|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
40-461 |
0e+00 |
|
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: 664.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 40 LGDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVFQAMYLLWKLM 119
Cdd:cd03816 11 LGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 120 WREPGDYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPSHPLVLLAKWYERFFGRLSHLNLCVTNAM 199
Cdd:cd03816 91 ELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 200 REDLA--ENWRISAVTVYDKPASFFKETPLDLQHWLFMKLggtyspfrarsepedpatersaFTERDAGSGLVTRLRERP 277
Cdd:cd03816 171 QRDLQqfENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 278 ALLISSTSWTEDEDFSILLAALEKFEQLILDGHK-LPSLVCVITGKGPLREYYSRLIQQKCFQRVQVCTPWLEAEDYPLL 356
Cdd:cd03816 229 ALLVSSTSWTPDEDFSILLDALKAYESSAATEPAlLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWLSAEDYPRL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 357 LGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFpdPAGKLNQ 436
Cdd:cd03816 309 LASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDF--DRGKLNV 386
|
410 420
....*....|....*....|....*
gi 967501484 437 FRKNLRESEQLRWDESWVQTVLPLV 461
Cdd:cd03816 387 LKKGAQEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
40-424 |
3.54e-151 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 434.87 E-value: 3.54e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 40 LGDVGRSPRMQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQYGVKVVFQAMYLL 115
Cdd:PLN02275 12 LGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALALLLKVAIQFLMLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 116 WKLMWREPG-DYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPSHPLVLLAKWYERFFGRLSHLNLC 194
Cdd:PLN02275 92 WFLCVKIPRpDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGHLC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 195 VTNAMREDLAENWRISAVTVYDKPASFFKETPLdlqhwlfmklggtyspfrarsepedpatersafterdagsglVTRLR 274
Cdd:PLN02275 172 VTKAMQHELDQNWGIRATVLYDQPPEFFRPASL------------------------------------------EIRLR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 275 E-RPALLISSTSWTEDEDFSILLAALEKFEQLI-----------LDGHKLPSLVCVITGKGPLREYYSRLIQQKCFQRVQ 342
Cdd:PLN02275 210 PnRPALVVSSTSWTPDEDFGILLEAAVMYDRRVaarlnesdsasGKQSLYPRLLFIITGKGPQKAMYEEKISRLNLRHVA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 343 VCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQM 422
Cdd:PLN02275 290 FRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELADQLLE 369
|
..
gi 967501484 423 LF 424
Cdd:PLN02275 370 LL 371
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
295-443 |
3.98e-08 |
|
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: 52.66 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 295 LLAALEKFEQlildghKLPSLVCVITGKGPLREYYSRLIQqKCFQRVQVC-TPWLEAEDYPLLLGSADLGVCLHTSSSgl 373
Cdd:pfam00534 20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAE-KLGLGDNVIfLGFVSDEDLPELLKIADVFVLPSRYEG-- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967501484 374 dLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRE 443
Cdd:pfam00534 91 -FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED----EELRERLGENARK 157
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
356-451 |
1.85e-07 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 49.60 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 356 LLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGK 433
Cdd:COG0438 17 LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpgDPEALAEAILRLLED----PEL 89
|
90 100
....*....|....*....|
gi 967501484 434 LNQFRKNLRE--SEQLRWDE 451
Cdd:COG0438 90 RRRLGEAAREraEERFSWEA 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
40-461 |
0e+00 |
|
