|
Name |
Accession |
Description |
Interval |
E-value |
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
3-428 |
1.90e-152 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 440.16 E-value: 1.90e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 3 MKVLLLGFEFLP-VKVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGE--------EIGKIRVFGEEVQVKVSYEERG 73
Cdd:TIGR02095 1 MRVLFVAAEMAPfAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEvddqvkvvELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 74 NLRIYRIGGGLL--DSEDVYGPGWDGLIRKAVTFGRASVLLLNdllREEPLPDVVHFHDWHTVFAGALIKKYFK---IPA 148
Cdd:TIGR02095 81 GVPVYFIDNPSLfdRPGGIYGDDYPDNAERFAFFSRAAAELLS---GLGWQPDVVHAHDWHTALVPALLKAVYRpnpIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 149 VFTIHRLN-----------KSKLPAFYFHEAG---------LSELAPYPDIDPEHTGGYIADIVTTvSRGYLIDEWGFFR 208
Cdd:TIGR02095 158 VFTIHNLAyqgvfpaddfsELGLPPEYFHMEGlefygrvnfLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 209 nfEGKITYVFNGIDCSFWN---ESYLTGS--------RDERKKSLLSKFGM---DEGVTFMFIGRFDRgQKGVDVLLKAI 274
Cdd:TIGR02095 237 --SGKLRGILNGIDTEVWNpatDPYLKANysaddlagKAENKEALQEELGLpvdDDVPLFGVISRLTQ-QKGVDLLLAAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 275 EILSSkkefQEMRFIIIGKGDPELEGWARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLG 354
Cdd:TIGR02095 314 PELLE----LGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 355 AIPIASAVGGLRDIITN-------ETGILVKAGDPGELANAILKALELSRSDLSKFReNCKKRAMS--FSWEKSAERYVK 425
Cdd:TIGR02095 390 TVPIVRRTGGLADTVVDgdpeaesGTGFLFEEYDPGALLAALSRALRLYRQDPSLWE-ALQKNAMSqdFSWDKSAKQYVE 468
|
...
3L01_B 426 AYA 428
Cdd:TIGR02095 469 LYR 471
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
4-427 |
1.92e-112 |
|
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: 338.38 E-value: 1.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 4 KVLLLGFEFLP-VKVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIGKIR-------VFGEEVQVKVSYEERGNL 75
Cdd:cd03791 1 KVLFVTSEVAPfAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRvlglevkVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 76 RIYrigggLLDSE---------DVYGPGWDGLIRKAVTFGRASVLLLndlLREEPLPDVVHFHDWHTVFAGALIKK---- 142
Cdd:cd03791 81 DYY-----FLDNPeffdrpglpGPPGYDYPDNAERFAFFSRAALELL---RRLGFQPDIIHANDWHTALVPAYLKTryrg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 143 --YFKIPAVFTIHRLN-----------KSKLPAFYFHEAGLselAPYPDIDPEHTGGYIADIVTTVSRGY----LIDEWG 205
Cdd:cd03791 153 pgFKKIKTVFTIHNLAyqglfpldtlaELGLPPELFHIDGL---EFYGQINFLKAGIVYADRVTTVSPTYakeiLTPEYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 206 F-----FRNFEGKITYVFNGIDCSFWNES--------YLTGSRDER---KKSLLSKFGM---DEGVTFMFIGRFDrGQKG 266
Cdd:cd03791 230 EgldgvLRARAGKLSGILNGIDYDEWNPAtdklipanYSANDLEGKaenKAALQKELGLpvdPDAPLFGFVGRLT-EQKG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 267 VDVLLKAIEILSSKKefqeMRFIIIGKGDPELEGWARSLEEKH-GNVKVITEMlSREFVRELYGSVDFVIIPSYFEPFGL 345
Cdd:cd03791 309 VDLILDALPELLEEG----GQLVVLGSGDPEYEQAFRELAERYpGKVAVVIGF-DEALAHRIYAGADFFLMPSRFEPCGL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 346 VALEAMCLGAIPIASAVGGLRDIITNE-------TGILVKAGDPGELANAILKALEL--SRSDLSKFRENCKKRAmsFSW 416
Cdd:cd03791 384 VQMYAMRYGTLPIVRRTGGLADTVFDYdpetgegTGFVFEDYDAEALLAALRRALALyrNPELWRKLQKNAMKQD--FSW 461
|
490
....*....|.
