|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
15-424 |
0e+00 |
|
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: 513.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 15 RIALISTHGYVAAHPplGAADTGGQVVYVLELARKLGQLGYTVDLYTRRFED-QPEFDEVDERVRVVRIPCGGRDFIPKE 93
Cdd:cd03800 1 RIALISVHGSPLAQP--GGADTGGQNVYVLELARALAELGYQVDIFTRRISPaDPEVVEIAPGARVIRVPAGPPEYLPKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 94 YLHRHLMEWCENALRFIKKNNLNYSFINSHYWDAGVAGQRLSEALKVPHLHTPHSLGLWKKRQMETDYPekadtfeleFN 173
Cdd:cd03800 79 ELWPYLEEFADGLLRFIAREGGRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHSLGRVKYRHLGAQDT---------YH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 174 FKERIQHELIIYRSCDMVIATTPVQLDVLIEDYGLKRKHIHMIPPGYDDNRFFPVSDATRQMIRQRFGFEGKVVLALGRL 253
Cdd:cd03800 150 PSLRITAEEQILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEARRARLLLPPDKPVVLALGRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 254 ATNKGYDLLIDGFSVLAAREPEARLHLAVGGENMDEQETTilNQLKERVKSLGLEDKVAFSGYVEDEDLPDIYRAADLFV 333
Cdd:cd03800 230 DPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDR--EELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 334 LSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARSLF 413
Cdd:cd03800 308 VPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHY 387
|
410
....*....|.
gi 490567231 414 TWTGIAQQLLA 424
Cdd:cd03800 388 TWESVADQLLT 398
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
15-427 |
1.27e-60 |
|
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: 201.61 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 15 RIALISTHGyvaahPPlgaaDTGGQVVYVLELARKLGQLGYTVDLYTRRFEDQPEFDEVDERVRVVRIPCGGRDFIPKey 94
Cdd:cd03801 1 KILLLSPEL-----PP----PVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARR-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 95 lhrhlmewcenALRFIKKNNLNYSF--INSHYWDAGVAGQRLSEALKVPHLHTPHSLGLWKKRQMETDYpekadtfelef 172
Cdd:cd03801 70 -----------LLRELRPLLRLRKFdvVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAE----------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 173 nfKERIQHELIIYRSCDMVIATTPVQLDVLIEDYGLKRKHIHMIPPGYDDNRFFPvsdatrqMIRQRFGF--EGKVVLAL 250
Cdd:cd03801 128 --RRLLARAEALLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSP-------PLRRKLGIppDRPVLLFV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 251 GRLATNKGYDLLIDGFSVLAAREPEARLHLaVGGEnmdeqeTTILNQLKERvkSLGLEDKVAFSGYVEDEDLPDIYRAAD 330
Cdd:cd03801 199 GRLSPRKGVDLLLEALAKLLRRGPDVRLVI-VGGD------GPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAAD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 331 LFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKAR 410
Cdd:cd03801 270 VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVA 349
|
410
....*....|....*..
gi 490567231 411 SLFTWTGIAQQLLALVE 427
Cdd:cd03801 350 ERFSWERVAERLLDLYR 366
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
35-362 |
1.07e-41 |
|
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: 151.66 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 35 DTGGQVVYVLELARKLGQLGYTVDLYTRRFeDQPEFDEVDERVRVVRIPcggrdfiPKEYLHRHLMEWCENALRFIKKNn 114
Cdd:cd03817 12 QVNGVATSVRNLARALEKRGHEVYVITPSD-PGAEDEEEVVRYRSFSIP-------IRKYHRQHIPFPFKKAVIDRIKE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 115 LNYSFINSHY-WDAGVAGQRLSEALKVPHLHTPHSlglwkkrQMETDYPEKADTFELEFNFKERIQHELiiYRSCDMVIA 193
Cdd:cd03817 83 LGPDIIHTHTpFSLGKLGLRIARKLKIPIVHTYHT-------MYEDYLHYIPKGKLLVKAVVRKLVRRF--YNHTDAVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 194 TTPVQLDVLIEdYGLKrKHIHMIPPGYDDNRFFPVSDATrqmIRQRFGF--EGKVVLALGRLATNKGYDLLIDGFsVLAA 271
Cdd:cd03817 154 PSEKIKDTLRE-YGVK-GPIEVIPNGIDLDKFEKPLNTE---ERRKLGLppDEPILLYVGRLAKEKNIDFLLRAF-AELK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 272 REPEARLHLAvgGENMDEQEttilnqLKERVKSLGLEDKVAFSGYVEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAMAS 351
Cdd:cd03817 228 KEPNIKLVIV--GDGPEREE------LKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAA 299
|
330
....*....|.
gi 490567231 352 GTPtVVTIHGG 362
Cdd:cd03817 300 GLP-VVAAKDP 309
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
43-384 |
3.70e-41 |
|
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: 149.82 E-value: 3.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 43 VLELARKLGQLGYTVDLYTRRFEDQpEFDEVDERVRVVRIPcggrdFIPKEYLHRHLMEWCENALRFIKKNNLNYSFINS 122
Cdd:cd03811 18 LLNLANALDKRGYDVTLVLLRDEGD-LDKQLNGDVKLIRLL-----IRVLKLIKLGLLKAILKLKRILKRAKPDVVISFL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 123 HYWDAGVAGQRLSEALKVPHLHTPhslglwkkrqmetdypekadtFELEFNFKERIQHELIIYRSCDMVIATTPVQLDVL 202
Cdd:cd03811 92 GFATYIVAKLAAARSKVIAWIHSS---------------------LSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 203 IEDYGLKRKHIHMIPPGYDDNRFFPVSDATRQmirqRFGFEGKVVLALGRLATNKGYDLLIDGFSVLAAREPEARLHLAv 282
Cdd:cd03811 151 IRLGPSPPEKIEVIYNPIDIDRIRALAKEPIL----NEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVIL- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 283 gGENMDEQEttilnqLKERVKSLGLEDKVAFSGYVEDedLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGG 362
Cdd:cd03811 226 -GDGPLREE------LEKLAKELGLAERVIFLGFQSN--PYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPG 296
|
330 340
....*....|....*....|..
gi 490567231 363 LFRAVSYGRHALFADPFDKEDL 384
Cdd:cd03811 297 PREILDDGENGLLVPDGDAAAL 318
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
18-425 |
2.77e-37 |
|
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: 139.82 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 18 LISTHGYVAAHPPLGAadtggqvVYVLELARKLGQLGYTVDLYTRRFEDQPEFDEVDERVRVVRIPCGGRDFIPKEYLHR 97
Cdd:cd03798 2 LILTNIYPNANSPGRG-------IFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 98 HLMEWCENALRFIKKNNLNYSF--INSHY-WDAGVAGQRLSEALKVPHLHTPHSlglwkkrqmetdypekADTFELEFNF 174
Cdd:cd03798 75 LLAPLRAPSLAKLLKRRRRGPPdlIHAHFaYPAGFAAALLARLYGVPYVVTEHG----------------SDINVFPPRS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 175 KERIQHeLIIYRSCDMVIATTPVQLDVLIEdYGLKRKHIHMIPPGYDDNRFFPVSDatrqmiRQRFGFEGKVVLALGRLA 254
Cdd:cd03798 139 LLRKLL-RWALRRAARVIAVSKALAEELVA-LGVPRDRVDVIPNGVDPARFQPEDR------GLGLPLDAFVILFVGRLI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 255 TNKGYDLLIDGFSVLAAREPEARLHLAVGGENMDeqettilnQLKERVKSLGLEDKVAFSGYVEDEDLPDIYRAADLFVL 334
Cdd:cd03798 211 PRKGIDLLLEAFARLAKARPDVVLLIVGDGPLRE--------ALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 335 SSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPFkHERLYGRLSRMGAHKARSLFT 414
Cdd:cd03798 283 PSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRAL-AEPYLRELGEAARARVAERFS 361
|
410
....*....|.
