|
Name |
Accession |
Description |
Interval |
E-value |
| thiol_BshA |
TIGR03999 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ... |
1-370 |
0e+00 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 274914 [Multi-domain] Cd Length: 374 Bit Score: 568.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 1 MKIGILCYPTYGGSGIVATELGMSLANKGYEVHFISNALPARLDITNPNIFFHRVNVQTYPLFQYQPYDIALSSMIYRVV 80
Cdd:TIGR03999 1 MKIGITCYPTYGGSGVVATELGKALAERGHEVHFITSSQPFRLEKFHPNIFFHEVEVNQYPLFQYPPYDLALASKIAEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 81 NLYKLDLLHAHYAIPYAYAAFTAKQMLKEDDNDIPLVTTLHGTDITLVGQHPSYKHAVEFSINQSDAITSVSESLKKDTL 160
Cdd:TIGR03999 81 KEEKLDLLHVHYAIPHAIAAYLARQMLGKEGIDIPIVTTLHGTDITLVGADPSFKPAVRFSIEKSDGVTAVSESLKEETY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 161 QFFNIKKEIQVITNFIDNSEF--DEPSDCQRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKSRLIIIGEGPD 238
Cdd:TIGR03999 161 ELFDIDKPIEVIPNFVDTDRYrrKNDPALKRKLGAPEDEKVLIHISNFRPVKRVEDVIEVFARVQQEVPAKLLLVGDGPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 239 MEKVNQFLEENPeLISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFL 318
Cdd:TIGR03999 241 RSPAEQLVRELG-LTDRVLFLGKQDDVAELLSISDLFLLPSEKESFGLAALEAMACGVPVIASNAGGIPEVVEHGVTGFL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1519542892 319 AEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAI-KFDLKNILPIYEEMYRT 370
Cdd:TIGR03999 320 CDVGDVETMAEYAISLLEDEELLQRFSAAARERAKeRFDSEKIVPQYEALYRR 372
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-370 |
1.85e-179 |
|
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: 503.04 E-value: 1.85e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 1 MKIGILCYPTYGGSGIVATELGMSLANKGYEVHFISNALPARLDITNPNIFFHRVNVQTYPLFQYQPYDIALSSMIYRVV 80
Cdd:cd04962 1 MKIGIVCYPSYGGSGVVATELGLELAERGHEVHFISSAIPFRLNLYSGNIFFHEVEVPNYPLFEYPPYTLALASKIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 81 NLYKLDLLHAHYAIPYAYAAFTAKQMLKEddnDIPLVTTLHGTDITLVGQHPSYKHAVEFSINQSDAITSVSESLKKDTL 160
Cdd:cd04962 81 KEHKLDVLHAHYAIPHASCAYLAREILGE---KIPIVTTLHGTDITLVGYDPSLQPAVRFSINKSDRVTAVSSSLRQETY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 161 QFFNIKKEIQVITNFIDNSEF--DEPSDCQRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKSRLIIIGEGPD 238
Cdd:cd04962 158 ELFDVDKDIEVIHNFIDEDVFkrKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPAKLLLVGDGPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 239 MEKVNQfLEENPELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFL 318
Cdd:cd04962 238 RVPAEE-LARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1519542892 319 AEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIK-FDLKNILPIYEEMYRT 370
Cdd:cd04962 317 SDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAErFDPERIVPQYEAYYRR 369
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-369 |
5.19e-68 |
|
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: 218.95 E-value: 5.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGILCY---PTYGGSGIVATELGMSLANKGYEVHFISNALPARLditnPNIFFHRVNVQTYPLFQYQPYDIALSSMIYR 78
Cdd:cd03801 1 KILLLSPelpPPVGGAERHVRELARALAARGHDVTVLTPADPGEP----PEELEDGVIVPLLPSLAALLRARRLLRELRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 79 VVNLYKLDLLHAHYAIPYAYAAFTAKQmlkeddNDIPLVTTLHGTDITLVGQHPSYKH----AVEFSINQSDAITSVSES 154
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALLALL------LGAPLVVTLHGAEPGRLLLLLAAERrllaRAEALLRRADAVIAVSEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 155 LKKDTLQFFNIKKE-IQVITNFIDNSEFdePSDCQRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS-RLII 232
Cdd:cd03801 151 LRDELRALGGIPPEkIVVIPNGVDLERF--SPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDvRLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 233 IGEGPDMEKvnQFLEENPELISKIRLLGKV--NDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVN 310
Cdd:cd03801 229 VGGDGPLRA--ELEELELGLGDRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 311 IQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIK-FDLKNILPIYEEMYR 369
Cdd:cd03801 307 EDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAErFSWERVAERLLDLYR 366
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
5-371 |
1.58e-49 |
|
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: 171.02 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 5 ILCYP--TYGGSGIVATELGMSLANKGYEVHFIS---------NALPARLDITNPNIFFHRVNVQTYPLFQYQPYDIALS 73
Cdd:cd03798 5 TNIYPnaNSPGRGIFVRRQVRALSRRGVDVEVLApapwgpaaaRLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 74 SMIYRVVNLYKLDLLHAHYAIPYAYAAFTAKQMLKeddndIPLVTTLHGTDItLVGQHPSYKHAVEFSI-NQSDAITSVS 152
Cdd:cd03798 85 AKLLKRRRRGPPDLIHAHFAYPAGFAAALLARLYG-----VPYVVTEHGSDI-NVFPPRSLLRKLLRWAlRRAARVIAVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 153 ESLKKDTLQFFNIKKEIQVITNFIDNSEFdEPSDcqRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS-RLI 231
Cdd:cd03798 159 KALAEELVALGVPRDRVDVIPNGVDPARF-QPED--RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDvVLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 232 IIGEGPDMEKVNQfLEENPELISKIRLLG-----KVNDLYRilqLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGI 306
Cdd:cd03798 236 IVGDGPLREALRA-LAEDLGLGDRVTFTGrlpheQVPAYYR---ACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGI 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 307 PEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFDLKNILPIYEEMYRTT 371
Cdd:cd03798 312 PEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-360 |
1.42e-45 |
|
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: 159.83 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGILCYP-TYGGSGIVATELGMSLANKGYEVHFISNALPARLDItNPNIFFHRVNVQTYPLFQYQPYDIALSSMIYRVV 80
Cdd:cd03811 1 KILFVIPSlSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDK-QLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 81 NLYKLDLLHAHYAIPYAYAAFTAKqmlkeddNDIPLVTTLHGTDITLVGQHPSYKHAVEFsINQSDAITSVSESLKKDTL 160
Cdd:cd03811 80 KRAKPDVVISFLGFATYIVAKLAA-------ARSKVIAWIHSSLSKLYYLKKKLLLKLKL-YKKADKIVCVSKGIKEDLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 161 QFFNIKKE-IQVITNFIDNSEFDEPSDCQRTQFaNPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS-RLIIIGEGPD 238