3L01_B 417 EKSAERYVKAY 427
Cdd:cd03791 462 DKSAKEYLELY 472
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
3-427 |
1.67e-78 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 250.78 E-value: 1.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 3 MKVLLLGFEFLP-VKVGGLAEALTAISEALASLGHEVLVFTPSHGR-----FQGEEIGKIRVF--GEEVQVKVSYEERGN 74
Cdd:COG0297 1 MKILFVASEAAPfAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSiddklKDLEVVASLEVPlgGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 75 LRIYRIG-GGLLDSEDVYG----PGWDGLIRKAVtFGRAsVLLLndLLREEPLPDVVHFHDWHTVFAGALIK------KY 143
Cdd:COG0297 81 VPVYFIDnPELFDRPGPYGdpdrDYPDNAERFAF-FSRA-ALEL--LKGLDWKPDIIHCHDWQTGLIPALLKtryaddPF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 144 FKIPAVFTIH-----------RLNKSKLPAFYFHEAGLselaPYPD-IDPEHTGGYIADIVTTVSRGY----LIDEWGF- 206
Cdd:COG0297 157 KRIKTVFTIHnlayqgifpaeILELLGLPPELFTPDGL----EFYGqINFLKAGIVYADRVTTVSPTYareiQTPEFGEg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 207 ----FRNFEGKITYVFNGIDCSFWN--------ESYLTGSRDER---KKSLLSKFGMDEGVT---FMFIGRFDRgQKGVD 268
Cdd:COG0297 233 ldglLRARSGKLSGILNGIDYDVWNpatdpylpANYSADDLEGKaanKAALQEELGLPVDPDaplIGMVSRLTE-QKGLD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 269 VLLKAIEILSSkkefQEMRFIIIGKGDPELEGWARSLEEKH-GNVKVIT---EMLSREfvreLYGSVDFVIIPSYFEPFG 344
Cdd:COG0297 312 LLLEALDELLE----EDVQLVVLGSGDPEYEEAFRELAARYpGRVAVYIgydEALAHR----IYAGADFFLMPSRFEPCG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 345 LVALEAMCLGAIPIASAVGGLRDIIT--NE-----TGILVKAGDPGELANAILKALELSRsDLSKFREnCKKRAMS--FS 415
Cdd:COG0297 384 LNQMYALRYGTVPIVRRTGGLADTVIdyNEatgegTGFVFDEYTAEALLAAIRRALALYR-DPEAWRK-LQRNAMKqdFS 461
|
490
....*....|..
3L01_B 416 WEKSAERYVKAY 427
Cdd:COG0297 462 WEKSAKEYLELY 473
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
3-427 |
8.15e-65 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 214.98 E-value: 8.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 3 MKVLLLGFEFLP-VKVGGLAEALTAISEALASLGHEVLVFTPSHgRFQGEEIGKIRVFGEE--VQVKVSYEERGNLRIYr 79
Cdd:PRK00654 1 MKILFVASECAPlIKTGGLGDVVGALPKALAALGHDVRVLLPGY-PAIREKLRDAQVVGRLdlFTVLFGHLEGDGVPVY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 80 igggLLDSEDVYG-----PGWDGLIRKAvTFGRASVLLLNDLLreePLPDVVHFHDWHTVFAGALIK-----KYFKIPAV 149
Cdd:PRK00654 79 ----LIDAPHLFDrpsgyGYPDNGERFA-FFSWAAAEFAEGLD---PRPDIVHAHDWHTGLIPALLKekywrGYPDIKTV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 150 FTIH-----------RLNKSKLPAFYFHEAGLselapypdidpEHTGG--------YIADIVTTVSR-----------GY 199
Cdd:PRK00654 151 FTIHnlayqglfpaeILGELGLPAEAFHLEGL-----------EFYGQisflkaglYYADRVTTVSPtyareittpefGY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 200 LIDewGFFRNFEGKITYVFNGIDCSFWN---ESYLT---GSRD-----ERKKSLLSKFGMDEGVTFMF--IGRFDRgQKG 266
Cdd:PRK00654 220 GLE--GLLRARSGKLSGILNGIDYDIWNpetDPLLAanySADDlegkaENKRALQERFGLPDDDAPLFamVSRLTE-QKG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 267 VDVLLKAIE-ILSskkefQEMRFIIIGKGDPELEGWARSLEEKH-GNVKVI---TEMLSREfvreLYGSVDFVIIPSYFE 341
Cdd:PRK00654 297 LDLVLEALPeLLE-----QGGQLVLLGTGDPELEEAFRALAARYpGKVGVQigyDEALAHR----IYAGADMFLMPSRFE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 342 PFGLVALEAMCLGAIPIASAVGGLRDIITN-------ETGILVKAGDPGELANAILKALEL--SRSDLSKFRenckKRAM 412
Cdd:PRK00654 368 PCGLTQLYALRYGTLPIVRRTGGLADTVIDynpedgeATGFVFDDFNAEDLLRALRRALELyrQPPLWRALQ----RQAM 443
|
490
....*....|....*..
