|
Name |
Accession |
Description |
Interval |
E-value |
| thiol_BshA |
TIGR03999 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ... |
1-365 |
9.37e-158 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 274914 [Multi-domain] Cd Length: 374 Bit Score: 447.44 E-value: 9.37e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 1 MRIGIINYPTFGGSGIVGTELGLELQKRGHEIHFISYQLPERL-KLEEKFTFHEVNILSYPLFKYKPYTIILAAKIVELF 79
Cdd:TIGR03999 1 MKIGITCYPTYGGSGVVATELGKALAERGHEVHFITSSQPFRLeKFHPNIFFHEVEVNQYPLFQYPPYDLALASKIAEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 80 KKYKIDLFHGHYAIPHSTSLYLAKQ----TNNRIKIVSTLHGSDIHLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIK 155
Cdd:TIGR03999 81 KEEKLDLLHVHYAIPHAIAAYLARQmlgkEGIDIPIVTTLHGTDITLVGADPSFKPAVRFSIEKSDGVTAVSESLKEETY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 156 KHYNITKEIKTIYNFVSPEKFNAKKRKKKTEQ-----EEFVFSHVSNFRQVKRSPDIIRAFALVyKKHKNIKLEMVGSGP 230
Cdd:TIGR03999 161 ELFDIDKPIEVIPNFVDTDRYRRKNDPALKRKlgapeDEKVLIHISNFRPVKRVEDVIEVFARV-QQEVPAKLLLVGDGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 231 ELEYCRDLAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFT 310
Cdd:TIGR03999 240 ERSPAEQLVRELGLTDRVLFLGKQDDVAELLSISDLFLLPSEKESFGLAALEAMACGVPVIASNAGGIPEVVEHGVTGFL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1491308087 311 AEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYEKLYEDLL 365
Cdd:TIGR03999 320 CDVGDVETMAEYAISLLEDEELLQRFSAAARERAKERFDSEKIVPQYEALYRRLL 374
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-364 |
2.72e-145 |
|
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: 415.98 E-value: 2.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 1 MRIGIINYPTFGGSGIVGTELGLELQKRGHEIHFISYQLPERL-KLEEKFTFHEVNILSYPLFKYKPYTIILAAKIVELF 79
Cdd:cd04962 1 MKIGIVCYPSYGGSGVVATELGLELAERGHEVHFISSAIPFRLnLYSGNIFFHEVEVPNYPLFEYPPYTLALASKIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 80 KKYKIDLFHGHYAIPHSTSLYLAKQ-TNNRIKIVSTLHGSDIHLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIKKHY 158
Cdd:cd04962 81 KEHKLDVLHAHYAIPHASCAYLAREiLGEKIPIVTTLHGTDITLVGYDPSLQPAVRFSINKSDRVTAVSSSLRQETYELF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 159 NITKEIKTIYNFVSPEKFNAKKRKKKTEQ-----EEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNiKLEMVGSGPELE 233
Cdd:cd04962 161 DVDKDIEVIHNFIDEDVFKRKPAGALKRRllappDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPA-KLLLVGDGPERV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 234 YCRDLAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEP 313
Cdd:cd04962 240 PAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1491308087 314 GNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYEKLYEDL 364
Cdd:cd04962 320 GDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-362 |
6.48e-70 |
|
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: 223.18 E-value: 6.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 2 RIGIINY---PTFGGSGIVGTELGLELQKRGHEIHFISYQLPERLKLEEKFTFHEVNILSYPLFKYKPYTIilaAKIVEL 78
Cdd:cd03801 1 KILLLSPelpPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLL---RELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 79 FKKYKIDLFHGHYAIPHSTSLYLAKQtnNRIKIVSTLHGSDIHLLGLDKAYKPIL----ETSLNNHDALTTVSNFMVRFI 154
Cdd:cd03801 78 LRLRKFDVVHAHGLLAALLAALLALL--LGAPLVVTLHGAEPGRLLLLLAAERRLlaraEALLRRADAVIAVSEALRDEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 155 KKHYNITKE-IKTIYNFVSPEKFNAKKRKKKT-EQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGS-GPE 231
Cdd:cd03801 156 RALGGIPPEkIVVIPNGVDLERFSPPLRRKLGiPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGdGPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 232 LEYCRDLaiSLGLKDQIVFRGSLLN--VPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGF 309
Cdd:cd03801 236 RAELEEL--ELGLGDRVRFLGFVPDeeLPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1491308087 310 TAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYEKLYE 362
Cdd:cd03801 314 VVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
12-364 |
1.35e-63 |
|
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: 207.23 E-value: 1.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 12 GGSGIVGTELGLELQKRGHEIHFISYQ--LPERLKLEEKFTFH----EVNILSYPLFKYKPYTIILAA----KIVELFKK 81
Cdd:cd03798 14 PGRGIFVRRQVRALSRRGVDVEVLAPApwGPAAARLLRKLLGEavppRDGRRLLPLKPRLRLLAPLRApslaKLLKRRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 82 YKIDLFHGHYAIPhstSLYLA--KQTNNRIKIVSTLHGSDIHLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIKKHYN 159
Cdd:cd03798 94 GPPDLIHAHFAYP---AGFAAalLARLYGVPYVVTEHGSDINVFPPRSLLRKLLRWALRRAARVIAVSKALAEELVALGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 160 ITKEIKTIYNFVSPEKFNAKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLA 239
Cdd:cd03798 171 PRDRVDVIPNGVDPARFQPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 240 ISLGLKDQIVFRGSLLN--VPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVK 317
Cdd:cd03798 251 EDLGLGDRVTFTGRLPHeqVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDAD 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1491308087 318 QLAQYMTILLEDNNLRQKfSEAAIKDARERFHPDKIISQYEKLYEDL 364
Cdd:cd03798 331 ALAAALRRALAEPYLREL-GEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
20-358 |
2.71e-52 |
|
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: 177.40 E-value: 2.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 20 ELGLELQKRGHEIHFISyqlPERLKLEEKFTFHEVNILSYPL---FKYKPYTIILAAKIVELFKKYKIDLFHGHYAIPhs 96
Cdd:cd03808 18 PLIKALVKKGYEVHVIA---PDGDKLSDELKELGVKVIDIPIlrrGINPLKDLKALFKLYKLLKKEKPDIVHCHTPKP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 97 tSLY--LAKQTNNRIKIVSTLHG--------SDIHLLgldkaYKPILETSLNNHDALTTVSNFMVRFIKKHYNITKEIKT 166
Cdd:cd03808 93 -GILgrLAARLAGVPKVIYTVHGlgfvftegKLLRLL-----YLLLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 167 IY--NFVSPEKFNakKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLAISLGL 244
Cdd:cd03808 167 LIpgSGVDLDRFQ--YSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 245 KDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMT 324
Cdd:cd03808 245 EGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIE 324
|
330 340 350
....*....|....*....|....*....|....