Cdd:cd03811 152 RLGPSPPEkIEVIYNPIDIDRIRALAKEPILNE-PEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDvKLVILGDGPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 239 MEKVNQFLEENpELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFL 318
Cdd:cd03811 231 REELEKLAKEL-GLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1519542892 319 AEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFDLKNI 360
Cdd:cd03811 310 VPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-367 |
1.53e-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: 149.74 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGIL--CY-PTYGGSGIVATELGMSLANKGYEVHFISNALPARLDITNPniffHRVNVQTYPLFQYQPYDIALS--SMI 76
Cdd:cd03817 1 KIAIFtdTYlPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEV----VRYRSFSIPIRKYHRQHIPFPfkKAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 77 YRVVNLYKLDLLHAHyaIPYAyAAFTAKQMLKEddNDIPLVTTLHgT-------DITLVGQHPSYKHAVEFS--INQSDA 147
Cdd:cd03817 77 IDRIKELGPDIIHTH--TPFS-LGKLGLRIARK--LKIPIVHTYH-TmyedylhYIPKGKLLVKAVVRKLVRrfYNHTDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 148 ITSVSESLKkDTLQFFNIKKEIQVITNFIDNSEFDEPS--DCQRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKK 225
Cdd:cd03817 151 VIAPSEKIK-DTLREYGVKGPIEVIPNGIDLDKFEKPLntEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 226 VKSRLIIIGEGPDMEKVNQFLEENpELISKIRLLGKVND--LYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNA 303
Cdd:cd03817 230 PNIKLVIVGDGPEREELKELAREL-GLADKVIFTGFVPReeLPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKD 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 304 GGIPEVNIQGETGFLAEiGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFDL-KNILPIYEEM 367
Cdd:cd03817 309 PAASELVEDGENGFLFE-PNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFaKSVEKLYEEV 372
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-366 |
1.98e-41 |
|
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: 148.92 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGILCYPTYGGSGI--VATELGMSLANKGYEVHFISnalparLDITNPNIFFH---RVNVqtYPLFQYQPYDIALSSMI 76
Cdd:cd03820 1 KIAIVIPSISNAGGAerVAINLANHLAKKGYDVTIIS------LDSAEKPPFYElddNIKI--KNLGDRKYSHFKLLLKY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 77 YRVVnlYKLdllhahyaipyayaaftaKQMLKEDDNDIpLVTTLHGT----------DITLVGQHPSYKH---------A 137
Cdd:cd03820 73 FKKV--RRL------------------RKYLKNNKPDV-VISFRTSLltflaliglkSKLIVWEHNNYEAynkglrrllL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 138 VEFSINQSDAITSVSESLKKDTLQFFNIKkeIQVITNFIDNSEFDEPSDCqrtqfanpDEKILIHVSNLRPVKRVDEVLQ 217
Cdd:cd03820 132 RRLLYKRADKIVVLTEADKLKKYKQPNSN--VVVIPNPLSFPSEEPSTNL--------KSKRILAVGRLTYQKGFDLLIE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 218 IFKNVQKKVKS-RLIIIGEGPDMEKVNQFLEENpELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYT 296
Cdd:cd03820 202 AWALIAKKHPDwKLRIYGDGPEREELEKLIDKL-GLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGL 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519542892 297 PVISSNA-GGIPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFDLKNILPIYEE 366
Cdd:cd03820 281 PIISFDCpTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQWEE 351
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
12-370 |
4.68e-40 |
|
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: 145.19 E-value: 4.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 12 GGSGIVATELGMSLANKGYEVHFISNALPA--RLDITNPNIFFHRVNVQTYPLFQYQpydialssmIYRVVNLYKLDLLH 89
Cdd:cd03819 11 GGAETYILDLARALAERGHRVLVVTAGGPLlpRLRQIGIGLPGLKVPLLRALLGNVR---------LARLIRRERIDLIH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 90 AHYAIPyAYAAFTAKQMLkeddnDIPLVTTLHGTDItLVGQHPSYKHAVEFSINQSDAitsVSESLKKDTLQFFNIKKE- 168
Cdd:cd03819 82 AHSRAP-AWLGWLASRLT-----GVPLVTTVHGSYL-ATYHPKDFALAVRARGDRVIA---VSELVRDHLIEALGVDPEr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 169 IQVITNFIDNSEFDEPSDCQRTQFANPDEKILI--HVSNLRPVKRVDEVLQIFKNVQKKVKSRLIIIGEGPDMEKVNQFL 246
Cdd:cd03819 152 IRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVvgYVGRLSPEKGWLLLVDAAAELKDEPDFRLLVAGDGPERDEIRRLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 247 EEnPELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEIGNVEA 326
Cdd:cd03819 232 ER-LGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEA 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1519542892 327 MSNYTIKLLSNVELltkmkkNAKEQAIKFDLKnilpIYEEMYRT 370
Cdd:cd03819 311 LADAIRAAKLLPEA------REKLQAAAALTE----AVRELLLR 344
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
196-351 |
1.38e-38 |
|
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: 135.48 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 196 DEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS-RLIIIGEGPDmEKVNQFLEENPELISKIRLLGKVN--DLYRILQLS 272
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNlKLVIAGDGEE-EKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519542892 273 DVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQ 351
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
20-365 |
2.58e-38 |
|
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: 140.81 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 20 ELGMSLANKGYEVHFISNALPARLD-ITNPNIFFHRVNVQTYPLFQYQpyDIALSSMIYRVVNLYKLDLLHAHYAIPYAY 98
Cdd:cd03808 18 PLIKALVKKGYEVHVIAPDGDKLSDeLKELGVKVIDIPILRRGINPLK--DLKALFKLYKLLKKEKPDIVHCHTPKPGIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 99 ---AAFTAKqmlkeddnDIPLVTTLHGTDITLVGQHPS-------YKHAVEFSinqsDAITSVSESLKKDTLQFFNIKKE 168
Cdd:cd03808 96 grlAARLAG--------VPKVIYTVHGLGFVFTEGKLLrllylllEKLALLFT----DKVIFVNEDDRDLAIKKGIIKKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 169 IQVItnfIDNSEFDEPSDCQRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNV-QKKVKSRLIIIGEGpDMEKVNQFLE 247
Cdd:cd03808 164 KTVL---IPGSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILkKKGPNVRFLLVGDG-ELENPSEILI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 248 ENPELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEIGNVEAM 327
Cdd:cd03808 240 EKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEAL 319
|
330 340 350
....*....|....*....|....*....|....*....
