|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
2-404 |
3.93e-148 |
|
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: 426.01 E-value: 3.93e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 2 KILCIHQNFPGQYKHLAPALAA-RGHEVVALTlkVKKPTRWQGVTILPYDIRGRSAKDI--HPWLQDFETKLIRATSCCN 78
Cdd:cd03818 1 NILFVHQNFPGQFKHLARHLARqPGNEVTFLT--RRNDQGIPGVRPVRYRPFRGVASPLegHRYVRDFEEGVLRGQAVLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 79 AAIALRKRGFVPDVILAHHGWGESLFLKDVWPQARMGLYCELYHQSLPVFTAFDPEFqrPQTQSDPLRLRLKNLNNRLHE 158
Cdd:cd03818 79 ALLALKREGFRPDVVVGHPGWGEALFVKDVFPDVPLIGYCEYYYRAEGADVGFDPEF--PLDLMIRCRLRNRNIALLLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 159 EIMDAGISPTAFQAGTFPDHWQDRITVAHDGVDTDLVVPGPNATLTVTDGRVLTREDEVITFINRNLEPYRGYHIFMRAL 238
Cdd:cd03818 157 EQADLGVTPTRWQRSLFPAAYRDRISVIHDGVDTDRLAPDPAARLRLLNGTELKAGDPVITYVARNLEPYRGFHVFMRAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 239 PDLLRRRPDAQVVLIGGDEVSYGAKAPDGTTWKQIFIDEIADrmppeDWARVHFLGRVPYDRFLSMMQVSRVHVYLTYPF 318
Cdd:cd03818 237 PRIQARRPDARVVVVGGDGVSYGSPPPDGGSWKQKMLAELGV-----DLERVHFVGKVPYDQYVRLLQLSDAHVYLTYPF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 319 VLSWSLLEAMSAECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDDADARARMGRAARAFVRDGYDLrTRC 398
Cdd:cd03818 312 VLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSL-DVC 390
|
....*.
gi 384468318 399 LPRHID 404
Cdd:cd03818 391 LARYLA 396
|
|
| Glyco_trans_4_3 |
pfam12000 |
Glycosyl transferase family 4 group; This domain is found associated with pfam00534. |
24-195 |
4.70e-68 |
|
Glycosyl transferase family 4 group; This domain is found associated with pfam00534.
Pssm-ID: 432252 Cd Length: 168 Bit Score: 213.18 E-value: 4.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 24 RGHEVVALTLKvkKPTRWQGVTILPYDIRGRSAKDIHPWLQDFETKLIRATSCCNAAIALRKRGFVPDVILAHHGWGESL 103
Cdd:pfam12000 1 RGHEVVFLTER--KDGELPGVRKVRYRPPRGPTPGAHPYVREFEAAVRRGQAVARAAQALRAEGFVPDVIVGHSGWGETL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 104 FLKDVWPQARMGLYCELYHQSLPVFTAFDPEFqrPQTQSDPLRLRLKNLNNRLHEEIMDAGISPTAFQAGTFPDHWQDRI 183
Cdd:pfam12000 79 FLKDVFPDAPLLGYFEFFYRAHGADVGFDPEF--PLSLDDRARLRLKNAPILLALASCDAGLSPTAWQRSQFPAEFRSKI 156
|
170
....*....|..