3L01_B 413 S--FSWEKSAERYVKAY 427
Cdd:PRK00654 444 AqdFSWDKSAEEYLELY 460
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
4-427 |
9.34e-54 |
|
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: 183.12 E-value: 9.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 4 KVLLLGFEFLPVkVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIGKIRVFGEEVQVKVSYEERGNLRIYRIGGG 83
Cdd:cd03801 1 KILLLSPELPPP-VGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 84 LLDsedvygpgwdglirkavtfgrasvlllndllreeplPDVVHFHDWHTVFAGALIKKYFKIPAVFTIHRLNKSKLPAF 163
Cdd:cd03801 80 LRK------------------------------------FDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 164 Y-FHEAGLSELAPYpdidpehtgGYIADIVTTVS---RGYLIDEWGFFRNfegKITYVFNGIDCSFWnesyltgSRDERK 239
Cdd:cd03801 124 LaAERRLLARAEAL---------LRRADAVIAVSealRDELRALGGIPPE---KIVVIPNGVDLERF-------SPPLRR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 240 KSLLSKfgmdEGVTFMFIGRFDRgQKGVDVLLKAIEILssKKEFQEMRFIIIGKGDPELEGWARSLEEKHGNVkVITEML 319
Cdd:cd03801 185 KLGIPP----DRPVLLFVGRLSP-RKGVDLLLEALAKL--LRRGPDVRLVIVGGDGPLRAELEELELGLGDRV-RFLGFV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 320 SREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKALElSRS 398
Cdd:cd03801 257 PDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDgEGGLVVPPDDVEALADALLRLLA-DPE 335
|
410 420 430
....*....|....*....|....*....|
3L01_B 399 DLSKFRENCKKRAMS-FSWEKSAERYVKAY 427
Cdd:cd03801 336 LRARLGRAARERVAErFSWERVAERLLDLY 365
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
28-424 |
9.77e-43 |
|
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: 154.71 E-value: 9.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 28 SEALASLGHEVLVFTPSHGRFQGEEIgkirvfgeevqvkvsyEERGNLRIYRIGGGLLDsedvygpgwdGLIRKAV---- 103
Cdd:cd03800 31 ARALAELGYQVDIFTRRISPADPEVV----------------EIAPGARVIRVPAGPPE----------YLPKEELwpyl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 104 -TFGRAsvlLLNDLLREEPLPDVVHFHDWHTVFAGALIKKYFKIPAVFTIHRLNKSKlpafYFHEAGLSELAPYPDIDPE 182
Cdd:cd03800 85 eEFADG---LLRFIAREGGRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHSLGRVK----YRHLGAQDTYHPSLRITAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 183 HTGGYIADIVTTVSRGYLIDEWGFFRNFEGKITYVFNGIDCsfwnESYLTGSRDERKKSLLsKFGMDEGVTFmFIGRFDR 262
Cdd:cd03800 158 EQILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDL----ERFFPVDRAEARRARL-LLPPDKPVVL-ALGRLDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 263 gQKGVDVLLKAIEilSSKKEFQEMRFIIIGKGDPEL----EGWARSLEEKHGNVKVITEM--LSREFVRELYGSVDFVII 336
Cdd:cd03800 232 -RKGIDTLVRAFA--QLPELRELANLVLVGGPSDDPlsmdREELAELAEELGLIDRVRFPgrVSRDDLPELYRAADVFVV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 337 PSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKALElSRSDLSKFRENCKKRAMS-F 414
Cdd:cd03800 309 PSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDgRTGLLVDPHDPEALAAALRRLLD-DPALWQRLSRAGLERARAhY 387
|
410
....*....|
3L01_B 415 SWEKSAERYV 424
Cdd:cd03800 388 TWESVADQLL 397
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
5-199 |
4.26e-36 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 132.45 E-value: 4.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 5 VLLLGFEFLP-VKVGGLAEALTAISEALASLGHEVLVFTPSHG-----RFQGEEIGKIRVFGE----EVQVKVSYEERGN 74