gi 1519542892 328 SNYTIKLLSNVELLTKMKKNAKEQAI-KFDLKNILPIYE 365
Cdd:cd03808 320 ADAIEKLIEDPELRKEMGEAARKRVEeKFDEEKVVNKLL 358
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
197-337 |
8.87e-38 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 132.64 E-value: 8.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 197 EKILIHVSNLRP-VKRVDEVLQIFKNVQKKVKS-RLIIIGEGPDMEkvnqFLEENPELISKIRLLGKVNDLYRILQLSDV 274
Cdd:pfam13692 1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDvRLVIVGDGPEEE----LEELAAGLEDRVIFTGFVEDLAELLAAADV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519542892 275 FLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVnIQGETGFLAEIGNVEAMSNYTIKLLSN 337
Cdd:pfam13692 77 FVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPEL-VDGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
3-360 |
8.60e-35 |
|
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: 131.24 E-value: 8.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 3 IGILCYPTYGGSGIVATELGMSLANKGYEVHFIS-NALPARLDITNPNIFFHRVnvqtyplfqyqPYDIALSSMIYR--- 78
Cdd:cd03795 5 VFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCfSKEKETPEKEENGIRIHRV-----------KSFLNVASTPFSpsy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 79 VVNLYKL----DLLHAHYAIPYAYAAFTAKQMLKeddndiPLVTTLHgTDItlVGQH---PSYKHAVEFSINQSDAITSV 151
Cdd:cd03795 74 IKRFKKLakeyDIIHYHFPNPLADLLLFFSGAKK------PVVVHWH-SDI--VKQKkllKLYKPLMTRFLRRADRIIAT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 152 SESLKKDTLQFFNIKKEIQVITNFIDNSEFDEPS-DCQRTQFANPDEKILIHVSNLRPVKRVDEVLqifkNVQKKVKSRL 230
Cdd:cd03795 145 SPNYVETSPTLREFKNKVRVIPLGIDKNVYNIPRvDFENIKREKKGKKIFLFIGRLVYYKGLDYLI----EAAQYLNYPI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 231 IIIGEGPDMEKVNQFLEENpeLISKIRLLGKVND--LYRILQLSDVFLLPS--EQESFGLAALEAMAAYTPVISSN-AGG 305
Cdd:cd03795 221 VIGGEGPLKPDLEAQIELN--LLDNVKFLGRVDDeeKVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNiGTG 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 306 IPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFDLKNI 360
Cdd:cd03795 299 VPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEK 353
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
76-369 |
5.04e-33 |
|
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: 126.66 E-value: 5.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 76 IYRVVNL---YKLDLLHAHYAIPYAYAAFTAKQMLKeddndIPLVTTLHGTDItlvgqhPSYKHAVEFSINQ-----SDA 147
Cdd:cd03807 68 LLRLAKLirkRNPDVVHTWMYHADLIGGLAAKLAGG-----VKVIWSVRSSNI------PQRLTRLVRKLCLllskfSPA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 148 ITSVSESLKKDTLQFFNIKKEIQVITNFIDNSEFDePSDCQRTQFANP-----DEKILIHVSNLRPVKRVDEVLQIFKNV 222
Cdd:cd03807 137 TVANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLS-PDDASRARARRRlglaeDRRVIGIVGRLHPVKDHSDLLRAAALL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 223 QKKVKS-RLIIIGEGPdmekvnqfLEENPELIS-------KIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAA 294
Cdd:cd03807 216 VETHPDlRLLLVGRGP--------ERPNLERLLlelgledRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMAC 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519542892 295 YTPVISSNAGGIPEVnIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKE-QAIKFDLKNILPIYEEMYR 369
Cdd:cd03807 288 GLPVVATDVGGAAEL-VDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARErIANEFSIDAMVRRYETLYY 362
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
2-359 |
6.49e-33 |
|
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: 126.32 E-value: 6.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGI-LCYPTYGGSGI--VATELGMSLANKGYEVHFIsnalpARLDITNPNIFFHRVNVQTYPLFQYQPYDIALSSMIYR 78
Cdd:cd03809 1 KILIdGRSLAQRLTGIgrYTRELLKALAKNDPDESVL-----AVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 79 VVNLYKLD----LLHAHYAIPYAYAaftakqmlkeddnDIPLVTTLHgtDITLVgQHPSYKHAVEF---------SINQS 145
Cdd:cd03809 76 QILLPKKDkpdlLHSPHNTAPLLLK-------------GCPQVVTIH--DLIPL-RYPEFFPKRFRlyyrlllpiSLRRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 146 DAITSVSESLKKDTLQFFNIKKE-IQVITNFIDNSEFDEPSDCQRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQK 224
Cdd:cd03809 140 DAIITVSEATRDDIIKFYGVPPEkIVVIPLGVDPSFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 225 KVKS-RLIIIGEGPDMEKVNQFLEENPELISKIRLLGKVND--LYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISS 301
Cdd:cd03809 220 QGGDlKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDedLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIAS 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1519542892 302 NAGGIPEVNiqGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFDLKN 359
Cdd:cd03809 300 NISVLPEVA--GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEK 355
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
8-365 |
1.14e-29 |
|
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: 117.40 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 8 YPTYGGSGIVATELGMSLANKGYEVHFISNALPARLDitnpNIFFHRVNVQTYPLFQYQPYDIALSSMIYRVVNLYKL-- 85
Cdd:cd03814 10 HPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAE----SAEGRVVSVPSFPLPFYPEYRLALPLPRRVRRLIKEFqp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 86 DLLHAHYAIPYAYAAFTAKQMLKeddndIPLVTTLHgtdiTLVGQHPSYKHAVEFSI----------NQSDAITSVSESL 155
Cdd:cd03814 86 DIIHIATPGPLGLAALRAARRLG-----LPVVTSYH----TDFPEYLSYYTLGPLSWlawaylrwfhNPFDTTLVPSPSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 156 KKDTLQffNIKKEIQVITNFIDNSEFDePSDCQ---RTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKSRLII 232
Cdd:cd03814 157 ARELEG--HGFERVRLWPRGVDTELFH-PSRRDaalRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVRLVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 233 IGEGPDMEkvnQFLEENPELISKIRLLGKvnDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQ 312
Cdd:cd03814 234 VGDGPARA---ELEARGPDVIFTGFLTGE--ELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRP 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1519542892 313 GETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFD----LKNILPIYE 365
Cdd:cd03814 309 GGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSweafLDNLLDYYA 365
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-365 |
2.15e-29 |
|
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: 117.06 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGILCY---PTYGGSGIVATELGMSLANKGYEVHFI--SNALPARLDITNPNIFFHRVNVQTYPLFQYQPYDI------ 70
Cdd:cd03794 1 KILLISQyypPPKGAAAARVYELAKELVRRGHEVTVLtpSPNYPLGRIFAGATETKDGIRVIRVKLGPIKKNGLirrlln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 71 ----ALSSMIYRVVNLYKLDLLHAHYAIPY-AYAAFTAKQMLKeddndIPLVttLHGTDI---------TLVGQHPS--Y 134
Cdd:cd03794 81 ylsfALAALLKLLVREERPDVIIAYSPPITlGLAALLLKKLRG-----APFI--LDVRDLwpeslialgVLKKGSLLklL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 135 KHAVEFSINQSDAITSVSESLKKDTLQFFNIKKEIQVITNFIDNSEFDE-PSDCQRTQFANPDEKILIHVSNLRPVKRVD 213
Cdd:cd03794 154 KKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPpPKDELRKKLGLDDKFVVVYAGNIGKAQGLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 214 EVLQIFKNVQKKVKSRLIIIGEGPDMEKVNQFLEEnpELISKIRLLGKVN--DLYRILQLSDVFLLPSEQESFGLAA--- 288
Cdd:cd03794 234 TLLEAAERLKRRPDIRFLFVGDGDEKERLKELAKA--RGLDNVTFLGRVPkeEVPELLSAADVGLVPLKDNPANRGSsps 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 289 --LEAMAAYTPVISSNAGGIPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAI-KFDLKNILPIYE 365
Cdd:cd03794 312 klFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEeKFSREKLADRLL 391
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
268-373 |
4.03e-29 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 109.31 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 268 ILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKN 347
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*..
