|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-371 |
2.56e-64 |
|
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: 209.32 E-value: 2.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 2 KIAMIGQKGiPARSGGIERHVEELSAELASRGHEVLVFCRSWYTWPIRDHRGVRCIKTWSLPSKHLDAIShtftsILRAV 81
Cdd:cd03801 1 KILLLSPEL-PPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARR-----LLREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 82 R-----EKVDVFHFHGVGPSLLAWLPKLLRpSAKVVVTFHCID--RHHQKWGRMARLMLYIGERFACTipDATIAVSKTL 154
Cdd:cd03801 75 RpllrlRKFDVVHAHGLLAALLAALLALLL-GAPLVVTLHGAEpgRLLLLLAAERRLLARAEALLRRA--DAVIAVSEAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 155 ETYCRLSYGVT---TKYIPNGtqIRLEDSDPILIKPFGLEPGKYMMMC-ARLVRHKGAHTLIAAWKRLKKTHPELvgdtK 230
Cdd:cd03801 152 RDELRALGGIPpekIVVIPNG--VDLERFSPPLRRKLGIPPDRPVLLFvGRLSPRKGVDLLLEALAKLLRRGPDV----R 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 231 LAIVGGSaftDDYVRELERLVKD-EPSIVLTGNQSGETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPEN 309
Cdd:cd03801 226 LVIVGGD---GPLRAELEELELGlGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGL 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818897881 310 LELTQD--HGLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYDWKDIAETTDYLYE 371
Cdd:cd03801 303 PEVVEDgeGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
10-366 |
1.43e-37 |
|
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: 139.04 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 10 GIPARSGGIERHVEELSAELASRGHEVLVFCRSW--------YTWPIRDHRGVRCIKTWSLPSKHLdaishtFTSILRAV 81
Cdd:cd03809 8 SLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPlpgellrlLREYPELSLGVIKIKLWRELALLR------WLQILLPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 82 REKVDVFH-FHGVGPsllawlpkLLRPSAKVVVTFH----CIDRHHQKWGR--MARLMLYIGERFActipDATIAVSKTL 154
Cdd:cd03809 82 KDKPDLLHsPHNTAP--------LLLKGCPQVVTIHdlipLRYPEFFPKRFrlYYRLLLPISLRRA----DAIITVSEAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 155 ETYCRLSYGV---TTKYIPNGT-QIRLEDSDPILIKPFGLEPGKYMMMCARLVRHKGAHTLIAAWKRLKKTHPELvgdtK 230
Cdd:cd03809 150 RDDIIKFYGVppeKIVVIPLGVdPSFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDL----K 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 231 LAIVGGSAFTDDYVRELERLVKDEPSIVLTGNQSGETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENL 310
Cdd:cd03809 226 LVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLP 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 818897881 311 ELTQDHGLTFEAGNEKDLASQLKMLLENPELVNAVgAEARIHIAKHYDWKDIAETT 366
Cdd:cd03809 306 EVAGDAALYFDPLDPESIADAILRLLEDPSLREEL-IRKGLERAKKFSWEKTAEKT 360
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-358 |
2.70e-37 |
|
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: 138.11 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 2 KIAMIGqkgipARSGGIERHVEELSAELASRGHEVLVFCrswytwPIRDHRGVRC----IKTWSLP-SKHLDAISHTFTS 76
Cdd:cd03808 1 KILFIV-----NVDGGFQSFRLPLIKALVKKGYEVHVIA------PDGDKLSDELkelgVKVIDIPiLRRGINPLKDLKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 77 ILRAVR----EKVDVFHFHGVGPSLLAWLPKLLRPSAKVVVTFHCIdRHHQKWGRMARLMLYIGERFACTIPDATIAVS- 151
Cdd:cd03808 70 LFKLYKllkkEKPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHGL-GFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNe 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 152 ---KTLETYCRLSYGVTTKYIPNGtqirlEDSDPILIKPFGLEPGKY-MMMCARLVRHKGAHTLIAAWKRLKKTHPELvg 227
Cdd:cd03808 149 ddrDLAIKKGIIKKKKTVLIPGSG-----VDLDRFQYSPESLPSEKVvFLFVARLLKDKGIDELIEAAKILKKKGPNV-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 228 dtKLAIVGGSAFTDDYVRELERLVKdEPSIVLTGNQSgeTLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIP 307
Cdd:cd03808 222 --RFLLVGDGELENPSEILIEKLGL-EGRIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVP 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 818897881 308 ENLELTQDH--GLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYD 358
Cdd:cd03808 297 GCRELVIDGvnGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFD 349
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
15-364 |
3.25e-30 |
|
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: 118.88 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 15 SGGIERHVEELSAELASRGHEVLVFcrSWYTWPIRD----HRGVRCIKTWSLPSKHLDAISHTFTSI--LRAVREKVDVF 88
Cdd:cd03820 12 AGGAERVAINLANHLAKKGYDVTII--SLDSAEKPPfyelDDNIKIKNLGDRKYSHFKLLLKYFKKVrrLRKYLKNNKPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 89 HFHGVGPSLLAWLPKLLRPSaKVVVTFHcIDRHHQKWGRMARLMLYIGERFActipDATIAVSKTLETYCRLSYGVTTKY 168
Cdd:cd03820 90 VVISFRTSLLTFLALIGLKS-KLIVWEH-NNYEAYNKGLRRLLLRRLLYKRA----DKIVVLTEADKLKKYKQPNSNVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 169 IPNgtqirledsdPILIKPFGLEP---GKYMMMCARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIVG-GSAFTddyv 244
Cdd:cd03820 164 IPN----------PLSFPSEEPSTnlkSKRILAVGRLTYQKGFDLLIEAWALIAKKHP----DWKLRIYGdGPERE---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 245 rELERLVKD---EPSIVLTGNQSGetLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENL-ELTQDH--GL 318
Cdd:cd03820 226 -ELEKLIDKlglEDRVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPsEIIEDGenGL 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 818897881 319 TFEAGNEKDLASQLKMLLENPELVNAVGAEARiHIAKHYDWKDIAE 364
Cdd:cd03820 303 LVPNGDVDALAEALLRLMEDEELRKKMGKNAR-KNAERFSIEKIIK 347
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
12-364 |
4.67e-29 |
|
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: 115.94 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 12 PARSGGIERHVEELSAELASRGHEVLVFCrsWYTWPIRDHRGVRCIKTWSLPSKHLDAISHTF---------------TS 76
Cdd:cd03798 10 NANSPGRGIFVRRQVRALSRRGVDVEVLA--PAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKprlrllaplrapslaKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 77 ILRAVREKVDVFHFHGVGPSLLAWLPKLLRPSAKVVVTFHCIDRH-HQKWGRMARLMLYIGERFACTIpdatiAVSKTL- 154
Cdd:cd03798 88 LKRRRRGPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHGSDINvFPPRSLLRKLLRWALRRAARVI-----AVSKALa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 155 ETYCRL-SYGVTTKYIPNGTQIRL-EDSDPILIKPfglEPGKYMMMCARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLA 232
Cdd:cd03798 163 EELVALgVPRDRVDVIPNGVDPARfQPEDRGLGLP---LDAFVILFVGRLIPRKGIDLLLEAFARLAKARP----DVVLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 233 IVG-GSAFtdDYVRELERLVKDEPSIVLTGnqsgETLHTLFSNSYAAIH----PSESEGLPIAVLEAMGYGKCVLSSN-- 305
Cdd:cd03798 236 IVGdGPLR--EALRALAEDLGLGDRVTFTG----RLPHEQVPAYYRACDvfvlPSRHEGFGLVLLEAMACGLPVVATDvg 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 306 -IPENLElTQDHGLTFEAGNEKDLASQLKMLLENPELvNAVGAEARIHIAKHYDWKDIAE 364
Cdd:cd03798 310 gIPEVVG-DPETGLLVPPGDADALAAALRRALAEPYL-RELGEAARARVAERFSWVKAAD 367
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
194-350 |
1.29e-28 |
|
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: 109.29 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 194 KYMMMCARLVRHKGAHTLIAAWKRLKKTHPELvgdtKLAIVGGSaftdDYVRELERLVKD---EPSIVLTGNQSGETLHT 270
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNL----KLVIAGDG----EEEKRLKKLAEKlglGDNVIFLGFVSDEDLPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 271 LFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQDH--GLTFEAGNEKDLASQLKMLLENPELVNAVGAE 348
Cdd:pfam00534 75 LLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGetGFLVKPNNAEALAEAIDKLLEDEELRERLGEN 154
|
..