gi 1491308087 325 ILLEDNNLRQKFSEAAIKDARERFHPDKIISQYE 358
Cdd:cd03808 325 KLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-359 |
4.61e-47 |
|
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: 163.18 E-value: 4.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 2 RIGIINYPTFGGSGI--VGTELGLELQKRGHEIHFISyqlperLKLEEKFTFHEV--NILSYPLFKYKPYTIILAAKIV- 76
Cdd:cd03820 1 KIAIVIPSISNAGGAerVAINLANHLAKKGYDVTIIS------LDSAEKPPFYELddNIKIKNLGDRKYSHFKLLLKYFk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 77 ------ELFKKYKIDLFhghYAIPHSTSLYLAKQTNNrIKIVSTLHGSDIHLLGLDKAYKPIlETSLNNHDALTTVSNFM 150
Cdd:cd03820 75 kvrrlrKYLKNNKPDVV---ISFRTSLLTFLALIGLK-SKLIVWEHNNYEAYNKGLRRLLLR-RLLYKRADKIVVLTEAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 151 VrfIKKHYNITKEIKTIYNFVSPEKFNAKkrkkkTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGP 230
Cdd:cd03820 150 K--LKKYKQPNSNVVVIPNPLSFPSEEPS-----TNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 231 ELEYCRDLAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTA-GGLPEVVKHEKTGF 309
Cdd:cd03820 223 EREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGL 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1491308087 310 TAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDArERFHPDKIISQYEK 359
Cdd:cd03820 303 LVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEKIIKQWEE 351
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-349 |
1.98e-45 |
|
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: 159.06 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 2 RIGIINYP-TFGGSGIVGTELGLELQKRGHEIHFISYQLPERLKLEEKFTFHEVNILSYPLFKYKPYTIILAAKIVELFK 80
Cdd:cd03811 1 KILFVIPSlSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 81 KYKIDLFHGHYaipHSTSLYLAKQTNNRIKIVSTLHGSDIHLLGLDKAYKPILEtSLNNHDALTTVSNFMVRFIKKHYNI 160
Cdd:cd03811 81 RAKPDVVISFL---GFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLK-LYKKADKIVCVSKGIKEDLIRLGPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 161 TKE-IKTIYNFVSPEKFN--AKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRD 237
Cdd:cd03811 157 PPEkIEVIYNPIDIDRIRalAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 238 LAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVK 317
Cdd:cd03811 237 LAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAA 316
|
330 340 350
....*....|....*....|....*....|..
gi 1491308087 318 QLAQYMTILLEDNNLRQKFSEAAIKDARERFH 349
Cdd:cd03811 317 ALAGILAALLQKKLDAALRERLAKAQEAVFRE 348
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-364 |
4.39e-43 |
|
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: 153.20 E-value: 4.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 2 RIGIIN---YPTFGGSGIVGTELGLELQKRGHEIHFISYQLPERLKLEEKftfHEVNILSYPLFKYKPYTIILAAK--IV 76
Cdd:cd03817 1 KIAIFTdtyLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEV---VRYRSFSIPIRKYHRQHIPFPFKkaVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 77 ELFKKYKIDLFHGHyaIPHST---SLYLAKQTNnrIKIVSTLHGSDIHLL-------GLDKAYKPILETSLNNH-DALTT 145
Cdd:cd03817 78 DRIKELGPDIIHTH--TPFSLgklGLRIARKLK--IPIVHTYHTMYEDYLhyipkgkLLVKAVVRKLVRRFYNHtDAVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 146 VSNFMVRFIKKhYNITKEIKTIYNFVSPEKFNAKKRKKKTEQ-----EEFVFSHVSNFRQVKRSPDIIRAFALVYKKhKN 220
Cdd:cd03817 154 PSEKIKDTLRE-YGVKGPIEVIPNGIDLDKFEKPLNTEERRKlglppDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 221 IKLEMVGSGPELEYCRDLAISLGLKDQIVFRGSLLN--VPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGL 298
Cdd:cd03817 232 IKLVIVGDGPEREELKELARELGLADKVIFTGFVPReeLPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491308087 299 PEVVKHEKTGFTAEPGNVKqLAQYMTILLEDNNLRQKFSEAAIKdARERFHPDKiisQYEKLYEDL 364
Cdd:cd03817 312 SELVEDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEI-SAREFAFAK---SVEKLYEEV 372
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
74-362 |
2.27e-41 |
|
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: 148.62 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 74 KIVELFKKYKIDLFHGHYAIPHSTSLYLAKQTNNRiKIVSTLHGSDI--HLLGLDKAYKPILETSLnnhDALTTVSNFMV 151
Cdd:cd03807 70 RLAKLIRKRNPDVVHTWMYHADLIGGLAAKLAGGV-KVIWSVRSSNIpqRLTRLVRKLCLLLSKFS---PATVANSSAVA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 152 RFIKKHYNITKEIKTIYNFVSPEKFNAKKRKKKTEQEE-------FVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLE 224
Cdd:cd03807 146 EFHQEQGYAKNKIVVIYNGIDLFKLSPDDASRARARRRlglaedrRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 225 MVGSGPELEYCRDLAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKh 304
Cdd:cd03807 226 LVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD- 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491308087 305 EKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYEKLYE 362
Cdd:cd03807 305 DGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
19-340 |
3.28e-40 |
|
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: 145.19 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 19 TELGLELQKRGHEIHFISYQLPERLKLEEkftfhevNILSYPLFKYKPYTIILAAK-IVELFKKYKIDLFHGHYAIPHST 97
Cdd:cd03819 18 LDLARALAERGHRVLVVTAGGPLLPRLRQ-------IGIGLPGLKVPLLRALLGNVrLARLIRRERIDLIHAHSRAPAWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 98 SLYLAKQTnnRIKIVSTLHGSDIhLLGLDKAYKPILETSLNNHDAlttVSNFMVRFIKKHYNITKE-IKTIYNFVSPEKF 176
Cdd:cd03819 91 GWLASRLT--GVPLVTTVHGSYL-ATYHPKDFALAVRARGDRVIA---VSELVRDHLIEALGVDPErIRVIPNGVDTDRF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 177 NAKKRKKKTEQ-----EEFVFSHVSNFRQVKRSPDIIRAFALVyKKHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFR 251
Cdd:cd03819 165 PPEAEAEERAQlglpeGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPERDEIRRLVERLGLRDRVTFT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 252 GSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNN 331
Cdd:cd03819 244 GFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPE 323
|
....*....