gi 384468318 184 TVAHDGVDTDLV 195
Cdd:pfam12000 157 SVIHDGIDTDAF 168
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
16-373 |
3.47e-28 |
|
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: 114.17 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 16 HLAPALAARGHEVVALTLkvkkptRWQGVTILPYDIRGRSAKDIHPWLQDFETKLIRAtsccnaaIALRKRGFVPDVILA 95
Cdd:cd03801 22 ELARALAARGHDVTVLTP------ADPGEPPEELEDGVIVPLLPSLAALLRARRLLRE-------LRPLLRLRKFDVVHA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 96 HhGWGESLFLKDVWPQARMGLycelyhqslpVFTAFDPEFQRPQTQSDPLRLRLKNLNNRLHEeiMDAGISPTAFQAGTF 175
Cdd:cd03801 89 H-GLLAALLAALLALLLGAPL----------VVTLHGAEPGRLLLLLAAERRLLARAEALLRR--ADAVIAVSEALRDEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 176 PDHWQ---DRITVAHDGVDTDLVVPGPNATLTVTDGRVltredeVITFINRnLEPYRGYHIFMRALPDLLRRRPDAQVVL 252
Cdd:cd03801 156 RALGGippEKIVVIPNGVDLERFSPPLRRKLGIPPDRP------VLLFVGR-LSPRKGVDLLLEALAKLLRRGPDVRLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 253 IGGDEVSYGAkapdgttwkqifideiADRMPPEDWARVHFLGRVPYDRFLSMMQVSRVHVYLTY--PFVLSwsLLEAMSA 330
Cdd:cd03801 229 VGGDGPLRAE----------------LEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRyeGFGLV--VLEAMAA 290
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 384468318 331 ECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDD 373
Cdd:cd03801 291 GLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLAD 333
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
214-373 |
2.43e-18 |
|
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: 81.55 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 214 EDEVITFINRnLEPYRGYHIFMRALPDLLRRRPDAQVVLIGGDEvsygakapdgttWKQIFIDEIADRMPPEdwaRVHFL 293
Cdd:pfam00534 1 KKKIILFVGR-LEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGE------------EEKRLKKLAEKLGLGD---NVIFL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 294 GRVPYDRFLSMMQVSRVHVYLTY--PFVLSwsLLEAMSAECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALL 371
Cdd:pfam00534 65 GFVSDEDLPELLKIADVFVLPSRyeGFGIV--LLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLL 142
|
..
gi 384468318 372 DD 373
Cdd:pfam00534 143 ED 144
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-373 |
1.96e-16 |
|
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: 80.09 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 2 KILCIHQNFPG-----QYKHLAPALAARGHEVVALTLKVKKPTRWQ-GVTILPYDIRGRSAKDIHPWLQDFETKLirats 75
Cdd:cd03811 1 KILFVIPSLSGggaerVLLNLANALDKRGYDVTLVLLRDEGDLDKQlNGDVKLIRLLIRVLKLIKLGLLKAILKL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 76 ccnAAIALRKRgfvPDVILAHHGWGESLFLKdvwpqarmglyceLYHQSLPVFT--AFDPEFQRPQTQSDPLRLRLKNLN 153
Cdd:cd03811 76 ---KRILKRAK---PDVVISFLGFATYIVAK-------------LAAARSKVIAwiHSSLSKLYYLKKKLLLKLKLYKKA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 154 NRLHeeimdaGISPTA---FQAgTFPDHwQDRITVAHDGVDTDLVVPGPNATLTVTDgrvltreDEVITFIN--RnLEPY 228
Cdd:cd03811 137 DKIV------CVSKGIkedLIR-LGPSP-PEKIEVIYNPIDIDRIRALAKEPILNEP-------EDGPVILAvgR-LDPQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 229 RGYHIFMRALPDLLRRRPDAQVVLIG-GDEvsygaKAPdgttwKQIFIDE--IADRmppedwarVHFLGRV--PYDrFLS 303
Cdd:cd03811 201 KGHDLLIEAFAKLRKKYPDVKLVILGdGPL-----REE-----LEKLAKElgLAER--------VIFLGFQsnPYP-YLK 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468318 304 MMQVsrvhvyltypFVLSwS--------LLEAMSAECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDD 373
Cdd:cd03811 262 KADL----------FVLS-SryegfpnvLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQK 328
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
217-373 |
