|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
4-363 |
3.34e-98 |
|
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: 296.04 E-value: 3.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 4 KVLFCATVDFHFQAFHLPYMKWFKEQGWEVHVAASGNMKLPYVDQKYNIAI------QRSPFHTGNMKAYRELKTVINEN 77
Cdd:cd03808 1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVidipilRRGINPLKDLKALFKLYKLLKKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 78 KYNIIHCHTPMGGVLARLAARKARkqGTKVIYTAHGFHFCKGAPPVNWLFYYPIEKTLAHYTDCLITINKEDYQLATKHF 157
Cdd:cd03808 81 KPDIVHCHTPKPGILGRLAARLAG--VPKVIYTVHGLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRDLAIKKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 158 KAKRIEHV--HGVGINTEKFKPANEKEKiqlkksfgyhPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGK 235
Cdd:cd03808 159 IIKKKKTVliPGSGVDLDRFQYSPESLP----------SEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 236 GPLLENCRELAANLGIFHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNG 315
Cdd:cd03808 229 GELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNG 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1865037855 316 WVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKVLIE 363
Cdd:cd03808 309 FLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNK 356
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
4-360 |
7.15e-46 |
|
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: 161.17 E-value: 7.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 4 KVLFCATVDFHFQ------AFHLpyMKWFKEQGWEVHVAASGNMKLPYVDQKYNIAIQRSPFHTGNMKAYR---ELKTVI 74
Cdd:cd03801 1 KILLLSPELPPPVggaerhVREL--ARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrELRPLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 75 NENKYNIIHCHTPMGGVLARLAARKARkqgTKVIYTAHGFHFCkgappVNWLFYYPIEKTLAHYTDCL------ITINKE 148
Cdd:cd03801 79 RLRKFDVVHAHGLLAALLAALLALLLG---APLVVTLHGAEPG-----RLLLLLAAERRLLARAEALLrradavIAVSEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 149 DYQLATKHF--KAKRIEHVHGvGINTEKFKPAnekekiqLKKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIP 226
Cdd:cd03801 151 LRDELRALGgiPPEKIVVIPN-GVDLERFSPP-------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 227 HAKLLLAGK-GPLLENCRELAANLGifHMVEFLGYR--NDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNR 303
Cdd:cd03801 223 DVRLVIVGGdGPLRAELEELELGLG--DRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVG 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1865037855 304 GHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKV 360
Cdd:cd03801 301 GLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERV 357
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
27-335 |
1.01e-36 |
|
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: 136.33 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 27 KEQGWEVHVAASGNMKLPYVDQkyniAIQRSPFHTGN----MKAYRELKTVINENKYNIIHCHTpmgGVLARLAARKARK 102
Cdd:cd03819 25 AERGHRVLVVTAGGPLLPRLRQ----IGIGLPGLKVPllraLLGNVRLARLIRRERIDLIHAHS---RAPAWLGWLASRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 103 QGTKVIYTAHGFHFCKGAPPVNWLFyypiektlahytdclITINKeDYQLATKHFKAKRIEHVHGV----------GINT 172
Cdd:cd03819 98 TGVPLVTTVHGSYLATYHPKDFALA---------------VRARG-DRVIAVSELVRDHLIEALGVdperirvipnGVDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 173 EKFKPANEKEKIQlkkSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEiPHAKLLLAGKGPLLENCRELAANLGIF 252
Cdd:cd03819 162 DRFPPEAEAEERA---QLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVAGDGPERDEIRRLVERLGLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 253 HMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFASKIKA 332
Cdd:cd03819 238 DRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRA 317
|
...
gi 1865037855 333 LAK 335
Cdd:cd03819 318 AKL 320
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
70-369 |
8.21e-36 |
|
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: 133.98 E-value: 8.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 70 LKTVINENKYNIIHCHTPMGGVLARLAARKARkqGTKVIYTAH-GFHFCKGAPPVNWLfyypieKTLAHYTDCLITINKE 148
Cdd:cd03807 71 LAKLIRKRNPDVVHTWMYHADLIGGLAAKLAG--GVKVIWSVRsSNIPQRLTRLVRKL------CLLLSKFSPATVANSS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 149 DYQ--LATKHFKAKRIEhVHGVGINTEKFKPaNEKEKIQLKKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIP 226
Cdd:cd03807 143 AVAefHQEQGYAKNKIV-VIYNGIDLFKLSP-DDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 227 HAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHR 306
Cdd:cd03807 221 DLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAA 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1865037855 307 ELVhNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKVLIEKSRIYK 369