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: 664.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 40 LGDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVFQAMYLLWKLM 119
Cdd:cd03816 11 LGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 120 WREPGDYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPSHPLVLLAKWYERFFGRLSHLNLCVTNAM 199
Cdd:cd03816 91 ELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 200 REDLA--ENWRISAVTVYDKPASFFKETPLDLQHWLFMKLggtyspfrarsepedpatersaFTERDAGSGLVTRLRERP 277
Cdd:cd03816 171 QRDLQqfENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 278 ALLISSTSWTEDEDFSILLAALEKFEQLILDGHK-LPSLVCVITGKGPLREYYSRLIQQKCFQRVQVCTPWLEAEDYPLL 356
Cdd:cd03816 229 ALLVSSTSWTPDEDFSILLDALKAYESSAATEPAlLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWLSAEDYPRL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 357 LGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFpdPAGKLNQ 436
Cdd:cd03816 309 LASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDF--DRGKLNV 386
|
410 420
....*....|....*....|....*
gi 967501484 437 FRKNLRESEQLRWDESWVQTVLPLV 461
Cdd:cd03816 387 LKKGAQEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
40-424 |
3.54e-151 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 434.87 E-value: 3.54e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 40 LGDVGRSPRMQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQYGVKVVFQAMYLL 115
Cdd:PLN02275 12 LGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALALLLKVAIQFLMLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 116 WKLMWREPG-DYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPSHPLVLLAKWYERFFGRLSHLNLC 194
Cdd:PLN02275 92 WFLCVKIPRpDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGHLC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 195 VTNAMREDLAENWRISAVTVYDKPASFFKETPLdlqhwlfmklggtyspfrarsepedpatersafterdagsglVTRLR 274
Cdd:PLN02275 172 VTKAMQHELDQNWGIRATVLYDQPPEFFRPASL------------------------------------------EIRLR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 275 E-RPALLISSTSWTEDEDFSILLAALEKFEQLI-----------LDGHKLPSLVCVITGKGPLREYYSRLIQQKCFQRVQ 342
Cdd:PLN02275 210 PnRPALVVSSTSWTPDEDFGILLEAAVMYDRRVaarlnesdsasGKQSLYPRLLFIITGKGPQKAMYEEKISRLNLRHVA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 343 VCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQM 422
Cdd:PLN02275 290 FRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELADQLLE 369
|
..
gi 967501484 423 LF 424
Cdd:PLN02275 370 LL 371
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
44-450 |
2.22e-13 |
|
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: 71.41 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 44 GRSPRMQYHALSLAMHGFSVTLlgFCNSKPHDELLQNNRIQIVgltelqSLAVGPRVFQYGVKVVFQamylLWKLMWREP 123
Cdd:cd03801 15 GAERHVRELARALAARGHDVTV--LTPADPGEPPEELEDGVIV------PLLPSLAALLRARRLLRE----LRPLLRLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 124 GDYIFLQNPPGLPSIAVCWFvgcLCGSKLVIDWHNYGYSIMGLVHGPSHPLvlLAKWyeRFFGRLSHLNLCVTNAMREDL 203
Cdd:cd03801 83 FDVVHAHGLLAALLAALLAL---LLGAPLVVTLHGAEPGRLLLLLAAERRL--LARA--EALLRRADAVIAVSEALRDEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 204 AENWRISA---VTVYdkpasffkeTPLDLQHWlfmklggtysPFRARSEPEDPATERSAFTerdagsglVTRLRERPALL 280
Cdd:cd03801 156 RALGGIPPekiVVIP---------NGVDLERF----------SPPLRRKLGIPPDRPVLLF--------VGRLSPRKGVD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 281 IsstswtededfsiLLAALEKFEqlildgHKLPSLVCVITGKGPlrEYYSRLIQQKCFQRVQV-CTPWLEAEDYPLLLGS 359
Cdd:cd03801 209 L-------------LLEALAKLL------RRGPDVRLVIVGGDG--PLRAELEELELGLGDRVrFLGFVPDEELPALYAA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 360 ADLGVCLHTSSSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSnfpDPAgKLNQF 437
Cdd:cd03801 268 ADVFVLPSRYEG---FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpdDVEALADALLRLLA---DPE-LRARL 340
|
410
....*....|...