2.91e-15 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 72.16 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 217 VITFINRNLEPYRGYHIFMRALPDLLRRRPDAQVVLIGGDEVSYgakapdgttwkqifIDEIADRMPPedwaRVHFLGRV 296
Cdd:pfam13692 3 VILFVGRLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE--------------LEELAAGLED----RVIFTGFV 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468318 297 P-YDRFLSMMQVSrVHVYLTYPFvlSWSLLEAMSAECAIVASGTAPVREVLtEGETGVMVDFFDTDGIVEKTCALLDD 373
Cdd:pfam13692 65 EdLAELLAAADVF-VLPSLYEGF--GLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-373 |
3.84e-14 |
|
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: 73.53 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 2 KILCIHQNFP------GQYKH-LAPALAARGHEVVALTLKVKKPTRWQ---------GVTILPYDI--RGRSAKDIHPWl 63
Cdd:cd03794 1 KILLISQYYPppkgaaAARVYeLAKELVRRGHEVTVLTPSPNYPLGRIfagatetkdGIRVIRVKLgpIKKNGLIRRLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 64 qdfetKLIRATscCNAAIALRKRGFVPDVILAHHG----WGESLFLK------------DVWPQARMGLYCELYHQSLPV 127
Cdd:cd03794 80 -----NYLSFA--LAALLKLLVREERPDVIIAYSPpitlGLAALLLKklrgapfildvrDLWPESLIALGVLKKGSLLKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 128 FTAFDpefqrpqtqsdplRLRLKN------LNNRLHEEIMDAGISPtafqagtfpdhwqDRITVAHDGVDTDLVVPGPNA 201
Cdd:cd03794 153 LKKLE-------------RKLYRLadaiivLSPGLKEYLLRKGVPK-------------EKIIVIPNWADLEEFKPPPKD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 202 TLtvtdgRVLTREDEVITFI-NRNLEPYRGYHIFMRALpDLLRRRPDAQVVLIG-GDEVsygakapdgttwkqifiDEIA 279
Cdd:cd03794 207 EL-----RKKLGLDDKFVVVyAGNIGKAQGLETLLEAA-ERLKRRPDIRFLFVGdGDEK-----------------ERLK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 280 DRMPPEDWARVHFLGRVPYDRFLSMMQVSRVHvYLTYPFVLSWS------LLEAMSAECAIVASGTAPVREVLTEGETGV 353
Cdd:cd03794 264 ELAKARGLDNVTFLGRVPKEEVPELLSAADVG-LVPLKDNPANRgsspskLFEYMAAGKPILASDDGGSDLAVEINGCGL 342
|
410 420
....*....|....*....|
gi 384468318 354 MVDFFDTDGIVEKTCALLDD 373
Cdd:cd03794 343 VVEPGDPEALADAILELLDD 362
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
305-409 |
3.11e-12 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 63.09 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 305 MQVSRVHVYLTYPFVLSWSLLEAMSAECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDDADARARMGRAA 384
Cdd:COG0438 18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAA 97
|
90 100
....*....|....*....|....*
gi 384468318 385 RAFVRDGYDLRtRCLPRHIDWVEDL 409
Cdd:COG0438 98 RERAEERFSWE-AIAERLLALYEEL 121
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
17-363 |
7.56e-11 |
|
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: 63.14 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 17 LAPALAARGHEVVALTLKVKKPTRWQGvTILPYDIRGRsakdihPWLQDFETKLIRAtsccnaAIALRKRgfvPDVILAH 96
Cdd:cd03819 20 LARALAERGHRVLVVTAGGPLLPRLRQ-IGIGLPGLKV------PLLRALLGNVRLA------RLIRRER---IDLIHAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 97 H---GWgeSLFLKDVWPQARmglYCELYHQSLPVFTAFDPEFQRPQTQSDPLRLRLKNLNNRLheeIMDAGISPtafqag 173
Cdd:cd03819 84 SrapAW--LGWLASRLTGVP---LVTTVHGSYLATYHPKDFALAVRARGDRVIAVSELVRDHL---IEALGVDP------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 174 tfpdhwqDRITVAHDGVDTDLVVPGPNATLTVTDGrvLTREDEVITFINRnLEPYRGYHIFMRALPDLLRRRPdaQVVLI 253
Cdd:cd03819 150 -------ERIRVIPNGVDTDRFPPEAEAEERAQLG--LPEGKPVVGYVGR-LSPEKGWLLLVDAAAELKDEPD--FRLLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 254 GGDevsyGAKAPdgttwkqiFIDEIADRMPPEDwaRVHFLGRVpyDRFLSMMQVSRVHVYLTYPFVLSWSLLEAMSAECA 333
Cdd:cd03819 218 AGD----GPERD--------EIRRLVERLGLRD--RVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTP 281
|
330 340 350
....*....|....*....|....*....|
gi 384468318 334 IVASGTAPVREVLTEGETGVMVDFFDTDGI 363