gi 818897881 349 AR 350
Cdd:pfam00534 155 AR 156
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
13-354 |
1.40e-27 |
|
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: 111.30 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 13 ARSGGIERHVEELSAELASRGHEVLVFCRS---WYTWPIRDHRGVRCIKTWSLPSKHLDAISHT--FTSILRavREKVDV 87
Cdd:cd03811 9 LSGGGAERVLLNLANALDKRGYDVTLVLLRdegDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAIlkLKRILK--RAKPDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 88 FHFHGVGPSllAWLPKLLRPSAKVVVTFHCiDRHHQKWGRMARLMLYIGERFActipDATIAVSKTLE---TYCRLSYGV 164
Cdd:cd03811 87 VISFLGFAT--YIVAKLAAARSKVIAWIHS-SLSKLYYLKKKLLLKLKLYKKA----DKIVCVSKGIKedlIRLGPSPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 165 TTKYIPNGtqIRLEDSDPILIKPFGLEP--GKYMMMCARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIVG-GSAFTd 241
Cdd:cd03811 160 KIEVIYNP--IDIDRIRALAKEPILNEPedGPVILAVGRLDPQKGHDLLIEAFAKLRKKYP----DVKLVILGdGPLRE- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 242 dyvrELERLVKD---EPSIVLTGNQSgetlhtlfsNSYAAI-------HPSESEGLPIAVLEAMGYGKCVLSSNIPENLE 311
Cdd:cd03811 233 ----ELEKLAKElglAERVIFLGFQS---------NPYPYLkkadlfvLSSRYEGFPNVLLEAMALGTPVVSTDCPGPRE 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 818897881 312 LTQDH--GLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIA 354
Cdd:cd03811 300 ILDDGenGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEA 344
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
14-357 |
9.34e-27 |
|
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: 108.98 E-value: 9.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 14 RSGGIERHVEELSAELASRGHEVLVFCRSWYTWPIRDHRGvrcIKTWSLPSKHLDAISHTFTSILRAVREKVDVFHFHGV 93
Cdd:cd03819 9 EIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIG---IGLPGLKVPLLRALLGNVRLARLIRRERIDLIHAHSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 94 GPSLLAWL-PKLLRPsaKVVVTFHCIDRHHQKWGRMARLMLYIGERFactipdatIAVSKTLETYCRLSYGVT---TKYI 169
Cdd:cd03819 86 APAWLGWLaSRLTGV--PLVTTVHGSYLATYHPKDFALAVRARGDRV--------IAVSELVRDHLIEALGVDperIRVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 170 PNGTQIR--LEDSDPILIKPFGLEPGKYM-MMCARLVRHKGAHTLIAAWKRLKKthpelvGDTKLAIVGGSAFTDDYVRE 246
Cdd:cd03819 156 PNGVDTDrfPPEAEAEERAQLGLPEGKPVvGYVGRLSPEKGWLLLVDAAAELKD------EPDFRLLVAGDGPERDEIRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 247 LERLVKDEPSIVLTGNQsgETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELT--QDHGLTFEAGN 324
Cdd:cd03819 230 LVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVvhGRTGLLVPPGD 307
|
330 340 350
....*....|....*....|....*....|...