Cdd:cd03807 301 ELV-DDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
60-369 |
2.99e-31 |
|
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: 122.10 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 60 HTGNMKAYRELKTVINENKYNIIHCHTPMG-GVLARLAARKArkqGTKVIYTAHGFHfCKGAPPVNWLFyyPIEK-TLAH 137
Cdd:cd03798 77 APLRAPSLAKLLKRRRRGPPDLIHAHFAYPaGFAAALLARLY---GVPYVVTEHGSD-INVFPPRSLLR--KLLRwALRR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 138 yTDCLITINKEDYQLATKHFKAKRIEHVHGVGINTEKFKPANEkekiqlkkSFGYHPDDFLLFYAAEFNKNKNQQLLLQS 217
Cdd:cd03798 151 -AARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDR--------GLGLPLDAFVILFVGRLIPRKGIDLLLEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 218 LALIKDEIPHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRndLQKIVP----MCDVAVASSLREGLPVNIMEAMAC 293
Cdd:cd03798 222 FARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRL--PHEQVPayyrACDVFVLPSRHEGFGLVLLEAMAC 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865037855 294 GIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFA-SKIKALAKIEgvKHKLGINGRDMILKKYSIDKVLIEKSRIYK 369
Cdd:cd03798 300 GLPVVATDVGGIPEVVGDPETGLLVPPGDADALAaALRRALAEPY--LRELGEAARARVAERFSWVKAADRIAAAYR 374
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
22-334 |
3.35e-30 |
|
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: 118.61 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 22 YMKWFKEQGWEVHV---AASGNMKLPyVDQKYNIAIQRSPF----HTGNMKAYRELKTVINENKYNIIHCHTPMGGVLAR 94
Cdd:cd03811 21 LANALDKRGYDVTLvllRDEGDLDKQ-LNGDVKLIRLLIRVlkliKLGLLKAILKLKRILKRAKPDVVISFLGFATYIVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 95 LAARKarkqGTKVIYTAHGFhfckgaPPVNWLFYYPIEKTLAHYT--DCLITIN---KEDYQlATKHFKAKRIEHVHGvG 169
Cdd:cd03811 100 KLAAA----RSKVIAWIHSS------LSKLYYLKKKLLLKLKLYKkaDKIVCVSkgiKEDLI-RLGPSPPEKIEVIYN-P 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 170 INTEKFKPANEKekiqlkKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGKGPLLENCRELAANL 249
Cdd:cd03811 168 IDIDRIRALAKE------PILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 250 GIFHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFASK 329
Cdd:cd03811 242 GLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGI 321
|
....*
gi 1865037855 330 IKALA 334
Cdd:cd03811 322 LAALL 326
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
195-350 |
1.34e-29 |
|
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: 111.98 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 195 DDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKI--VPMCD 272
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPelLKIAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1865037855 273 VAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDM 350
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
22-371 |
1.41e-28 |
|
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: 114.68 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 22 YMKWFKEQGWEVHVAASGNMKLPYVDQKYNIAIQRSPFHT----GNMKAYRELKTV-INENKYNIIHCHTPMGgvLARLA 96
Cdd:cd03817 23 LARALEKRGHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKyhrqHIPFPFKKAVIDrIKELGPDIIHTHTPFS--LGKLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 97 ARKARKQGTKVIYTAHG-----FHFckGAPPVNWLFYY--PIEKTLAHYTDCLITINKEDYQLATKHFKAKRIEhVHGVG 169
Cdd:cd03817 101 LRIARKLKIPIVHTYHTmyedyLHY--IPKGKLLVKAVvrKLVRRFYNHTDAVIAPSEKIKDTLREYGVKGPIE-VIPNG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 170 INTEKF-KPANEKEKIQLKKSfgyhPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEiPHAKLLLAGKGPLLENCRELAAN 248
Cdd:cd03817 178 IDLDKFeKPLNTEERRKLGLP----PDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 249 LGIFHMVEFLGY--RNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNGWVIDSTsRVEF 326
Cdd:cd03817 253 LGLADKVIFTGFvpREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPN-DETL 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1865037855 327 ASKIKALAKIEGVKHKLGINGRDMILKKYSIDKVLieksRIYKSY 371
Cdd:cd03817 332 AEKLLHLRENLELLRKLSKNAEISAREFAFAKSVE----KLYEEV 372
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
221-333 |
5.09e-28 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 106.83 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 221 IKDEIPHAKLLLAGKGPLlENCRELAANLGifHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVAL 300
Cdd:pfam13692 27 LRKRDNDVRLVIVGDGPE-EELEELAAGLE--DRVIFTGFVEDLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVAT 103
|
90 100 110
....*....|....*....|....*....|...
