNI 311
Cdd:cd03818 253 GDgvsygsppPDGGSWKQKMLAELGVDLERVHFVGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDT 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818302960 312 PENLEPLSD--FGFSFKVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVEK 370
Cdd:cd03818 333 APVREVIRDgrNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLAR 393
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
296-369 |
1.23e-03 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 37.97 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818302960 296 VLEAMAySNCVLASNIPENLEPL----SDFGFsfkVGNVDDLKEKLVNLLHKPKLIKETGEKARLYVRKKYSWDQIVE 369
Cdd:pfam13524 16 VFEAAA-CGAPLLTDRTPGLEELfepgEEILL---YRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAE 89
|
|
| |