gi 818897881 325 EKDLASQLKMLLENPELvnAVGAEARIHIAKHY 357
Cdd:cd03819 308 AEALADAIRAAKLLPEA--REKLQAAAALTEAV 338
|
|
| GT4-like |
cd04955 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-364 |
1.03e-26 |
|
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: 109.51 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 2 KIAMIGQKGIPARSGGIERHVEELSAELASRGHEVLVFCRSW-YTWPIRDHRGVRCIKTwSLPS-KHLDAISHTFTSILR 79
Cdd:cd04955 1 HIFIIGSRGLPAKYGGFETFVEKLTERQQSDNIKYHVACLSEnSKQQHFEYNGADCFYV-KVPKiGPARAIAYDIAALNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 80 AVRE------KVDVFHFHG--VGPSLLAWLPKLLRPSAKVVVTFHCIDRHHQKWGRMARLMLYIGERFACTIPDATIAVS 151
Cdd:cd04955 80 ALKYikeqniKNPIFYILAcrIGPFIAPYIKKIHKLGGKLFVNPDGLEWKRAKWSLPVRKYWKFSESLMVKHADLLICDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 152 KTLETYCRLSYG-VTTKYIPNGTQIR---LEDSDPILI---KPFGLEPGKYMMMCARLVRHKGAHTLIAAW--KRLKKth 222
Cdd:cd04955 160 KNIEKYIRKEYGkSNTTFIAYGTDTLkssLSDEDEKVRewyKEKGVKPGKYYLIVGRFVPENNYETMIREFmkSSTKR-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 223 pelvgdtKLAIVGGSAFTDDYVRELERLVKD-EPSIVLTG---NQsgETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYG 298
Cdd:cd04955 238 -------DLVIITNVEGNAYYELLLKKTAFDhDERIKFVGtvyDQ--ELLKYIRENAFAYLHGHEVGGTNPSLLEALGST 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818897881 299 KCVLSSNIPENLELTQDHGLTFEAGNEKDLASQLKMLleNPELVNAVGAEARIHIAKHYDWKDIAE 364
Cdd:cd04955 309 DLNLLLDVGFNREVAEDAALYWKKEPLASLIDEVDNL--NPDEISDLGKKAKQRIEEAYTWEKIVD 372
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-364 |
1.65e-26 |
|
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: 109.35 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 2 KIAMIGQKGIPArSGGIERHVEELSAELASRGHEVLVFCRSW-------YTWPIRDHRGVRCIKTWSLPSK-------HL 67
Cdd:cd03794 1 KILLISQYYPPP-KGAAAARVYELAKELVRRGHEVTVLTPSPnyplgriFAGATETKDGIRVIRVKLGPIKknglirrLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 68 DAISHTFTSILRAV--REKVDVFHFHgVGPSLLAWLPKLL--RPSAKVVVTFHciDRHHQ--------KWGRMARLMLYI 135
Cdd:cd03794 80 NYLSFALAALLKLLvrEERPDVIIAY-SPPITLGLAALLLkkLRGAPFILDVR--DLWPEslialgvlKKGSLLKLLKKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 136 gERFACTIPDATIAVSKTLETYCRLSYGVTTK--YIPNGTQI-RLEDSDPILIKPFGLEPGKYMMMCARLVRHK-GAHTL 211
Cdd:cd03794 157 -ERKLYRLADAIIVLSPGLKEYLLRKGVPKEKiiVIPNWADLeEFKPPPKDELRKKLGLDDKFVVVYAGNIGKAqGLETL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 212 IAAWKRLKKTHpelvgDTKLAIVGGSaftdDYVRELERLVKDE--PSIVLTGNQSGETLHTLFSNS---YAAIHPSESEG 286
Cdd:cd03794 236 LEAAERLKRRP-----DIRFLFVGDG----DEKERLKELAKARglDNVTFLGRVPKEEVPELLSAAdvgLVPLKDNPANR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 287 --LPIAVLEAMGYGKCVLSSNIPEN--LELTQDHGLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYDWKDI 362
Cdd:cd03794 307 gsSPSKLFEYMAAGKPILASDDGGSdlAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKL 386
|
..
gi 818897881 363 AE 364
Cdd:cd03794 387 AD 388
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
15-371 |
3.30e-25 |
|
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: 105.09 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 15 SGGIERHVEELSAELASRGHEVLVFCRSwytwpirdHRGVRC--IKTWSLPSKHLDAIS-HTFTSILRA----VREKVDV 87
Cdd:cd03807 11 VGGAETMLLRLLEHMDKSRFEHVVISLT--------GDGVLGeeLLAAGVPVVCLGLSSgKDPGVLLRLakliRKRNPDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 88 FHFHGVGPSLLAWLPKLLrpsAKVVVTFHCIdRHHQKWGRMARLMLYIgERFACTIPDATIAVSKT-LETYcrLSYGV-- 164
Cdd:cd03807 83 VHTWMYHADLIGGLAAKL---AGGVKVIWSV-RSSNIPQRLTRLVRKL-CLLLSKFSPATVANSSAvAEFH--QEQGYak 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 165 -TTKYIPNGtqIRLEDSDP------ILIKPFGLEPGKYMMMC-ARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIVGG 236
Cdd:cd03807 156 nKIVVIYNG--IDLFKLSPddasraRARRRLGLAEDRRVIGIvGRLHPVKDHSDLLRAAALLVETHP----DLRLLLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 237 SAFTDDYVRELERLVKDEpSIVLTGNQSgeTLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQDH 316
Cdd:cd03807 230 GPERPNLERLLLELGLED-RVHLLGERS--DVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 818897881 317 -GLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYDWKDIAETTDYLYE 371
Cdd:cd03807 307 tGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
12-354 |
1.28e-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: 103.18 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 12 PARSGGIERHVEELSAELASRGHEVLVFC----RSWYTWPIRDHRGVRCIKTWSLPSKHLDAISHTFT-------SILRA 80
Cdd:cd03823 11 PQRVGGAEISVHDLAEALVAEGHEVAVLTagvgPPGQATVARSVVRYRRAPDETLPLALKRRGYELFEtynpglrRLLAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 81 V--REKVDVFHFH---GVGPSLLAWLPKLLRPsakVVVTFH-----CiDRHHQ-KWGRmarlmlyigerfactipDATIA 149
Cdd:cd03823 91 LleDFRPDVVHTHnlsGLGASLLDAARDLGIP---VVHTLHdywllC-PRQFLfKKGG-----------------DAVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 150 VSK-TLETYCRLsyGVTTK---YIPNG-------TQIRLEDSDPILIKPFGlepgkymmmcaRLVRHKGAHTLIAAWKRL 218
Cdd:cd03823 150 PSRfTANLHEAN--GLFSArisVIPNAvepdlapPPRRRPGTERLRFGYIG-----------RLTEEKGIDLLVEAFKRL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 219 KKTHPELVgdtklaIVGGSAFTDdyvrelERLVKDEPSIVLTGNQSGETLHTLFSNSYAAIHPSE-SEGLPIAVLEAMGY 297
Cdd:cd03823 217 PREDIELV------IAGHGPLSD------ERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAA 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 818897881 298 GKCVLSSNIPENLELTQD--HGLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIA 354
Cdd:cd03823 285 GLPVIASDLGGIAELIQPgvNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRS 343
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
16-172 |
5.64e-23 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 94.52 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 16 GGIERHVEELSAELASRGHEVLVFCRSWYTWPIRDHRGVRCIKTWSLPSKHLDAISHTFTSILRAV--REKVDVFHFHGV 93
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLlrRERPDVVHAHSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 94 GPSLLAWLPKLLRPSAKVVVTFHCID----RHHQKWGRMARLMLYIgERFACTIPDATIAVSKTLETYCRLSYGVT---T 166
Cdd:pfam13439 81 FPLGLAALAARLRLGIPLVVTYHGLFpdykRLGARLSPLRRLLRRL-ERRLLRRADRVIAVSEAVADELRRLYGVPpekI 159
|
....*.
gi 818897881 167 KYIPNG 172
Cdd:pfam13439 160 RVIPNG 165
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
268-371 |
1.26e-22 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 91.98 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 268 LHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQD--HGLTFEAGNEKDLASQLKMLLENPELVNAV 345
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDgeTGLLVPPGDPEALAEAILRLLEDPELRRRL 93
|
90 100
....*....|....*....|....*.