Cdd:cd03819 282 VVATDVGGAREIVVHGRTGLLVPPGDAEAL 311
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
16-373 |
5.99e-10 |
|
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: 60.72 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 16 HLAPALAARGHEVVALTLKV--KKPT--RW-QGVTIL-----PYdiRGRSAKDIHPWLQDFetkliratsCCNAAIALRK 85
Cdd:cd03800 29 ELARALAELGYQVDIFTRRIspADPEvvEIaPGARVIrvpagPP--EYLPKEELWPYLEEF---------ADGLLRFIAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 86 RGFVPDVILAHH---GWGESLfLKDVW--PQarmglyCELYHqSLpvfTAFDPEFQRPQTQSDPlRLRLKnlnnrlHEE- 159
Cdd:cd03800 98 EGGRYDLIHSHYwdsGLVGAL-LARRLgvPL------VHTFH-SL---GRVKYRHLGAQDTYHP-SLRIT------AEEq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 160 IMDAG---ISPTAFQAGTFPDHWQ---DRITVAHDGVDTDLVVPGPNATLTVTdgRVLTREDE-VITFINRnLEPYRGYH 232
Cdd:cd03800 160 ILEAAdrvIASTPQEADELISLYGadpSRINVVPPGVDLERFFPVDRAEARRA--RLLLPPDKpVVLALGR-LDPRKGID 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 233 IFMRALPDLLRRRPDAQVVLIGGDEVSYGAKAPdgttwkqIFIDEIADRMPPEDwaRVHFLGRVPYDRFLSMMQVSRVHV 312
Cdd:cd03800 237 TLVRAFAQLPELRELANLVLVGGPSDDPLSMDR-------EELAELAEELGLID--RVRFPGRVSRDDLPELYRAADVFV 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384468318 313 Y--LTYPFVLSwsLLEAMSAECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDD 373
Cdd:cd03800 308 VpsLYEPFGLT--AIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDD 368
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
181-396 |
1.12e-09 |
|
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: 59.77 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 181 DRITVAHDGVDTDLVVPGPNATltvtdgrvltrEDEVITFINRNLEpYRGYHIFMRALPDLLRRRPDAQVVLIGGdevsy 260
Cdd:cd05844 166 ERIHVHYIGIDPAKFAPRDPAE-----------RAPTILFVGRLVE-KKGCDVLIEAFRRLAARHPTARLVIAGD----- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 261 GAKAPdgttwkqifidEIADRMPPEDwaRVHFLGRVPYDRFLSMMQVSRVhvyLTYPFVLSWS---------LLEAMSAE 331
Cdd:cd05844 229 GPLRP-----------ALQALAAALG--RVRFLGALPHAEVQDWMRRAEI---FCLPSVTAASgdseglgivLLEAAACG 292
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384468318 332 CAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDDADARARMGRAARAFVRDGYDLRT 396
Cdd:cd05844 293 VPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRV 357
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
182-352 |
3.73e-09 |
|
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: 57.03 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 182 RITVAHDGVDTDLVVPGPNATLTVTDGRVLTREDevitFINRnLEPYRGYHIFMRALPDLLRRRPDAQVVLIGGDEVSYG 261
Cdd:cd01635 81 IVVTVHGPDSLESTRSELLALARLLVSLPLADKV----SVGR-LVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 262 AKApdgttwkqifidEIADRMppeDWARVHFLGRVPYDRFLSMMQvSRVHVYLTYPF--VLSWSLLEAMSAECAIVASGT 339
Cdd:cd01635 156 EEA------------LAAALG---LLERVVIIGGLVDDEVLELLL-AAADVFVLPSRseGFGLVLLEAMAAGKPVIATDV 219
|
170
....*....|...
gi 384468318 340 APVREVLTEGETG 352
Cdd:cd01635 220 GGIPEFVVDGENG 232
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
181-375 |
3.87e-09 |
|
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: 57.76 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 181 DRITVAHDGVDTDLVVPGPNATLTVTDGRVltreDEVITFINrNLEPYRGYHIFMRALPDLLRRRPDAQVVLIGGDEvsy 260
Cdd:cd03809 162 EKIVVIPLGVDPSFFPPESAAVLIAKYLLP----EPYFLYVG-TLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKG--- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 261 gakapdgttWKqiFIDEIADRMPPEDWARVHFLGRVPYDRFLSMMQVSRVHVYLTY--PFVLSwsLLEAMSAECAIVASG 338
Cdd:cd03809 234 ---------WE--DEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLyeGFGLP--VLEAMACGTPVIASN 300
|
170 180 190
....*....|....*....|....*....|....*..