gi 967501484 438 RKNLRESEQLRWD 450
Cdd:cd03801 341 GRAARERVAERFS 353
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
41-426 |
2.02e-10 |
|
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: 62.36 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 41 GDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNN-------RIQIVGLTELQSLAVGPRVFQYgvkVVFQAMY 113
Cdd:cd03794 12 PKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGAtetkdgiRVIRVKLGPIKKNGLIRRLLNY---LSFALAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 114 LLWKLMWREPGDYIFLQNPPGLPSIAVCWFVGcLCGSKLVID----WHNygySIMGLVHGPSHPLVLLAKWYERFFGRLS 189
Cdd:cd03794 89 LLKLLVREERPDVIIAYSPPITLGLAALLLKK-LRGAPFILDvrdlWPE---SLIALGVLKKGSLLKLLKKLERKLYRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 190 HLNLCVTNAMREDLAE------------NWrISAVTVYDKPASFFKETPLDLQHWLFMKLGGTYSPfrarsepedpater 257
Cdd:cd03794 165 DAIIVLSPGLKEYLLRkgvpkekiivipNW-ADLEEFKPPPKDELRKKLGLDDKFVVVYAGNIGKA-------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 258 safterdagsglvtrlrerpallisstswtedEDFSILLAALEKFEQLilDGHKLpslvcVITGKGPLREYYSRLIQQKC 337
Cdd:cd03794 230 --------------------------------QGLETLLEAAERLKRR--PDIRF-----LFVGDGDEKERLKELAKARG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 338 FQRVQVcTPWLEAEDYPLLLGSADLG-VCLHTS-SSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DS 413
Cdd:cd03794 271 LDNVTF-LGRVPKEEVPELLSAADVGlVPLKDNpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEpgDP 349
|
410
....*....|...
gi 967501484 414 EELAAQLQMLFSN 426
Cdd:cd03794 350 EALADAILELLDD 362
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
295-443 |
3.98e-08 |
|
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: 52.66 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 295 LLAALEKFEQlildghKLPSLVCVITGKGPLREYYSRLIQqKCFQRVQVC-TPWLEAEDYPLLLGSADLGVCLHTSSSgl 373
Cdd:pfam00534 20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAE-KLGLGDNVIfLGFVSDEDLPELLKIADVFVLPSRYEG-- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967501484 374 dLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRE 443
Cdd:pfam00534 91 -FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED----EELRERLGENARK 157
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
252-410 |
9.71e-08 |
|
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: 52.79 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 252 DPATERSAFTERDAGSGLVTRLRERPALLISStsWTEDEDFSILLAALEKFeqlildGHKLPSLVCVITGKGPLREYYSR 331
Cdd:cd01635 87 GPDSLESTRSELLALARLLVSLPLADKVSVGR--LVPEKGIDLLLEALALL------KARLPDLVLVLVGGGGEREEEEA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 332 LI-QQKCFQRVQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVF 410
Cdd:cd01635 159 LAaALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEG---FGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
60-446 |
1.10e-07 |
|
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: 53.52 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 60 GFSVTLLGFCNSKPHDELLqNNRIQIVGLTELQSLAVGPRVFQYGVKvvfqamylLWKLMWREPGDYI--FLQNPPGLPS 137
Cdd:cd03811 29 GYDVTLVLLRDEGDLDKQL-NGDVKLIRLLIRVLKLIKLGLLKAILK--------LKRILKRAKPDVVisFLGFATYIVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 138 IAVCWfvgclcGSKLVIDWHNYgysimglvhgPSHPLVLLAKWYERF-FGRLSHLNLCVTNAMREDLAENWRISA---VT 213
Cdd:cd03811 100 KLAAA------RSKVIAWIHSS----------LSKLYYLKKKLLLKLkLYKKADKIVCVSKGIKEDLIRLGPSPPekiEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 214 VYDkpasffketPLDLQhwlfmklggtyspfrarsEPEDPATERSAFTERDA---GSglVTRLrerpallisstswTEDE 290
Cdd:cd03811 164 IYN---------PIDID------------------RIRALAKEPILNEPEDGpviLA--VGRL-------------DPQK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 291 DFSILLAALEKFEQlildghKLPSLVCVITGKGPLREYYSRLIQQkcfqrvqvctpwLEAEDYPLLLG----------SA 360
Cdd:cd03811 202 GHDLLIEAFAKLRK------KYPDVKLVILGDGPLREELEKLAKE------------LGLAERVIFLGfqsnpypylkKA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 361 DLGVclHTSSS-GLdlPMKVVDMFGCCLPVCAVNFKCLHELVKHEENG-LVFEDSEELAAQLQMLFSNFPDPAGKLNQFR 438
Cdd:cd03811 264 DLFV--LSSRYeGF--PNVLLEAMALGTPVVSTDCPGPREILDDGENGlLVPDGDAAALAGILAALLQKKLDAALRERLA 339
|
....*...