gi 1519542892 348 AKEQAI-KFDLKNILPIYEEMYRTTIE 373
Cdd:COG0438 97 ARERAEeRFSWEAIAERLLALYEELLA 123
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
5-365 |
1.00e-26 |
|
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: 109.34 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 5 ILCYPTY------GGSGIVATELGMSLANKGYEVHFIS--------NALPARLDITNPNIFFHRVNVQTYPLFQ-YQPYD 69
Cdd:cd03823 2 ILLVNSLyppqrvGGAEISVHDLAEALVAEGHEVAVLTagvgppgqATVARSVVRYRRAPDETLPLALKRRGYElFETYN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 70 IALSSMIYRVVNLYKLDLLHAHYAIPYAYAA-FTAKQMLkeddndIPLVTTLHgtDITLVgqHPSykhaVEFSINQSDAI 148
Cdd:cd03823 82 PGLRRLLARLLEDFRPDVVHTHNLSGLGASLlDAARDLG------IPVVHTLH--DYWLL--CPR----QFLFKKGGDAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 149 TSVSESLKKDTLQFFNIKKEIQVITNFIdnsEFDEPsDCQRTQFANPDEKILiHVSNLRPVKRVDEVLQIFKNVQKKvKS 228
Cdd:cd03823 148 LAPSRFTANLHEANGLFSARISVIPNAV---EPDLA-PPPRRRPGTERLRFG-YIGRLTEEKGIDLLVEAFKRLPRE-DI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 229 RLIIIGEGPDMEkvnqflEENPELISKIRLLGKVN--DLYRILQLSDVFLLPSE-QESFGLAALEAMAAYTPVISSNAGG 305
Cdd:cd03823 222 ELVIAGHGPLSD------ERQIEGGRRIAFLGRVPtdDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGG 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519542892 306 IPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKE-QAIKFDLKNILPIYE 365
Cdd:cd03823 296 IAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPpRSTESQAEEYLKLYR 356
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
61-356 |
6.62e-26 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 108.26 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 61 PLFQYQPYDIALSSMIYRVVNLYKLDLLHAHYAIPYAYAAFTAKQMLKeddndIPLVTTLHgTDITLVGQHPSYKHAVE- 139
Cdd:PLN02871 121 PFYQKVPLSLALSPRIISEVARFKPDLIHASSPGIMVFGALFYAKLLC-----VPLVMSYH-THVPVYIPRYTFSWLVKp 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 140 ------FSINQSDAITSVSESLKKD-TLQFFNIKKEIQVITNFIDNSEFDeP---SDCQRTQFAN--PDEKILIHVSNLR 207
Cdd:PLN02871 195 mwdiirFLHRAADLTLVTSPALGKElEAAGVTAANRIRVWNKGVDSESFH-PrfrSEEMRARLSGgePEKPLIVYVGRLG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 208 PVKRVD---EVLQIFKNVqkkvksRLIIIGEGPDMEKVNQFLEENPELISKIrLLGkvNDLYRILQLSDVFLLPSEQESF 284
Cdd:PLN02871 274 AEKNLDflkRVMERLPGA------RLAFVGDGPYREELEKMFAGTPTVFTGM-LQG--DELSQAYASGDVFVMPSESETL 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 285 GLAALEAMAAYTPVISSNAGGIPEV---NIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIKFD 356
Cdd:PLN02871 345 GFVVLEAMASGVPVVAARAGGIPDIippDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWD 419
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
9-318 |
1.18e-24 |
|
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: 100.94 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 9 PTYGGSGIVATELGMSLANKGYEVHFISNALPARLditnpniffhrvnvqtyplfqyqpydialssMIYRVVNLYKLDLL 88
Cdd:cd01635 10 PLRGGLELHVRALARALAALGHEVTVLALLLLALR-------------------------------RILKKLLELKPDVV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 89 HAHYAIPYAYAAFTAKQMLkeddnDIPLVTTLHGTDITLVGQHPSYKHAVEFSINqsdaitsvseslkkdtlqffnikke 168
Cdd:cd01635 59 HAHSPHAAALAALLAARLL-----GIPIVVTVHGPDSLESTRSELLALARLLVSL------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 169 iqvitnfidnsefdepsdcqrtqfanpDEKILIHVSNLRPVKRVDEVLQIFKNVQKKV-KSRLIIIGEGPDMEKVNQfLE 247
Cdd:cd01635 109 ---------------------------PLADKVSVGRLVPEKGIDLLLEALALLKARLpDLVLVLVGGGGEREEEEA-LA 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519542892 248 ENPELISKIRLLGKVND---LYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFL 318
Cdd:cd01635 161 AALGLLERVVIIGGLVDdevLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
12-352 |
1.93e-24 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 103.47 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 12 GGSGIVATELGMSLANKGYEVHF----ISNALPARLDITnPNIFFHRV------NVQTYPLFQY-QPYDIALSSMIYRVV 80
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIftrrISPADPEVVEIA-PGARVIRVpagppeYLPKEELWPYlEEFADGLLRFIAREG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 81 NLYklDLLHAHYAIPyAYAAFTAKQMLKeddndIPLVTTLHgtdiTL-----------VGQHPSYKHAVE-FSINQSDA- 147
Cdd:cd03800 100 GRY--DLIHSHYWDS-GLVGALLARRLG-----VPLVHTFH----SLgrvkyrhlgaqDTYHPSLRITAEeQILEAADRv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 148 ITSVSESLK--KDTLQFFniKKEIQVITNFIDNSEFDEPSDCQRTQFA---NPDEKILIHVSNLRPVKRVDEVLQIF-KN 221
Cdd:cd03800 168 IASTPQEADelISLYGAD--PSRINVVPPGVDLERFFPVDRAEARRARlllPPDKPVVLALGRLDPRKGIDTLVRAFaQL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 222 VQKKVKSRLIIIGEGPDM------EKVNQFLEENpELISKIRLLGKVN--DLYRILQLSDVFLLPSEQESFGLAALEAMA 293
Cdd:cd03800 246 PELRELANLVLVGGPSDDplsmdrEELAELAEEL-GLIDRVRFPGRVSrdDLPELYRAADVFVVPSLYEPFGLTAIEAMA 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1519542892 294 AYTPVISSNAGGIPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQA 352
Cdd:cd03800 325 CGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERA 383
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
12-177 |
1.99e-24 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 98.37 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 12 GGSGIVATELGMSLANKGYEVHFISNALPARLDITNPNIffHRVNVQTYPLFQYQPYDIALSSMIYRVVNLYKLDLLHAH 91
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRV--VRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 92 YAIPYAYAAFTAKQMLkeddnDIPLVTTLHGTDI--TLVGQHPSYKHAVEFSI-----NQSDAITSVSESLKKDTLQFFN 164
Cdd:pfam13439 79 SPFPLGLAALAARLRL-----GIPLVVTYHGLFPdyKRLGARLSPLRRLLRRLerrllRRADRVIAVSEAVADELRRLYG 153
|
170
....*....|....