gi 1865037855 301 DNRGHRELVHnNKNGWVIDSTSRVEFASKIKAL 333
Cdd:pfam13692 104 DVGGIPELVD-GENGLLVPPGDPEALAEAILRL 135
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
73-369 |
1.71e-27 |
|
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: 111.67 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 73 VINENKYNIIHCHTPMGGVLARLAARKARKQGTKVIYTAHGFHFC-KGAPPvnwlFYYPIEKTLAHYTDCLITINKEDYQ 151
Cdd:cd04962 79 VAKEHKLDVLHAHYAIPHASCAYLAREILGEKIPIVTTLHGTDITlVGYDP----SLQPAVRFSINKSDRVTAVSSSLRQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 152 LATKHFKAKR-IEHVHGVgINTEKFKPaneKEKIQLKKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPhAKL 230
Cdd:cd04962 155 ETYELFDVDKdIEVIHNF-IDEDVFKR---KPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIP-AKL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 231 LLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVH 310
Cdd:cd04962 230 LLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVK 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1865037855 311 NNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKVLIEKSRIYK 369
Cdd:cd04962 310 HGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYR 368
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
45-368 |
9.45e-27 |
|
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: 109.46 E-value: 9.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 45 YVDQKYNIAIQRSPFhtGNMKAYRELKTVINENKYNIIHCHTPMGGVLARLAarKARKQGTKVIYTAHGfhfcKGAPPVN 124
Cdd:cd04951 48 NNIIIYNLGMDKNPR--SLLKALLKLKKIISAFKPDVVHSHMFHANIFARFL--RMLYPIPLLICTAHN----KNEGGRI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 125 WLFYYpiektlaHYTDCLITIN----KE--DYQLATKHFKAKRIEHVHGvGINTEKFKPANEKeKIQLKKSFGYHPDDFL 198
Cdd:cd04951 120 RMFIY-------RLTDFLCDITtnvsREalDEFIAKKAFSKNKSVPVYN-GIDLNKFKKDINV-RLKIRNKLNLKNDEFV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 199 LFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKIVPMCDVAVASS 278
Cdd:cd04951 191 ILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 279 LREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKngWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSID 358
Cdd:cd04951 271 EWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN--YVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSIN 348
|
330
....*....|
gi 1865037855 359 KVLIEKSRIY 368
Cdd:cd04951 349 TIVNEWERLY 358
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
75-360 |
8.36e-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: 101.55 E-value: 8.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 75 NENKYNIIHCHTPMGGvlaRLAARKARKQGTKVIYTAH--------------GFHFCKGappvnwlfyYPIEKTLAHYTD 140
Cdd:cd03800 98 EGGRYDLIHSHYWDSG---LVGALLARRLGVPLVHTFHslgrvkyrhlgaqdTYHPSLR---------ITAEEQILEAAD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 141 CLITINKEDYQLATKHFKAKRiEHVHGV--GINTEKFKPANEKEKiqLKKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSL 218
Cdd:cd03800 166 RVIASTPQEADELISLYGADP-SRINVVppGVDLERFFPVDRAEA--RRARLLLPPDKPVVLALGRLDPRKGIDTLVRAF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 219 ALIKDEIPHAKLLLAGkGPL-------LENCRELAANLGIFHMVEFLGY--RNDLQKIVPMCDVAVASSLREGLPVNIME 289
Cdd:cd03800 243 AQLPELRELANLVLVG-GPSddplsmdREELAELAEELGLIDRVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAIE 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865037855 290 AMACGIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKV 360
Cdd:cd03800 322 AMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESV 392
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
65-361 |
5.84e-23 |
|
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: 98.46 E-value: 5.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 65 KAYRELKTVINENKYNIIHchTPMGGVLARLAARKArkqGTKVIYTahgFHFCKGAPPVNWLFYYPIEKTLAhYTDCLIT 144
Cdd:cd03820 74 KKVRRLRKYLKNNKPDVVI--SFRTSLLTFLALIGL---KSKLIVW---EHNNYEAYNKGLRRLLLRRLLYK-RADKIVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 145 INKEDyqlatkHFKAKRIEHVHGVGINTekFKPANEKEKIQLKKSF-----G-YHPD---DFLLFYAAEfnknknqqlll 215
Cdd:cd03820 145 LTEAD------KLKKYKQPNSNVVVIPN--PLSFPSEEPSTNLKSKrilavGrLTYQkgfDLLIEAWAL----------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 216 qslalIKDEIPHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGI 295
Cdd:cd03820 206 -----IAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGL 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865037855 296 PVVALD-NRGHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMIlKKYSIDKVL 361
Cdd:cd03820 281 PIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEKII 346
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
22-302 |
9.12e-22 |
|
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: 95.05 E-value: 9.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 22 YMKWFKEQGWEVHVAASGNMKLPYVD--QKYNIAIQRSPFH-TGNMKAYRELKTVINENKYNIIHCHTPMGGVLARLAAR 98
Cdd:cd03812 21 LYRKLDKSKIEFDFLATSDDKGEYDEelEELGGKIFYIPPKkKNIIKYFIKLLKLIKKEKYDIVHVHGSSSNGIILLLAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 99 KArkqGTKV-IYTAHGFHFCKGapPVNWLFYYPIEK-TLAHYTDCLITINKEDYQLATKHFKAKriEHVHGVGINTEKFK 176
Cdd:cd03812 101 KA---GVPVrIAHSHNTKDSSI--KLRKIRKNVLKKlIERLSTKYLACSEDAGEWLFGEVENGK--FKVIPNGIDIEKYK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 177 PANEKEKIQLKKSFGyhPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGKGPLLENCRELAANLGIFHMVE 256
Cdd:cd03812 174 FNKEKRRKRRKLLIL--EDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVI 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1865037855 257 FLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDN 302
Cdd:cd03812 252 FLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDT 297
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
271-361 |
1.29e-21 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 89.28 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 271 CDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDM 350
Cdd:COG0438 21 ADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAARER 100
|
90
....*....|.