gi 384468318 339 TAPVREVLteGETGVMVDFFDTDGIVEKTCALLDDAD 375
Cdd:cd03809 301 ISVLPEVA--GDAALYFDPLDPESIADAILRLLEDPS 335
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-373 |
2.17e-08 |
|
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: 55.41 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 2 KILCIHQNFPGQY--------KHLAPALAARGHEVVALTLKVKKPtrWQGVTILPYDIRGRSAKDIHPWLQ------DFE 67
Cdd:cd03823 1 KILLVNSLYPPQRvggaeisvHDLAEALVAEGHEVAVLTAGVGPP--GQATVARSVVRYRRAPDETLPLALkrrgyeLFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 68 TKLIRATSCCNAAIALRKrgfvPDVILAHH--GWGESlflkdVWPQARmglycelyHQSLP-VFTAFDPEFQRP-QTQSD 143
Cdd:cd03823 79 TYNPGLRRLLARLLEDFR----PDVVHTHNlsGLGAS-----LLDAAR--------DLGIPvVHTLHDYWLLCPrQFLFK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 144 PLRlrlknlnnrlheeimDAGISPTAFQAGTFPDH--WQDRITVAHDGVDTDLVVPGPnatltvtdgRVLTREDEVITFI 221
Cdd:cd03823 142 KGG---------------DAVLAPSRFTANLHEANglFSARISVIPNAVEPDLAPPPR---------RRPGTERLRFGYI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 222 NRnLEPYRGYHIFMRALPDLlrRRPDAQVVLIGGDEVSYGAKAPDGTtwkqifideiadrmppedwaRVHFLGRVPYDRF 301
Cdd:cd03823 198 GR-LTEEKGIDLLVEAFKRL--PREDIELVIAGHGPLSDERQIEGGR--------------------RIAFLGRVPTDDI 254
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468318 302 LSMMQvsRVHVYL-------TYPFVlswsLLEAMSAECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDD 373
Cdd:cd03823 255 KDFYE--KIDVLVvpsiwpePFGLV----VREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTD 327
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
181-380 |
1.73e-07 |
|
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: 52.70 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 181 DRITVAHDGVDTDLVVPGPNATLTVTDGRVLTREDEVITFINRnLEPYRGYHIFMRALPDLLRRRPDAQVVLIGGDEVSy 260
Cdd:cd03807 156 NKIVVIYNGIDLFKLSPDDASRARARRRLGLAEDRRVIGIVGR-LHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPER- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 261 gakaPDgttwkqifIDEIADRMPPEDwaRVHFLGR---VPydRFLSMMQVsrvhvyltypFVLSW-------SLLEAMSA 330
Cdd:cd03807 234 ----PN--------LERLLLELGLED--RVHLLGErsdVP--ALLPAMDI----------FVLSSrtegfpnALLEAMAC 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 384468318 331 ECAIVASGTAPVREVLTEGeTGVMVDFFDTDGIVEKTCALLDDADARARM 380
Cdd:cd03807 288 GLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAIRALLEDPEKRARL 336
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
78-373 |
5.57e-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: 51.23 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 78 NAAIALRKRGfvPDVILAHHGWGeslFLKDvwpqaRMGLY--CELYHQSLPVFTAFdpefQRPQTQSDPLRLRLKNLNN- 154
Cdd:cd03822 66 RLLDHLNFKK--PDVVHIQHEFG---IFGG-----KYGLYalGLLLHLRIPVITTL----HTVLDLSDPGKQALKVLFRi 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 155 -RLHEEIMDAGISpTAFQAGTFPDHWQDRITVAHDGV-DTDLV-VPGPNATLTVTDGRVLtredevITF--INrnlePYR 229
Cdd:cd03822 132 aTLSERVVVMAPI-SRFLLVRIKLIPAVNIEVIPHGVpEVPQDpTTALKRLLLPEGKKVI------LTFgfIG----PGK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 230 GYHIFMRALPDLLRRRPDAQVVLIGGDEVSYGAKAPDGTTWKQIfideiaDRMPPEDWARVHfLGRVPYD---RFLSMMq 306
Cdd:cd03822 201 GLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGERYRKAAI------EELGLQDHVDFH-NNFLPEEevpRYISAA- 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384468318 307 vsrvHVYLT-YPFVL---SWSLLEAMSAECAIVASGTAPVREVLTEGEtGVMVDFFDTDGIVEKTCALLDD 373
Cdd:cd03822 273 ----DVVVLpYLNTEqssSGTLSYAIACGKPVISTPLRHAEELLADGR-GVLVPFDDPSAIAEAILRLLED 338
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
180-373 |