Cdd:pfam08323 1 ILFVASEVAPfAKTGGLADVVGALPKALAALGHDVRVIMPRYGnipeeRNQLEDVIRLSVAAGvpvrPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 75 LRIYRIGGG-LLDSEDVYGP---GWDGLIRKAVTFGRASVLLLNDLLREeplPDVVHFHDWHTVFAGALIKKYFK----- 145
Cdd:pfam08323 81 VDVYFLDNPdYFDRPGLYGDdgrDYEDNAERFAFFSRAALELAKKLGWI---PDIIHCHDWHTALVPAYLKEAYAddpfk 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3L01_B 146 -IPAVFTIH-----------RLNKSKLPAFYFHEAGLSElapYPDIDPEHTGGYIADIVTTVSRGY 199
Cdd:pfam08323 158 nIKTVFTIHnlayqgrfpadLLDLLGLPPEDFNLDGLEF---YGQINFLKAGIVYADAVTTVSPTY 220
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
3-427 |
2.06e-33 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 130.99 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 3 MKVLLLGFEFLP-VKVGGLAEALTAISEALASLGHEVLVFTPSH-----GRFQGEEIGKIR-VFGeevqvkvsyeerGNL 75
Cdd:PRK14099 4 LRVLSVASEIFPlIKTGGLADVAGALPAALKAHGVEVRTLVPGYpavlaGIEDAEQVHSFPdLFG------------GPA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 76 RIYRIG-GGL----LDSEDVYG-PG----------W-DGLIRKAvTFGRASVLLLNDLLreeP--LPDVVHFHDWHTVFA 136
Cdd:PRK14099 72 RLLAARaGGLdlfvLDAPHLYDrPGnpyvgpdgkdWpDNAQRFA-ALARAAAAIGQGLV---PgfVPDIVHAHDWQAGLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 137 GALIKkYFKIPA---VFTIHRLN-KSKLPAFYFHEAGLSELA-------PYPDIDPEHTGGYIADIVTTVSRGYLI---- 201
Cdd:PRK14099 148 PAYLH-YSGRPApgtVFTIHNLAfQGQFPRELLGALGLPPSAfsldgveYYGGIGYLKAGLQLADRITTVSPTYALeiqg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 202 DEWG-----FFRNFEGKITYVFNGIDCSFWN---ESYLT--------GSRDERKKSLLSKFGMDEGVTFMFIGRFDR--G 263
Cdd:PRK14099 227 PEAGmgldgLLRQRADRLSGILNGIDTAVWNpatDELIAatydvetlAARAANKAALQARFGLDPDPDALLLGVISRlsW 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 264 QKGVDVLLKAIEILSSkkefQEMRFIIIGKGDPELEGWARSLEEKH-GNVKVIT---EMLSREfvreLYGSVDFVIIPSY 339
Cdd:PRK14099 307 QKGLDLLLEALPTLLG----EGAQLALLGSGDAELEARFRAAAQAYpGQIGVVIgydEALAHL----IQAGADALLVPSR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 340 FEPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAGDPGEL------ANAILKALELSR---SDLSKFReNCKKR 410
Cdd:PRK14099 379 FEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMAIATGVATGVqfspvtADALAAALRKTAalfADPVAWR-RLQRN 457
|
490
....*....|....*....
3L01_B 411 AMS--FSWEKSAERYVKAY 427
Cdd:PRK14099 458 GMTtdVSWRNPAQHYAALY 476
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
251-394 |
3.49e-33 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 121.46 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 251 GVTFMFIGRFDRGQKGVDVLLKAIEILssKKEFQEMRFIIIGKGDP-ELEGWARSLEEK---HGNVKVitemlsrefVRE 326
Cdd:pfam13692 1 RPVILFVGRLHPNVKGVDYLLEAVPLL--RKRDNDVRLVIVGDGPEeELEELAAGLEDRvifTGFVED---------LAE 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3L01_B 327 LYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAGDPGELANAILKALE 394
Cdd:pfam13692 70 LLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLE 137
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
7-395 |
8.14e-31 |
|
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: 120.92 E-value: 8.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 7 LLGFEFLPVkvGGLAEALTAISEALASLGHEVLVFTPshgrfqgeeigkirvfgeevqvkvsyeergnlriyriGGGLLD 86