gi 1865037855 351 ILKKYSIDKVL 361
Cdd:COG0438 101 AEERFSWEAIA 111
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
24-360 |
9.21e-20 |
|
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: 89.71 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 24 KWFKEQGWEVHVAAS------GNMKLPYVDQKYNIAIQR--SPFHTGNMKAYR-----------ELKTVINENKYNIIHC 84
Cdd:cd03794 25 KELVRRGHEVTVLTPspnyplGRIFAGATETKDGIRVIRvkLGPIKKNGLIRRllnylsfalaaLLKLLVREERPDVIIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 85 HTP--MGGVLARLAARKARKqgtKVIYTAHGFH--------FCKGAPPVNWLFYypIEKTLAHYTDCLITINK--EDYqL 152
Cdd:cd03794 105 YSPpiTLGLAALLLKKLRGA---PFILDVRDLWpeslialgVLKKGSLLKLLKK--LERKLYRLADAIIVLSPglKEY-L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 153 ATKHFKAKRIEHVHgVGINTEKFKPANEKEKIQLKKSfgyhPDDFLLFYAAEFNKNKNQQLLLQSLALIKdEIPHAKLLL 232
Cdd:cd03794 179 LRKGVPKEKIIVIP-NWADLEEFKPPPKDELRKKLGL----DDKFVVVYAGNIGKAQGLETLLEAAERLK-RRPDIRFLF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 233 AGKGPLLENCRELAANLGIfHMVEFLGY--RNDLQKIVPMCDVAVAS-----SLREGLPVNIMEAMACGIPVVALDNRGH 305
Cdd:cd03794 253 VGDGDEKERLKELAKARGL-DNVTFLGRvpKEEVPELLSAADVGLVPlkdnpANRGSSPSKLFEYMAAGKPILASDDGGS 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1865037855 306 RELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKV 360
Cdd:cd03794 332 DLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKL 386
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
81-359 |
1.22e-18 |
|
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: 86.35 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 81 IIHCHTPMGGVLArLAArkARKQGTKVIYTAHGF------HFCKGAPPvnWLFYYPIEKTLAHYTDCLITINKE---DYQ 151
Cdd:cd05844 84 LVHAHFGRDGVYA-LPL--ARALGVPLVVTFHGFdittsrAWLAASPG--WPSQFQRHRRALQRPAALFVAVSGfirDRL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 152 LAtKHFKAKRIeHVHGVGINTEKFKPANEKEkiqlkksfgyhPDDFLLFyAAEFNKNKNQQLLLQSLALIKDEIPHAKLL 231
Cdd:cd05844 159 LA-RGLPAERI-HVHYIGIDPAKFAPRDPAE-----------RAPTILF-VGRLVEKKGCDVLIEAFRRLAARHPTARLV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 232 LAGKGPLLENCRELAANLGifhMVEFLGY--RNDLQ------KIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNR 303
Cdd:cd05844 225 IAGDGPLRPALQALAAALG---RVRFLGAlpHAEVQdwmrraEIFCLPSVTAASGDSEGLGIVLLEAAACGVPVVSSRHG 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1865037855 304 GHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDK 359
Cdd:cd05844 302 GIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRV 357
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
56-318 |
6.69e-17 |
|
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: 79.37 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 56 RSPFHTGNMKAYRELKTVINENKYNIIHCHTPMGGVLArlAARKARKQGTKVIYTAHGFHFckGAPPVNWLFYYPIEKTL 135
Cdd:cd01635 32 EVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAALA--ALLAARLLGIPIVVTVHGPDS--LESTRSELLALARLLVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 136 AHYTDCLItinkedyqlatkhfkAKRIEHVHGVgintekfkpanekekiqlkksfgyhpdDFLLFYAAEfnknknqqlll 215
Cdd:cd01635 108 LPLADKVS---------------VGRLVPEKGI---------------------------DLLLEALAL----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 216 qslalIKDEIPHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKIV---PMCDVAVASSLREGLPVNIMEAMA 292
Cdd:cd01635 135 -----LKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLElllAAADVFVLPSRSEGFGLVLLEAMA 209
|
250 260
....*....|....*....|....*.
gi 1865037855 293 CGIPVVALDNRGHRELVHNNKNGWVI 318
Cdd:cd01635 210 AGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
224-369 |
1.50e-16 |
|
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: 80.84 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 224 EIPHAKLLLAG---KGPL-LENCRELAANLGIFHMVEFLGYRNdLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVA 299
Cdd:cd03813 321 AMPDAEGWLIGpedEDPEyAQECKRLVASLGLENKVKFLGFQN-IKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVA 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1865037855 300 LDNRGHRELVHNNKN-----GWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKVLIEKSRIYK 369
Cdd:cd03813 400 TDVGSCRELIYGADDalgqaGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
74-370 |
2.84e-16 |
|
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: 79.30 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 74 INENKYNIIHCHTPMGG-----VLARLAARKarkqgtKVIYTAH-------GFHF---CKGappvnW---LFYYPiekTL 135
Cdd:cd03825 47 PEFIEADIIHLHWIHGGylslkALFKLLRRK------PVVWTLHdmwpftgGCHYpmeCEG-----WktgCGNCP---NL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 136 AHYTDCLITINKEDYQLATKHFKAKRIE-----------------------HVHGVGINTEKFKPANEKEkiqLKKSFGY 192
Cdd:cd03825 113 NSYPPAKKDLSRQLFRRKREALAKKRLTivapsrwladmvrrspllkglpvVVIPNGIDTEIFAPVDKAK---ARKRLGI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 193 HPDDFLLFYAAE--FNKNKNQQLLLQSLALIKDeipHAKLLLAGKGPLLENCRELAanlgiFHMVEFlGYRND---LQKI 267
Cdd:cd03825 190 PQDKKVILFGAEsvTKPRKGFDELIEALKLLAT---KDDLLLVVFGKNDPQIVILP-----FDIISL-GYIDDdeqLVDI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 268 VPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGING 347
Cdd:cd03825 261 YSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERA 340
|
330 340
....*....|....*....|...