gi 490567231 415 WTGIAQQLLAL 425
Cdd:cd03798 362 WVKAADRIAAA 372
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
36-424 |
1.14e-36 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 137.88 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 36 TGGQVvYVLELARKLGQLGYTVDLYTRRFEDQpefdevdERVRVVRIPCGGRDFIPKEYLHRHLMEWCENALRFIKKNNL 115
Cdd:cd03809 14 TGIGR-YTRELLKALAKNDPDESVLAVPPLPG-------ELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 116 NYSFINSHYwdagvAGQRLSealKVPHLHTPHSLglwkkrqMETDYPEkadtfelEFNFKERIQHELIIYRSC---DMVI 192
Cdd:cd03809 86 DLLHSPHNT-----APLLLK---GCPQVVTIHDL-------IPLRYPE-------FFPKRFRLYYRLLLPISLrraDAII 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 193 ATTPVQLDVLIEDYGLKRKHIHMIPPGYDDNRFFPVSDA---TRQMIRQRFgfegkvVLALGRLATNKGYDLLIDGFSVL 269
Cdd:cd03809 144 TVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAvliAKYLLPEPY------FLYVGTLEPRKNHERLLKAFALL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 270 AAREPEARLHLAVGGENMDEQettilnqLKERVKSLGLEDKVAFSGYVEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAM 349
Cdd:cd03809 218 KKQGGDLKLVIVGGKGWEDEE-------LLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAM 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490567231 350 ASGTPtVVTIHGGLFRAVsYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARsLFTWTGIAQQLLA 424
Cdd:cd03809 291 ACGTP-VIASNISVLPEV-AGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWEKTAEKTLE 362
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
243-384 |
5.25e-35 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 127.39 E-value: 5.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 243 EGKVVLALGRLATNKGYDLLIDGFSVLAAREPEARLHLaVGGENMDEQettilnqLKERVKSLGLEDKVAFSGYVEDEDL 322
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVI-AGDGEEEKR-------LKKLAEKLGLGDNVIFLGFVSDEDL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490567231 323 PDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDL 384
Cdd:pfam00534 73 PELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEAL 134
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
31-384 |
5.31e-35 |
|
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: 132.86 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 31 LGAADTGGQVVYVLELARKLGQLGYTVDLYTRRFEDQPEFDEVDERVRVVRIPcGGRDFIPKEYLHRHLMEWcenalrfi 110
Cdd:cd03819 5 TPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVP-LLRALLGNVRLARLIRRE-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 111 kknnlNYSFINSHYWDAGVAGQRLSEALKVPHLHTPHSLGLwkkrqmetdypekadtfeLEFNFKERiqHELIIYRScDM 190
Cdd:cd03819 76 -----RIDLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYL------------------ATYHPKDF--ALAVRARG-DR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 191 VIATTPVQLDVLIEDYGLKRKHIHMIPPGYDDNRFFPVSDATRqmiRQRFGFEGK--VVLALGRLATNKGYDLLIDgfsv 268
Cdd:cd03819 130 VIAVSELVRDHLIEALGVDPERIRVIPNGVDTDRFPPEAEAEE---RAQLGLPEGkpVVGYVGRLSPEKGWLLLVD---- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 269 LAAR-EPEARLHLAVGGENMDEQEttilnqLKERVKSLGLEDKVAFSGYveDEDLPDIYRAADLFVLSSRYEPFGMTAIE 347
Cdd:cd03819 203 AAAElKDEPDFRLLVAGDGPERDE------IRRLVERLGLRDRVTFTGF--REDVPAALAASDVVVLPSLHEEFGRVALE 274
|
330 340 350
....*....|....*....|....*....|....*..
gi 490567231 348 AMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDL 384
Cdd:cd03819 275 AMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEAL 311
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
16-415 |
1.74e-34 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 136.83 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 16 IALISTHGYV-AAHPPLGA-ADTGGQVVYVLELARKLGQLG--YTVDLYTRRFEdQPEFD----EVDERVR--------- 78
Cdd:TIGR02468 172 IVLISLHGLVrGENMELGRdSDTGGQVKYVVELARALGSMPgvYRVDLLTRQVS-SPDVDwsygEPTEMLTprssendgd 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 79 ---------VVRIPCGGRD-FIPKEYLHRHLMEWCENALRFIkknnLNYS----------------FINSHYWDAGVAGQ 132
Cdd:TIGR02468 251 emgessgayIIRIPFGPRDkYIPKEELWPYIPEFVDGALSHI----VNMSkvlgeqigsghpvwpyVIHGHYADAGDSAA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 133 RLSEALKVPHLHTPHSLGLWKKRQMETDYPEKADTFELEFNFKERIQHELIIYRSCDMVIATTPVQLDvliEDYGL---- 208
Cdd:TIGR02468 327 LLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIE---EQWGLydgf 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 209 ----KRK-----------------HIHMIPPGYDDNRFFPVSDatrQMIRQRFGFEGK---------------------- 245
Cdd:TIGR02468 404 dvilERKlrararrgvscygrfmpRMAVIPPGMEFSHIVPHDG---DMDGETEGNEEHpakpdppiwseimrfftnprkp 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 246 VVLALGRLATNKGYDLLIDGFSVLAAREPEARLHLAVGG-ENMDEQETT---ILNQLKERVKSLGLEDKVAFSGYVEDED 321
Cdd:TIGR02468 481 MILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNrDDIDEMSSGsssVLTSVLKLIDKYDLYGQVAYPKHHKQSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 322 LPDIYRAA----DLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGG---LFRAVSYGrhaLFADPFDKEDLGITMMKPFKH 394
Cdd:TIGR02468 561 VPDIYRLAaktkGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGpvdIHRVLDNG---LLVDPHDQQAIADALLKLVAD 637
|
490 500
....*....|....*....|.
