|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
30-461 |
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: 682.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 30 RAARHVVAVVLGDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVL 109
Cdd:cd03816 1 PKKKRVCVLVLGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 110 QAMYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLS 189
Cdd:cd03816 81 QALSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 190 HLNLCVTNAMREDLA--DNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGS 267
Cdd:cd03816 161 DAHLCVTKAMQRDLQqfENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 268 GLVTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTP 346
Cdd:cd03816 219 GAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 347 WLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSN 426
Cdd:cd03816 299 WLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSD 378
|
410 420 430
....*....|....*....|....*....|....*
gi 41350216 427 FpdPAGKLNQFRKNLRESQQLRWDESWVQTVLPLV 461
Cdd:cd03816 379 F--DRGKLNVLKKGAQEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
27-424 |
2.02e-154 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 442.96 E-value: 2.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 27 RRGRAArhvvAVVLGDVGRSPRMQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQ 102
Cdd:PLN02275 3 RRGRAA----VVVLGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 103 YGVKVVLQAMYLLWKLMWREPGAYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWY 181
Cdd:PLN02275 79 LLLKVAIQFLMLLWFLCVKIPRPDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 182 EKFFGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLdlqhrlfmklgsmhspfrarsepedpvtersaft 261
Cdd:PLN02275 159 ERHYGKMADGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASL---------------------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 262 erdagsglVTRLRE-RPALLVSSTSWTEDEDFSILLAALEKFEQL---TLDGHN--------LPSLVCVITGKGPLREYY 329
Cdd:PLN02275 205 --------EIRLRPnRPALVVSSTSWTPDEDFGILLEAAVMYDRRvaaRLNESDsasgkqslYPRLLFIITGKGPQKAMY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 330 SRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 409
Cdd:PLN02275 277 EEKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLL 356
|
410
....*....|....*
gi 41350216 410 FEDSEELAAQLQMLF 424
Cdd:PLN02275 357 FSSSSELADQLLELL 371
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
295-443 |
2.42e-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: 53.05 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 295 LLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgld 374
Cdd:pfam00534 20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41350216 375 LPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRE 443
Cdd:pfam00534 91 FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED----EELRERLGENARK 157
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
330-450 |
4.08e-08 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 51.53 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 330 SRLIHQKHFQHIqvctpwLEAedyplLLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 409
Cdd:COG0438 2 GRLVPRKGLDLL------LEA-----LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 41350216 410 FE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRESQQLRWD 450
Cdd:COG0438 68 VPpgDPEALAEAILRLLED----PELRRRLGEAARERAEERFS 106
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
30-461 |
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: 682.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 30 RAARHVVAVVLGDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVL 109
Cdd:cd03816 1 PKKKRVCVLVLGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 110 QAMYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLS 189
Cdd:cd03816 81 QALSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 190 HLNLCVTNAMREDLA--DNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGS 267
Cdd:cd03816 161 DAHLCVTKAMQRDLQqfENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 268 GLVTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTP 346
Cdd:cd03816 219 GAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 347 WLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSN 426
Cdd:cd03816 299 WLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSD 378