gi 1865037855 348 RDMILKKYSIDKVLIEKSRIYKS 370
Cdd:cd03825 341 RALAENHFDQRVQAQRYLELYKD 363
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
16-359 |
1.02e-14 |
|
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: 74.41 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 16 QAFHLPYMKWFKEQGWEVHVAASGNMKLPYVD---QKYNIAIQRSpfhtgnmkayreLKTVINENK---YNIIHCHTPMG 89
Cdd:cd03799 14 ETFILNQITGLIDRGHEVDIYAVNPGDLVKRHpdvEKYNVPSLNL------------LYAIVGLNKkgaYDIIHCQFGPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 90 GVLARLAARKARKQGtKVIYTAHG-----FHFCKGAPPVNWLFyypiektlaHYTDCLITInkedyqlaTKHFKAKRIE- 163
Cdd:cd03799 82 GALGALLRRLKVLKG-KLVTSFRGydismYVILEGNKVYPQLF---------AQGDLFLPN--------CELFKHRLIAl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 164 -------HVHGVGINTEKFKPANEkekiqlkksfgYHPDD--FLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAG 234
Cdd:cd03799 144 gcdekkiIVHRSGIDCNKFRFKPR-----------YLPLDgkIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 235 KGPLLENCRELAANLGIFHMVEFLGYRN--DLQKIVPMCDVAVASSL------REGLPVNIMEAMACGIPVVALDNRGHR 306
Cdd:cd03799 213 DGDLKEQLQQLIQELNIGDCVKLLGWKPqeEIIEILDEADIFIAPSVtaadgdQDGPPNTLKEAMAMGLPVISTEHGGIP 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1865037855 307 ELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDK 359
Cdd:cd03799 293 ELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINK 345
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
30-360 |
1.37e-14 |
|
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: 74.33 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 30 GWEVHVAASGNMKLPYVDQKYNIAIQRSPFHTgnmkAYR-ELKTVINEN--KYNIIHCHtpmgGVLARL---AARKARKQ 103
Cdd:cd03821 43 YESLVVEENGRYIPPQDGFASIPLLRQGAGRT----DFSpGLPNWLRRNlrEYDVVHIH----GVWTYTslaACKLARRR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 104 GTKVIYTAHGF--HFCKGAPPVNW-LFYYPIEKTLAHYTDCLITINKEDYQ-LATKHFKAKR--IEHvhgvGINTEKFKP 177
Cdd:cd03821 115 GIPYVVSPHGMldPWALQQKHWKKrIALHLIERRNLNNAALVHFTSEQEADeLRRFGLEPPIavIPN----GVDIPEFDP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 178 ANEkekiqLKKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGKGPLLENC-RELAANLGIFHMVE 256
Cdd:cd03821 191 GLR-----DRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAYPAfLQLQSSLGLGDRVT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 257 FLGYRNDLQKIVPM--CDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVhNNKNGWVIDSTSRvEFASKIKALA 334
Cdd:cd03821 266 FTGPLYGEAKWALYasADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELV-EAGCGVVVDPNVS-SLAEALAEAL 343
|
330 340
....*....|....*....|....*...
gi 1865037855 335 KIEGVKHKLGINGR--DMILKKYSIDKV 360
Cdd:cd03821 344 RDPADRKRLGEMARraRQVEENFSWEAV 371
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
234-359 |
2.40e-14 |
|
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: 73.65 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 234 GKGPLLENCRELAANLGIFHMVEFLGY--RNDLQKIVPM--CDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELV 309
Cdd:cd04946 264 GGGPLKERLEKLAENKLENVKVNFTGEvsNKEVKQLYKEndVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIV 343
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1865037855 310 HNNKNGWVIDSTSRV-EFASKIKALAKIEGVKHKLGINGRDMILKKYSIDK 359
Cdd:cd04946 344 ENETNGLLLDKDPTPnEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEV 394
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
4-146 |
8.81e-14 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 67.73 E-value: 8.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 4 KVLFCATVDfhfQAFHLPYMKWFKEQGWEVHVAASGNMKLPYvDQKYNIAIQR----SPFHTGNMKAyRELKTVINENKY 79
Cdd:pfam13477 1 KILLLANAD---SIHTLRWADALADRGYDVHVISSKGPAKDE-LIAEGIHVHRlkvpRKGPLGYLKA-FRLKKLIKKIKP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1865037855 80 NIIHCHTPMG-GVLARLAARKARKQgtKVIYTAHGFHFCKGAPPVNWlfYYPIEKTLAHYTDCLITIN 146
Cdd:pfam13477 76 DVVHVHYAKPyGLLAGLAARLSGFP--PVVLSAWGLDVYKFPNKSRL--KKLLLKLNLKKATLIISTS 139
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
24-173 |
1.35e-13 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 68.33 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 24 KWFKEQGWEVHVAASGNMKLPYVDQKYNIAIQRSPFHTG-----NMKAYRELKTVINENKYNIIHCHTPMGGVLARLAAR 98
Cdd:pfam13439 12 RALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPprllrSLAFLRRLRRLLRRERPDVVHAHSPFPLGLAALAAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 99 KARkqGTKVIYTAHG----FHFCKGAPPVNWLFYYPIEKTLAHYTDCLITINKEDYQLATKHF--KAKRIEHVHGvGINT 172
Cdd:pfam13439 92 LRL--GIPLVVTYHGlfpdYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYgvPPEKIRVIPN-GVDL 168
|
.