gi 490567231 395 ERLYGRlSRMGAHKARSLFTW 415
Cdd:TIGR02468 638 KQLWAE-CRQNGLKNIHLFSW 657
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
167-421 |
5.69e-32 |
|
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: 124.66 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 167 TFELEFNFKERIQHELIIYRSCDMVIATTPvqlDVLIEDYGLKRKHIHMIPpgyddNrffPVSDATRQMIRQRfgfEGKV 246
Cdd:cd03820 118 NYEAYNKGLRRLLLRRLLYKRADKIVVLTE---ADKLKKYKQPNSNVVVIP-----N---PLSFPSEEPSTNL---KSKR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 247 VLALGRLATNKGYDLLIDGFSVLAAREPEARLHLAvgGENMDEQEttilnqLKERVKSLGLEDKVAFSGYVEDEDlpDIY 326
Cdd:cd03820 184 ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIY--GDGPEREE------LEKLIDKLGLEDRVKLLGPTKNIA--EEY 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 327 RAADLFVLSSRYEPFGMTAIEAMASGTPTV----------VTIHgglfravsyGRHALFADPFDKEDLGITMMKPFKHER 396
Cdd:cd03820 254 ANSSIFVLSSRYEGFPMVLLEAMAYGLPIIsfdcptgpseIIED---------GENGLLVPNGDVDALAEALLRLMEDEE 324
|
250 260
....*....|....*....|....*
gi 490567231 397 LYGRLSRmGAHKARSLFTWTGIAQQ 421
Cdd:cd03820 325 LRKKMGK-NARKNAERFSIEKIIKQ 348
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
244-384 |
4.17e-31 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 116.46 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 244 GKVVLALGRLATN-KGYDLLIDGFSVLAAREPEARLHLaVGGENMDEqettilnqLKERVKslGLEDKVAFSGYVEDedL 322
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVI-VGDGPEEE--------LEELAA--GLEDRVIFTGFVED--L 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490567231 323 PDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSyGRHALFADPFDKEDL 384
Cdd:pfam13692 68 AELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEAL 128
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
30-423 |
1.30e-30 |
|
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: 121.71 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 30 PLGAADTGGQVVYVLELARKLGQLGYTVDLYTrrfedqpeFDEVDERVRVVRIpcgGRDFIPKEYLHRHLM------EW- 102
Cdd:cd03821 7 PSISPKAGGPVKVVLRLAAALAALGHEVTIVS--------TGDGYESLVVEEN---GRYIPPQDGFASIPLlrqgagRTd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 103 -CENALRFIKKNNLNYSFINSH-YWD-AGVAGQRLSEALKVPHLHTPH-SLGLWKKRQMEtdypekadtfelefnFKERI 178
Cdd:cd03821 76 fSPGLPNWLRRNLREYDVVHIHgVWTyTSLAACKLARRRGIPYVVSPHgMLDPWALQQKH---------------WKKRI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 179 QHELIIYR--SCDMVIATTPVQLDVLIEDYGLkRKHIHMIPPGYDDNRFFPvsdatRQMIRQRFGF--EGKVVLALGRLA 254
Cdd:cd03821 141 ALHLIERRnlNNAALVHFTSEQEADELRRFGL-EPPIAVIPNGVDIPEFDP-----GLRDRRKHNGleDRRIILFLGRIH 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 255 TNKGYDLLIDGFSVLAAREPEARLHLAvgGEnmDEQETTILNQLkerVKSLGLEDKVAFSGYVEDEDLPDIYRAADLFVL 334
Cdd:cd03821 215 PKKGLDLLIRAARKLAEQGRDWHLVIA--GP--DDGAYPAFLQL---QSSLGLGDRVTFTGPLYGEAKWALYASADLFVL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 335 SSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGrHALFADPfDKEDL--GITMMKPFKHERLYGRLSRMGAHKARSL 412
Cdd:cd03821 288 PSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLaeALAEALRDPADRKRLGEMARRARQVEEN 365
|
410
....*....|.
gi 490567231 413 FTWTGIAQQLL 423
Cdd:cd03821 366 FSWEAVAGQLG 376
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
37-384 |
2.89e-27 |
|
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: 111.92 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 37 GGQVVYVLELARKLGQLGYTVDLYTRRFEDQPEFdEVDERVRVVRIPCGGRDFIP-KEYlhRHLMEWcenaLRFIKKnnL 115
Cdd:cd03808 10 GGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDE-LKELGVKVIDIPILRRGINPlKDL--KALFKL----YKLLKK--E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 116 NYSFINSHYWDAGVAGqRL-SEALKVPH-LHTPHSLGLwkkrqmetdypEKADTFELEFNFKeRIqhELIIYRSCDMVIA 193
Cdd:cd03808 81 KPDIVHCHTPKPGILG-RLaARLAGVPKvIYTVHGLGF-----------VFTEGKLLRLLYL-LL--EKLALLFTDKVIF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 194 TTPVQLDVLIEDYGLKRKHIHMIPP-GYDDNRFFPVSDATRQmirqrfgfEGKVVLALGRLATNKGYDLLIDGFSVLAAR 272
Cdd:cd03808 146 VNEDDRDLAIKKGIIKKKKTVLIPGsGVDLDRFQYSPESLPS--------EKVVFLFVARLLKDKGIDELIEAAKILKKK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 273 EPEARLHLAVGGEnmdeqettILNQLKERVKSLGLEDKVAFSGYVEDedLPDIYRAADLFVLSSRYEPFGMTAIEAMASG 352
Cdd:cd03808 218 GPNVRFLLVGDGE--------LENPSEILIEKLGLEGRIEFLGFRSD--VPELLAESDVFVLPSYREGLPRSLLEAMAAG 287
|
330 340 350
....*....|....*....|....*....|..
gi 490567231 353 TPTVVTIHGGLFRAVSYGRHALFADPFDKEDL 384
Cdd:cd03808 288 RPVITTDVPGCRELVIDGVNGFLVPPGDVEAL 319
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
116-362 |
5.14e-27 |
|
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: 111.25 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 116 NYSFINSHYWDAGVAGqRLSE--ALKVPHLHTPHSLGLWKKRQmetdypekadtfelefnfKERIQHELIIYRSCDMVIA 193
Cdd:cd03807 79 NPDVVHTWMYHADLIG-GLAAklAGGVKVIWSVRSSNIPQRLT------------------RLVRKLCLLLSKFSPATVA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 194 TTPVQLDVLIEDYGLKRKhIHMIPPGYDDNRFFPvSDATRQMIRQRFGF--EGKVVLALGRLATNKGYDLLIDGFSVLAA 271
Cdd:cd03807 140 NSSAVAEFHQEQGYAKNK-IVVIYNGIDLFKLSP-DDASRARARRRLGLaeDRRVIGIVGRLHPVKDHSDLLRAAALLVE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 272 REPEARLhLAVGGEnmdEQETTILNQLKErvksLGLEDKVAFSGYVEDedLPDIYRAADLFVLSSRYEPFGMTAIEAMAS 351
Cdd:cd03807 218 THPDLRL-LLVGRG---PERPNLERLLLE----LGLEDRVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALLEAMAC 287
|
250
....*....|.
gi 490567231 352 GTPTVVTIHGG 362
Cdd:cd03807 288 GLPVVATDVGG 298
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
15-423 |
5.94e-27 |
|
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: 111.67 E-value: 5.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 15 RIALISTHGYvaahPPLGAADTggqvvYVLELARKLGQLGYTVDLYTRRFEDQPEFD-----EVDERVRVVRIPCGGRDF 89
Cdd:cd03794 1 KILLISQYYP----PPKGAAAA-----RVYELAKELVRRGHEVTVLTPSPNYPLGRIfagatETKDGIRVIRVKLGPIKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 90 IPKEYLHRHLMEWCENALRFIKKNNLNY--SFINSHYWDAGVAGQRLSEALKVP---HLHTPHSLGLWKKRQMETDYPEK 164
Cdd:cd03794 72 NGLIRRLLNYLSFALAALLKLLVREERPdvIIAYSPPITLGLAALLLKKLRGAPfilDVRDLWPESLIALGVLKKGSLLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 165 AdtfeleFNFKERIqheliIYRSCDMVIATTPVQLDVLIEDyGLKRKHIHMIPPGYDDNRFFPVSdatRQMIRQRFGFEG 244
Cdd:cd03794 152 L------LKKLERK-----LYRLADAIIVLSPGLKEYLLRK-GVPKEKIIVIPNWADLEEFKPPP---KDELRKKLGLDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 245 KVVLALGRLATNK-GYDLLIDGFSVLAaREPEARLHLAVGGenmDEQEttilnQLKERVKSLGLeDKVAFSGYVEDEDLP 323
Cdd:cd03794 217 KFVVVYAGNIGKAqGLETLLEAAERLK-RRPDIRFLFVGDG---DEKE-----RLKELAKARGL-DNVTFLGRVPKEEVP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 324 DIYRAADLFVLSSRYEPFGMTAI-----EAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDL--GItmmkpfkhER 396
Cdd:cd03794 287 ELLSAADVGLVPLKDNPANRGSSpsklfEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALadAI--------LE 358
|
410 420 430
....*....|....*....|....*....|....