Cdd:cd03819 2 LMLTPALEI--GGAETYILDLARALAERGHRVLVVTA-------------------------------------GGPLLP 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 87 SEDVYGPGWDGLIRKAVTFGRASVLLLNDLLREEPlpDVVHFHDWHTVFAGALIKKYFKIPAVFTIH-RLNKSKLPAFYF 165
Cdd:cd03819 43 RLRQIGIGLPGLKVPLLRALLGNVRLARLIRRERI--DLIHAHSRAPAWLGWLASRLTGVPLVTTVHgSYLATYHPKDFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 166 HEaglselapypdidpEHTGGYIADIVTTVSRGYLIDEWGFFRnfeGKITYVFNGIDCSFWnesyltgsRDERKKSLLSK 245
Cdd:cd03819 121 LA--------------VRARGDRVIAVSELVRDHLIEALGVDP---ERIRVIPNGVDTDRF--------PPEAEAEERAQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 246 FGMDEGV-TFMFIGRFDRgQKGVDVLLKAIEILSSKKEFqemRFIIIGKGDPELEgwARSLEEKHGNVKVITEMLSREFV 324
Cdd:cd03819 176 LGLPEGKpVVGYVGRLSP-EKGWLLLVDAAAELKDEPDF---RLLVAGDGPERDE--IRRLVERLGLRDRVTFTGFREDV 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3L01_B 325 RELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKALEL 395
Cdd:cd03819 250 PAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHgRTGLLVPPGDAEALADAIRAAKLL 321
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
254-410 |
1.28e-30 |
|
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: 115.45 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 254 FMFIGRFDRgQKGVDVLLKAIEILssKKEFQEMRFIIIGKGDPE--LEGWARSLEEKHgNVKVITEmLSREFVRELYGSV 331
Cdd:pfam00534 5 ILFVGRLEP-EKGLDLLIKAFALL--KEKNPNLKLVIAGDGEEEkrLKKLAEKLGLGD-NVIFLGF-VSDEDLPELLKIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 332 DFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKALELSRSdLSKFRENCKKR 410
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDgETGFLVKPNNAEALAEAIDKLLEDEEL-RERLGENARKR 158
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
4-424 |
4.95e-30 |
|
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: 119.75 E-value: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 4 KVLLLGFEFLPVKVGGlAEALTAISEALASLGHEVLVFTPSHGRFQGEEigkirvfgeevqVKVSYEERGNLRIYRIggg 83
Cdd:cd03794 1 KILLISQYYPPPKGAA-AARVYELAKELVRRGHEVTVLTPSPNYPLGRI------------FAGATETKDGIRVIRV--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 84 lldseDVYGPGWDGLIRKAVTFGRASVLLLNDLLREEPLPDVVHFHDWH--TVFAGALIKKYFKIPAVFTIH-------- 153
Cdd:cd03794 65 -----KLGPIKKNGLIRRLLNYLSFALAALLKLLVREERPDVIIAYSPPitLGLAALLLKKLRGAPFILDVRdlwpesli 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 154 --RLNKSKLPAFYFHEAglsELAPYPDidpehtggyiADIVTTVSRGyLIDEWGFFRNFEGKITYVFNGIDCSFWNESyl 231
Cdd:cd03794 140 alGVLKKGSLLKLLKKL---ERKLYRL----------ADAIIVLSPG-LKEYLLRKGVPKEKIIVIPNWADLEEFKPP-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 232 tgsrdeRKKSLLSKFGMDEGVTFMFIGRFDRGQkGVDVLLKAIEILSSKKEfqeMRFIIIGKGD--PELEGWARslEEKH 309
Cdd:cd03794 204 ------PKDELRKKLGLDDKFVVVYAGNIGKAQ-GLETLLEAAERLKRRPD---IRFLFVGDGDekERLKELAK--ARGL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 310 GNVKVItEMLSREFVRELYGSVDFVIIPSYFEPFGLVA-----LEAMCLGaIPI-ASAVGGLRDIIT-NETGILVKAGDP 382
Cdd:cd03794 272 DNVTFL-GRVPKEEVPELLSAADVGLVPLKDNPANRGSspsklFEYMAAG-KPIlASDDGGSDLAVEiNGCGLVVEPGDP 349
|
410 420 430 440
....*....|....*....|....*....|....*....|...