gi 1491308087 332 LRQKFSEAA 340
Cdd:cd03819 324 AREKLQAAA 332
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
188-343 |
1.03e-39 |
|
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: 138.18 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 188 EEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFRGSLLN--VPKVLCETD 265
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDedLPELLKIAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491308087 266 VFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKD 343
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
265-366 |
6.63e-35 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 124.33 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 265 DVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDA 344
Cdd:COG0438 22 DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAARERA 101
|
90 100
....*....|....*....|..
gi 1491308087 345 RERFHPDKIISQYEKLYEDLLK 366
Cdd:COG0438 102 EERFSWEAIAERLLALYEELLA 123
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
189-329 |
1.38e-34 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 124.16 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 189 EFVFSHVSNF-RQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYcrdLAISLGLKDQIVFRGSLLNVPKVLCETDVF 267
Cdd:pfam13692 1 RPVILFVGRLhPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEEL---EELAAGLEDRVIFTGFVEDLAELLAAADVF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491308087 268 IIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVkHEKTGFTAEPGNVKQLAQYMTILLED 329
Cdd:pfam13692 78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-363 |
8.73e-34 |
|
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: 128.22 E-value: 8.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 2 RIGIIN--YPT--FGGSGIVGTELGLELQKRGHEIHFIS-------YQLPERLKLEEKFTFHEVNILSYPLFKYKP---Y 67
Cdd:cd03823 1 KILLVNslYPPqrVGGAEISVHDLAEALVAEGHEVAVLTagvgppgQATVARSVVRYRRAPDETLPLALKRRGYELfetY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 68 TIILAAKIVELFKKYKIDLFHGHYAIPHSTS-LYLAKQTNnrIKIVSTLHgsDIHLL----GLDKaykpiletslNNHDA 142
Cdd:cd03823 81 NPGLRRLLARLLEDFRPDVVHTHNLSGLGASlLDAARDLG--IPVVHTLH--DYWLLcprqFLFK----------KGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 143 LTTVSNFMVRFIKKHYNITKEIKTIYNFVSPEKfnAKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVykKHKNIK 222
Cdd:cd03823 147 VLAPSRFTANLHEANGLFSARISVIPNAVEPDL--APPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRL--PREDIE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 223 LEMVGSGPELEYCRDLAislglKDQIVFRGSLLN--VPKVLCETDVFIIPSeI--ESFGLAALEALSCGIPVIASTAGGL 298
Cdd:cd03823 223 LVIAGHGPLSDERQIEG-----GRRIAFLGRVPTddIKDFYEKIDVLVVPS-IwpEPFGLVVREAIAAGLPVIASDLGGI 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491308087 299 PEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLrqkfSEAAIKDARERFHPDKIISQYEKLYED 363
Cdd:cd03823 297 AELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPAL----LERLRAGAEPPRSTESQAEEYLKLYRD 357
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
2-359 |
7.32e-33 |
|
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: 125.94 E-value: 7.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 2 RIGI-INYPTFGGSGI--VGTELGLELQKR-GHEIHFISYQLPERLKLEEKFTFHEVNILSYPLFKYKPYTIILAAKIVE 77
Cdd:cd03809 1 KILIdGRSLAQRLTGIgrYTRELLKALAKNdPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 78 LFKKykIDLFHghyaIPHSTSLYLAKQtnnrIKIVSTLHgsDI--------HLLGLDKAYKPILETSLNNHDALTTVSNF 149
Cdd:cd03809 81 KKDK--PDLLH----SPHNTAPLLLKG----CPQVVTIH--DLiplrypefFPKRFRLYYRLLLPISLRRADAIITVSEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 150 MVRFIKKHYNITKE-IKTIYNFVSPEKF----NAKKRKKKTEQEEFVFsHVSNFRQVKRSPDIIRAFALVYKKHKNIKLE 224
Cdd:cd03809 149 TRDDIIKFYGVPPEkIVVIPLGVDPSFFppesAAVLIAKYLLPEPYFL-YVGTLEPRKNHERLLKAFALLKKQGGDLKLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 225 MVGS-GPELEYCRDLAISLGLKDQIVFRGSL--LNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEV 301
Cdd:cd03809 228 IVGGkGWEDEELLDLVKKLGLGGRVRFLGYVsdEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEV 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491308087 302 VkhEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDAReRFHPDKIISQYEK 359
Cdd:cd03809 308 A--GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWEKTAEKTLE 362
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
3-358 |
1.64e-28 |
|
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: 114.36 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 3 IGIINYPTFGGSGIVGTELGLELQKRGHEIHFIS---YQLPERLKLEEKFTFHEVNILSYPLFKYKPYTII--------- 70
Cdd:cd03794 5 ISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTpspNYPLGRIFAGATETKDGIRVIRVKLGPIKKNGLIrrllnylsf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 71 -LAAKIVELFKKYKIDLFHgHYAIPHSTSL--YLAKQtNNRIKIV---------STLHGSDIHLLGLDKAYKPILETSLN 138
Cdd:cd03794 85 aLAALLKLLVREERPDVII-AYSPPITLGLaaLLLKK-LRGAPFIldvrdlwpeSLIALGVLKKGSLLKLLKKLERKLYR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 139 NHDALTTVSNFMVRFIKKHYNITKEIKTIYNFVSPEKFNA----KKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALV 214
Cdd:cd03794 163 LADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPppkdELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 215 yKKHKNIKLEMVGSGPELEYCRDLAISLGLKDqIVFRGSL--LNVPKVLCETDVFIIP-SEIESFGLAA----LEALSCG 287
Cdd:cd03794 243 -KRRPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVpkEEVPELLSAADVGLVPlKDNPANRGSSpsklFEYMAAG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308087 288 IPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYE 358
Cdd:cd03794 321 KPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
85-348 |
2.64e-27 |
|
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: 110.62 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 85 DLFHGHYAIPHSTSLYLAKQTNnrIKIVSTLHGSDIHL-------LGLDKAYKPILETSLNNHDAL-TTVSNFM-VRFIK 155
Cdd:cd05844 83 ALVHAHFGRDGVYALPLARALG--VPLVVTFHGFDITTsrawlaaSPGWPSQFQRHRRALQRPAALfVAVSGFIrDRLLA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 156 KHYNITKeIKTIYNFVSPEKFNAKKRKkkteQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYC 235