gi 490567231 397 LY---GRLSRMGAhKARSL----FTWTGIAQQLL 423
Cdd:cd03794 359 LLddpELRRAMGE-NGRELaeekFSREKLADRLL 391
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
186-414 |
2.97e-24 |
|
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: 103.12 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 186 RSCDMVIATTPVQLDV--LIEDYglkRKHIHMIPPGYDDNRFfPVSDATRQMIRQRFGFEgKVVLALGRLATNKGYDLLI 263
Cdd:cd03795 136 RRADRIIATSPNYVETspTLREF---KNKVRVIPLGIDKNVY-NIPRVDFENIKREKKGK-KIFLFIGRLVYYKGLDYLI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 264 DgfsvlAAREpeARLHLAVGGENMDEQEttilnqLKERVKsLGLEDKVAFSGYVEDEDLPDIYRAADLFVLSS--RYEPF 341
Cdd:cd03795 211 E-----AAQY--LNYPIVIGGEGPLKPD------LEAQIE-LNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSvlRSEAF 276
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490567231 342 GMTAIEAMASGTPTVVTIHGGlfrAVSY----GRHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARSLFT 414
Cdd:cd03795 277 GIVLLEAMMCGKPVISTNIGT---GVPYvnnnGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFT 350
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
325-427 |
3.91e-23 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 93.90 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 325 IYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSRM 404
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|...
gi 490567231 405 GAHKARSLFTWTGIAQQLLALVE 427
Cdd:COG0438 97 ARERAEERFSWEAIAERLLALYE 119
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
172-375 |
8.19e-23 |
|
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: 96.70 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 172 FNFKERIQHELIIYRsCDMVIATTP----VQLDVLIEDYGLKRKHIHMIPPGYDDNRFFPvsdatRQMIRQRFGFEGKVV 247
Cdd:cd01635 40 LLALRRILKKLLELK-PDVVHAHSPhaaaLAALLAARLLGIPIVVTVHGPDSLESTRSEL-----LALARLLVSLPLADK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 248 LALGRLATNKGYDLLIDGFSVLAAREPEARLHLAVGGENMDEQETTILN-QLKERVKSLGledkvafsGYVEDEDLPDIY 326
Cdd:cd01635 114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAAlGLLERVVIIG--------GLVDDEVLELLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490567231 327 RAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALF 375
Cdd:cd01635 186 AAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
37-423 |
6.71e-22 |
|
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: 96.59 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 37 GGQVVYVLELARKLGQLGYTVDLYTRRFEDqPEFDEVDERVRVVRIPCGGRDFIPKEYLHRHLMEwcenalRFIKKnnLN 116
Cdd:cd03814 14 NGVVRTLERLVDHLRRRGHEVRVVAPGPFD-EAESAEGRVVSVPSFPLPFYPEYRLALPLPRRVR------RLIKE--FQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 117 YSFINSHYWD-AGVAGQRLSEALKVPHLHTPHslglwkkrqmeTDYPEKADTFELEFNFKERIQHELIIYRSCDMVIATT 195
Cdd:cd03814 85 PDIIHIATPGpLGLAALRAARRLGLPVVTSYH-----------TDFPEYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 196 PVQLDVLiEDYGLKRkhIHMIPPGYDDNRFFPvsdATR-QMIRQRFGFEGK-VVLALGRLATNKGYDLLIDGFSVLAARE 273
Cdd:cd03814 154 PSIAREL-EGHGFER--VRLWPRGVDTELFHP---SRRdAALRRRLGPPGRpLLLYVGRLAPEKNLEALLDADLPLAASP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 274 PearLHLAVGGENMDEQEttilnqLKERVkslgleDKVAFSGYVEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGT 353
Cdd:cd03814 228 P---VRLVVVGDGPARAE------LEARG------PDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGL 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 354 PTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPFKHERLYGRLsRMGAHKARSLFTWTGIAQQLL 423
Cdd:cd03814 293 PVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRM-AARARAEAERYSWEAFLDNLL 361
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
37-221 |
1.24e-21 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 91.44 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 37 GGQVVYVLELARKLGQLGYTVDLYTRRFeDQPEFDEVDERVRVVRIPcggrdfIPKEYLHRHLMEWCENALRFIKKNnlN 116
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGG-PGPLAEEVVRVVRVPRVP------LPLPPRLLRSLAFLRRLRRLLRRE--R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 117 YSFINSHYW-DAGVAGQRLSEALKVPHLHTPHSLGLWKKRQMETDYPEKADTFELEFNFkeriqheliiYRSCDMVIATT 195
Cdd:pfam13439 72 PDVVHAHSPfPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRL----------LRRADRVIAVS 141
|
170 180
....*....|....*....|....*.
gi 490567231 196 PVQLDVLIEDYGLKRKHIHMIPPGYD 221
Cdd:pfam13439 142 EAVADELRRLYGVPPEKIRVIPNGVD 167
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
208-425 |
1.31e-21 |
|
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: 95.86 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 208 LKRKHIHMIPPGYDDNRFFPVSdatRQMIRQRFGFEG--KVVLALGRLATN--KGYDLLIDgfsVLAAREPEARLHLAVG 283
Cdd:cd03825 158 LKGLPVVVIPNGIDTEIFAPVD---KAKARKRLGIPQdkKVILFGAESVTKprKGFDELIE---ALKLLATKDDLLLVVF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 284 GENmDEQettiLNQLKERVKSLGLEDkvafsgyvEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGL 363
Cdd:cd03825 232 GKN-DPQ----IVILPFDIISLGYID--------DDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGS 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490567231 364 FRAVSYGRHALFADPFDKEDL--GITMMKPFKHERL-YGRLSRM--GAHKARSLftwtgIAQQLLAL 425
Cdd:cd03825 299 PEIVQHGVTGYLVPPGDVQALaeAIEWLLANPKEREsLGERARAlaENHFDQRV-----QAQRYLEL 360
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
15-402 |
1.60e-21 |
|
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: 95.47 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 15 RIALISTHgyvaaHPPLgaaDTGGQVVYVLELARKLGQLGYTVDLYTRRFEDQPefdeVDERVRVVRipcggrdfipkeY 94
Cdd:cd03823 1 KILLVNSL-----YPPQ---RVGGAEISVHDLAEALVAEGHEVAVLTAGVGPPG----QATVARSVV------------R 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 95 LHRHLMEWCENALRFIkknnlnySFINSHYWDAGVAG--QRLSEALK--VPHLHTP--HSLGLWKK-RQME-------TD 160
Cdd:cd03823 57 YRRAPDETLPLALKRR-------GYELFETYNPGLRRllARLLEDFRpdVVHTHNLsgLGASLLDAaRDLGipvvhtlHD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 161 YpekadtfelefnFKERIQHELIIYRScDMVIATTPVQLDVLIEDyGLKRKHIHMIPPGyddNRFFPVSDATRQMIRQ-- 238
Cdd:cd03823 130 Y------------WLLCPRQFLFKKGG-DAVLAPSRFTANLHEAN-GLFSARISVIPNA---VEPDLAPPPRRRPGTErl 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 239 RFGFegkvvlaLGRLATNKGYDLLIDgfSVLAAREPEARLHLAvgGENMDEQEttilnqlkervKSLGLEDKVAFSGYVE 318
Cdd:cd03823 193 RFGY-------IGRLTEEKGIDLLVE--AFKRLPREDIELVIA--GHGPLSDE-----------RQIEGGRRIAFLGRVP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 319 DEDLPDIYRAADLFVLSSR-YEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPFKHERL 397
Cdd:cd03823 251 TDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPAL 330
|
....*
gi 490567231 398 YGRLS 402
Cdd:cd03823 331 LERLR 335
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
35-357 |
5.84e-21 |
|
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: 93.89 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 35 DTGGQVVYVLELARKLGQLGYTVDLYTRRFEDQPEFDEVDER-VRVVRIPcggrdfIPKEYLHRHLMEwcenALRFIKKN 113
Cdd:cd03812 10 NVGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEELEELgGKIFYIP------PKKKNIIKYFIK----LLKLIKKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 114 NlnYSFInshywdagvagqrlsealkvpHLHTPHSLG---LW-KKRQMETD-YPEKADTFELEFNFKERIQH-ELIIYRS 187
Cdd:cd03812 80 K--YDIV---------------------HVHGSSSNGiilLLaAKAGVPVRiAHSHNTKDSSIKLRKIRKNVlKKLIERL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 188 CDMVIAttpVQLDVLIEDYGLKRKHIHM-IPPGYDDNRFFPvSDATRQMIRQRFGFEGKVVLA-LGRLATNKGYDLLIDG 265
Cdd:cd03812 137 STKYLA---CSEDAGEWLFGEVENGKFKvIPNGIDIEKYKF-NKEKRRKRRKLLILEDKLVLGhVGRFNEQKNHSFLIDI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 266 FSVLAAREPEARLHLAVGGEnmdeqettILNQLKERVKSLGLEDKVAFSGYVEDedLPDIYRAADLFVLSSRYEPFGMTA 345
Cdd:cd03812 213 FEELKKKNPNVKLVLVGEGE--------LKEKIKEKVKELGLEDKVIFLGFRND--VSEILSAMDVFLFPSLYEGLPLVA 282
|
330
....*....|..