gi 1865037855 173 E 173
Cdd:pfam13439 169 E 169
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
77-359 |
2.39e-13 |
|
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: 70.47 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 77 NKYNIIHCHTPMGGVlarlaarkaRKQGTKVIYTAHGFHFCK---GAPPVNWLFYYPIEKTLAHYTDCLITIN---KEDy 150
Cdd:cd03809 83 DKPDLLHSPHNTAPL---------LLKGCPQVVTIHDLIPLRypeFFPKRFRLYYRLLLPISLRRADAIITVSeatRDD- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 151 qlATKHFK--AKRIEHVHGvGINTEKFKPANEKEKIQLKKSfgyhPDDFLLfYAAEFNKNKNQQLLLQSLALIKDEIPHA 228
Cdd:cd03809 153 --IIKFYGvpPEKIVVIPL-GVDPSFFPPESAAVLIAKYLL----PEPYFL-YVGTLEPRKNHERLLKAFALLKKQGGDL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 229 KLLLAG-KGPLLENCRELAANLGIFHMVEFLGY--RNDLQKIVPMCDVAVASSLRE--GLPVniMEAMACGIPVVALDNR 303
Cdd:cd03809 225 KLVIVGgKGWEDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEgfGLPV--LEAMACGTPVIASNIS 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1865037855 304 GHRELVhnNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDmILKKYSIDK 359
Cdd:cd03809 303 VLPEVA--GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLE-RAKKFSWEK 355
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
80-334 |
2.48e-13 |
|
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: 70.40 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 80 NIIHCHTPmgGVLARLAARKARKQGTKVI--YTAHGFHFCK--GAPPVNWL-------FYYPIEKTLAhytdclitinke 148
Cdd:cd03814 86 DIIHIATP--GPLGLAALRAARRLGLPVVtsYHTDFPEYLSyyTLGPLSWLawaylrwFHNPFDTTLV------------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 149 dyqlAT----KHFKAKRIEHVHGV--GINTEKFKPANEKEKiqLKKSFGyHPDDFLLFYAAEFNKNKNQQLLLQSLALIK 222
Cdd:cd03814 152 ----PSpsiaRELEGHGFERVRLWprGVDTELFHPSRRDAA--LRRRLG-PPGRPLLLYVGRLAPEKNLEALLDADLPLA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 223 DEIPHaKLLLAGKGPLLEncrELAAnlgIFHMVEFLGYRN--DLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVAL 300
Cdd:cd03814 225 ASPPV-RLVVVGDGPARA---ELEA---RGPDVIFTGFLTgeELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAA 297
|
250 260 270
....*....|....*....|....*....|....*
gi 1865037855 301 DNRGHRELVHNNKNGwVIDSTSRVE-FASKIKALA 334
Cdd:cd03814 298 DAGGPRDIVRPGGTG-ALVEPGDAAaFAAALRALL 331
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
240-310 |
3.48e-12 |
|
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: 67.65 E-value: 3.48e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865037855 240 ENCRELAANLGIFHMVEFLGYRNdLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVH 310
Cdd:NF038011 354 AECRSLVASLGLQDKVKFLGFQK-IDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIE 423
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
24-166 |
1.54e-11 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 62.03 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 24 KWFKEQGWEVHVAASGnmklPYVDQK---------YNIAIQRSPFHTGNMKAYRELKTVINENKYNIIHCHTPMGGVLAR 94
Cdd:pfam13579 12 RALAALGHEVRVVTPG----GPPGRPelvgdgvrvHRLPVPPRPSPLADLAALRRLRRLLRAERPDVVHAHSPTAGLAAR 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1865037855 95 LAARKArkqGTKVIYTAHGFHFCKGAPPVNWLfYYPIEKTLAHYTDCLITINKEDY-QLATKHFKAKRIEHVH 166
Cdd:pfam13579 88 LARRRR---GVPLVVTVHGLALDYGSGWKRRL-ARALERRLLRRADAVVVVSEAEAeLLRALGVPAARVVVVP 156
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
182-333 |
1.86e-11 |
|
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: 64.63 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 182 EKIQLKKSFGYHP-DDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGY 260
Cdd:cd04949 145 YVDQLDTAESNHErKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGY 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1865037855 261 RNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALD-NRGHRELVHNNKNGWVIDSTSRVEFASKIKAL 333
Cdd:cd04949 225 HSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDALADKIIEL 298
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
226-369 |
9.00e-11 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 63.51 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 226 PHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGH 305
Cdd:PRK15179 547 PKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGA 626
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865037855 306 RELVHNNKNGWVIDSTSrVEFASKIKALAKI-------EGVKHKlginGRDMILKKYSIDKVLIEKSRIYK 369
Cdd:PRK15179 627 GEAVQEGVTGLTLPADT-VTAPDVAEALARIhdmcaadPGIARK----AADWASARFSLNQMIASTVRCYQ 692
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
22-370 |
2.81e-10 |
|
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: 61.19 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 22 YMKWFKEQGWEVHVAASGNM----------------KLPYVDQKYNIAIQRSPFHTGNMKAYRELKTVINENKYNIIHCH 85