6.96e-07 |
|
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: 50.84 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 180 QDRITVAHDGVDTDLVVPGPNATLTVTDGRVltredevITFINRnLEPYRGYHIFMRALPDLLRRRPDAQVVLIGGDevs 259
Cdd:cd03798 172 RDRVDVIPNGVDPARFQPEDRGLGLPLDAFV-------ILFVGR-LIPRKGIDLLLEAFARLAKARPDVVLLIVGDG--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 260 ygakaPDGTTWKQIFIDEIADrmppedwARVHFLGRVPYD---RFLSMMQVsrvhvyltypFVL-SWS------LLEAMS 329
Cdd:cd03798 241 -----PLREALRALAEDLGLG-------DRVTFTGRLPHEqvpAYYRACDV----------FVLpSRHegfglvLLEAMA 298
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 384468318 330 AECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKTCALLDD 373
Cdd:cd03798 299 CGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAE 342
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-395 |
2.70e-06 |
|
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: 49.13 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 2 KILCIHQNFPGQYKH---LAPALAARGHEVVALT----LKVKKPTRwQGVTILPYDIRGRSakdIHPwLQDFET-----K 69
Cdd:cd03808 1 KILFIVNVDGGFQSFrlpLIKALVKKGYEVHVIApdgdKLSDELKE-LGVKVIDIPILRRG---INP-LKDLKAlfklyK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 70 LIRATSC----CNAAIA------LRKRGFVPDVILAHHGWGeSLFLKDVWPQArmgLYCELYHQSLP----VFTafdpef 135
Cdd:cd03808 76 LLKKEKPdivhCHTPKPgilgrlAARLAGVPKVIYTVHGLG-FVFTEGKLLRL---LYLLLEKLALLftdkVIF------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 136 qrpqtQSDPLRLRLKNLNNRLHEEImdagisptafqagtfpdhwqdrITVAHDGVDTDLVVPGPNatltvtdgrVLTRED 215
Cdd:cd03808 146 -----VNEDDRDLAIKKGIIKKKKT----------------------VLIPGSGVDLDRFQYSPE---------SLPSEK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 216 EVITFINRNLEPyRGYHIFMRALPDLLRRRPDAQVVLIGGDEVsygaKAPDGTTWKQIFIDEiadrmppedwaRVHFLG- 294
Cdd:cd03808 190 VVFLFVARLLKD-KGIDELIEAAKILKKKGPNVRFLLVGDGEL----ENPSEILIEKLGLEG-----------RIEFLGf 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 295 RVPYDRFLSMMQVsrvhvyltypFVL-SW------SLLEAMSAECAIVASGTAPVREVLTEGETGVMVDFFDTDGIVEKT 367
Cdd:cd03808 254 RSDVPELLAESDV----------FVLpSYreglprSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAI 323
|
410 420
....*....|....*....|....*...
gi 384468318 368 CALLDDADARARMGRAARAFVRDGYDLR 395
Cdd:cd03808 324 EKLIEDPELRKEMGEAARKRVEEKFDEE 351
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
280-373 |
1.30e-05 |
|
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: 46.96 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 280 DRMPPEDWAR-------VHFLGRVpyDRFLSMMQVSRVHVYLTYPFVLSWSLLEAMSAECAIVASGTAPVREVLTEGETG 352
Cdd:cd04962 237 ERVPAEELARelgvedrVLFLGKQ--DDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETG 314
|
90 100
....*....|....*....|.
gi 384468318 353 VMVDFFDTDGIVEKTCALLDD 373
Cdd:cd04962 315 FLSDVGDVDAMAKSALSILED 335
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
213-382 |
6.34e-03 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 38.37 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 213 REDEVITFINRnLEPYRGYHIFMRALPDLLRRRPDAQVVLIGgdevsygakapDGTtwKQIFIDEIADRMPPEDwaRVHF 292
Cdd:cd03820 179 LKSKRILAVGR-LTYQKGFDLLIEAWALIAKKHPDWKLRIYG-----------DGP--EREELEKLIDKLGLED--RVKL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468318 293 LGRVpydrflsmmqvSRVHVYltYP----FVLS--W-----SLLEAMSAECAIVASG--TAPvREVLTEGETGVMVDFFD 359
Cdd:cd03820 243 LGPT-----------KNIAEE--YAnssiFVLSsrYegfpmVLLEAMAYGLPIISFDcpTGP-SEIIEDGENGLLVPNGD 308
|
170 180
....*....|....*....|...
gi 384468318 360 TDGIVEKTCALLDDADARARMGR 382
Cdd:cd03820 309 VDALAEALLRLMEDEELRKKMGK 331
|
|
| |