|
410 420 430
....*....|....*....|....*....|....*
gi 41350216 427 FpdPAGKLNQFRKNLRESQQLRWDESWVQTVLPLV 461
Cdd:cd03816 379 F--DRGKLNVLKKGAQEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
27-424 |
2.02e-154 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 442.96 E-value: 2.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 27 RRGRAArhvvAVVLGDVGRSPRMQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQ 102
Cdd:PLN02275 3 RRGRAA----VVVLGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 103 YGVKVVLQAMYLLWKLMWREPGAYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWY 181
Cdd:PLN02275 79 LLLKVAIQFLMLLWFLCVKIPRPDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 182 EKFFGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLdlqhrlfmklgsmhspfrarsepedpvtersaft 261
Cdd:PLN02275 159 ERHYGKMADGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASL---------------------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 262 erdagsglVTRLRE-RPALLVSSTSWTEDEDFSILLAALEKFEQL---TLDGHN--------LPSLVCVITGKGPLREYY 329
Cdd:PLN02275 205 --------EIRLRPnRPALVVSSTSWTPDEDFGILLEAAVMYDRRvaaRLNESDsasgkqslYPRLLFIITGKGPQKAMY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 330 SRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 409
Cdd:PLN02275 277 EEKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLL 356
|
410
....*....|....*
gi 41350216 410 FEDSEELAAQLQMLF 424
Cdd:PLN02275 357 FSSSSELADQLLELL 371
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
44-450 |
2.25e-09 |
|
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: 59.09 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 44 GRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIvgltelqsLAVGPRVFQYGVKVVLQamylLWKLMWREP 123
Cdd:cd03801 15 GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVP--------LLPSLAALLRARRLLRE----LRPLLRLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 124 GAYIFLQNPPGLPSIAVCWFvgcLCGSKLVIDWHNYGYSIMGLVHGPNHPLvlLAKWyeKFFGRLSHLNLCVTNAMREDL 203
Cdd:cd03801 83 FDVVHAHGLLAALLAALLAL---LLGAPLVVTLHGAEPGRLLLLLAAERRL--LARA--EALLRRADAVIAVSEALRDEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 204 ADNWHI---RAVTVYdkpasffkeTPLDLQHrlfmklgsmhSPFRARSEPEDPVTERSAFTerdagsglVTRLRERPALL 280
Cdd:cd03801 156 RALGGIppeKIVVIP---------NGVDLER----------FSPPLRRKLGIPPDRPVLLF--------VGRLSPRKGVD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 281 VsstswtededfsiLLAALEKFEQLtldghnLPSLVCVITGKGPlrEYYSRLIHQKHFQHIQV-CTPWLEAEDYPLLLGS 359
Cdd:cd03801 209 L-------------LLEALAKLLRR------GPDVRLVIVGGDG--PLRAELEELELGLGDRVrFLGFVPDEELPALYAA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 360 ADLGVCLHTSSSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSnfpDPAgKLNQF 437
Cdd:cd03801 268 ADVFVLPSRYEG---FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpdDVEALADALLRLLA---DPE-LRARL 340
|
410
....*....|...
gi 41350216 438 RKNLRESQQLRWD 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 |
1.55e-08 |
|
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: 56.58 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 41 GDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNN-------RIQIVGLTELQSLAVGPRVFQYgvkVVLQAMY 113
Cdd:cd03794 12 PKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGAtetkdgiRVIRVKLGPIKKNGLIRRLLNY---LSFALAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 114 LLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGcLCGSKLVID----WHNygySIMGLVHGPNHPLVLLAKWYEKFFGRLS 189
Cdd:cd03794 89 LLKLLVREERPDVIIAYSPPITLGLAALLLKK-LRGAPFILDvrdlWPE---SLIALGVLKKGSLLKLLKKLERKLYRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 190 HLNLCVTNAMREdladnwHIRAVTVYDKPASFFKEtpldlqhrlfmklGSMHSPFRarsePEDPVTERSAFTERDagsgl 269
Cdd:cd03794 165 DAIIVLSPGLKE------YLLRKGVPKEKIIVIPN-------------WADLEEFK----PPPKDELRKKLGLDD----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 270 vtrlrerPALLVSSTSWTEDEDFSILLAALEKFEQLtldghnlPSLVCVITGKGPLREYYSRLIHQKHfqhIQVCT--PW 347
Cdd:cd03794 217 -------KFVVVYAGNIGKAQGLETLLEAAERLKRR-------PDIRFLFVGDGDEKERLKELAKARG---LDNVTflGR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 348 LEAEDYPLLLGSADLG-VCLHTS-SSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQML 423
Cdd:cd03794 280 VPKEEVPELLSAADVGlVPLKDNpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEpgDPEALADAILEL 359
|
...