gi 1519542892 165 IKKE-IQVITNFID 177
Cdd:pfam13439 154 VPPEkIRVIPNGVD 167
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
5-313 |
5.18e-24 |
|
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: 102.06 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 5 ILCY-----PTYGGSGIVATELGMSLANKGYEVHFISNALPARLDITNPNIFF--HRVNVQTYPLFQYQP--YDIALSSM 75
Cdd:cd03821 2 ILHVtpsisPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYipPQDGFASIPLLRQGAgrTDFSPGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 76 IYRVVNLYKLDLLHAHyAI--PYAYAAFTAKQMLKeddndIPLVTTLHGTDITLVGQHPS-----YKHAVE-FSINQSDA 147
Cdd:cd03821 82 NWLRRNLREYDVVHIH-GVwtYTSLAACKLARRRG-----IPYVVSPHGMLDPWALQQKHwkkriALHLIErRNLNNAAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 148 ITSVSESlKKDTLQFFNIKKEIQVITNFIDNSEFDePSDCQRTQFAN-PDEKILIHVSNLRPVKRVDEVLQIFKNVQKK- 225
Cdd:cd03821 156 VHFTSEQ-EADELRRFGLEPPIAVIPNGVDIPEFD-PGLRDRRKHNGlEDRRIILFLGRIHPKKGLDLLIRAARKLAEQg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 226 VKSRLIIIGEGPDMEKVNQFLEENPELISKIRLLGKV--NDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNA 303
Cdd:cd03821 234 RDWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGPLygEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDK 313
|
330
....*....|
gi 1519542892 304 GGIPEVNIQG 313
Cdd:cd03821 314 CGLSELVEAG 323
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
85-358 |
4.12e-23 |
|
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: 99.06 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 85 LDLLHAHYAIPYAYAAFTAKQMlkeddnDIPLVTTLHGTDIT-----------LVGQHPSYKHAVEfsiNQSDAITSVSE 153
Cdd:cd05844 82 PALVHAHFGRDGVYALPLARAL------GVPLVVTFHGFDITtsrawlaaspgWPSQFQRHRRALQ---RPAALFVAVSG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 154 SLKKDTLQFFNIKKEIQVITNFIDNSEFdEPSDcqrtqfANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKK-VKSRLII 232
Cdd:cd05844 153 FIRDRLLARGLPAERIHVHYIGIDPAKF-APRD------PAERAPTILFVGRLVEKKGCDVLIEAFRRLAARhPTARLVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 233 IGEGPDMEKvnqfLEENPELISKIRLLGKVN--DLYRILQLSDVFLLPS------EQESFGLAALEAMAAYTPVISSNAG 304
Cdd:cd05844 226 AGDGPLRPA----LQALAAALGRVRFLGALPhaEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHG 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 305 GIPEVNIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIK-FDLK 358
Cdd:cd05844 302 GIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEqFDIR 356
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
184-328 |
1.32e-21 |
|
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: 94.66 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 184 PSDCQRTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKkvksRLIIIGEGPDMEKVNQFLEENpeliskIRLLGKVN 263
Cdd:cd03804 186 PVDTDAFAPAADKEDYYLTASRLVPYKRIDLAVEAFNELPK----RLVVIGDGPDLDRLRAMASPN------VEFLGYQP 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519542892 264 D--LYRILQLSDVFLLPSEqESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEIGNVEAMS 328
Cdd:cd03804 256 DevLKELLSKARAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLK 321
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
104-361 |
3.64e-21 |
|
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: 93.13 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 104 KQMLKEDDNDIPLVTTLHGT---DITLVGQHP---SYKHAVEfSINQSDAITSVSESLKKDTLQFFNIKKEIQVITNFID 177
Cdd:cd04949 68 GQVILNTKGPAKKGAVLHNEhvkNNDDPEHSLiknFYKYVFE-NLNKYDAIIVSTEQQKQDLSERFNKYPPIFTIPVGYV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 178 NSEFDEPSDCQRTQfanpdeKILIHVSNLRPVKRVDEVLQIFKNVQKKV-KSRLIIIGEGPDMEKVNQFLEENpELISKI 256
Cdd:cd04949 147 DQLDTAESNHERKS------NKIITISRLAPEKQLDHLIEAVAKAVKKVpEITLDIYGYGEEREKLKKLIEEL-HLEDNV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 257 RLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAG-GIPEVNIQGETGFLAEIGNVEAMSNYTIKLL 335
Cdd:cd04949 220 FLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELL 299
|
250 260
....*....|....*....|....*.
gi 1519542892 336 SNVELLTKMKKNAKEQAIKFDLKNIL 361
Cdd:cd04949 300 NDPEKLQQFSEESYKIAEKYSTENVM 325
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
166-371 |
1.36e-20 |
|
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: 92.01 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 166 KKEIQVITNFIDNSEFdEPSDCQ--RTQFANPDEKILI---HVSNLRPVKRVDEVLQIFKNVQKKVKSRLIIIGEGPdme 240
Cdd:cd03825 160 GLPVVVIPNGIDTEIF-APVDKAkaRKRLGIPQDKKVIlfgAESVTKPRKGFDELIEALKLLATKDDLLLVVFGKND--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 241 kvnqflEENPELISKIRLLGKVND---LYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGF 317
Cdd:cd03825 236 ------PQIVILPFDIISLGYIDDdeqLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGY 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 318 LAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIK-FDLKNILPIYEEMYRTT 371
Cdd:cd03825 310 LVPPGDVQALAEAIEWLLANPKERESLGERARALAENhFDQRVQAQRYLELYKDL 364
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
2-330 |
2.46e-20 |
|
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: 90.81 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGILCYP-------TYGGSGIVATELGMSLANKGYEVHFIS---NALPARLDITNPNIFFHRVNVQTYPLFqyqpydiA 71
Cdd:cd03802 1 RIAQVSPPrgpvppgKYGGTELVVSALTEGLVRRGHEVTLFApgdSHTSAPLVAVIPRALRLDPIPQESKLA-------E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 72 LSSMIYRVVNLYKLDLLHAH--YAIPYaYAAFTakqmlkeddnDIPLVTTLHGTDITLVGQHPSYKHAVEFsinqsdaiT 149
Cdd:cd03802 74 LLEALEVQLRASDFDVIHNHsyDWLPP-FAPLI----------GTPFVTTLHGPSIPPSLAIYAAEPPVNY--------V 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 150 SVSESLKKDTLQFfnikKEIQVITNFIDNSEFDepsdcqrtqFANPDEKILIHVSNLRPVKRVDEVLQifknVQKKVKSR 229
Cdd:cd03802 135 SISDAQRAATPPI----DYLTVVHNGLDPADYR---------FQPDPEDYLAFLGRIAPEKGLEDAIR----VARRAGLP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 230 LIIIGEGPDMEKVnqFLEENPELISKIRLLGKVND--LYRILQLSDVFLLPSE-QESFGLAALEAMAAYTPVISSNAGGI 306
Cdd:cd03802 198 LKIAGKVRDEDYF--YYLQEPLPGPRIEFIGEVGHdeKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGL 275
|
330 340
....*....|....*....|....
gi 1519542892 307 PEVNIQGETGFLAEigNVEAMSNY 330
Cdd:cd03802 276 PEVIQHGETGFLVD--SVEEMAEA 297
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
169-372 |
2.47e-19 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 88.24 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 169 IQVITNFIDNSEFdEPSDCQRTQ-----FANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKV-----KSRLIIIGEGPD 238
Cdd:TIGR03088 162 IHQIYNGVDTERF-HPSRGDRSPilppdFFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLpegaeRLRLVIVGDGPA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 239 MEKVNQFLEEnPELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFL 318
Cdd:TIGR03088 241 RGACEQMVRA-AGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGAL 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 319 AEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQA-IKFDLKNILPIYEEMYRTTI 372
Cdd:TIGR03088 320 VPPGDAVALARALQPYVSDPAARRAHGAAGRARAeQQFSINAMVAAYAGLYDQLL 374
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
84-369 |
7.06e-19 |
|
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: 87.78 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 84 KLDLLHAHYAipyAYAAFTAkqMLKEDDNDIPLVTTLHGT-------DITLVGQHPSY--KHAVEF-------SINQSDA 147
Cdd:cd03813 173 EADLYHSVST---GYAGLLG--ALARHRRGIPFLLTEHGIytrerkiEILQSTWIMGYikKLWIRFferlgklAYQQADK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 148 ITSVSESLKKDTLQFFNIKKEIQVITNFIDNSEFDEPSdcqrtqfANPDEKILIHVSN-LR--PVKRVDEVLQIFKNVQK 224
Cdd:cd03813 248 IISLYEGNRRRQIRLGADPDKTRVIPNGIDIQRFAPAR-------EERPEKEPPVVGLvGRvvPIKDVKTFIRAFKLVRR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 225 KV-KSRLIIIG---EGPDMEKVNQFLEENPELISKIRLLGKVN--DLYRILqlsDVFLLPSEQESFGLAALEAMAAYTPV 298
Cdd:cd03813 321 AMpDAEGWLIGpedEDPEYAQECKRLVASLGLENKVKFLGFQNikEYYPKL---GLLVLTSISEGQPLVILEAMASGVPV 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519542892 299 ISSNAGGIPEV-----NIQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIK-FDLKNILPIYEEMYR 369
Cdd:cd03813 398 VATDVGSCRELiygadDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKyYTLEGMIDSYRKLYL 474
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
145-318 |
7.15e-19 |
|
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: 86.96 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 145 SDAITSVSESLKKDTLQFFNIKKeIQVITN--FIDNSEFDEPSDCQRTQFANPDEKILI-HVSNLRPVKRVDEVLQIFKN 221
Cdd:cd03812 137 STKYLACSEDAGEWLFGEVENGK-FKVIPNgiDIEKYKFNKEKRRKRRKLLILEDKLVLgHVGRFNEQKNHSFLIDIFEE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 222 VQKKVK-SRLIIIGEGPDMEKVNQFLEENpELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVIS 300
Cdd:cd03812 216 LKKKNPnVKLVLVGEGELKEKIKEKVKEL-GLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLL 294
|
170
....*....|....*...