3L01_B 383 GELANAILKALElSRSDLSKFRENCKKRAMS-FSWEKSAERYV 424
Cdd:cd03794 350 EALADAILELLD-DPELRRAMGENGRELAEEkFSREKLADRLL 391
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
4-427 |
2.06e-29 |
|
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: 117.43 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 4 KVLLLGFEFLPVKVGGlAEALTA-ISEALASLGHEVLVFTPShgrfqgeeigkirvFGEEVQVKVSYEERGNLRIYrigg 82
Cdd:cd03823 1 KILLVNSLYPPQRVGG-AEISVHdLAEALVAEGHEVAVLTAG--------------VGPPGQATVARSVVRYRRAP---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 83 glldSEDVYGPGWDGLIRKAVTFGRASVLLLNDLLREEPlPDVVHFHDWHTVFAGAL--IKKYfKIPAVFTIHrlnkskl 160
Cdd:cd03823 62 ----DETLPLALKRRGYELFETYNPGLRRLLARLLEDFR-PDVVHTHNLSGLGASLLdaARDL-GIPVVHTLH------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 161 pafyfheaglselaPYPDIDPEHT----GGyiaDIVTTVSRgYLID---EWGFFRNfegKITYVFNGIDcsfwNESYLTG 233
Cdd:cd03823 129 --------------DYWLLCPRQFlfkkGG---DAVLAPSR-FTANlheANGLFSA---RISVIPNAVE----PDLAPPP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 234 SRDERkksllskfgmDEGVTFMFIGRFDRgQKGVDVLLKAIEILSskkeFQEMRFIIIGKGD--PELEGWARSLEEKHGN 311
Cdd:cd03823 184 RRRPG----------TERLRFGYIGRLTE-EKGIDLLVEAFKRLP----REDIELVIAGHGPlsDERQIEGGRRIAFLGR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 312 VkvitemlSREFVRELYGSVDFVIIPSYF-EPFGLVALEAMCLGAIPIASAVGGLRDII-TNETGILVKAGDPGELANAI 389
Cdd:cd03823 249 V-------PTDDIKDFYEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIqPGVNGLLFAPGDAEDLAAAM 321
|
410 420 430
....*....|....*....|....*....|....*...
3L01_B 390 LKALElSRSDLSKFRENCKKRAmsfSWEKSAERYVKAY 427
Cdd:cd03823 322 RRLLT-DPALLERLRAGAEPPR---STESQAEEYLKLY 355
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
46-425 |
2.15e-29 |
|
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: 117.46 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 46 GRFQGEEIGKIRVFGEEVQVKVSYEERGNLRIYRIGGGLLDSEDVYGPGWDGLIRKAvtFGRASVLLLNDllreeplPDV 125
Cdd:cd03809 17 GRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLR--WLQILLPKKDK-------PDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 126 VHFHDWhtvfagALIKKYFKIPAVFTIHRLNKSKLPAFY------FHEAGLSELAPYpdidpehtggyiADIVTTVS--- 196
Cdd:cd03809 88 LHSPHN------TAPLLLKGCPQVVTIHDLIPLRYPEFFpkrfrlYYRLLLPISLRR------------ADAIITVSeat 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 197 RGYLIDewgFFRNFEGKITYVFNGIDCSFwnesyltgSRDERKKSLLSKFGMDEGvTFMFIGRFDRgQKGVDVLLKAIEI 276
Cdd:cd03809 150 RDDIIK---FYGVPPEKIVVIPLGVDPSF--------FPPESAAVLIAKYLLPEP-YFLYVGTLEP-RKNHERLLKAFAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 277 LssKKEFQEMRFIIIGKGDPELEGWARSLEEKHGNVKVI-TEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGA 355
Cdd:cd03809 217 L--KKQGGDLKLVIVGGKGWEDEELLDLVKKLGLGGRVRfLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGT 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3L01_B 356 IPIASAVGGLRdIITNETGILVKAGDPGELANAILKALElsRSDL-SKFRENCKKRAMSFSWEKSAERYVK 425
Cdd:cd03809 295 PVIASNISVLP-EVAGDAALYFDPLDPESIADAILRLLE--DPSLrEELIRKGLERAKKFSWEKTAEKTLE 362
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
5-427 |
9.93e-29 |
|
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: 115.94 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 5 VLLLGFEFLPVKVGGLAEALTAISEALASLGHEVLVFTPSHGrfqgeeiGKIRVFGEEVQVKVSYEERGNLRIYRigggl 84
Cdd:cd03798 1 VLILTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLAPAPW-------GPAAARLLRKLLGEAVPPRDGRRLLP----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 85 ldsedvYGPGWDGLIRKavtfgRASvlLLNDLL--REEPLPDVVHFH-DWHTVFAGALIKKYFKIPAVFTIHRlnksklp 161
Cdd:cd03798 69 ------LKPRLRLLAPL-----RAP--SLAKLLkrRRRGPPDLIHAHfAYPAGFAAALLARLYGVPYVVTEHG------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 162 afyfheAGLSELAPYPDIDPEHtgGYI---ADIVTTVSRgYLIDEWGFFRNFEGKITYVFNGIDcsfwnESYLTGSRDER 238
Cdd:cd03798 129 ------SDINVFPPRSLLRKLL--RWAlrrAARVIAVSK-ALAEELVALGVPRDRVDVIPNGVD-----PARFQPEDRGL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 239 KKSLlskfgmdEGVTFMFIGRFdRGQKGVDVLLKAIEILssKKEFQEMRFIIIGKGdPELEGWARSLEEKHGNVKVI-TE 317
Cdd:cd03798 195 GLPL-------DAFVILFVGRL-IPRKGIDLLLEAFARL--AKARPDVVLLIVGDG-PLREALRALAEDLGLGDRVTfTG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 318 MLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKALElS 396
Cdd:cd03798 264 RLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDpETGLLVPPGDADALAAALRRALA-E 342
|
410 420 430
....*....|....*....|....*....|.