Cdd:cd05844 161 RGLPAER-IHVHYIGIDPAKFAPRDPA----ERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 236 RDLAISLGlkdQIVFRGSLlNVPKVLCETD---VFIIPS------EIESFGLAALEALSCGIPVIASTAGGLPEVVKHEK 306
Cdd:cd05844 236 QALAAALG---RVRFLGAL-PHAEVQDWMRraeIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGE 311
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1491308087 307 TGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERF 348
Cdd:cd05844 312 TGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQF 353
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
8-354 |
4.88e-27 |
|
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: 109.67 E-value: 4.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 8 YPTFGGSGIVGTELGLELQKRGHEIHFI--SYQLPERLKLEEKFTFHEV----NILSYPLFkykpYTIILAAKivELFKK 81
Cdd:cd03795 10 YPDIGGIEQVIYDLAEGLKKKGIEVDVLcfSKEKETPEKEENGIRIHRVksflNVASTPFS----PSYIKRFK--KLAKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 82 YkiDLFHGHYAIPHSTSLYLAKQTNNriKIVSTLHgSDI-HLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIKKHYNI 160
Cdd:cd03795 84 Y--DIIHYHFPNPLADLLLFFSGAKK--PVVVHWH-SDIvKQKKLLKLYKPLMTRFLRRADRIIATSPNYVETSPTLREF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 161 TKEIKTIYNFVSPEKFNAKkrkkkteQEEFVFSHvsnfRQVKRSPDIIRAFALVYKKHKNIKLE----------MVGSGP 230
Cdd:cd03795 159 KNKVRVIPLGIDKNVYNIP-------RVDFENIK----REKKGKKIFLFIGRLVYYKGLDYLIEaaqylnypivIGGEGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 231 ELEYCRDLaISLGLKDQIVFRGSLLNVPKV--LCETDVFIIPSEI--ESFGLAALEALSCGIPVIAST-AGGLPEVVKHE 305
Cdd:cd03795 228 LKPDLEAQ-IELNLLDNVKFLGRVDDEEKViyLHLCDVFVFPSVLrsEAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNG 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1491308087 306 KTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKII 354
Cdd:cd03795 307 ETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
103-357 |
2.67e-26 |
|
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: 107.00 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 103 KQTNNRIKIVSTLHGS------DIHLLGLDKAYKPILEtSLNNHDALTTVSNFMVRFIKKHYNITKEIKTIYNFVSPEKF 176
Cdd:cd04949 72 LNTKGPAKKGAVLHNEhvknndDPEHSLIKNFYKYVFE-NLNKYDAIIVSTEQQKQDLSERFNKYPPIFTIPVGYVDQLD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 177 NAKKRKkktEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFRGSLLN 256
Cdd:cd04949 151 TAESNH---ERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 257 VPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIA-STAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQK 335
Cdd:cd04949 228 LDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSyDVKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQ 307
|
250 260
....*....|....*....|..
gi 1491308087 336 FSEAAIKDArERFHPDKIISQY 357
Cdd:cd04949 308 FSEESYKIA-EKYSTENVMEKW 328
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
3-361 |
6.47e-25 |
|
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: 104.06 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 3 IGIINYPTFGGSGIVGTELGLELQKRGHEIHFISYQLPERLK-LEEKFTFHEVNIlsyplfKYKPYTIILAA-KIVELFK 80
Cdd:cd04951 3 LYVITGLGLGGAEKQTVLLADQMFIRGHDVNIVYLTGEVEVKpLNNNIIIYNLGM------DKNPRSLLKALlKLKKIIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 81 KYKIDLFHGHyaIPHSTSLY-LAKQTNNRIKIVSTLHGSDIHllglDKAYKPILETSLNNHDALTTVSNFMVR-FIKKHY 158
Cdd:cd04951 77 AFKPDVVHSH--MFHANIFArFLRMLYPIPLLICTAHNKNEG----GRIRMFIYRLTDFLCDITTNVSREALDeFIAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 159 NITKEIKTIYNFVSPEKFNAKKRKKKT-------EQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPE 231
Cdd:cd04951 151 FSKNKSVPVYNGIDLNKFKKDINVRLKirnklnlKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 232 LEYCRDLAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVkhEKTGFTA 311
Cdd:cd04951 231 RNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV--GDHNYVV 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1491308087 312 EPGNVKQLAQYMT-ILLEDNNLRQKFSEAAiKDARERFHPDKIISQYEKLY 361
Cdd:cd04951 309 PVSDPQLLAEKIKeIFDMSDEERDILGNKN-EYIAKNFSINTIVNEWERLY 358
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
265-364 |
7.91e-25 |
|
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: 103.57 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 265 DVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDA 344
Cdd:cd03825 265 DLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALA 344
|
90 100
....*....|....*....|
gi 1491308087 345 RERFHPDKIISQYEKLYEDL 364
Cdd:cd03825 345 ENHFDQRVQAQRYLELYKDL 364
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
85-358 |
2.68e-24 |
|
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: 102.70 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 85 DLFHGHYAIPHSTSLYLAKQTNnrIKIVSTLHGsdihlLGLDK--------AYKPIL-----ETSLNNHDALTTVSNFMV 151
Cdd:cd03800 103 DLIHSHYWDSGLVGALLARRLG--VPLVHTFHS-----LGRVKyrhlgaqdTYHPSLritaeEQILEAADRVIASTPQEA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 152 RFIKKHY-NITKEIKTIY------NFVSPEKFNAKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLE 224
Cdd:cd03800 176 DELISLYgADPSRINVVPpgvdleRFFPVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 225 MVG-------SGPELEYcRDLAISLGLKDQIVFRGSLL--NVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTA 295
Cdd:cd03800 256 LVGgpsddplSMDREEL-AELAEELGLIDRVRFPGRVSrdDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAV 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491308087 296 GGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYE 358
Cdd:cd03800 335 GGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLL 397
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
12-174 |
3.23e-24 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 97.60 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 12 GGSGIVGTELGLELQKRGHEIHFISYQLPERLKlEEKFTFHEVNILSYPLFKYKPYTIILAAKIVELFKKYKIDLFHGHY 91
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLA-EEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 92 AIPHSTSlYLAKQTNNRIKIVSTLHGSDI-------HLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIKKHYNITKE- 163
Cdd:pfam13439 80 PFPLGLA-ALAARLRLGIPLVVTYHGLFPdykrlgaRLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEk 158
|
170
....*....|.