gi 1519542892 301 SNAGGiPEVNIQGETGFL 318
Cdd:cd03812 295 SDTIT-KECDITNNVEFL 311
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
145-368 |
7.99e-19 |
|
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: 86.73 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 145 SDAITSVSeslkKDTLQFFNIKK-----EIQVITNFIDNSEFDEPSDCQ---RTQFA-NPDEKILIHVSNLRPVK-RVDE 214
Cdd:cd04951 131 CDITTNVS----REALDEFIAKKafsknKSVPVYNGIDLNKFKKDINVRlkiRNKLNlKNDEFVILNVGRLTEAKdYPNL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 215 VLQIFKNVQKKVKSRLIIIGEGPDMEKVNQFLEeNPELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAA 294
Cdd:cd04951 207 LLAISELILSKNDFKLLIAGDGPLRNELERLIC-NLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMAC 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519542892 295 YTPVISSNAGGIPEVniQGETGFLAEIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIK-FDLKNILPIYEEMY 368
Cdd:cd04951 286 ERPVVATDAGGVAEV--VGDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKnFSINTIVNEWERLY 358
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
194-350 |
1.10e-18 |
|
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: 86.61 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 194 NPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS-RLIIIGEG----PDMEKV-NQFLE--ENPELISKIRLLGKVNDL 265
Cdd:cd03792 194 DPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEpQLVICGHGavddPEGSVVyEEVMEyaGDDHDIHVLRLPPSDQEI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 266 YRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEigNVEAMSNYTIKLLSNVELLTKMK 345
Cdd:cd03792 274 NALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVN--SVEGAAVRILRLLTDPELRRKMG 351
|
....*
gi 1519542892 346 KNAKE 350
Cdd:cd03792 352 LAARE 356
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
25-350 |
1.93e-17 |
|
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: 82.50 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 25 LANKGYEVHFISnALPARLDITNPNIffhrvnvqtyplfqyQPYDIALSSMIYRVVNLYK---LDLLHAHYAipyaYAAF 101
Cdd:cd03799 24 LIDRGHEVDIYA-VNPGDLVKRHPDV---------------EKYNVPSLNLLYAIVGLNKkgaYDIIHCQFG----PLGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 102 TAKQMLKEDDNDIPLVTTLHGTDITLvgQHPSYKHAV-EFSINQSDAITSVSESLKKDTLQFFNIKKEIQVITNFIDNSE 180
Cdd:cd03799 84 LGALLRRLKVLKGKLVTSFRGYDISM--YVILEGNKVyPQLFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 181 FDepsdcQRTQFANPDEKILIhVSNLRPVKR---------VDEVLQIFKNVQKKvksrliIIGEGPDMEKVNQFLEENpE 251
Cdd:cd03799 162 FR-----FKPRYLPLDGKIRI-LTVGRLTEKkgleyaieaVAKLAQKYPNIEYQ------IIGDGDLKEQLQQLIQEL-N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 252 LISKIRLLG--KVNDLYRILQLSDVFLLPS------EQESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEIGN 323
Cdd:cd03799 229 IGDCVKLLGwkPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERD 308
|
330 340
....*....|....*....|....*..
gi 1519542892 324 VEAMSNYTIKLLSNVELLTKMKKNAKE 350
Cdd:cd03799 309 AEAIAEKLTYLIEHPAIWPEMGKAGRA 335
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
168-359 |
3.91e-15 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 75.98 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 168 EIQVITNFIDNSEFDE-PSDCQRTQFA-NPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS-RLIIIGEGPDMEK--- 241
Cdd:PRK15484 162 DISIVPNGFCLETYQSnPQPNLRQQLNiSPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNlKLVVVGDPTASSKgek 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 242 ---VNQFLEENPELISKIRLLGKV--NDLYRILQLSDVFLLPSE-QESFGLAALEAMAAYTPVISSNAGGIPEVNIQGET 315
Cdd:PRK15484 242 aayQKKVLEAAKRIGDRCIMLGGQppEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGIT 321
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1519542892 316 GF-LAEIGNVEAMSNYTIKLLSNVELLtkmkkNAKEQAIKFDLKN 359
Cdd:PRK15484 322 GYhLAEPMTSDSIISDINRTLADPELT-----QIAEQAKDFVFSK 361
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
138-309 |
1.45e-14 |
|
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: 74.58 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 138 VEFSINQSDAITSVSESLKKDTLQFFNIKKE-IQVITNFIDNSEFdEPSDCQRtqfaNPDEKILIHVSNLRPVKRVDEVL 216
Cdd:cd03796 138 LRFSLADIDHVICVSHTSKENTVLRASLDPRiVSVIPNAVDSSDF-TPDPSKP----DPNKITIVVISRLVYRKGIDLLV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 217 QIFKNVQKKVKS-RLIIIGEGPDMEKVNQFLEENpELISKIRLLGKV--NDLYRILQLSDVFLLPSEQESFGLAALEAMA 293
Cdd:cd03796 213 GIIPRICKKHPNvRFIIGGDGPKRIELEEMREKY-QLQDRVELLGAVphEEVRDVLVQGHIFLNTSLTEAFCIAIVEAAS 291
|
170
....*....|....*.