3L01_B 397 RSDLSKFRENCKKRAMSFSWEKSAERYVKAY 427
Cdd:cd03798 343 PYLRELGEAARARVAERFSWVKAADRIAAAY 373
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
4-428 |
3.45e-28 |
|
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: 114.31 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 4 KVLLLGFEFLPVkVGGLAEALTAISEALASLGHEVLVFTP-SHGRFQGEEIGKIRVFGeevqvkVSYEERGNLRIyrigg 82
Cdd:cd03814 1 RIALVTDTYHPQ-VNGVVRTLERLVDHLRRRGHEVRVVAPgPFDEAESAEGRVVSVPS------FPLPFYPEYRL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 83 glldsedVYGPGWdGLIRKAVTFGrasvlllndllreeplPDVVHFHDWHTV-FAGALIKKYFKIPAVFTIHrlnkSKLP 161
Cdd:cd03814 69 -------ALPLPR-RVRRLIKEFQ----------------PDIIHIATPGPLgLAALRAARRLGLPVVTSYH----TDFP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 162 AF--YFHEAGLSELAP------YPDIDpehtggyiADIVTTVSRGYLIDEWGFFRnfegkITYVFNGIDCSFWNESyltg 233
Cdd:cd03814 121 EYlsYYTLGPLSWLAWaylrwfHNPFD--------TTLVPSPSIARELEGHGFER-----VRLWPRGVDTELFHPS---- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 234 srdERKKSLLSKFGMDEGVTFMFIGRFDRgQKGVDVLLKAIEILSSKKEFqemRFIIIGKGdPELEgwarSLEEKHGNVk 313
Cdd:cd03814 184 ---RRDAALRRRLGPPGRPLLLYVGRLAP-EKNLEALLDADLPLAASPPV---RLVVVGDG-PARA----ELEARGPDV- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 314 VITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILkA 392
Cdd:cd03814 251 IFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPgGTGALVEPGDAAAFAAALR-A 329
|
410 420 430
....*....|....*....|....*....|....*.
3L01_B 393 LELSRSDLSKFRENCKKRAMSFSWEKSAERYVKAYA 428
Cdd:cd03814 330 LLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
12-427 |
1.06e-27 |
|
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: 113.14 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 12 FLPvKVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIGKIRvfgeevqvkvsyeergnlRIYRIGGGLLDSEDVY 91
Cdd:cd03817 9 YLP-QVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRY------------------RSFSIPIRKYHRQHIP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 92 GPGWDGLIRKAVTFGrasvlllndllreeplPDVVHFHdwhTVF----AGALIKKYFKIPAVFTIHrlnksKLPAFYFHE 167
Cdd:cd03817 70 FPFKKAVIDRIKELG----------------PDIIHTH---TPFslgkLGLRIARKLKIPIVHTYH-----TMYEDYLHY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 168 AGLSELAPYPDIDP---EHTGGyiADIVTTVSRG---YLIDewgffRNFEGKITYVFNGIDCSFWNESyltGSRDERKKS 241
Cdd:cd03817 126 IPKGKLLVKAVVRKlvrRFYNH--TDAVIAPSEKikdTLRE-----YGVKGPIEVIPNGIDLDKFEKP---LNTEERRKL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 242 LLSkfgmDEGVTFMFIGRFDRgQKGVDVLLKAIEILSSKKEFqemRFIIIGKGD--PELEGWARSLEeKHGNVkVITEML 319
Cdd:cd03817 196 GLP----PDEPILLYVGRLAK-EKNIDFLLRAFAELKKEPNI---KLVIVGDGPerEELKELARELG-LADKV-IFTGFV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 320 SREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPgELANAILKALELSRS 398
Cdd:cd03817 266 PREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDgENGFLFEPNDE-TLAEKLLHLRENLEL 344
|
410 420
....*....|....*....|....*....
