|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
53-483 |
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: 699.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 53 AHLNVCVLVLGDIGRSPRMQYHALSLSKHGYNVTIIGFLGTKPHQDILEDDRIDILPISELKGLTVGPRIFRYISKVTLQ 132
Cdd:cd03816 2 KKKRVCVLVLGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 133 SFQLLYVLMTIEDQGYILMQNPPGLPAIAVTWMASRIRGNQFIIDWHNYGYTIMALSHGENHLIVRLAKWYEKIFGCLSD 212
Cdd:cd03816 82 ALSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 213 HNLCVTSAMREDLCK--NWNIEATTLYDKPPSIFRETPLKLQHELFVRMgsaylpfrpssavtkeymeltaFTERNTQTG 290
Cdd:cd03816 162 AHLCVTKAMQRDLQQfeNWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 291 AVTRSAGRPALLISSTSWTEDEDFSVLLQALEEYEKFVETEN-RLPSLVCVITGKGPQKEYYKKLIDSREFHHVKICTPW 369
Cdd:cd03816 220 AVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 370 LEAEDYPVLLGSADLGVCLHKSSSGLDLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFKDSSELAEQLKLLFLDF 449
Cdd:cd03816 300 LSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDF 379
|
410 420 430
....*....|....*....|....*....|....
gi 41054089 450 pgDQGKLGIFRKNLQESRQQRWDENWDQNVLPLI 483
Cdd:cd03816 380 --DRGKLNVLKKGAQEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
57-446 |
4.19e-160 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 458.37 E-value: 4.19e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 57 VCVLVLGDIGRSPRMQYHALSLSKH-GYNVTIIGFLGTKPHQDILEDDRIDILPISE---LKGLTVGPRIFRYISKVTLQ 132
Cdd:PLN02275 7 AAVVVLGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIHLMVQprlLQRLPRVLYALALLLKVAIQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 133 SFQLLYVL-MTIEDQGYILMQNPPGLPAIAVTWMASRIRGNQFIIDWHNYGYTIMALSHGENHLIVRLAKWYEKIFGCLS 211
Cdd:PLN02275 87 FLMLLWFLcVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 212 DHNLCVTSAMREDLCKNWNIEATTLYDKPPSIFRETPLklqhELFVRmgsaylpfrpssavtkeymeltafterntqtga 291
Cdd:PLN02275 167 DGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASL----EIRLR--------------------------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 292 vtrsAGRPALLISSTSWTEDEDFSVLLQALEEYEKFVETE-----------NRLPSLVCVITGKGPQKEYYKKLIDSREF 360
Cdd:PLN02275 210 ----PNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARlnesdsasgkqSLYPRLLFIITGKGPQKAMYEEKISRLNL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 361 HHVKICTPWLEAEDYPVLLGSADLGVCLHKSSSGLDLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFKDSSELAE 440
Cdd:PLN02275 286 RHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELAD 365
|
....*.
gi 41054089 441 QLKLLF 446
Cdd:PLN02275 366 QLLELL 371
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
314-448 |
1.48e-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: 53.82 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 314 FSVLLQALEEYEKfvetenRLPSLVCVITGKGPQKEYYKKLIDSREF-HHVKIcTPWLEAEDYPVLLGSADLGVCLHKSS 392
Cdd:pfam00534 17 LDLLIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLgDNVIF-LGFVSDEDLPELLKIADVFVLPSRYE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41054089 393 SgldLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFKDSS--ELAEQLKLLFLD 448
Cdd:pfam00534 90 G---FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNaeALAEAIDKLLED 144
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
377-479 |
3.77e-05 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 43.06 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 377 VLLGSADLGVCLHKSSSgldLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFK--DSSELAEQLKLLFLDfPGDQG 454
Cdd:COG0438 16 ALLAAADVFVLPSRSEG---FGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpgDPEALAEAILRLLED-PELRR 91
|
90 100
....*....|....*....|....*
gi 41054089 455 KLGifrKNLQESRQQRWDenWDQNV 479
Cdd:COG0438 92 RLG---EAARERAEERFS--WEAIA 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
53-483 |
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: 699.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 53 AHLNVCVLVLGDIGRSPRMQYHALSLSKHGYNVTIIGFLGTKPHQDILEDDRIDILPISELKGLTVGPRIFRYISKVTLQ 132
Cdd:cd03816 2 KKKRVCVLVLGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 133 SFQLLYVLMTIEDQGYILMQNPPGLPAIAVTWMASRIRGNQFIIDWHNYGYTIMALSHGENHLIVRLAKWYEKIFGCLSD 212
Cdd:cd03816 82 ALSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 213 HNLCVTSAMREDLCK--NWNIEATTLYDKPPSIFRETPLKLQHELFVRMgsaylpfrpssavtkeymeltaFTERNTQTG 290
Cdd:cd03816 162 AHLCVTKAMQRDLQQfeNWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 291 AVTRSAGRPALLISSTSWTEDEDFSVLLQALEEYEKFVETEN-RLPSLVCVITGKGPQKEYYKKLIDSREFHHVKICTPW 369
Cdd:cd03816 220 AVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 370 LEAEDYPVLLGSADLGVCLHKSSSGLDLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFKDSSELAEQLKLLFLDF 449
Cdd:cd03816 300 LSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDF 379
|
410 420 430
....*....|....*....|....*....|....