gi 490567231 346 IEAMASGTPTVV 357
Cdd:cd03812 283 VEAQASGLPCLL 294
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
182-368 |
1.82e-20 |
|
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: 92.51 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 182 LIIYRSCDMVIA-TTPVQ---LDVLIEDYGLKRKHIHMIPPGYDDNRFfPVSDATRQMIRQRFG--FEGKVVLALGRLAT 255
Cdd:cd04951 121 MFIYRLTDFLCDiTTNVSreaLDEFIAKKAFSKNKSVPVYNGIDLNKF-KKDINVRLKIRNKLNlkNDEFVILNVGRLTE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 256 NKGYDLLIDGFSVLAAREPEARLHLAVGGENMDEQETTILNqlkervksLGLEDKVAFSGYVEDedLPDIYRAADLFVLS 335
Cdd:cd04951 200 AKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICN--------LNLVDRVILLGQISN--ISEYYNAADLFVLS 269
|
170 180 190
....*....|....*....|....*....|...
gi 490567231 336 SRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVS 368
Cdd:cd04951 270 SEWEGFGLVVAEAMACERPVVATDAGGVAEVVG 302
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
104-356 |
2.09e-19 |
|
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: 88.90 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 104 ENALR--FIKKNNLNYS--FINshywD-AGVAGQRL----SEALKVPHLHTPHslglwkkrqmetdYPEKADTFELEFN- 173
Cdd:cd04949 40 EQELFafFIEQLNLQKGdiFIS----DrPTLTGQVIlntkGPAKKGAVLHNEH-------------VKNNDDPEHSLIKn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 174 -FKERIQHeliIYRsCDMVIATTPVQLDVLIEDYGlKRKHIHMIPPGYDDNRFFPVSDATRqmirqrfgfEGKVVLALGR 252
Cdd:cd04949 103 fYKYVFEN---LNK-YDAIIVSTEQQKQDLSERFN-KYPPIFTIPVGYVDQLDTAESNHER---------KSNKIITISR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 253 LATNKGYDLLIDGFSVLAAREPEARLHL-AVGGENmdeqettilNQLKERVKSLGLEDKVAFSGYVEDEDlpDIYRAADL 331
Cdd:cd04949 169 LAPEKQLDHLIEAVAKAVKKVPEITLDIyGYGEER---------EKLKKLIEELHLEDNVFLKGYHSNLD--QEYQDAYL 237
|
250 260
....*....|....*....|....*
gi 490567231 332 FVLSSRYEPFGMTAIEAMASGTPTV 356
Cdd:cd04949 238 SLLTSQMEGFGLTLMEAIGHGLPVV 262
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
173-414 |
1.05e-18 |
|
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: 88.16 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 173 NFKERIQHelIIYRSCDMVIA----TTPVQldvliEDYGLKRKHIHMIPPGYDDNRFFPVSdatrqmiRQRFGFEGKVVL 248
Cdd:cd03813 232 RFFERLGK--LAYQQADKIISlyegNRRRQ-----IRLGADPDKTRVIPNGIDIQRFAPAR-------EERPEKEPPVVG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 249 ALGRLATNKGYDLLIDGFSVLAAREPEARLHLaVGGENMDEQettILNQLKERVKSLGLEDKVAFSGYVedeDLPDIYRA 328
Cdd:cd03813 298 LVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWL-IGPEDEDPE---YAQECKRLVASLGLENKVKFLGFQ---NIKEYYPK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 329 ADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAV-----SYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSR 403
Cdd:cd03813 371 LGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGE 450
|
250
....*....|.
gi 490567231 404 MGAHKARSLFT 414
Cdd:cd03813 451 AGRKRVEKYYT 461
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
120-418 |
2.85e-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: 85.97 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 120 INSHYWDAGVAGQRLSEALKVPHLHTPHSLGLWKKRQMETDYPEKADTFELefnfkeriqHELIIYRSCDMVIATTPVQL 199
Cdd:cd05844 85 VHAHFGRDGVYALPLARALGVPLVVTFHGFDITTSRAWLAASPGWPSQFQR---------HRRALQRPAALFVAVSGFIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 200 DVLIEdYGLKRKHIHMIPPGYDDNRFFPVSDATRQmirqrfgfegKVVLALGRLATNKGYDLLIDGFSVLAAREPEARLH 279
Cdd:cd05844 156 DRLLA-RGLPAERIHVHYIGIDPAKFAPRDPAERA----------PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 280 LAVGGenmdeqetTILNQLKERVKSLGledKVAFSGYVEDEDLPDIYRAADLFVLSSRY------EPFGMTAIEAMASGT 353
Cdd:cd05844 225 IAGDG--------PLRPALQALAAALG---RVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGV 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490567231 354 PTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARSLF---TWTGI 418
Cdd:cd05844 294 PVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFdirVQTAK 361
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
209-413 |
4.77e-18 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 85.48 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 209 KRKHIHMIPPGYDDNRFFPvsDATRQMIRQRFGFEG-KVVLALGRLATNKGYDLLIDGFSVLAAREPeARLHLAVGGENM 287
Cdd:cd04962 162 VDKDIEVIHNFIDEDVFKR--KPAGALKRRLLAPPDeKVVIHVSNFRPVKRIDDVVRVFARVRRKIP-AKLLLVGDGPER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 288 DEQEttilnqlkERVKSLGLEDKVAFSGYVEDEDlpDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAV 367
Cdd:cd04962 239 VPAE--------ELARELGVEDRVLFLGKQDDVE--ELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVV 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490567231 368 SYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARSLF 413
Cdd:cd04962 309 KHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERF 354
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
37-219 |
2.28e-15 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 73.20 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 37 GGQVVYVLELARKLGQLGYTVDLYTRRfEDQPEFDEVDERVRVVRIPCGGRDfipkeyLHRHLMEWCENALRFIKKnnLN 116
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPG-GPPGRPELVGDGVRVHRLPVPPRP------SPLADLAALRRLRRLLRA--ER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 117 YSFINSHYWDAGVAGQRLSEALKVPHLHTPHSLGL-----WKKRqmetdypekadtfelefnFKERIQHELiiYRSCDMV 191
Cdd:pfam13579 72 PDVVHAHSPTAGLAARLARRRRGVPLVVTVHGLALdygsgWKRR------------------LARALERRL--LRRADAV 131
|
170 180
....*....|....*....|....*...