Cdd:cd03823 24 LAEALVAEGHEVAVLTAGVGppgqatvarsvvryrrAPDETLPLALKRRGYELFETYNPGLRRLLARLLEDFRPDVVHTH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 86 TPMGgvLARLAARKARKQGTKVIYTAHGFhfckgappvnWLFYYpiektlahytDCLITINKEDYQLATKHFKAKRIE-- 163
Cdd:cd03823 104 NLSG--LGASLLDAARDLGIPVVHTLHDY----------WLLCP----------RQFLFKKGGDAVLAPSRFTANLHEan 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 164 -------HVHGVGIN-----TEKFKPANEKEKI----QLKKSFGYHpddfLLFYAAEFNKNKNqqlllqslalikdeiph 227
Cdd:cd03823 162 glfsariSVIPNAVEpdlapPPRRRPGTERLRFgyigRLTEEKGID----LLVEAFKRLPRED----------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 228 AKLLLAGKGPLLEnCRELAANLGIfhmvEFLG-YRND-----LQKIvpmcDVAVASSL-REGLPVNIMEAMACGIPVVAL 300
Cdd:cd03823 221 IELVIAGHGPLSD-ERQIEGGRRI----AFLGrVPTDdikdfYEKI----DVLVVPSIwPEPFGLVVREAIAAGLPVIAS 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 301 DNRGHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKVLieksRIYKS 370
Cdd:cd03823 292 DLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYL----KLYRD 357
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
74-349 |
1.00e-09 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 59.72 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 74 INENKYNIIHCHTPMGGVLARLAARKARKQGTKVIYTAH------GFHFCKGAPPVnWLFYYPIEKTlAHYTDCLITINK 147
Cdd:PLN02871 140 VARFKPDLIHASSPGIMVFGALFYAKLLCVPLVMSYHTHvpvyipRYTFSWLVKPM-WDIIRFLHRA-ADLTLVTSPALG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 148 EDYQlATKHFKAKRIEhVHGVGINTEKFKPANEKEKIQLKKSFGyHPDDFLLFYAAEFNKNKNQQLLLQslalIKDEIPH 227
Cdd:PLN02871 218 KELE-AAGVTAANRIR-VWNKGVDSESFHPRFRSEEMRARLSGG-EPEKPLIVYVGRLGAEKNLDFLKR----VMERLPG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 228 AKLLLAGKGPLLENCRELAANLGifhmVEFLGYR--NDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGH 305
Cdd:PLN02871 291 ARLAFVGDGPYREELEKMFAGTP----TVFTGMLqgDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGI 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1865037855 306 RELVHN---NKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRD 349
Cdd:PLN02871 367 PDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAARE 413
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
224-358 |
4.34e-09 |
|
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: 57.60 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 224 EIPHAKLLLAG--KGPLLENC------RELAANLGIF-HMVEFLGYRNDLQKIVPM--CDVAVASSLRE--GL-PVnimE 289
Cdd:cd03805 242 EFENVRLVIAGgyDPRVAENVeyleelQRLAEELLNVeDQVLFLRSISDSQKEQLLssALALLYTPSNEhfGIvPL---E 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1865037855 290 AMACGIPVVALDNRGHRELVHNNKNGWVIDSTSrVEFASKIKALAKIEGVKHKLGINGRDMILKKYSID 358
Cdd:cd03805 319 AMYAGKPVIACNSGGPLETVVEGVTGFLCEPTP-EAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSRE 386
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
230-360 |
4.64e-07 |
|
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: 51.12 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 230 LLLAGKGPLLENCRELAAnLGIFHMVEFLGYRNDLQKIVPM--CDVAVASS-LR-EGLPVNIMEAMACGIPVVALD-NRG 304
Cdd:cd03795 220 IVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEEKVIYLhlCDVFVFPSvLRsEAFGIVLLEAMMCGKPVISTNiGTG 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1865037855 305 HRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKV 360
Cdd:cd03795 299 VPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKM 354
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
186-348 |
5.81e-07 |
|
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: 51.17 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 186 LKKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAGKGP--------LLENCRELAANLGIFHMVEF 257
Cdd:cd03792 187 LEKPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAvddpegsvVYEEVMEYAGDDHDIHVLRL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 258 LGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNGWVIDStsrVEFASK-IKALAKI 336
Cdd:cd03792 267 PPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS---VEGAAVrILRLLTD 343
|
170
....*....|..
gi 1865037855 337 EGVKHKLGINGR 348
Cdd:cd03792 344 PELRRKMGLAAR 355
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
226-336 |
3.12e-06 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 48.93 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 226 PHAKLLLAGKGPLLENCRELAANLGIFHMVEFLGYRNDLQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALDNRGH 305
Cdd:PRK15490 428 PATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGS 507
|
90 100 110
....*....|....*....|....*....|.