gi 967501484 439 KNLRESEQ 446
Cdd:cd03811 340 KAQEAVFR 347
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
356-451 |
1.85e-07 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 49.60 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 356 LLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGK 433
Cdd:COG0438 17 LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpgDPEALAEAILRLLED----PEL 89
|
90 100
....*....|....*....|
gi 967501484 434 LNQFRKNLRE--SEQLRWDE 451
Cdd:COG0438 90 RRRLGEAAREraEERFSWEA 109
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
56-211 |
5.69e-05 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 43.68 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 56 LAMHGFSVTLlgFCNSKPHDELLQNNRIQIVGLTelqslavgPRVFQYGVKVVFQAMYLLWKLMWREPGDYIFLQNPPgl 135
Cdd:pfam13439 14 LARRGHEVTV--VTPGGPGPLAEEVVRVVRVPRV--------PLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPF-- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967501484 136 PSIAVCWFVGCLCGSKLVIDWHNyGYSIMGLVHGPSHPLVLLAKWYERFFGRLSHLNLCVTNAMREDLAENWRISA 211
Cdd:pfam13439 82 PLGLAALAARLRLGIPLVVTYHG-LFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPP 156
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
292-418 |
3.31e-04 |
|
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: 42.65 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 292 FSILLAALEKFeqlildgHKLPSLVCVITGKGPLREYYSRLIQQKCFQRVQVCTPWLEAEDYPLLLGSADLGVclHTSSS 371
Cdd:cd03817 216 IDFLLRAFAEL-------KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFV--FASTT 286
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 967501484 372 GLdLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAA 418
Cdd:cd03817 287 ET-QGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLA 332
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
292-426 |
1.71e-03 |
|
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: 40.30 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 292 FSILLAALEKFEQlILDGHKLpslvcVITGKGPLREYYSRLIQQKCF-QRVQVCTPWLEAEDYpllLGSADLGVClhtSS 370
Cdd:cd03820 196 FDLLIEAWALIAK-KHPDWKL-----RIYGDGPEREELEKLIDKLGLeDRVKLLGPTKNIAEE---YANSSIFVL---SS 263
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967501484 371 S--GLdlPMKVVDMFGCCLPVcaVNFKCLH---ELVKHEENGLVFE--DSEELAAQLQMLFSN 426
Cdd:cd03820 264 RyeGF--PMVLLEAMAYGLPI--ISFDCPTgpsEIIEDGENGLLVPngDVDALAEALLRLMED 322
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
53-205 |
4.46e-03 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 37.77 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501484 53 ALSLAMHGFSVTLLGFCNSKPHDELLQNnriqivgLTELQSLAVGPRVFQYGVkvvFQAMYLLWKLMWREPGDYIFLQNP 132
Cdd:pfam13579 11 ARALAALGHEVRVVTPGGPPGRPELVGD-------GVRVHRLPVPPRPSPLAD---LAALRRLRRLLRAERPDVVHAHSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967501484 133 PglpSIAVCWFVGCLCGSKLVIDWHNygysimGLVHGPSHPLVLLAKWYERFFGRLSHLNLCVTNAMREDLAE 205
Cdd:pfam13579 81 T---AGLAARLARRRRGVPLVVTVHG------LALDYGSGWKRRLARALERRLLRRADAVVVVSEAEAELLRA 144
|
|
| |