gi 818897881 346 GAEARIHIAKHYDWKDIAETTDYLYE 371
Cdd:COG0438 94 GEAARERAEERFSWEAIAERLLALYE 119
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
193-338 |
1.56e-22 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 92.19 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 193 GKYMMMCARLV-RHKGAHTLIAAWKRLKKTHpelvGDTKLAIVGgsaftDDYVRELERLVKD-EPSIVLTGNQsgETLHT 270
Cdd:pfam13692 1 RPVILFVGRLHpNVKGVDYLLEAVPLLRKRD----NDVRLVIVG-----DGPEEELEELAAGlEDRVIFTGFV--EDLAE 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818897881 271 LFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLEL-TQDHGLTFEAGNEKDLASQLKMLLEN 338
Cdd:pfam13692 70 LLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELvDGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
16-357 |
5.66e-22 |
|
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: 95.80 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 16 GGIERHVEELSAELASRGHEVLVFCRS----WYTWPIRDHRgVRCIKTW----SLPskhldaISHTFTSILRAVREKVDV 87
Cdd:cd03795 14 GGIEQVIYDLAEGLKKKGIEVDVLCFSkekeTPEKEENGIR-IHRVKSFlnvaSTP------FSPSYIKRFKKLAKEYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 88 FHFHgvGPSLLAWLPKLL-RPSAKVVVTFHCiDRHHQKWGRM-----ARLMLYIGERFACTIPDaTIAVSKTLEtycrlS 161
Cdd:cd03795 87 IHYH--FPNPLADLLLFFsGAKKPVVVHWHS-DIVKQKKLLKlykplMTRFLRRADRIIATSPN-YVETSPTLR-----E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 162 YGVTTKYIPNGTQIRLEDSDPILIKPFGLE-PGKYMMM-CARLVRHKGAHTLIAAWKRLKkthPELVgdtklaIVGGSAF 239
Cdd:cd03795 158 FKNKVRVIPLGIDKNVYNIPRVDFENIKREkKGKKIFLfIGRLVYYKGLDYLIEAAQYLN---YPIV------IGGEGPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 240 TDDYVRELERLVKDEpsIVLTGNQSGETLHTLFSNSYAAIHPS--ESEGLPIAVLEAMGYGKCVLSSNIPENLELTQDH- 316
Cdd:cd03795 229 KPDLEAQIELNLLDN--VKFLGRVDDEEKVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNg 306
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 818897881 317 --GLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHY 357
Cdd:cd03795 307 etGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELF 349
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
16-363 |
2.46e-19 |
|
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: 88.58 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 16 GGIERHVEELSAELASRGHEVLVFCRSWYTWPIRDHRGVR-CIKTWSLPSKHL--DAISHTFTS--ILRAVREKV---DV 87
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRyIPPQDGFASIPLlrQGAGRTDFSpgLPNWLRRNLreyDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 88 FHFHGV-GPSLLAWL--------PKLLRPSAKVVVTFHciDRHHQKWgrmaRLMLYIGERFACTIPDATIAVSKTLETYC 158
Cdd:cd03821 94 VHIHGVwTYTSLAACklarrrgiPYVVSPHGMLDPWAL--QQKHWKK----RIALHLIERRNLNNAALVHFTSEQEADEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 159 RlSYGVTTK--YIPNGTQIRLEDSDPILIKPFGLEPG-KYMMMCARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIVG 235
Cdd:cd03821 168 R-RFGLEPPiaVIPNGVDIPEFDPGLRDRRKHNGLEDrRIILFLGRIHPKKGLDLLIRAARKLAEQGR----DWHLVIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 236 GSafTDDYVRELERLVKD--EPSIVLTGNQSGETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSS---NIPEnl 310
Cdd:cd03821 243 PD--DGAYPAFLQLQSSLglGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITdkcGLSE-- 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 818897881 311 ELTQDHGLTFEAgNEKDLASQLKMLLENPELVNAVGAEAR--IHIAKHYDWKDIA 363
Cdd:cd03821 319 LVEAGCGVVVDP-NVSSLAEALAEALRDPADRKRLGEMARraRQVEENFSWEAVA 372
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
3-320 |
2.61e-19 |
|
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: 85.92 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 3 IAMIGQkGIPARSGGIERHVEELSAELASRGHEVLVFCRswytwpirdhrgvrciktwslpskhldAISHTFTSILRAVR 82
Cdd:cd01635 1 ILLVTG-EYPPLRGGLELHVRALARALAALGHEVTVLAL---------------------------LLLALRRILKKLLE 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 83 EKVDVFHFHGVGPSLLAWLPKLLRPSAKVVVTFHCIDRHHQKWGRMarlmlyigerfactipdatiavsktletycrlsy 162
Cdd:cd01635 53 LKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSLESTRSEL---------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 163 gvttkyipngtqirledsdPILIKPFGLEPGKYMMMCARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIVGGSAFTDD 242
Cdd:cd01635 99 -------------------LALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLP----DLVLVLVGGGGEREE 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818897881 243 YVRELERLVKDEPSIVLTGNQSGETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQDHGLTF 320
Cdd:cd01635 156 EEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
16-172 |
4.12e-18 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 80.52 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 16 GGIERHVEELSAELASRGHEVLVFCRSWYTW-PIRDHRGVRCIKTWsLPSKHLDAISHTFTSILRAV--REKVDVFHFHG 92
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGrPELVGDGVRVHRLP-VPPRPSPLADLAALRRLRRLlrAERPDVVHAHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 93 VGPSLLAWLPKLLRpSAKVVVTFHCIDRHHQKW--GRMARLMlyigERFACTIPDATIAVSKTLETYCRlSYGVT---TK 167
Cdd:pfam13579 80 PTAGLAARLARRRR-GVPLVVTVHGLALDYGSGwkRRLARAL----ERRLLRRADAVVVVSEAEAELLR-ALGVPaarVV 153
|
....*