gi 490567231 192 IATTPVQLDVLIEdYGLKRKHIHMIPPG 219
Cdd:pfam13579 132 VVVSEAEAELLRA-LGVPAARVVVVPNG 158
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
202-425 |
2.74e-11 |
|
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: 64.71 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 202 LIEDYGLKRKHIHMIPPGYDDNRFFPVSDATRQmirqrFGFEGK-VVLALGRLATNKGYDLLIDGFSVLAAREPEARLHL 280
Cdd:cd03822 149 LVRIKLIPAVNIEVIPHGVPEVPQDPTTALKRL-----LLPEGKkVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVI 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 281 AvGGENMDEQETTILNQLKERVKSLGLEDKVAF-SGYVEDEDLPDIYRAADLFVLSSRYEPFGM--TAIEAMASGTPTVV 357
Cdd:cd03822 224 A-GELHPSLARYEGERYRKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPYLNTEQSSsgTLSYAIACGKPVIS 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490567231 358 TIHGGLFRAVSYGRHALFaDPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARSLfTWTGIAQQLLAL 425
Cdd:cd03822 303 TPLRHAEELLADGRGVLV-PFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAM-TWESIADRYLRL 368
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
213-363 |
1.28e-10 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 62.89 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 213 IHMIPPGYDDNRFfpvSDATRQMIRQRFGF--EGKVVLALGRLATNKGYDLLIDGFSVLaaREPEARLHLAVGGENMDE- 289
Cdd:PRK15484 163 ISIVPNGFCLETY---QSNPQPNLRQQLNIspDETVLLYAGRISPDKGILLLMQAFEKL--ATAHSNLKLVVVGDPTASs 237
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490567231 290 --QETTILNQLKERVKSLGleDKVAFSGYVEDEDLPDIYRAADLFVLSSRY-EPFGMTAIEAMASGTPTVVTIHGGL 363
Cdd:PRK15484 238 kgEKAAYQKKVLEAAKRIG--DRCIMLGGQPPEKMHNYYPLADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGI 312
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
36-428 |
1.63e-10 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 62.97 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 36 TGGQVVYVLELARKLGQLGYTV--------------DLYTRRFEDQPEFDEVDERVRVVRIPCGGRDFI---PKEYLHR- 97
Cdd:cd03791 15 TGGLGDVAGALPKALAKLGHDVrvilprygqipdelDGYLRVLGLEVKVGGRGEEVGVFELPVDGVDYYfldNPEFFDRp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 98 -----HLMEWCENALRF----------IKKNNLNYSFINSHYWDAGVA------GQRLSEALKVPHLHTPHSL---GLWK 153
Cdd:cd03791 95 glpgpPGYDYPDNAERFaffsraalelLRRLGFQPDIIHANDWHTALVpaylktRYRGPGFKKIKTVFTIHNLayqGLFP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 154 KRQM-ETDYPEKADTFE-LEF----NF-KERIQHeliiyrsCDMVIATTP-----VQLDVLIED-YGLKRKH---IHMIP 217
Cdd:cd03791 175 LDTLaELGLPPELFHIDgLEFygqiNFlKAGIVY-------ADRVTTVSPtyakeILTPEYGEGlDGVLRARagkLSGIL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 218 PGYDDNRFFPVSDAT----------------RQMIRQRFGFE---GKVVLAL-GRLATNKGYDLLIDGFSVLAAREpeAR 277
Cdd:cd03791 248 NGIDYDEWNPATDKLipanysandlegkaenKAALQKELGLPvdpDAPLFGFvGRLTEQKGVDLILDALPELLEEG--GQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 278 LHLAVGGE-NMDEQETTILNQLKERVKslgledkvAFSGYveDEDL-PDIYRAADLFVLSSRYEPFGMTAIEAMASGTPT 355
Cdd:cd03791 326 LVVLGSGDpEYEQAFRELAERYPGKVA--------VVIGF--DEALaHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 356 VVTIHGGLFRAVSYGRHA-------LFaDPFDKEDLGITMMKP---FKHERLYGRLSRMGAHKArslFTWTGIAQQLLAL 425
Cdd:cd03791 396 IVRRTGGLADTVFDYDPEtgegtgfVF-EDYDAEALLAALRRAlalYRNPELWRKLQKNAMKQD---FSWDKSAKEYLEL 471
|
...
gi 490567231 426 VEG 428
Cdd:cd03791 472 YRS 474
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
213-362 |
1.17e-09 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 59.94 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 213 IHMIPPGYDDNRFFPvsDATRQMIrqrfgfEGKVVLALGRLATNKGYDLLIDGFSVLAAREPEARLHLAVGGENMDEQET 292
Cdd:cd03796 170 VSVIPNAVDSSDFTP--DPSKPDP------NKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEE 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490567231 293 TI-LNQLKERVKSLGledkvafsgYVEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGG 362
Cdd:cd03796 242 MReKYQLQDRVELLG---------AVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGG 303
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
236-428 |
2.47e-09 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 59.20 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 236 IRQRFGFE---GKVVLAL-GRLATNKGYDLLIDgfSVLAAREPEARLH-LAVGGENMDEQettiLNQLKERvkslgLEDK 310
Cdd:TIGR02095 279 LQEELGLPvddDVPLFGViSRLTQQKGVDLLLA--ALPELLELGGQLVvLGTGDPELEEA----LRELAER-----YPGN 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 311 VAFS-GYveDEDLPD-IYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHA-------LFaDPFDK 381
Cdd:TIGR02095 348 VRVIiGY--DEALAHlIYAGADFILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDPEaesgtgfLF-EEYDP 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490567231 382 EDLGITMMKPFKHERLYGRL-SRMGAHKARSLFTWTGIAQQLLALVEG 428
Cdd:TIGR02095 425 GALLAALSRALRLYRQDPSLwEALQKNAMSQDFSWDKSAKQYVELYRS 472
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
213-363 |
4.35e-09 |
|
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: 57.68 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 213 IHMIPPGYDDNRFFPVSDatrqmirqrfgfEGKVVLALGRLATNKGYDLLIDgfsvlAAREpeARLHLAVGGENMDEQET 292
Cdd:cd03802 150 LTVVHNGLDPADYRFQPD------------PEDYLAFLGRIAPEKGLEDAIR-----VARR--AGLPLKIAGKVRDEDYF 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490567231 293 TILNQLKervkslgLEDKVAFSGYVEDEDLPD-IYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGL 363
Cdd:cd03802 211 YYLQEPL-------PGPRIEFIGEVGHDEKQElLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGL 275
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
186-363 |
7.61e-09 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 57.41 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 186 RSCDMVIATTPVQLDVLIEDYGLKRKHIHMIPPGYDDNRFFP--VSDATRQmiRQRFG-FEGKVVLALGRLATNKGYDLL 262
Cdd:PLN02871 204 RAADLTLVTSPALGKELEAAGVTAANRIRVWNKGVDSESFHPrfRSEEMRA--RLSGGePEKPLIVYVGRLGAEKNLDFL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 263 IDgfsVLAaREPEARLhlAVGGENMDEQEttilnqLKERVKSLgledKVAFSGYVEDEDLPDIYRAADLFVLSSRYEPFG 342
Cdd:PLN02871 282 KR---VME-RLPGARL--AFVGDGPYREE------LEKMFAGT----PTVFTGMLQGDELSQAYASGDVFVMPSESETLG 345
|
170 180
....*....|....*....|.