gi 1491308087 164 IKTIYNFVSPE 174
Cdd:pfam13439 159 IRVIPNGVDLE 169
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
24-347 |
1.42e-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: 100.06 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 24 ELQKRGHEIHFISyqlPERLKLEEKFTFHEVNILSYPLFKYKPYTIILAA--KIVELFKKYKIDLFH-------GHYAip 94
Cdd:cd03814 26 HLRRRGHEVRVVA---PGPFDEAESAEGRVVSVPSFPLPFYPEYRLALPLprRVRRLIKEFQPDIIHiatpgplGLAA-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 95 hstsLYLAKQtnNRIKIVSTLHG------SDIHLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIKKH--YNI---TKE 163
Cdd:cd03814 101 ----LRAARR--LGLPVVTSYHTdfpeylSYYTLGPLSWLAWAYLRWFHNPFDTTLVPSPSIARELEGHgfERVrlwPRG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 164 IKTIYnFvSPEKFNAKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVyKKHKNIKLEMVGSGP---ELEYCRDLAI 240
Cdd:cd03814 175 VDTEL-F-HPSRRDAALRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPL-AASPPVRLVVVGDGParaELEARGPDVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 241 SLGLKDqivfrGSLLnvPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLA 320
Cdd:cd03814 252 FTGFLT-----GEEL--ARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFA 324
|
330 340
....*....|....*....|....*..
gi 1491308087 321 QYMTILLEDNNLRQKFSEAAIKDARER 347
Cdd:cd03814 325 AALRALLEDPELRRRMAARARAEAERY 351
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
24-302 |
1.44e-23 |
|
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: 100.06 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 24 ELQKRGHEIHFISYQLPErLKLEEKF------TFHEVNILSYPLFKYKpytiilaaKIVELFKKYKIDLFHGHyaIPHST 97
Cdd:cd03812 24 KLDKSKIEFDFLATSDDK-GEYDEELeelggkIFYIPPKKKNIIKYFI--------KLLKLIKKEKYDIVHVH--GSSSN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 98 SLYL--AKQTNNRIKIV---STLHGSDIHLLGLDKAYKPILETSLNNHDAlttVSNFMVRFIKKHYNItKEIKTIYNFVS 172
Cdd:cd03812 93 GIILllAAKAGVPVRIAhshNTKDSSIKLRKIRKNVLKKLIERLSTKYLA---CSEDAGEWLFGEVEN-GKFKVIPNGID 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 173 PEKFN------AKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLAISLGLKD 246
Cdd:cd03812 169 IEKYKfnkekrRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLED 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491308087 247 QIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVV 302
Cdd:cd03812 249 KVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDI 304
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
162-362 |
2.12e-23 |
|
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: 100.87 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 162 KEIKTIYNFVSPEKFnAKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPE----LEYCRD 237
Cdd:cd03813 267 DKTRVIPNGIDIQRF-APAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGPEDEdpeyAQECKR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 238 LAISLGLKDQIVFRGsLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVV-----KHEKTGFTAE 312
Cdd:cd03813 346 LVASLGLENKVKFLG-FQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVP 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491308087 313 PGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYEKLYE 362
Cdd:cd03813 425 PADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
29-309 |
1.42e-22 |
|
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: 94.78 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 29 GHEIHFISYqLPERLKLeekftFHEVNILSYPLFKYKPYTIILAakivelfkKYKIDLFHGHYAIPHSTSLYLAKQTNnR 108
Cdd:cd01635 14 GLELHVRAL-ARALAAL-----GHEVTVLALLLLALRRILKKLL--------ELKPDVVHAHSPHAAALAALLAARLL-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 109 IKIVSTLHGSDIHLLgldkaykpiletslnnhdalttvsnfmvrfiKKHYNITKEIKTIYNFVSPEKFnakkrkkkteqe 188
Cdd:cd01635 79 IPIVVTVHGPDSLES-------------------------------TRSELLALARLLVSLPLADKVS------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 189 efvfshVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFRGSLLNVPKV---LCETD 265
Cdd:cd01635 116 ------VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLellLAAAD 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1491308087 266 VFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGF 309
Cdd:cd01635 190 VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
9-358 |
5.22e-21 |
|
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: 93.20 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 9 PTFGGSGIVGTELGLELQKRGHEIHFISYQLP-ERLKLEE--KFTFHEVNILSYPLFKYKPYTIILAAKIVELFKKY--K 83
Cdd:cd03821 11 PKAGGPVKVVLRLAAALAALGHEVTIVSTGDGyESLVVEEngRYIPPQDGFASIPLLRQGAGRTDFSPGLPNWLRRNlrE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 84 IDLFHGHyAIPHSTSLYLAKQT-NNRIKIVSTLHG-----SDIHLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIKKH 157
Cdd:cd03821 91 YDVVHIH-GVWTYTSLAACKLArRRGIPYVVSPHGmldpwALQQKHWKKRIALHLIERRNLNNAALVHFTSEQEADELRR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 158 YNITKEIKTIYNFVSPEKF---NAKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGP-ELE 233
Cdd:cd03821 170 FGLEPPIAVIPNGVDIPEFdpgLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDgAYP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 234 YCRDLAISLGLKDQIVFRGSL--LNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEkTGFTA 311
Cdd:cd03821 250 AFLQLQSSLGLGDRVTFTGPLygEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1491308087 312 EPgNVKQLAQYMTILLEDNNLRQKFSEAA--IKDARERFHPDKIISQYE 358
Cdd:cd03821 329 DP-NVSSLAEALAEALRDPADRKRLGEMArrARQVEENFSWEAVAGQLG 376
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
2-364 |