gi 818897881 168 YIPNG 172
Cdd:pfam13579 154 VVPNG 158
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
22-371 |
3.34e-15 |
|
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: 76.16 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 22 VEELSAELASRGHEVLVFCrswytwPIRDHRG-----VRCIKTWSLPSKHLDA---ISHTFTSILRAVREKVDVFHFH-- 91
Cdd:cd03817 20 VRNLARALEKRGHEVYVIT------PSDPGAEdeeevVRYRSFSIPIRKYHRQhipFPFKKAVIDRIKELGPDIIHTHtp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 92 -GVGPSLLAWLPKLLRPsakVVVTFHCIDRHHQKWGRMARL-----MLYIGERFACTIpDATIAVSKTLETYCRlSYGVT 165
Cdd:cd03817 94 fSLGKLGLRIARKLKIP---IVHTYHTMYEDYLHYIPKGKLlvkavVRKLVRRFYNHT-DAVIAPSEKIKDTLR-EYGVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 166 TKY--IPNGTQIRL--EDSDPILIKPFGLEPGKYMMMCA-RLVRHKGAHTLIAAWKRLKKTHpelvgDTKLAIVGGSaft 240
Cdd:cd03817 169 GPIevIPNGIDLDKfeKPLNTEERRKLGLPPDEPILLYVgRLAKEKNIDFLLRAFAELKKEP-----NIKLVIVGDG--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 241 dDYVRELERLVKD---EPSIVLTG----NQSGE--TLHTLFsnsyaaIHPSESEGLPIAVLEAMGYGKCVL---SSNIPE 308
Cdd:cd03817 241 -PEREELKELARElglADKVIFTGfvprEELPEyyKAADLF------VFASTTETQGLVYLEAMAAGLPVVaakDPAASE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818897881 309 NLELTQDhGLTFEAGNEKdLASQLKMLLENPELVNAVGAEARIHIAKHydwkDIAETTDYLYE 371
Cdd:cd03817 314 LVEDGEN-GFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEISAREF----AFAKSVEKLYE 370
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
12-337 |
1.21e-14 |
|
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: 74.25 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 12 PARSGGIERHVEELSAELASRGHEVLVF--------CRSWYTWPirdhrgvrciKTWSLPSKHLDAISHTFTSILRAVRE 83
Cdd:cd03802 14 PGKYGGTELVVSALTEGLVRRGHEVTLFapgdshtsAPLVAVIP----------RALRLDPIPQESKLAELLEALEVQLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 84 --KVDVFHFHgvgpSLLAWLPKLLRPSAKVVVTFHCIDRhhqkwgrmarlmLYIGERFACTIPDATIAVSKTLETYCRLS 161
Cdd:cd03802 84 asDFDVIHNH----SYDWLPPFAPLIGTPFVTTLHGPSI------------PPSLAIYAAEPPVNYVSISDAQRAATPPI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 162 YGVTTkyIPNGtqIRLEDSdpilikPFGLEPGKYMMMCARLVRHKGAHTLIAAWKRLKKthpelvgdtKLAIVGGsAFTD 241
Cdd:cd03802 148 DYLTV--VHNG--LDPADY------RFQPDPEDYLAFLGRIAPEKGLEDAIRVARRAGL---------PLKIAGK-VRDE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 242 DYVRELERlVKDEPSIVLTGNQSGETLHTLFSNSYAAIHPS---ESEGLpiAVLEAMGYGKCVLSSN---IPEnlelTQD 315
Cdd:cd03802 208 DYFYYLQE-PLPGPRIEFIGEVGHDEKQELLGGARALLFPInwdEPFGL--VMIEAMACGTPVIAYRrggLPE----VIQ 280
|
330 340
....*....|....*....|...
gi 818897881 316 HGLT-FEAGNEKDLASQLKMLLE 337
Cdd:cd03802 281 HGETgFLVDSVEEMAEAIANIDR 303
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
82-371 |
3.28e-14 |
|
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: 73.19 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 82 REKVDVFHF--HGV---GPSLLAWLPKLLRPSAKVVVTFHCI----DRHHQKWGRMARL---------MLYIGERFACTI 143
Cdd:cd03822 73 FKKPDVVHIqhEFGifgGKYGLYALGLLLHLRIPVITTLHTVldlsDPGKQALKVLFRIatlservvvMAPISRFLLVRI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 144 ---PDATIAVsktletycrlsygvttkyIPNGTQIRLEDSDPILIKPFGLEPGKYMMMCARLVRHKGAHTLIAAWKRLKK 220
Cdd:cd03822 153 kliPAVNIEV------------------IPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 221 THPELVgdtkLAIVGGSAFTDDY-------VRELERLVKDEPSIVLTGNQSGETLHTLFSNS--YAAIHPSESEGLPIAV 291
Cdd:cd03822 215 EFPDVR----LVIAGELHPSLARyegeryrKAAIEELGLQDHVDFHNNFLPEEEVPRYISAAdvVVLPYLNTEQSSSGTL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 292 LEAMGYGKCVLSSNIPENLE-LTQDHGLTFEAGNEKDLASQLKMLLENPELVNAVgAEARIHIAKHYDWKDIAETTDYLY 370
Cdd:cd03822 291 SYAIACGKPVISTPLRHAEElLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAI-AERAYAYARAMTWESIADRYLRLF 369
|
.
gi 818897881 371 E 371
Cdd:cd03822 370 N 370
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-373 |
3.62e-14 |
|
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: 73.15 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 1 MKIAM-----IGQKGIPArsggierhvEELSAELASRGHEVLVFCrswYTWPIR---DHRGVRC--IKTWSLPSKHLDAI 70
Cdd:cd04962 1 MKIGIvcypsYGGSGVVA---------TELGLELAERGHEVHFIS---SAIPFRlnlYSGNIFFheVEVPNYPLFEYPPY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 71 SHTFTSILRAV--REKVDVFHFHGVGP-SLLAWLPK-LLRPSAKVVVTFHCID-----RHHQkwgrmarlmLYIGERFAC 141
Cdd:cd04962 69 TLALASKIVEVakEHKLDVLHAHYAIPhASCAYLAReILGEKIPIVTTLHGTDitlvgYDPS---------LQPAVRFSI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 142 TIPDATIAVSKTLETYCRLSYGVTTKY--IPN---GTQIRLEDSDPILIKPFGLEPGKYMMMCARLVRHKGAHTLIAAWK 216
Cdd:cd04962 140 NKSDRVTAVSSSLRQETYELFDVDKDIevIHNfidEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 217 RLKKTHPelvgdTKLAIVGGS---AFTDDYVRELErlVKDEpsIVLTGNQsgETLHTLFSNSYAAIHPSESEGLPIAVLE 293
Cdd:cd04962 220 RVRRKIP-----AKLLLVGDGperVPAEELARELG--VEDR--VLFLGKQ--DDVEELLSIADLFLLPSEKESFGLAALE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 294 AMGYGKCVLSSN---IPENLeltqDHGLT---FEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYDWKDIAETTD 367
Cdd:cd04962 289 AMACGVPVVSSNaggIPEVV----KHGETgflSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYE 364
|
....*.