gi 490567231 343 MTAIEAMASGTPTVVTIHGGL 363
Cdd:PLN02871 346 FVVLEAMASGVPVVAARAGGI 366
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
237-363 |
1.77e-07 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 53.17 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 237 RQRFGFE---GKVVLAL-GRLATNKGYDLLIDGFSVLAAREpearLHLAVGGENmDEQETTILNQLKERvkslgLEDKVA 312
Cdd:COG0297 284 QEELGLPvdpDAPLIGMvSRLTEQKGLDLLLEALDELLEED----VQLVVLGSG-DPEYEEAFRELAAR-----YPGRVA 353
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 490567231 313 FS-GYveDEDLPD-IYRAADLFVLSSRYEPFGMTAIEAMASGTPTVV--TihGGL 363
Cdd:COG0297 354 VYiGY--DEALAHrIYAGADFFLMPSRFEPCGLNQMYALRYGTVPIVrrT--GGL 404
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
252-433 |
2.69e-07 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 53.11 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 252 RLATNKGYDLLIDGFSVLAAREPEARLHLAVGGEnmdeqettILNQLKERVKSLGLEDKVAFSGYveDEDLPDIYRAADL 331
Cdd:PRK15179 525 RVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGP--------LLESVREFAQRLGMGERILFTGL--SRRVGYWLTQFNA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 332 FVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYG--RHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKA 409
Cdd:PRK15179 595 FLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGvtGLTLPADTVTAPDVAEALARIHDMCAADPGIARKAADWA 674
|
170 180
....*....|....*....|....
gi 490567231 410 RSLFTWTGIAQQLLALVEgrplMP 433
Cdd:PRK15179 675 SARFSLNQMIASTVRCYQ----MP 694
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
248-362 |
2.96e-07 |
|
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: 52.29 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 248 LALGRLATNKGYDLLIDGFSVLAARepearlhLAVGGENMDeqettiLNQLKERVKslgleDKVAFSGYVEDEDLPDIYR 327
Cdd:cd03804 203 LTASRLVPYKRIDLAVEAFNELPKR-------LVVIGDGPD------LDRLRAMAS-----PNVEFLGYQPDEVLKELLS 264
|
90 100 110
....*....|....*....|....*....|....*
gi 490567231 328 AADLFVLSSRyEPFGMTAIEAMASGTPTVVTIHGG 362
Cdd:cd03804 265 KARAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGG 298
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
219-413 |
1.05e-06 |
|
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: 50.53 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 219 GYDDNRF--FPVSDATRQMIRqrfgfegkvVLALGRLATNKGYDLLIDGFSVLAAREPEARLHLAVGGEnmdeqettILN 296
Cdd:cd03799 156 GIDCNKFrfKPRYLPLDGKIR---------ILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGD--------LKE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 297 QLKERVKSLGLEDKVAFSGYVEDEDLPDIYRAADLFVLSSRYEPFG------MTAIEAMASGTPTVVTIHGGLFRAVSYG 370
Cdd:cd03799 219 QLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPELVEDG 298
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490567231 371 RHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARSLF 413
Cdd:cd03799 299 VSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEY 341
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
188-425 |
1.07e-06 |
|
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: 50.40 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 188 CDMVIATTP--VQLDVLIedyglkRKHIhmIPPGYDdnrffPVSDATRQMIRQRFGFEG----------KVVLALGRLAT 255
Cdd:cd03792 142 YDLFVFHPPefVPPQVPP------PKFY--IPPSID-----PLSGKNKDLSPADIRYYLekpfvidperPYILQVARFDP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 256 NKGYDLLIDGFSVLAAREPEARLHLAVGGENMDEQETTILNQLKErvKSLGLEDKVAFSGYVEDEDLPDIYRAADLFVLS 335
Cdd:cd03792 209 SKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPEGSVVYEEVME--YAGDDHDIHVLRLPPSDQEINALQRAATVVLQL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 336 SRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPfdKEDLGITMMKPFKHERLYGRLSRMGAHKARSLFTW 415
Cdd:cd03792 287 STREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAVRILRLLTDPELRRKMGLAAREHVRDNFLI 364
|
250
....*....|
gi 490567231 416 TGIAQQLLAL 425
Cdd:cd03792 365 TGNLRAWLYL 374
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
205-356 |
1.17e-06 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 50.48 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 205 DYGLKRKHIHMIppgyddnrFFPVsDATRQMIRQRFGFEGKVVLALGRLaTNKGYDLLIDGFSVLAAREPEARLHLAVGG 284
Cdd:PRK09922 150 ARGISAQRISVI--------YNPV-EIKTIIIPPPERDKPAVFLYVGRL-KFEGQKNVKELFDGLSQTTGEWQLHIIGDG 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490567231 285 ENMDeqettilnQLKERVKSLGLEDKVAFSGYVED--EDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTV 356
Cdd:PRK09922 220 SDFE--------KCKAYSRELGIEQRIIWHGWQSQpwEVVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCI 285
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
332-425 |
3.04e-06 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 49.59 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 332 FVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHALFADPFDKEDLGITMMKPF---KHERLY-GRLSRMGAH 407
Cdd:PLN00142 670 FVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKIADFFekcKEDPSYwNKISDAGLQ 749
|
90
....*....|....*...
gi 490567231 408 KARSLFTWTGIAQQLLAL 425
Cdd:PLN00142 750 RIYECYTWKIYAERLLTL 767
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
207-363 |
7.97e-06 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 48.18 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 207 GLKRK---HIHMIPPGYDDNRFFPVSD----------------ATRQMIRQRFGFEGKV-VLALG---RLATNKGYDLLI 263
Cdd:PRK14099 235 GLLRQradRLSGILNGIDTAVWNPATDeliaatydvetlaaraANKAALQARFGLDPDPdALLLGvisRLSWQKGLDLLL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 264 DGFSVLAArepeARLHLAVGGENMDEQETTILNQLKERVKSLGledkvAFSGYveDEDLPDIYRA-ADLFVLSSRYEPFG 342
Cdd:PRK14099 315 EALPTLLG----EGAQLALLGSGDAELEARFRAAAQAYPGQIG-----VVIGY--DEALAHLIQAgADALLVPSRFEPCG 383
|
170 180
....*....|....*....|.
gi 490567231 343 MTAIEAMASGTPTVVTIHGGL 363
Cdd:PRK14099 384 LTQLCALRYGAVPVVARVGGL 404
|
|
| Sucrose_synth |
pfam00862 |
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ... |
15-50 |
7.98e-06 |
|
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.