gi 1865037855 306 RELVHNNKNGWVIDSTSRVEFASKIKALAKI 336
Cdd:PRK15490 508 AECFIEGVSGFILDDAQTVNLDQACRYAEKL 538
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
159-301 |
3.50e-06 |
|
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: 48.55 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 159 AKRIEHVHGV-------GINTEKFKPANEKEKIQLKKSFGYHPDDFLLFYAAeFNKNKNQQLLLQSLALIKDEIPHAKLL 231
Cdd:TIGR04047 150 AAELRAEWGIdatvvpnGVDAARFSPAADAADAALRRRLGLRGGPYVLAVGG-IEPRKNTIDLLEAFALLRARRPQAQLV 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1865037855 232 LAGKGPLL------ENCRELAANLGI-FHMVEFLGYRND--LQKIVPMCDVAVASSLREGLPVNIMEAMACGIPVVALD 301
Cdd:TIGR04047 229 IAGGATLFdydayrREFRARAAELGVdPGPVVITGPVPDadLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASD 307
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
277-356 |
4.53e-06 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 44.52 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 277 SSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNgwVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYS 356
Cdd:pfam13524 6 SRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEE--ILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHT 83
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
144-316 |
9.73e-06 |
|
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: 47.28 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 144 TINKEDYQLATKHFKAKRIEHVHGVG-------INTEKFKPANEKEkiqlkksfgyhpDDFLlfYAAEFNKNKNQqlllq 216
Cdd:cd03804 154 TAQRVDLFIANSQFVARRIKKFYGREstviyppVDTDAFAPAADKE------------DYYL--TASRLVPYKRI----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 217 slalikDEIPHA------KLLLAGKGPLLENCRELAANlgifhMVEFLGYRND--LQKIVPMCDVAVASSlREGLPVNIM 288
Cdd:cd03804 215 ------DLAVEAfnelpkRLVVIGDGPDLDRLRAMASP-----NVEFLGYQPDevLKELLSKARAFVFAA-EEDFGIVPV 282
|
170 180
....*....|....*....|....*...
gi 1865037855 289 EAMACGIPVVALDNRGHRELVHNNKNGW 316
Cdd:cd03804 283 EAQACGTPVIAFGKGGALETVRPGPTGI 310
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
287-361 |
1.06e-05 |
|
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: 46.97 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1865037855 287 IMEAMACGIPVVALDNRGHRELVHNNKNGWVIDSTSRVEFASKIKALAKIEGVKHKLGINGRDMILKKYSIDKVL 361
Cdd:cd03818 317 LLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCL 391
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
95-367 |
9.31e-05 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 43.93 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 95 LAARKARKQgtkviytahgfhFCKGAPPVNWLFYYPIEKTLAHYTDclitINKEDYQLATkhfkAKRIEH-VHGVGINTE 173
Cdd:PRK09922 97 LYANKARKK------------SGKQFKIFSWPHFSLDHKKHAECKK----ITCADYHLAI----SSGIKEqMMARGISAQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 174 K----FKPANEKEKI--QLKKSfgyHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDeipHAKLLLAGKGPLLENCRELAA 247
Cdd:PRK09922 157 RisviYNPVEIKTIIipPPERD---KPAVFLYVGRLKFEGQKNVKELFDGLSQTTG---EWQLHIIGDGSDFEKCKAYSR 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 248 NLGIFHMVEFLGYRNDLQKIVpMCDVAVASSL-----REGLPVNIMEAMACGIPVVALDNR-GHRELVHNNKNGWVIDST 321
Cdd:PRK09922 231 ELGIEQRIIWHGWQSQPWEVV-QQKIKNVSALlltskFEGFPMTLLEAMSYGIPCISSDCMsGPRDIIKPGLNGELYTPG 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1865037855 322 SRVEFASKIKALakIEGVKHKLGINGRDMILKKYS------IDKVLIEKSRI 367
Cdd:PRK09922 310 NIDEFVGKLNKV--ISGEVKYQHDAIPNSIERFYEvlyfknLNNALFSKLQK 359
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
289-336 |
6.41e-04 |
|
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: 41.50 E-value: 6.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1865037855 289 EAMACGIPVVALDNRGHRELVHNNKNGWVIDSTSrvEFASKIKALAKI 336
Cdd:cd03802 259 EAMACGTPVIAYRRGGLPEVIQHGETGFLVDSVE--EMAEAIANIDRI 304
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
169-360 |
7.78e-04 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 41.31 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 169 GINTEKFKPANEKEkiqLKKSFGYHPDDFLLFYAAEFNKNKNQQLLLQSLALIKDEIPHAKLLLAG---------KGPLL 239
Cdd:PRK15484 169 GFCLETYQSNPQPN---LRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGdptasskgeKAAYQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 240 ENCRELAANLGI-FHMvefLGYR--NDLQKIVPMCD-VAVASSLREGLPVNIMEAMACGIPVVALDNRGHRELVHNNKNG 315
Cdd:PRK15484 246 KKVLEAAKRIGDrCIM---LGGQppEKMHNYYPLADlVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITG 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1865037855 316 WVIDSTSRVE-FASKI-KALAKIEgvKHKLGINGRDMILKKYSIDKV 360
Cdd:PRK15484 323 YHLAEPMTSDsIISDInRTLADPE--LTQIAEQAKDFVFSKYSWEGV 367
|
|
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
222-333 |
7.95e-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: 38.02 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865037855 222 KDEIPHAKLLLA---GKGPLLENCRELAANLGIFHM------VEFlgyrNDLQKIVPMCDVAVA---SSLREGLPVNIME 289
Cdd:cd03816 258 ATEPALLPSLLCiitGKGPLKEMYLELIKELKLKKVtirtpwLSA----EDYPRLLASADLGVClhtSSSGLDLPMKVVD 333
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1865037855 290 AMACGIPVVALDNRGHRELVHNNKNGWVIdsTSRVEFASKIKAL 333
Cdd:cd03816 334 MFGCGLPVCAMDFKCIGELVKHGVNGLVF--GDSEELAEQLIDL 375
|
|
| |