gi 818897881 368 YLYELL 373
Cdd:cd04962 365 AYYRRL 370
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
2-366 |
6.15e-14 |
|
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: 72.66 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 2 KIAMIGQKGIP------ARSGGIERHVEELSAELASRGHEVLVFCR-------SWytwpIRDHRGVRCI----------- 57
Cdd:cd03800 1 RIALISVHGSPlaqpggADTGGQNVYVLELARALAELGYQVDIFTRrispadpEV----VEIAPGARVIrvpagppeylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 58 KTWSLPskHLDAISHTFTSILRAVREKVDVFHFH----GVGPSLLAwlpKLLRpsAKVVVTFHCIDR----HHQKWGR-- 127
Cdd:cd03800 77 KEELWP--YLEEFADGLLRFIAREGGRYDLIHSHywdsGLVGALLA---RRLG--VPLVHTFHSLGRvkyrHLGAQDTyh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 128 -MARLmlyIGERFACTIPDATIAVSK--TLETYCRLS-YGVTTKYIPNGTQIRL----EDSDPILIkPFGLEPGKYMMM- 198
Cdd:cd03800 150 pSLRI---TAEEQILEAADRVIASTPqeADELISLYGaDPSRINVVPPGVDLERffpvDRAEARRA-RLLLPPDKPVVLa 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 199 CARLVRHKGAHTLIAAWKRLkkthPELVGDTKLAIVGGS-----AFTDDYVRELERLVKDEPSIVLTGNQSGETLHTLFS 273
Cdd:cd03800 226 LGRLDPRKGIDTLVRAFAQL----PELRELANLVLVGGPsddplSMDREELAELAEELGLIDRVRFPGRVSRDDLPELYR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 274 NSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQD--HGLTFEAGNEKDLASQLKMLLENPELVNAVGAEARI 351
Cdd:cd03800 302 AADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDgrTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLE 381
|
410
....*....|....*
gi 818897881 352 HIAKHYDWKDIAETT 366
Cdd:cd03800 382 RARAHYTWESVADQL 396
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
88-358 |
8.14e-14 |
|
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: 72.10 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 88 FHFHGVgpslLAWlPKLLRPSAKVVVTFHCID---RHHQKWGRMARLMLYIGERFACTIPDAT-IAVSKtletycrlsyG 163
Cdd:cd05844 89 FGRDGV----YAL-PLARALGVPLVVTFHGFDittSRAWLAASPGWPSQFQRHRRALQRPAALfVAVSG----------F 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 164 VTTKYIPNGTQIRLEDSDPILIKPFGLEPG------KYMMMCARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIVGGS 237
Cdd:cd05844 154 IRDRLLARGLPAERIHVHYIGIDPAKFAPRdpaeraPTILFVGRLVEKKGCDVLIEAFRRLAARHP----TARLVIAGDG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 238 AFTddyvRELERLVKDEPSIVLTGNQSGETLHTLFSNSYAAIHPS------ESEGLPIAVLEAMGYGKCVLSS---NIPE 308
Cdd:cd05844 230 PLR----PALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSrhgGIPE 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 818897881 309 NLELTQDhGLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYD 358
Cdd:cd05844 306 AILDGET-GFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFD 354
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
191-360 |
2.69e-13 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 70.90 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 191 EPGKYMMMC-ARLvrhkGAHTLIAAWKRLKKTHPElvgdTKLAIVGGSAftddYVRELERLVKDEPSiVLTGNQSGETLh 269
Cdd:PLN02871 260 EPEKPLIVYvGRL----GAEKNLDFLKRVMERLPG----ARLAFVGDGP----YREELEKMFAGTPT-VFTGMLQGDEL- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 270 tlfSNSYAA----IHPSESEGLPIAVLEAMGYG---KCVLSSNIPENL--ELTQDHGLTFEAGNEKDLASQLKMLLENPE 340
Cdd:PLN02871 326 ---SQAYASgdvfVMPSESETLGFVVLEAMASGvpvVAARAGGIPDIIppDQEGKTGFLYTPGDVDDCVEKLETLLADPE 402
|
170 180
....*....|....*....|
gi 818897881 341 LVNAVGAEARIHIAKhYDWK 360
Cdd:PLN02871 403 LRERMGAAAREEVEK-WDWR 421
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
179-375 |
5.39e-12 |
|
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: 66.58 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 179 DSDPILIKPFGLEPGK-YMMMCARLVRHKGAHTLIAAWKRLKKTHPELvgdtKLAIVGGSAfTDD-----YVRELERLVK 252
Cdd:cd03792 182 DIRYYLEKPFVIDPERpYILQVARFDPSKDPLGVIDAYKLFKRRAEEP----QLVICGHGA-VDDpegsvVYEEVMEYAG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 253 DEPSI-VLTGNQSGETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSN---IPENLEltqdHGLT-FEAGNEKD 327
Cdd:cd03792 257 DDHDIhVLRLPPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPaggIPLQVI----DGETgFLVNSVEG 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818897881 328 LASQLKMLLENPELVNAVGAEARIHIAKHYDwkdiaeTTDYLYELLWL 375
Cdd:cd03792 333 AAVRILRLLTDPELRRKMGLAAREHVRDNFL------ITGNLRAWLYL 374
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
14-359 |
6.38e-12 |
|
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: 66.16 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 14 RSGGIERHVEELSAELASRGHEVLVF-CRSWYTWPIRDHRGVRCiKTWSLP---SKHLdAISHTFTSILRAVREKVDVFH 89
Cdd:cd03814 12 QVNGVVRTLERLVDHLRRRGHEVRVVaPGPFDEAESAEGRVVSV-PSFPLPfypEYRL-ALPLPRRVRRLIKEFQPDIIH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 90 FHGVGP---SLLAWLPKLLRPsakVVVTFHC-----IDRHHQKW--GRMARLMLYIGERFactipDATIAVSKTLETYC- 158
Cdd:cd03814 90 IATPGPlglAALRAARRLGLP---VVTSYHTdfpeyLSYYTLGPlsWLAWAYLRWFHNPF-----DTTLVPSPSIARELe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 159 --------RLSYGVTTkyipngTQIRLEDSDPILIKPFGLEPGKYMMMCARLVRHKGAHTLIAAWKRLKKTHPelvgdTK 230
Cdd:cd03814 162 ghgfervrLWPRGVDT------ELFHPSRRDAALRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPP-----VR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 231 LAIVGGSAftddyvrELERLVKDEPSIVLTGNQSGETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENL 310
Cdd:cd03814 231 LVVVGDGP-------ARAELEARGPDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPR 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 818897881 311 ELTQDH--GLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHiAKHYDW 359
Cdd:cd03814 304 DIVRPGgtGALVEPGDAAAFAAALRALLEDPELRRRMAARARAE-AERYSW 353
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
16-370 |
1.14e-11 |
|
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: 65.54 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 16 GGIERHVEELSAELASRGHEVLVFC---RSWYTwPIRDHrgvrcIKTWSLpskhldAISHTFTSILRAVRE--------K 84