1.78e-20 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 90.81 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 2 RIGIINYPTF----GGSGivGTELGL-----ELQKRGHEIHFI-SYQLPERLKLEekFTFHEVNILSYPLFKYKPYTIIL 71
Cdd:cd03802 1 RIAQVSPPRGpvppGKYG--GTELVVsalteGLVRRGHEVTLFaPGDSHTSAPLV--AVIPRALRLDPIPQESKLAELLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 72 AAKIVElfKKYKIDLFHGH--YAIPHSTSLYlakqtnnRIKIVSTLHG-SDIHLLGLDKAYKPILETSLNNHDAlttvsn 148
Cdd:cd03802 77 ALEVQL--RASDFDVIHNHsyDWLPPFAPLI-------GTPFVTTLHGpSIPPSLAIYAAEPPVNYVSISDAQR------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 149 fmvrfikKHYNITKEIKTIYNFVSPEKFnakkrkKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVykkhkNIKLEMVGS 228
Cdd:cd03802 142 -------AATPPIDYLTVVHNGLDPADY------RFQPDPEDYLAFLGRIAPEKGLEDAIRVARRA-----GLPLKIAGK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 229 GPELEYCRDLaISLGLKDQIVFRG--------------SLLNVPKVLCETdvfiipseiesFGLAALEALSCGIPVIAST 294
Cdd:cd03802 204 VRDEDYFYYL-QEPLPGPRIEFIGevghdekqellggaRALLFPINWDEP-----------FGLVMIEAMACGTPVIAYR 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308087 295 AGGLPEVVKHEKTGFTAEPgnVKQLAQYMTILlednnlrQKFSEAAIKD-ARERFHPDKIISQYEKLYEDL 364
Cdd:cd03802 272 RGGLPEVIQHGETGFLVDS--VEEMAEAIANI-------DRIDRAACRRyAEDRFSAARMADRYEALYRKV 333
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
188-364 |
3.59e-17 |
|
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: 81.98 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 188 EEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGP------ELEYCRDLAISLGLKDQIVFR----GSLLNV 257
Cdd:cd03792 196 ERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAvddpegSVVYEEVMEYAGDDHDIHVLRlppsDQEINA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 258 pkVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPgnVKQLAQYMTILLEDNNLRQKFS 337
Cdd:cd03792 276 --LQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAVRILRLLTDPELRRKMG 351
|
170 180
....*....|....*....|....*..
gi 1491308087 338 EAAIKDARERFHPDKIISQYEKLYEDL 364
Cdd:cd03792 352 LAAREHVRDNFLITGNLRAWLYLIAKL 378
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
52-356 |
5.33e-16 |
|
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: 78.26 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 52 HEVNIlsYPLF------------KYKPYTIILAAKIVELFKKYKIDLFHGHYAIPHSTSLYLAKQTNNRIKIVSTLHGSD 119
Cdd:cd03799 29 HEVDI--YAVNpgdlvkrhpdveKYNVPSLNLLYAIVGLNKKGAYDIIHCQFGPLGALGALLRRLKVLKGKLVTSFRGYD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 120 I---HLLGLDKAYKPILEtslNNHDALTTVSNFMVRFIKKHYNiTKEIKTIYNFVSPEKFNAKKRKKKTEQEEFVFShVS 196
Cdd:cd03799 107 IsmyVILEGNKVYPQLFA---QGDLFLPNCELFKHRLIALGCD-EKKIIVHRSGIDCNKFRFKPRYLPLDGKIRILT-VG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 197 NFRQVKRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFRG--SLLNVPKVLCETDVFIIPS--- 271
Cdd:cd03799 182 RLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGwkPQEEIIEILDEADIFIAPSvta 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 272 ---EIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERF 348
Cdd:cd03799 262 adgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEY 341
|
....*...
gi 1491308087 349 HPDKIISQ 356
Cdd:cd03799 342 DINKLNDE 349
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
265-344 |
1.86e-15 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 77.44 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 265 DVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHE---KTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAI 341
Cdd:PLN02871 333 DVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDqegKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAR 412
|
...
gi 1491308087 342 KDA 344
Cdd:PLN02871 413 EEV 415
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
141-348 |
1.40e-14 |
|
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: 73.86 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 141 DALTTVSNFMVRFIKKHYNITKEIktIYNFVSPEKFnakkrKKKTEQEEFVFShVSNFRQVKRSPDIIRAFALVYKKhkn 220
Cdd:cd03804 159 DLFIANSQFVARRIKKFYGRESTV--IYPPVDTDAF-----APAADKEDYYLT-ASRLVPYKRIDLAVEAFNELPKR--- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 221 ikLEMVGSGPELEYCRDLAislglKDQIVFRGSLLN--VPKVLCETDVFIIPSEiESFGLAALEALSCGIPVIASTAGGL 298
Cdd:cd03804 228 --LVVIGDGPDLDRLRAMA-----SPNVEFLGYQPDevLKELLSKARAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGA 299
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491308087 299 PEVVKHEKTGFTAEPGNVKQLAQYMTILLEdnnLRQKFSEAAIKDARERF 348
Cdd:cd03804 300 LETVRPGPTGILFGEQTVESLKAAVEEFEQ---NFDRFKPQAIRANAERF 346
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
103-367 |
3.33e-14 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 72.82 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 103 KQTNNRIKIVSTLHGSDIHllglDKAYKPILETSLNNHDALTTV--SNFMVRFIKkhyniTKEIKTIYNFVSPeKFNAKK 180
Cdd:PRK09922 104 KKSGKQFKIFSWPHFSLDH----KKHAECKKITCADYHLAISSGikEQMMARGIS-----AQRISVIYNPVEI-KTIIIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 181 RKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVykkHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFRGSLLN---- 256
Cdd:PRK09922 174 PPERDKPAVFLYVGRLKFEGQKNVKELFDGLSQT---TGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQpwev 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 257 VPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPE-VVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQK 335
Cdd:PRK09922 251 VQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRdIIKPGLNGELYTPGNIDEFVGKLNKVISGEVKYQH 330
|
250 260 270
....*....|....*....|....*....|..