Pssm-ID: 395692 Cd Length: 540 Bit Score: 48.03 E-value: 7.98e-06
10 20 30
....*....|....*....|....*....|....*.
gi 490567231 15 RIALISTHGYVAAHPPLGAADTGGQVVYVLELARKL 50
Cdd:pfam00862 265 NVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRAL 300
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
238-362 |
1.08e-05 |
|
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: 47.58 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 238 QRFGFEGKVVLALGRLATNKGYDLLIDGFSVLAAREPE-ARLHLAVGG-------ENMDE-QEttiLNQLKErvKSLGLE 308
Cdd:cd03805 205 LIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPEfENVRLVIAGgydprvaENVEYlEE---LQRLAE--ELLNVE 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490567231 309 DKVAFSGYVEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGG 362
Cdd:cd03805 280 DQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGG 333
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
244-352 |
6.24e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 45.11 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 244 GKVVLALGRLATNKGYDLLIDGFSV----LAAREPEARLHLAVGGENMDEQETtiLNQLKERVKSLGLEDKVAFSGYVED 319
Cdd:PLN02949 268 PPYIISVAQFRPEKAHALQLEAFALalekLDADVPRPKLQFVGSCRNKEDEER--LQKLKDRAKELGLDGDVEFHKNVSY 345
|
90 100 110
....*....|....*....|....*....|...
gi 490567231 320 EDLPDIYRAADLFVLSSRYEPFGMTAIEAMASG 352
Cdd:PLN02949 346 RDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAG 378
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
237-425 |
8.79e-05 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 44.72 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 237 RQRFGFE--GKVVLAL-GRLATNKGYDLLIDGFSVLAAREPearlHLAV--GGENMDEQEttiLNQLKERvkslgLEDKV 311
Cdd:PRK00654 272 QERFGLPddDAPLFAMvSRLTEQKGLDLVLEALPELLEQGG----QLVLlgTGDPELEEA---FRALAAR-----YPGKV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 312 AFS-GYveDEDLPD-IYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGRHA-------LFaDPFDKE 382
Cdd:PRK00654 340 GVQiGY--DEALAHrIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYNPEdgeatgfVF-DDFNAE 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490567231 383 DLGITMMKP---FKHERLYGRLSR--MGAHkarslFTWTGIAQQLLAL 425
Cdd:PRK00654 417 DLLRALRRAlelYRQPPLWRALQRqaMAQD-----FSWDKSAEEYLEL 459
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
302-358 |
1.51e-04 |
|
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: 44.15 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490567231 302 VKSLGLEDKVAFSGYVE-DEDLPDIyraaDLFVLSSRYEPFGMTAIEAMASGTPTVVT 358
Cdd:NF038011 360 VASLGLQDKVKFLGFQKiDDLLPQV----GLMVLSSISEALPLVVLEAFAAGVPVVTT 413
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
298-377 |
9.92e-04 |
|
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: 41.29 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 298 LKERVKSLG---LED-KVAFSGYVEDEDLPDIYR--AADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVSYGR 371
Cdd:cd04946 268 LKERLEKLAenkLENvKVNFTGEVSNKEVKQLYKenDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENET 347
|
....*.
gi 490567231 372 HALFAD 377
Cdd:cd04946 348 NGLLLD 353
|
|
| PHA01630 |
PHA01630 |
putative group 1 glycosyl transferase |
317-361 |
1.73e-03 |
|
putative group 1 glycosyl transferase
Pssm-ID: 164861 Cd Length: 331 Bit Score: 40.16 E-value: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490567231 317 VEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHG 361
Cdd:PHA01630 198 LPDDDIYSLFAGCDILFYPVRGGAFEIPVIEALALGLDVVVTEKG 242
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
220-367 |
2.71e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 220 YDDNrFFPVS----------DATRQMIRQRFGFEG---KVVLALGRLATNKGYDLLI---------DGFSVLAAREPEAR 277
Cdd:PLN02316 804 YNDN-FIPVPytsenvvegkRAAKEALQQRLGLKQadlPLVGIITRLTHQKGIHLIKhaiwrtlerNGQVVLLGSAPDPR 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 278 LHlavggenmdEQETTILNQLK----ERVKsLGLedkvafsgyVEDEDLPD-IYRAADLFVLSSRYEPFGMTAIEAMASG 352
Cdd:PLN02316 883 IQ---------NDFVNLANQLHsshhDRAR-LCL---------TYDEPLSHlIYAGADFILVPSIFEPCGLTQLTAMRYG 943
|
170
....*....|....*
gi 490567231 353 TPTVVTIHGGLFRAV 367
Cdd:PLN02316 944 SIPVVRKTGGLFDTV 958
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
257-357 |
2.75e-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: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 257 KGYDLLIDGFSVLAAREPE-----ARLHLAVGGENMDEQETtiLNQLKERVKSLGLEDKVAFSGYVEDEDLPDIYRAADL 331
Cdd:cd03806 250 KNHPLQLRAFAELLKRLPEsirsnPKLVLIGSCRNEEDKER--VEALKLLAKELILEDSVEFVVDAPYEELKELLSTASI 327
|
90 100
....*....|....*....|....*.
gi 490567231 332 FVLSSRYEPFGMTAIEAMASGTPTVV 357
Cdd:cd03806 328 GLHTMWNEHFGIGVVEYMAAGLIPLA 353
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
221-367 |
3.54e-03 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 39.57 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 221 DDNRFFPVSDATRQMIRQRFGF--EGKVVLALGRLATNKGYDLLIDGFSVLAARepeARLHLAVGGENmdeqetTILNQL 298
Cdd:PRK10307 204 EVARFQPVADADVDALRAQLGLpdGKKIVLYSGNIGEKQGLELVIDAARRLRDR---PDLIFVICGQG------GGKARL 274
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490567231 299 KERVKSLGLeDKVAFSGYVEDEDLPDIYRAADLFVLSSRYE------PFGMTAIeaMASGTPTVVTIHGG--LFRAV 367
Cdd:PRK10307 275 EKMAQCRGL-PNVHFLPLQPYDRLPALLKMADCHLLPQKAGaadlvlPSKLTNM--LASGRNVVATAEPGteLGQLV 348
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
274-370 |
4.87e-03 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 39.21 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 274 PEARLHLavggenMDEQETTILNQLKERVKSLGLE-DKVAFSGYVEDEDLPDIYRAADLFvLSSryEPF--GMTAIEAMA 350
Cdd:COG3914 498 PNSVLLL------KGGGLPEARERLRAAAAARGVDpDRLIFLPRLPRAEHLARYALADLF-LDT--FPYngGTTTLEALW 568
|
90 100
....*....|....*....|.
gi 490567231 351 SGTPtVVTIHGGLFRA-VSYG 370
Cdd:COG3914 569 MGVP-VVTLAGETFASrVGAS 588
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
319-421 |
5.55e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.11 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 319 DEDLPD-IYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAVsygrhalfadpFDKEDL--------GITMM 389
Cdd:PLN02939 846 DEALSHsIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSV-----------FDFDDEtipvelrnGFTFL 914
|
90 100 110
....*....|....*....|....*....|..
gi 490567231 390 KPFKHErLYGRLSRMGAHKARSLFTWTGIAQQ 421
Cdd:PLN02939 915 TPDEQG-LNSALERAFNYYKRKPEVWKQLVQK 945
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
189-363 |
5.89e-03 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 38.95 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 189 DMVIATTPVQLDVLIED----YGLKR------KHIHMIPPGYDDNRFFPVSDatrQMIRQRFGFE---GK---------- 245
Cdd:PRK14098 222 DLLTTTSPRYAEEIAGDgeeaFGLDKvleerkMRLHGILNGIDTRQWNPSTD---KLIKKRYSIErldGKlenkkallee 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490567231 246 ----------VVLALGRLATNKGYDLLIDGFSVLAAREpearLHLAVGGENMDEQEttilNQLKERVKSLglEDKVAFSG 315
Cdd:PRK14098 299 vglpfdeetpLVGVIINFDDFQGAELLAESLEKLVELD----IQLVICGSGDKEYE----KRFQDFAEEH--PEQVSVQT 368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490567231 316 YVEDEDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGL 363
Cdd:PRK14098 369 EFTDAFFHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGI 416
|
|
| |