gi 1519542892 294 AYTPVISSNAGGIPEV 309
Cdd:cd03796 292 CGLLVVSTRVGGIPEV 307
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
13-152 |
1.81e-14 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 69.66 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 13 GSGIVATELGMSLANKGYEVHFISNALPARLDITNPNIFFHRVNVQTYPLFQYqpydiALSSMIYRVVNLYKLDLLHAHY 92
Cdd:pfam13477 8 ADSIHTLRWADALADRGYDVHVISSKGPAKDELIAEGIHVHRLKVPRKGPLGY-----LKAFRLKKLIKKIKPDVVHVHY 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519542892 93 AIPYAYAAFTAKQMLKeddnDIPLVTTLHGTDITLVGQHPS-YKHAVEFSINQSDAITSVS 152
Cdd:pfam13477 83 AKPYGLLAGLAARLSG----FPPVVLSAWGLDVYKFPNKSRlKKLLLKLNLKKATLIISTS 139
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
139-358 |
2.07e-12 |
|
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: 68.00 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 139 EFSINQSDAITSVSESLKKDTLQFFN--IKKEIQVITNFIDNSEFDEPSDC--QRTQFANPDEKILIHVSNLRPVKRVDE 214
Cdd:cd03805 149 EFTTGMADQIVVNSNFTAGVFKKTFPslAKNPPEVLYPCVDTDSFDSTSEDpdPGDLIAKSNKKFFLSINRFERKKNIAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 215 VLQIFKNVQKKVKS----RLIIIGeGPD---MEKVnQFLEE---------NPEliSKIRLLGKVNDLYRILQLSDVFLL- 277
Cdd:cd03805 229 AIEAFAKLKQKLPEfenvRLVIAG-GYDprvAENV-EYLEElqrlaeellNVE--DQVLFLRSISDSQKEQLLSSALALl 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 278 --PSEqESFGLAALEAMAAYTPVISSNAGGIPEVNIQGETGFLAEiGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAI-K 354
Cdd:cd03805 305 ytPSN-EHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PTPEAFAEAMLKLANDPDLADRMGAAGRKRVKeK 382
|
....
gi 1519542892 355 FDLK 358
Cdd:cd03805 383 FSRE 386
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
12-174 |
4.69e-11 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 60.49 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 12 GGSGIVATELGMSLANKGYEVHFIS-NALPARLDITNPNIFFHRVNVQTYPLFqyqPYDIALSSMIYRVVNLYKLDLLHA 90
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTpGGPPGRPELVGDGVRVHRLPVPPRPSP---LADLAALRRLRRLLRAERPDVVHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 91 HYAIPYAYAAFTAKQMlkeddnDIPLVTTLHGTDITLVG--QHPSYKHAVEFSINQSDAITSVSESLkKDTLQFFNIKKE 168
Cdd:pfam13579 78 HSPTAGLAARLARRRR------GVPLVVTVHGLALDYGSgwKRRLARALERRLLRRADAVVVVSEAE-AELLRALGVPAA 150
|
....*..
gi 1519542892 169 -IQVITN 174
Cdd:pfam13579 151 rVVVVPN 157
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
194-369 |
2.94e-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: 61.43 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 194 NPDEKILIHVSNLRPVKRVDEVLQIFKN-VQKKVksRLIIIGEG-PDMEK-VNQFLEENPElisKIRLLGKVND-LY-RI 268
Cdd:cd03791 291 DPDAPLFGFVGRLTEQKGVDLILDALPElLEEGG--QLVVLGSGdPEYEQaFRELAERYPG---KVAVVIGFDEaLAhRI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 269 LQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGG-----IPEVNIQGE-TGFLAEIGNVEAMS---NYTIKLLSNVE 339
Cdd:cd03791 366 YAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGladtvFDYDPETGEgTGFVFEDYDAEALLaalRRALALYRNPE 445
|
170 180 190
....*....|....*....|....*....|
gi 1519542892 340 LLTKMKKNAKEQAikFDLKNILPIYEEMYR 369
Cdd:cd03791 446 LWRKLQKNAMKQD--FSWDKSAKEYLELYR 473
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
244-364 |
8.13e-09 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 56.99 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 244 QFLEENPELISKIRLLGKVN--DLYRILQLSDVFLLPSEQ--ESFGLaaLEAMAAYTPVISSNAGGIPEVNIQGETGFLA 319
Cdd:cd03818 271 KMLAELGVDLERVHFVGKVPydQYVRLLQLSDAHVYLTYPfvLSWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLLV 348
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1519542892 320 EIGNVEAMSNYTIKLLSNVELLTKMKKNAKEQAIK-FDLKNILPIY 364
Cdd:cd03818 349 DFFDPDALAAAVLELLEDPDRAAALRRAARRTVERsDSLDVCLARY 394
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
2-302 |
1.39e-07 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 52.78 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 2 KIGILCYPTYGGSGIVAT-ELGMSLANKGYEVHFISNALPARLDITNPniffhRVNVQTYPlFQYQPYDIA--LSSMIYR 78
Cdd:TIGR04047 1 RIALLTYSTKPRGGVVHTlELAEALTALGHDVTVWALAADGFGFFRDP-----PCAVRLVP-VAPAPGDTDamVEQRIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 79 VVNLYK------LDLLHAHYAIPyAYAAFTAKQMLKEDDndipLVTTLHGTDitlVGQHPSYKHAVEFSINQSDAITSVS 152
Cdd:TIGR04047 75 SIDHLRahfargFDVVHAQDCIS-GNALATLRAEGLIPG----FVRTVHHLD---DFDDPRLAACQERAIVEADAVLCVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 153 ESLKKDTLQFFNIkkEIQVITNFIDNSEFDEPSDCQ----RTQFANPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS 228
Cdd:TIGR04047 147 AAWAAELRAEWGI--DATVVPNGVDAARFSPAADAAdaalRRRLGLRGGPYVLAVGGIEPRKNTIDLLEAFALLRARRPQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 229 RLIIIGEGP---DMEKVN-QFLEENPEL---ISKIRLLGKVND-----LYRilqLSDVFLLPSEQESFGLAALEAMAAYT 296
Cdd:TIGR04047 225 AQLVIAGGAtlfDYDAYRrEFRARAAELgvdPGPVVITGPVPDadlpaLYR---CADAFAFPSLKEGFGLVVLEALASGI 301
|
....*.
gi 1519542892 297 PVISSN 302
Cdd:TIGR04047 302 PVVASD 307
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
196-348 |
2.52e-07 |
|
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: 52.00 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 196 DEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS-RLIIIGE-GPDMEKVNQFLEENPEliskIRLLGKVN---------- 263
Cdd:cd03822 186 GKKVILTFGFIGPGKGLEILLEALPELKAEFPDvRLVIAGElHPSLARYEGERYRKAA----IEELGLQDhvdfhnnflp 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 264 --DLYRILQLSDVFLLP---SEQESFGLAALeAMAAYTPVISSNAGGIPEVNIQGEtGFLAEIGNVEAMSNYTIKLLSNV 338
Cdd:cd03822 262 eeEVPRYISAADVVVLPylnTEQSSSGTLSY-AIACGKPVISTPLRHAEELLADGR-GVLVPFDDPSAIAEAILRLLEDD 339
|
170
....*....|
gi 1519542892 339 ELLTKMKKNA 348
Cdd:cd03822 340 ERRQAIAERA 349
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
220-336 |
5.46e-07 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 51.62 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 220 KNVQKKVKSRLIIIGEGpDMEKVNQFLEENPELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVI 299
Cdd:PRK15490 422 RYLQHHPATRFVLVGDG-DLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVI 500
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1519542892 300 SSNAGGIPEVNIQGETGFL---AEIGNVEAMSNYTIKLLS 336
Cdd:PRK15490 501 STPAGGSAECFIEGVSGFIlddAQTVNLDQACRYAEKLVN 540
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
78-350 |
8.40e-07 |
|
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: 50.54 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 78 RVVNLYKLDLLHAHYAIPYAY---AAFTAKQMLKEDDNDIPLVTTLHGTDItLVGQHPSYKHAVEFSINQS-DAITSVSE 153
Cdd:cd04946 108 RVLALLQFVSIFGQGTVVYSYwlnHTALGLGLLKDEYYRDVVISRAHRYDL-YEDQYGSYYLPLREYLVSYlDAVFLISK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 154 SlKKDTLQ--FFNIKKEIQVitnfidnSEFDEPSDCQRTQFANPDEKILIHVSNLRPVKRVDevlQIFKNVQKKVKSRLI 231
Cdd:cd04946 187 E-GKDYLQkcYPAYKEKIFV-------SRLGVSDKEQYSKVKKEGDLRLVSCSSIVPVKRID---LIIETLNSLCVAHPS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 232 I------IGEGPDMEKVNQFLEENPELIsKIRLLGKVND-----LYRiLQLSDVFLLPSEQESFGLAALEAMAAYTPVIS 300
Cdd:cd04946 256 IciswthIGGGPLKERLEKLAENKLENV-KVNFTGEVSNkevkqLYK-ENDVDVFVNVSESEGIPVSIMEAISFGIPVIA 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1519542892 301 SNAGGIPEVNIQGETGFL-AEIGNVEAMSNYTIKLLSNVELLTKMKKNAKE 350
Cdd:cd04946 334 TNVGGTREIVENETNGLLlDKDPTPNEIVSSIMKFYLDGGDYKTMKISARE 384
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
194-355 |
9.34e-06 |
|
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: 47.22 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 194 NPDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKS------RLIIIG----EGpDMEKVNQFLEENPELISKIRLLGKVN 263
Cdd:cd03806 234 KTRENQILSIAQFRPEKNHPLQLRAFAELLKRLPEsirsnpKLVLIGscrnEE-DKERVEALKLLAKELILEDSVEFVVD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 264 ----DLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGiPEVNI-----QGETGFLAEigNVE--AMSNYTI 332
Cdd:cd03806 313 apyeELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAG-PLLDIvvpwdGGPTGFLAS--TPEeyAEAIEKI 389
|
170 180
....*....|....*....|...