gi 41054089 450 pgDQGKLGIFRKNLQESRQQRWDENWDQNVLPLI 483
Cdd:cd03816 380 --DRGKLNVLKKGAQEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
57-446 |
4.19e-160 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 458.37 E-value: 4.19e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 57 VCVLVLGDIGRSPRMQYHALSLSKH-GYNVTIIGFLGTKPHQDILEDDRIDILPISE---LKGLTVGPRIFRYISKVTLQ 132
Cdd:PLN02275 7 AAVVVLGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIHLMVQprlLQRLPRVLYALALLLKVAIQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 133 SFQLLYVL-MTIEDQGYILMQNPPGLPAIAVTWMASRIRGNQFIIDWHNYGYTIMALSHGENHLIVRLAKWYEKIFGCLS 211
Cdd:PLN02275 87 FLMLLWFLcVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 212 DHNLCVTSAMREDLCKNWNIEATTLYDKPPSIFRETPLklqhELFVRmgsaylpfrpssavtkeymeltafterntqtga 291
Cdd:PLN02275 167 DGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASL----EIRLR--------------------------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 292 vtrsAGRPALLISSTSWTEDEDFSVLLQALEEYEKFVETE-----------NRLPSLVCVITGKGPQKEYYKKLIDSREF 360
Cdd:PLN02275 210 ----PNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARlnesdsasgkqSLYPRLLFIITGKGPQKAMYEEKISRLNL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 361 HHVKICTPWLEAEDYPVLLGSADLGVCLHKSSSGLDLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFKDSSELAE 440
Cdd:PLN02275 286 RHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELAD 365
|
....*.
gi 41054089 441 QLKLLF 446
Cdd:PLN02275 366 QLLELL 371
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
63-448 |
9.74e-17 |
|
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: 82.00 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 63 GDIGRSPRMQYHALSLSKHGYNVTII-----GFLGTKPHQDILEDDRIDIL--PISELKGLTVGPRIFRYISkvtLQSFQ 135
Cdd:cd03794 12 PKGAAAARVYELAKELVRRGHEVTVLtpspnYPLGRIFAGATETKDGIRVIrvKLGPIKKNGLIRRLLNYLS---FALAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 136 LLYVLMTIEDQGYILMQNPPGLPAIAVTWmASRIRGNQFIID----WHNygyTIMALSHGENHLIVRLAKWYEKIFGCLS 211
Cdd:cd03794 89 LLKLLVREERPDVIIAYSPPITLGLAALL-LKKLRGAPFILDvrdlWPE---SLIALGVLKKGSLLKLLKKLERKLYRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 212 DHNLCVTSAMREDLCKnwnieattLYDKPPSIFretplklqhelfvrmgsaYLPFrpssavtkeYMELTAFTERNTQTGA 291
Cdd:cd03794 165 DAIIVLSPGLKEYLLR--------KGVPKEKII------------------VIPN---------WADLEEFKPPPKDELR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 292 VTRSAGRPALLISSTSWTEDEDFSVLLQALEEYEkfvetenRLPSLVCVITGKGPQKEYYKKLIDSREFHHVKIcTPWLE 371
Cdd:cd03794 210 KKLGLDDKFVVVYAGNIGKAQGLETLLEAAERLK-------RRPDIRFLFVGDGDEKERLKELAKARGLDNVTF-LGRVP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 372 AEDYPVLLGSADLG-VCLHKS-SSGLDLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFK--DSSELAEQLKLLFL 447
Cdd:cd03794 282 KEEVPELLSAADVGlVPLKDNpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEpgDPEALADAILELLD 361
|
.
gi 41054089 448 D 448
Cdd:cd03794 362 D 362
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
66-484 |
1.91e-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: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 66 GRSPRMQYHALSLSKHGYNVTIIGFLGTKPHQDILEDDRIDILPISELKGLTVGPRIFRYISKVTLQSFQLLYVlmtied 145
Cdd:cd03801 15 GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHA------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 146 qgyilmQNPPGLPAIAVTWMASRIRgnqFIIDWHNYGYTIMA-LSHGENHLIVRLAKWYEKIfgclsDHNLCVTSAMRED 224
Cdd:cd03801 89 ------HGLLAALLAALLALLLGAP---LVVTLHGAEPGRLLlLLAAERRLLARAEALLRRA-----DAVIAVSEALRDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 225 LCKNWNIEATTLydkppsifretplklqheLFVRMGSAYLPFRPSSAVTKEymeltafterntqtgavtRSAGRPaLLIS 304
Cdd:cd03801 155 LRALGGIPPEKI------------------VVIPNGVDLERFSPPLRRKLG------------------IPPDRP-VLLF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 305 STSWTEDEDFSVLLQALEEYEKfvetenRLPSLVCVITGK-GPQKEYYKKLiDSREFHHVKIcTPWLEAEDYPVLLGSAD 383
Cdd:cd03801 198 VGRLSPRKGVDLLLEALAKLLR------RGPDVRLVIVGGdGPLRAELEEL-ELGLGDRVRF-LGFVPDEELPALYAAAD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 384 LGVClhkSSSGLDLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIF--KDSSELAEQLKLLFLDfPGDQGKLGifrK 461
Cdd:cd03801 270 VFVL---PSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVppDDVEALADALLRLLAD-PELRARLG---R 342
|
410 420
....*....|....*....|...