Cdd:cd04951 12 GGAEKQTVLLADQMFIRGHDVNIVYltgEVEVK-PLNNN-----IIIYNL------GMDKNPRSLLKALLKlkkiisafK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 85 VDVFHFHGVGPSLLAWLPKLLRPSAKVVVTfhcidRHHQKWGRMARLMLYIGERFACtipDATIAVSKTLETYCrLSYGV 164
Cdd:cd04951 80 PDVVHSHMFHANIFARFLRMLYPIPLLICT-----AHNKNEGGRIRMFIYRLTDFLC---DITTNVSREALDEF-IAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 165 TTKY----IPNGTQIRLEDSDPILIK----PFGLEPGKYMMMC-ARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIVG 235
Cdd:cd04951 151 FSKNksvpVYNGIDLNKFKKDINVRLkirnKLNLKNDEFVILNvGRLTEAKDYPNLLLAISELILSKN----DFKLLIAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 236 GSAFTDdyvrELERLVKD---EPSIVLTGNQSgeTLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLEL 312
Cdd:cd04951 227 DGPLRN----ELERLICNlnlVDRVILLGQIS--NISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEV 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 818897881 313 TQDHGLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYDWKDIAETTDYLY 370
Cdd:cd04951 301 VGDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
86-358 |
6.48e-11 |
|
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: 63.24 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 86 DVFHFHgVGPSLL--AWLPKLLRPSAKVVVTFHCID--RHHQKWGRMARLMLY-IGERFactIPDATIAVSKTLETYCrl 160
Cdd:cd03799 72 DIIHCQ-FGPLGAlgALLRRLKVLKGKLVTSFRGYDisMYVILEGNKVYPQLFaQGDLF---LPNCELFKHRLIALGC-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 161 sygvttkyipngtqirleDSDPILIKPFGLEPGKY--------------MMMCARLVRHKGAHTLIAAWKRLKKTHPelv 226
Cdd:cd03799 146 ------------------DEKKIIVHRSGIDCNKFrfkprylpldgkirILTVGRLTEKKGLEYAIEAVAKLAQKYP--- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 227 gDTKLAIVGGSAFTDDyvreLERLVKD---EPSIVLTGNQSGETLHTLFSNSYAAIHPS------ESEGLPIAVLEAMGY 297
Cdd:cd03799 205 -NIEYQIIGDGDLKEQ----LQQLIQElniGDCVKLLGWKPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAM 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897881 298 GKCVLS---SNIPENLEltqdHGLTFEAGNEKD---LASQLKMLLENPELVNAVGAEARIHIAKHYD 358
Cdd:cd03799 280 GLPVIStehGGIPELVE----DGVSGFLVPERDaeaIAEKLTYLIEHPAIWPEMGKAGRARVEEEYD 342
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
117-371 |
7.71e-10 |
|
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: 60.04 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 117 CIDRHHQKWGRmaRLMLYIGERFacTIpdatIAVSKTLETYCRLSYGVTTK---YIPNG--TQIRLEDSDPILIKPFGLE 191
Cdd:cd03825 119 KKDLSRQLFRR--KREALAKKRL--TI----VAPSRWLADMVRRSPLLKGLpvvVIPNGidTEIFAPVDKAKARKRLGIP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 192 PGKYMMMCARLV---RHKGAHTLIAAWKRLKkTHPELVgdtkLAIVGGSAftddyvrelERLVKDEPSIVLTGN-QSGET 267
Cdd:cd03825 191 QDKKVILFGAESvtkPRKGFDELIEALKLLA-TKDDLL----LVVFGKND---------PQIVILPFDIISLGYiDDDEQ 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 268 LHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQD--HGLTFEAGNEKDLASQLKMLLENPELVNAV 345
Cdd:cd03825 257 LVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHgvTGYLVPPGDVQALAEAIEWLLANPKERESL 336
|
250 260
....*....|....*....|....*...
gi 818897881 346 GAEARIHIAKHYDWKDIAEttDY--LYE 371
Cdd:cd03825 337 GERARALAENHFDQRVQAQ--RYleLYK 362
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
169-355 |
2.88e-09 |
|
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: 57.70 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 169 IPNGTqirledSDPILIKPFGLEPGKY-MMMCARLVRHKGAHTLIAAWKRLKKTHPELvgdtKLAIVGgSAFTDDYVREL 247
Cdd:cd04949 141 IPVGY------VDQLDTAESNHERKSNkIITISRLAPEKQLDHLIEAVAKAVKKVPEI----TLDIYG-YGEEREKLKKL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 248 ERLVKDEPSIVLTGNQSgeTLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPE-NLELTQDH--GLTFEAGN 324
Cdd:cd04949 210 IEELHLEDNVFLKGYHS--NLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYgPSELIEDGenGYLIEKNN 287
|
170 180 190
....*....|....*....|....*....|.
gi 818897881 325 EKDLASQLKMLLENPELVNAVGAEARIHIAK 355
Cdd:cd04949 288 IDALADKIIELLNDPEKLQQFSEESYKIAEK 318
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
76-358 |
3.66e-09 |
|
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: 58.12 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 76 SILRAVREKVDVFHFHGVGPSLLAWLPKLLRPSAKVVVTFHCIdrhhqkwgrmarlmlYIGERFAcTIPDATIAVS--KT 153
Cdd:cd03813 165 AIAADDLPEADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGI---------------YTRERKI-EILQSTWIMGyiKK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 154 L-----ETYCRLSYGVTTKYIP--NGT---QIRL-EDSDPILIKPFGLEPGKY--------------MMMCARLVRHKGA 208
Cdd:cd03813 229 LwirffERLGKLAYQQADKIISlyEGNrrrQIRLgADPDKTRVIPNGIDIQRFapareerpekeppvVGLVGRVVPIKDV 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 209 HTLIAAWKRLKKTHPELvgdtKLAIVGGSAFTDDYVRELERLVKD---EPSIVLTGNQSgetlhtlFSNSYAA----IHP 281
Cdd:cd03813 309 KTFIRAFKLVRRAMPDA----EGWLIGPEDEDPEYAQECKRLVASlglENKVKFLGFQN-------IKEYYPKlgllVLT 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 282 SESEGLPIAVLEAMGYGKCVLSSNIPENLELTQDHGLTF-EAG------NEKDLASQLKMLLENPELVNAVGAEARIHIA 354
Cdd:cd03813 378 SISEGQPLVILEAMASGVPVVATDVGSCRELIYGADDALgQAGlvvppaDPEALAEALIKLLRDPELRQAFGEAGRKRVE 457
|
....
gi 818897881 355 KHYD 358
Cdd:cd03813 458 KYYT 461
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
200-358 |
3.12e-07 |
|
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: 51.98 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 200 AR-LVRHKGAHTLIAAWKRLKKTHPE----LVGDTKLA----IVGGSAFTDDYVRELErlvkDEPS-IVLTGNQSGETLH 269
Cdd:cd03818 220 ARnLEPYRGFHVFMRALPRIQARRPDarvvVVGGDGVSygspPPDGGSWKQKMLAELG----VDLErVHFVGKVPYDQYV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 270 TLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQD--HGLTFEAGNEKDLASQLKMLLENPELVNAVGA 347
Cdd:cd03818 296 RLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDgrNGLLVDFFDPDALAAAVLELLEDPDRAAALRR 375
|
170
....*....|.