gi 1519542892 333 KLLSNVELLtKMKKNAKEQAIKF 355
Cdd:cd03806 390 LTLSEEERL-QRREAARSSAERF 411
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
227-326 |
2.86e-05 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 46.18 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 227 KSRLIIIGEGPDMEKVNQFLEEnPELISKIRLLGKVNDLYRILQLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGI 306
Cdd:PRK15179 548 KVRFIMVGGGPLLESVREFAQR-LGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGA 626
|
90 100
....*....|....*....|
gi 1519542892 307 PEVNIQGETGFLAEIGNVEA 326
Cdd:PRK15179 627 GEAVQEGVTGLTLPADTVTA 646
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
262-360 |
9.76e-05 |
|
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: 44.39 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 262 VNDLYRIL-QLSDVFLLPSEQESFGLAALEAMAAYTPVISSNAGGipEVNIQG--ETGFLAEIGNVEAMSNYTIKLLSNV 338
Cdd:TIGR02468 561 VPDIYRLAaKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGG--PVDIHRvlDNGLLVDPHDQQAIADALLKLVADK 638
|
90 100
....*....|....*....|..
gi 1519542892 339 ELLTKMKKNAkeqaikfdLKNI 360
Cdd:TIGR02468 639 QLWAECRQNG--------LKNI 652
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
84-369 |
1.06e-03 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 40.85 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 84 KLDLLHAH--YAipyAYAAFTAKQMLKEDD-NDIPLVTTLH---------GTDITLVGQHPSY--KHAVEFS-------- 141
Cdd:COG0297 129 KPDIIHCHdwQT---GLIPALLKTRYADDPfKRIKTVFTIHnlayqgifpAEILELLGLPPELftPDGLEFYgqinflka 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 142 -INQSDAITSVSESLKKDTLQ-FF---------NIKKEIQVITNFIDNSEFDEPSD----------------------CQ 188
Cdd:COG0297 206 gIVYADRVTTVSPTYAREIQTpEFgegldgllrARSGKLSGILNGIDYDVWNPATDpylpanysaddlegkaankaalQE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 189 RTQFANPDEKILI-HVSNLRPVKRVDEVLQIF-----KNVQkkvksrLIIIGEG-PDMEkvNQFLE---ENPElisKIRL 258
Cdd:COG0297 286 ELGLPVDPDAPLIgMVSRLTEQKGLDLLLEALdelleEDVQ------LVVLGSGdPEYE--EAFRElaaRYPG---RVAV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 259 LGKVND-LYRILQL-SDVFLLPSEQESFGLAALEAMAAYTPVISSNAGG----IPEVNIQGE--TGFLAEIGNVEAMSN- 329
Cdd:COG0297 355 YIGYDEaLAHRIYAgADFFLMPSRFEPCGLNQMYALRYGTVPIVRRTGGladtVIDYNEATGegTGFVFDEYTAEALLAa 434
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1519542892 330 --YTIKLLSNVELLTKMKKNAKEQaiKFDLKNILPIYEEMYR 369
Cdd:COG0297 435 irRALALYRDPEAWRKLQRNAMKQ--DFSWEKSAKEYLELYR 474
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
147-381 |
1.73e-03 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 40.08 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 147 AITSVSeslkKDTLQFFNIK-KEIQVITNFIDNSEFDEPsdcqRTQFANPdeKILIHVSNLR--PVKRVDEVLQIFKNVQ 223
Cdd:PRK09922 139 AISSGI----KEQMMARGISaQRISVIYNPVEIKTIIIP----PPERDKP--AVFLYVGRLKfeGQKNVKELFDGLSQTT 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 224 KKVKsrLIIIGEGPDMEKVNQFLEEnPELISKIRLLGKVNDLYRILQLS----DVFLLPSEQESFGLAALEAMAAYTPVI 299
Cdd:PRK09922 209 GEWQ--LHIIGDGSDFEKCKAYSRE-LGIEQRIIWHGWQSQPWEVVQQKiknvSALLLTSKFEGFPMTLLEAMSYGIPCI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 300 SSNAGGIPEVNIQ-GETGFLAEIGNVEAMSNYTIKLLSNvelltkmKKNAKEQAIKfdlKNILPIYEEMYrttIENFKNE 378
Cdd:PRK09922 286 SSDCMSGPRDIIKpGLNGELYTPGNIDEFVGKLNKVISG-------EVKYQHDAIP---NSIERFYEVLY---FKNLNNA 352
|
...
gi 1519542892 379 LTK 381
Cdd:PRK09922 353 LFS 355
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
195-360 |
3.96e-03 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). 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: 340861 [Multi-domain] Cd Length: 364 Bit Score: 38.84 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 195 PDEKILIHVSNLRPVKRVDEVLQIFKNVQKKVKSrLIIIGegpDMEKVNQFLEENPELISKIRLLGKVNDLYRILQLSDV 274
Cdd:cd17507 195 PDKPTVLLMGGGGGMGPVKETVEALLDSLRAGQV-LVVCG---KNKKLYEKLSGLEEDYINVRVLGYVDDMNELMAASDL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519542892 275 FLlpseQESFGLAALEAMAAYTPVISSNAggipevnIQGEtgflaEIGNVEAMSNYTI---------------KLLSNVE 339
Cdd:cd17507 271 VI----TKPGGLTISEALARGLPVIIYDP-------IPGQ-----EEENADFLENNGAgiiardpeelleivaRLIDPPS 334
|
170 180
....*....|....*....|.
gi 1519542892 340 LLTKMKKNAKEQAIKFDLKNI 360
Cdd:cd17507 335 LLRMMSEAAKELKPPAAAKVI 355
|
|
| |