gi 41054089 462 NLQESRQQRWDenWDQNVLPLIK 484
Cdd:cd03801 343 AARERVAERFS--WERVAERLLD 363
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
314-448 |
1.48e-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: 53.82 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 314 FSVLLQALEEYEKfvetenRLPSLVCVITGKGPQKEYYKKLIDSREF-HHVKIcTPWLEAEDYPVLLGSADLGVCLHKSS 392
Cdd:pfam00534 17 LDLLIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLgDNVIF-LGFVSDEDLPELLKIADVFVLPSRYE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41054089 393 SgldLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFKDSS--ELAEQLKLLFLD 448
Cdd:pfam00534 90 G---FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNaeALAEAIDKLLED 144
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
377-479 |
3.77e-05 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 43.06 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 377 VLLGSADLGVCLHKSSSgldLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFK--DSSELAEQLKLLFLDfPGDQG 454
Cdd:COG0438 16 ALLAAADVFVLPSRSEG---FGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpgDPEALAEAILRLLED-PELRR 91
|
90 100
....*....|....*....|....*
gi 41054089 455 KLGifrKNLQESRQQRWDenWDQNV 479
Cdd:COG0438 92 RLG---EAARERAEERFS--WEAIA 111
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
314-440 |
3.01e-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: 43.04 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 314 FSVLLQALEEYEKFVETenRLpslvcVITGKGPQKEYYKKLIDSREFHHVKICTPWLEAEDYPVLLGSADLGVCLHKSSS 393
Cdd:cd03817 216 IDFLLRAFAELKKEPNI--KL-----VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTET 288
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 41054089 394 gldLPMKVVDMFGCCLPVCAIHFECLHELVKHEENGLIFKDSSELAE 440
Cdd:cd03817 289 ---QGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLA 332
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
313-469 |
3.58e-04 |
|
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: 42.73 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 313 DFSVLLQALEEYEKfvetenRLPSLVCVITGKGPQKEYYKKLIDSrefhhvkictpwLEAEDYPVLLG----------SA 382
Cdd:cd03811 202 GHDLLIEAFAKLRK------KYPDVKLVILGDGPLREELEKLAKE------------LGLAERVIFLGfqsnpypylkKA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 383 DLGVClhkSSS--GldLPMKVVDMFGCCLPVcaIHFEC--LHELVKHEENGLIFKDSSELAEQLKL-LFLDFPGDQGKLG 457
Cdd:cd03811 264 DLFVL---SSRyeG--FPNVLLEAMALGTPV--VSTDCpgPREILDDGENGLLVPDGDAAALAGILaALLQKKLDAALRE 336
|
170
....*....|..
gi 41054089 458 IFRKNLQESRQQ 469
Cdd:cd03811 337 RLAKAQEAVFRE 348
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
314-445 |
3.80e-04 |
|
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: 42.61 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 314 FSVLLQAleeyekFVETENRLPSLVCVITGKGPQKEYYKKLIDSREF-HHVKICTPWLEAEDYpvlLGSADLGVClhkSS 392
Cdd:cd03820 196 FDLLIEA------WALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLeDRVKLLGPTKNIAEE---YANSSIFVL---SS 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41054089 393 SGLDLPMKVVDMFGCCLPVcaIHFECLH---ELVKHEENGLIFK--DSSELAEQLKLL 445
Cdd:cd03820 264 RYEGFPMVLLEAMAYGLPI--ISFDCPTgpsEIIEDGENGLLVPngDVDALAEALLRL 319
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
78-233 |
1.00e-03 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 39.82 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054089 78 LSKHGYNVTIIGFLGTKPHQDilEDDRIDILPISELKGLTVGPRIFRYISKVTLQsfqllyvlmtIEDQGY---ILMQNP 154
Cdd:pfam13439 14 LARRGHEVTVVTPGGPGPLAE--EVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRL----------LRRERPdvvHAHSPF 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054089 155 PGLPAIAVTWMASRIRgnqFIIDWHNyGYTIMALSHGENHLIVRLAKWYEKIFGCLSDHNLCVTSAMREDLCKNWNIEA 233
Cdd:pfam13439 82 PLGLAALAARLRLGIP---LVVTYHG-LFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPP 156
|
|
| |