gi 1491308087 336 fseAAIKDARERFhpdkiisqYEKLYEDLLKK 367
Cdd:PRK09922 331 ---DAIPNSIERF--------YEVLYFKNLNN 351
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
19-147 |
4.35e-14 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 68.50 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 19 TELGLELQKRGHEIH-FISYQLPERLKLEEKFTFHEVNILSYPLFKYkpytiILAAKIVELFKKYKIDLFHGHYAIPHST 97
Cdd:pfam13477 14 LRWADALADRGYDVHvISSKGPAKDELIAEGIHVHRLKVPRKGPLGY-----LKAFRLKKLIKKIKPDVVHVHYAKPYGL 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1491308087 98 SLYLAKQTNNRIKIVSTLHGSDIHLLGLDKA-YKPILETSLNNHDALTTVS 147
Cdd:pfam13477 89 LAGLAARLSGFPPVVLSAWGLDVYKFPNKSRlKKLLLKLNLKKATLIISTS 139
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
79-352 |
1.87e-13 |
|
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: 70.95 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 79 FKKYKIDLFHGHYAIPHSTSLYLAKQTNNRIKIVSTLHGSDIHLLGLDKAYKPILETSLNNHDALTTVSNFMVRFIKKHY 158
Cdd:cd04946 117 SIFGQGTVVYSYWLNHTALGLGLLKDEYYRDVVISRAHRYDLYEDQYGSYYLPLREYLVSYLDAVFLISKEGKDYLQKCY 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 159 NITKEIKTIYNFVSPEKfnaKKRKKKTEQEEFVFSHVSNFRQVKRSPDIIRAFALVYKKHKNIKLEM--VGSGPELEYCR 236
Cdd:cd04946 197 PAYKEKIFVSRLGVSDK---EQYSKVKKEGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSICISWthIGGGPLKERLE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 237 DLAISLGLKDQIVFRGSLLN--VPKVLCET--DVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFT-A 311
Cdd:cd04946 274 KLAENKLENVKVNFTGEVSNkeVKQLYKENdvDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLlD 353
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1491308087 312 EPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDK 352
Cdd:cd04946 354 KDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEV 394
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
202-362 |
5.58e-11 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 63.90 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 202 KRSPDIIRAFALVYKKHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAAL 281
Cdd:PRK15179 530 KRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLI 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 282 EALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQ--LAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYEK 359
Cdd:PRK15179 610 EAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTApdVAEALARIHDMCAADPGIARKAADWASARFSLNQMIASTVR 689
|
...
gi 1491308087 360 LYE 362
Cdd:PRK15179 690 CYQ 692
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
204-363 |
1.91e-10 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 61.73 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 204 SPD-----IIRAFALVYKKHKNIKLEMVG------SGPELEYCRD-LAISLGLKDQIVFRGSLlnVPKVLCE----TDVF 267
Cdd:PRK15484 203 SPDkgillLMQAFEKLATAHSNLKLVVVGdptassKGEKAAYQKKvLEAAKRIGDRCIMLGGQ--PPEKMHNyyplADLV 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 268 IIPSEI-ESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGF-TAEPGNVKQLAQYMTILLEDNNLRQkFSEAAIKDAR 345
Cdd:PRK15484 281 VVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADPELTQ-IAEQAKDFVF 359
|
170
....*....|....*...
gi 1491308087 346 ERFHPDKIISQYEKLYED 363
Cdd:PRK15484 360 SKYSWEGVTQRFEEQIHN 377
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
207-348 |
3.71e-10 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 60.68 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 207 IIRAFALVYKKH---KNIKLEMVGS----GPE----LEYCRDLAISL-GLKDQIVF--------RGSLLNVPKVLCETdv 266
Cdd:cd03805 229 AIEAFAKLKQKLpefENVRLVIAGGydprVAEnveyLEELQRLAEELlNVEDQVLFlrsisdsqKEQLLSSALALLYT-- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 267 fiiPSEiESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPgNVKQLAQYMTILLEDNNLRQKFSEAAIKDARE 346
Cdd:cd03805 307 ---PSN-EHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKE 381
|
..
gi 1491308087 347 RF 348
Cdd:cd03805 382 KF 383
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
154-348 |
5.53e-10 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 60.32 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 154 IKKHYNITKEIKTIYNFVSPEKFNAKKRKKKTEQEEFVFshVSNFRQVKRSPDIIRAFALVYKKHK-----NIKLEMVGS 228
Cdd:cd03806 204 IRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRENQILS--IAQFRPEKNHPLQLRAFAELLKRLPesirsNPKLVLIGS 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 229 --GPE----LEYCRDLAISLGLKDQIVFRgslLNVP----KVLCETDVFIIPS-EIESFGLAALEALSCG-IPVIASTAG 296
Cdd:cd03806 282 crNEEdkerVEALKLLAKELILEDSVEFV---VDAPyeelKELLSTASIGLHTmWNEHFGIGVVEYMAAGlIPLAHASAG 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491308087 297 GLPEVV---KHEKTGFTAEpgNVKQLAQYM-TILLEDNNLRQKFSEAAIKDArERF 348
Cdd:cd03806 359 PLLDIVvpwDGGPTGFLAS--TPEEYAEAIeKILTLSEEERLQRREAARSSA-ERF 411
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
216-313 |
7.71e-10 |
|
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: 59.94 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 216 KKHKNIKLEMVGSGP---ELEYCRDlaiSLGLKDQIVFRGSL--LNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPV 290
Cdd:cd03796 220 KKHPNVRFIIGGDGPkriELEEMRE---KYQLQDRVELLGAVphEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLV 296
|
90 100
....*....|....*....|...