gi 818897881 348 EARIHIAKHYD 358
Cdd:cd03818 376 AARRTVERSDS 386
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
16-370 |
4.15e-07 |
|
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: 51.47 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 16 GGIERHVEELSAELASRGHEVLVFCRSWytwpiRDHRGVRC----IKTWSLPSK--HLDAISHTFTS---ILRAV--REK 84
Cdd:cd03796 14 GGVETHIYQLSQCLIKRGHKVIVITHAY-----GNRVGVRYltngLKVYYLPFKvfYNQSTLPTLFStfpLLRNIliRER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 85 VDVFHFHGvGPSLLAwLPKLLRPSA---KVVVTFHCIdrhhQKWGRMARLMLYIGERFACTIPDATIAVSKT------LE 155
Cdd:cd03796 89 IQIVHGHQ-AFSSLA-HEALFHARTlglKTVFTDHSL----FGFADASSILTNKLLRFSLADIDHVICVSHTskentvLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 156 TYCRLSYgVTTkyIPNGTqirleDSDPILIKPFGLEPGKY-MMMCARLVRHKGAHTLIAAWKRLKKTHPelvgDTKLAIV 234
Cdd:cd03796 163 ASLDPRI-VSV--IPNAV-----DSSDFTPDPSKPDPNKItIVVISRLVYRKGIDLLVGIIPRICKKHP----NVRFIIG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 235 GGSAFTDDY--VRELERLVKdepSIVLTGNQSGETLHTLFSNSYAAIHPSESEGLPIAVLEAMGYGKCVLSSN---IPEN 309
Cdd:cd03796 231 GDGPKRIELeeMREKYQLQD---RVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRvggIPEV 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818897881 310 LEltqDHGLTFEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAKHYDWKDIAETTDYLY 370
Cdd:cd03796 308 LP---PDMILLAEPDPEDIVRKLEEAISILRTGKHDPWSFHNRVKKMYSWEDVARRTEKVY 365
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
278-365 |
9.43e-07 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 46.44 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 278 AIHPSES-EGLPIAVLEAMGYGKCVLSSNIPENLEL--TQDHGLTFEagNEKDLASQLKMLLENPELVNAVGAEARIHIA 354
Cdd:pfam13524 2 VLNPSRRpDSPNMRVFEAAACGAPLLTDRTPGLEELfePGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVL 79
|
90
....*....|.
gi 818897881 355 KHYDWKDIAET 365
Cdd:pfam13524 80 AEHTYAHRAEQ 90
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
175-315 |
4.05e-05 |
|
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: 45.14 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 175 IRLEDSDPILIKPFGLEPGKYMMMCARLVRHKGAHTLIAAWKRLKKTHPELvgDTKLAIVGGSAFTddyvRELERLVKDE 254
Cdd:cd04946 206 SRLGVSDKEQYSKVKKEGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSI--CISWTHIGGGPLK----ERLEKLAENK 279
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818897881 255 P---SIVLTGNQSGETLHTLF-SNSYAA-IHPSESEGLPIAVLEAMGYGKCVLSSNIPENLELTQD 315
Cdd:cd04946 280 LenvKVNFTGEVSNKEVKQLYkENDVDVfVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVEN 345
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
16-355 |
3.53e-04 |
|
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: 42.19 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 16 GGIERHVEELSAELASRGHEVlvfcrSWYT------WPIRDHRG----VRCIKTWsLPsKHLDAISHTFTSILRAV---- 81
Cdd:cd03805 13 GGAERLVVDAALALQSRGHEV-----TIYTshhdpsHCFEETKDgtlpVRVRGDW-LP-RSIFGRFHALCAYLRMLylal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 82 ------REKVDVFhfhgVGPSLLAWLP--KLLRPSaKVVvtFHC------IDRHHQKWGRMARLMLYIGERFACTIPDaT 147
Cdd:cd03805 86 ylllfsGEKYDVF----IVDQVSACVPllKLFRPS-KIL--FYChfpdqlLAQRKSLLKRLYRKPFDWLEEFTTGMAD-Q 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 148 IAV-SK-TLETYC----RLS-YGVTTKYIP-NGTQIRLEDSDPILIKPFGLEPGKYMMMCARLVRHKGAHTLIAAWKRLK 219
Cdd:cd03805 158 IVVnSNfTAGVFKktfpSLAkNPPEVLYPCvDTDSFDSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 220 KTHPELvGDTKLAIVGGsafTDD-------YVRELERLVKD----EPSIVLTGNQSGETLHTLFSNSYAAIHPSESEGLP 288
Cdd:cd03805 238 QKLPEF-ENVRLVIAGG---YDPrvaenveYLEELQRLAEEllnvEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFG 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818897881 289 IAVLEAMGYGKCVLSSNIPENLElTQDHGLT--FEAGNEKDLASQLKMLLENPELVNAVGAEARIHIAK 355
Cdd:cd03805 314 IVPLEAMYAGKPVIACNSGGPLE-TVVEGVTgfLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKE 381
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
218-376 |
6.05e-04 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 41.62 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 218 LKKTHpelvGDTKLAIVG-GSAFtdDYVRELERLVKDEPSIVLTGNQSG--ETLHTLFSNSYAAIHPSESEGLPIAVLEA 294
Cdd:PRK09922 204 LSQTT----GEWQLHIIGdGSDF--EKCKAYSRELGIEQRIIWHGWQSQpwEVVQQKIKNVSALLLTSKFEGFPMTLLEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 295 MGYGKCVLSSNI---PENLELTQDHGLTFEAGNEKDLASQLKMLLENpelvnavgaearihiAKHYDWKDIAETTDYLYE 371
Cdd:PRK09922 278 MSYGIPCISSDCmsgPRDIIKPGLNGELYTPGNIDEFVGKLNKVISG---------------EVKYQHDAIPNSIERFYE 342
|
....*
gi 818897881 372 LLWLE 376
Cdd:PRK09922 343 VLYFK 347
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
209-298 |
2.33e-03 |
|
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: 39.90 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897881 209 HTL-IAAWKRLKKTHPELVG-DTKLAIVGGSAFTDD--YVRELERLVKD---EPSIVLTGNQSGETLHTLFSNSYAAIHP 281
Cdd:cd03806 252 HPLqLRAFAELLKRLPESIRsNPKLVLIGSCRNEEDkeRVEALKLLAKElilEDSVEFVVDAPYEELKELLSTASIGLHT 331
|
90
....*....|....*..
gi 818897881 282 SESEGLPIAVLEAMGYG 298
Cdd:cd03806 332 MWNEHFGIGVVEYMAAG 348
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
281-313 |
5.98e-03 |
|
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: 38.42 E-value: 5.98e-03
10 20 30
....*....|....*....|....*....|....
gi 818897881 281 PSESEGLPIAVLEAMGYG-KCVLSSNIPENLELT 313
Cdd:cd03812 272 PSLYEGLPLVAVEAQASGlPCLLSDTITKECDIT 305
|
|
| |