gi 41350216 424 FSN 426
Cdd:cd03794 360 LDD 362
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
295-443 |
2.42e-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: 53.05 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 295 LLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgld 374
Cdd:pfam00534 20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41350216 375 LPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRE 443
Cdd:pfam00534 91 FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED----EELRERLGENARK 157
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
330-450 |
4.08e-08 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 51.53 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 330 SRLIHQKHFQHIqvctpwLEAedyplLLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 409
Cdd:COG0438 2 GRLVPRKGLDLL------LEA-----LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 41350216 410 FE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRESQQLRWD 450
Cdd:COG0438 68 VPpgDPEALAEAILRLLED----PELRRRLGEAARERAEERFS 106
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
252-410 |
1.33e-07 |
|
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: 52.41 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 252 DPVTERSAFTERDAGSGLVTRLRERPALLVSStsWTEDEDFSILLAALEKFeqltldGHNLPSLVCVITGKGPLREYYSR 331
Cdd:cd01635 87 GPDSLESTRSELLALARLLVSLPLADKVSVGR--LVPEKGIDLLLEALALL------KARLPDLVLVLVGGGGEREEEEA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 332 LI-HQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVF 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 |
4.00e-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: 51.98 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 60 GFSVTLLGFCNSKPHDELLqNNRIQIVGLTELQSLAVGPRVFqygvKVVLQAMYLLWKLM------WREPGAYIF-LQNP 132
Cdd:cd03811 29 GYDVTLVLLRDEGDLDKQL-NGDVKLIRLLIRVLKLIKLGLL----KAILKLKRILKRAKpdvvisFLGFATYIVaKLAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 133 PGLPSIAVCwfvgclcgsklvidwHNYgYSImglvhgpNHPLVLLAKWYEKFFGRLSHLnLCVTNAMREDLADNWHI--- 209
Cdd:cd03811 104 ARSKVIAWI---------------HSS-LSK-------LYYLKKKLLLKLKLYKKADKI-VCVSKGIKEDLIRLGPSppe 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 210 RAVTVYDkpasffketPLDLQHrlfmklgsmhspFRARSEPEDPVTERSAFTerdagsgLVT--RLrerpallvsstswT 287
Cdd:cd03811 160 KIEVIYN---------PIDIDR------------IRALAKEPILNEPEDGPV-------ILAvgRL-------------D 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 288 EDEDFSILLAAlekFEQLTLDGHNLPslvCVITGKGPLREYYSRLIHQkhfqhiqvctpwLEAEDYPLLLG--------- 358
Cdd:cd03811 199 PQKGHDLLIEA---FAKLRKKYPDVK---LVILGDGPLREELEKLAKE------------LGLAERVIFLGfqsnpypyl 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 359 -SADLGVclHTSSS-GLdlPMKVVDMFGCCLPVCAVNFKCLHELVKHEENG-LVFEDSEELAAQLQMLFSNFPDPAGKLN 435
Cdd:cd03811 261 kKADLFV--LSSRYeGF--PNVLLEAMALGTPVVSTDCPGPREILDDGENGlLVPDGDAAALAGILAALLQKKLDAALRE 336
|
410
....*....|.
gi 41350216 436 QFRKNLRESQQ 446
Cdd:cd03811 337 RLAKAQEAVFR 347
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
292-418 |
4.27e-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: 42.27 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 292 FSILLAALEKFeqltldgHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVclHTSSS 371
Cdd:cd03817 216 IDFLLRAFAEL-------KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFV--FASTT 286
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 41350216 372 GLdLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAA 418
Cdd:cd03817 287 ET-QGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLA 332
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
109-426 |
8.95e-04 |
|
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: 41.43 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 109 LQAMYLLWKLMWREPGAYIFLQNP-PG-LPSIAvcwfvGCLCGSKLVIdwhnygYSI--MGLVHGPNHPLVLLAKWYEKF 184
Cdd:cd03808 67 LKALFKLYKLLKKEKPDIVHCHTPkPGiLGRLA-----ARLAGVPKVI------YTVhgLGFVFTEGKLLRLLYLLLEKL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 185 FGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASffketPLDLQHRlfmklgsmhsPFRARSEPEDPVTersaFterd 264
Cdd:cd03808 136 ALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGS-----GVDLDRF----------QYSPESLPSEKVV----F---- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 265 agsGLVTRLRErpallvsstswteDEDFSILLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVC 344
Cdd:cd03808 193 ---LFVARLLK-------------DKGIDELIEAAKILKK------KGPNVRFLLVGDGELENPSEILIEKLGLEGRIEF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41350216 345 TPWLEaeDYPLLLGSADLgVCLHTSSSGLdlPMKVV------------DMFGCClpvcavnfkclhELVKHEENGLVFE- 411
Cdd:cd03808 251 LGFRS--DVPELLAESDV-FVLPSYREGL--PRSLLeamaagrpvittDVPGCR------------ELVIDGVNGFLVPp 313
|
330
....*....|....*.
gi 41350216 412 -DSEELAAQLQMLFSN 426
Cdd:cd03808 314 gDVEALADAIEKLIED 329
|
|
| |