gi 1491308087 291 IASTAGGLPEVVKHEKTGFtAEP 313
Cdd:cd03796 297 VSTRVGGIPEVLPPDMILL-AEP 318
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
202-329 |
4.68e-09 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 57.41 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 202 KRSPDIIRAFALVYKKHKNIKLEMVGSGPELEY----------CRDLAISLGlkdQIVFRGSLLN--VPKVLCETDVFII 269
Cdd:TIGR04047 206 KNTIDLLEAFALLRARRPQAQLVIAGGATLFDYdayrrefrarAAELGVDPG---PVVITGPVPDadLPALYRCADAFAF 282
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 270 PSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEkTGFTAEPGNVKQLAQYMTILLED 329
Cdd:TIGR04047 283 PSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRF-DAAWADPSDPDSIADALALALDP 341
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
266-348 |
5.72e-08 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 54.60 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 266 VFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQ----LAQYMTILLEDNNLRQKFSEAAI 341
Cdd:PLN00142 669 AFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEaankIADFFEKCKEDPSYWNKISDAGL 748
|
....*..
gi 1491308087 342 KDARERF 348
Cdd:PLN00142 749 QRIYECY 755
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
12-154 |
1.95e-07 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 50.09 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 12 GGSGIVGTELGLELQKRGHEIHFISYQLPERL--KLEEKFTFHEVNILSYPLFkykPYTIILAAKIVELFKKYKIDLFHG 89
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRpeLVGDGVRVHRLPVPPRPSP---LADLAALRRLRRLLRAERPDVVHA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491308087 90 HYaiPHSTSLYLAKQTNNRIKIVSTLHGSDIHLLG--LDKAYKPILETSLNNHDALTTVSNFMVRFI 154
Cdd:pfam13579 78 HS--PTAGLAARLARRRRGVPLVVTVHGLALDYGSgwKRRLARALERRLLRRADAVVVVSEAEAELL 142
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
206-362 |
7.57e-07 |
|
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: 50.46 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 206 DIIRAFALVYKKHKNIKLEMVGS-GPEL------EYCRDLAISLGLKDQIVF-RGSLLN--VPKVLCETDVFIIP--SEI 273
Cdd:cd03822 204 ILLEALPELKAEFPDVRLVIAGElHPSLaryegeRYRKAAIEELGLQDHVDFhNNFLPEeeVPRYISAADVVVLPylNTE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 274 ESFGLAALEALSCGIPVIASTAGGLPEVVkHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPdKI 353
Cdd:cd03822 284 QSSSGTLSYAIACGKPVISTPLRHAEELL-ADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWE-SI 361
|
....*....
gi 1491308087 354 ISQYEKLYE 362
Cdd:cd03822 362 ADRYLRLFN 370
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
229-361 |
1.04e-06 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 50.31 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 229 GPELE---Y---CRDLAISLGLKDQIVFRGsLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVV 302
Cdd:NF038011 344 GPEEEdpaYaaeCRSLVASLGLQDKVKFLG-FQKIDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLI 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491308087 303 KhektGFTAE------PGNV------KQLAQYMTILLEDNNLRQKFSEAAIkdAR-ERFHPDK-IISQYEKLY 361
Cdd:NF038011 423 E----GLDEEdralgaAGEVvaiadpQALARAALDLLRDPQRWQAAQAAGL--ARvERYYTEElMFDRYRELY 489
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
211-359 |
4.58e-06 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 48.54 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 211 FALVY-KKHKNIKLEMVGSGPELEYCRDLAISLGLKDQIVFRGSLLNVPKVLCETDVFIIPSEIESFGLAALEALSCGIP 289
Cdd:PRK15490 419 FAARYlQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVP 498
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491308087 290 VIASTAGGLPEVVKHEKTGFT---AEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYEK 359
Cdd:PRK15490 499 VISTPAGGSAECFIEGVSGFIlddAQTVNLDQACRYAEKLVNLWRSRTGICQQTQSFLQERFTVEHMVGTFVK 571
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
265-363 |
2.00e-05 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 46.40 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 265 DVFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVK------HEKTGFTAEPGNVKQLAQYM--TILLEDNnlRQKF 336
Cdd:cd03791 370 DFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFdydpetGEGTGFVFEDYDAEALLAALrrALALYRN--PELW 447
|
90 100
....*....|....*....|....*..
gi 1491308087 337 SEAAIKDARERFHPDKIISQYEKLYED 363
Cdd:cd03791 448 RKLQKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
281-358 |
2.95e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 42.21 E-value: 2.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491308087 281 LEALSCGIPVIASTAGGLPEVVKHEKTGFTAEpgNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKIISQYE 358
Cdd:pfam13524 17 FEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAEQLL 92
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
266-335 |
1.19e-04 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 44.00 E-value: 1.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 266 VFIIPSEIESFGLAALEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQK 335
Cdd:TIGR02468 574 VFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLWAE 643
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
275-357 |
1.77e-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: 43.12 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308087 275 SFGLaaLEALSCGIPVIASTAGGLPEVVKHEKTGFTAEPGNVKQLAQYMTILLEDNNLRQKFSEAAIKDARERFHPDKII 354
Cdd:cd03818 314 SWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCL 391
|
...
gi 1491308087 355 SQY 357
Cdd:cd03818 392 ARY 394
|
|
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
286-349 |
3.23e-03 |
|
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
Pssm-ID: 340843 [Multi-domain] Cd Length: 411 Bit Score: 39.18 E-value: 3.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491308087 286 CGIPVIASTAGGLPEVVKHEKTGFTAEPGnvKQLAQYMTILLED--NNLRQKFSEAAIKDARERFH 349
Cdd:cd03816 337 CGLPVCAMDFKCIGELVKHGVNGLVFGDS--EELAEQLIDLLSDfdRGKLNVLKKGAQEESENRWD 400
|
|
| PRK07417 |
PRK07417 |
prephenate/arogenate dehydrogenase; |
1-38 |
4.94e-03 |
|
prephenate/arogenate dehydrogenase;
Pssm-ID: 180970 [Multi-domain] Cd Length: 279 Bit Score: 38.34 E-value: 4.94e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1491308087 1 MRIGIInyptfgGSGIVGTELGLELQKRGHEIHFISYQ 38
Cdd:PRK07417 1 MKIGIV------GLGLIGGSLGLDLRSLGHTVYGVSRR 32
|
|
| |