3L01_B 399 dLSKFRENCKKRAMSFSWEKSAERYVKAY 427
Cdd:cd03817 345 -LRKLSKNAEISAREFAFAKSVEKLYEEV 372
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
109-423 |
4.93e-27 |
|
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: 110.76 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 109 SVLLLNDLLREEPlPDVVHFHDWHTVFAGALIKKYFKIPA-VFTIHRLnksklpAFYFHEAGLSELAPYPdidPEHTGGY 187
Cdd:cd03808 69 ALFKLYKLLKKEK-PDIVHCHTPKPGILGRLAARLAGVPKvIYTVHGL------GFVFTEGKLLRLLYLL---LEKLALL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 188 IADIVTTVS---RGYLIDEwgFFRNFEGKITYVFNGIDCSFWNESyltgsrderkksllSKFGMDEGVTFMFIGRFDRgQ 264
Cdd:cd03808 139 FTDKVIFVNeddRDLAIKK--GIIKKKKTVLIPGSGVDLDRFQYS--------------PESLPSEKVVFLFVARLLK-D 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 265 KGVDVLLKAIEILSSKKEfqEMRFIIIGKGDPELEgwARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFG 344
Cdd:cd03808 202 KGIDELIEAAKILKKKGP--NVRFLLVGDGELENP--SEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 345 LVALEAMCLGAIPIASAVGGLRDIIT-NETGILVKAGDPGELANAILKaLELSRSDLSKFRENCKKRA-MSFSWEKSAER 422
Cdd:cd03808 278 RSLLEAMAAGRPVITTDVPGCRELVIdGVNGFLVPPGDVEALADAIEK-LIEDPELRKEMGEAARKRVeEKFDEEKVVNK 356
|
.
3L01_B 423 Y 423
Cdd:cd03808 357 L 357
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
322-428 |
1.67e-26 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 103.15 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 322 EFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKALElSRSDL 400
Cdd:COG0438 12 LLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDgETGLLVPPGDPEALAEAILRLLE-DPELR 90
|
90 100
....*....|....*....|....*....
3L01_B 401 SKFRENCKKRAMS-FSWEKSAERYVKAYA 428
Cdd:COG0438 91 RRLGEAARERAEErFSWEAIAERLLALYE 119
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
11-427 |
5.94e-26 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 110.76 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 11 EFLPV-KVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIGKIRVFGEEVQvkvSYEErGNLRIYRIGGGLLDSED 89
Cdd:PLN02939 490 EMAPVaKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKVLDVVVE---SYFD-GNLFKNKIWTGTVEGLP 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 90 VY-----GPG---WDGLI-------RKAVTFGRASVLLLndlLREEPLPDVVHFHDWHTVFAGALikkYFKIPA------ 148
Cdd:PLN02939 566 VYfiepqHPSkffWRAQYygehddfKRFSYFSRAALELL---YQSGKKPDIIHCHDWQTAFVAPL---YWDLYApkgfns 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 149 ---VFTIHRLN-KSKLPAFYFHEAGLS-ELAPYPDIDPEHTGGYI---------ADIVTTVSRGY-----------LIDE 203
Cdd:PLN02939 640 ariCFTCHNFEyQGTAPASDLASCGLDvHQLDRPDRMQDNAHGRInvvkgaivySNIVTTVSPTYaqevrseggrgLQDT 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 204 WGFF-RNFEGkityVFNGIDCSFWNESY------------LTGsRDERKKSLLSKFGM-DEGVTFMFIGRFDR--GQKGV 267
Cdd:PLN02939 720 LKFHsKKFVG----ILNGIDTDTWNPSTdrflkvqynandLQG-KAANKAALRKQLGLsSADASQPLVGCITRlvPQKGV 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 268 DVLLKAIeilsskKEFQEM--RFIIIGKG-----DPELEGWARSLEeKHGNVKVI---TEMLSREfvreLYGSVDFVIIP 337
Cdd:PLN02939 795 HLIRHAI------YKTAELggQFVLLGSSpvphiQREFEGIADQFQ-SNNNIRLIlkyDEALSHS----IYAASDMFIIP 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 338 SYFEPFGLVALEAMCLGAIPIASAVGGLRDI---ITNET-------GILVKAGDPGELANAILKALELSRSDLSKFRENC 407
Cdd:PLN02939 864 SMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSvfdFDDETipvelrnGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLV 943
|
490 500
....*....|....*....|.
3L01_B 408 KK-RAMSFSWEKSAERYVKAY 427
Cdd:PLN02939 944 QKdMNIDFSWDSSASQYEELY 964
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
108-427 |
9.96e-25 |
|
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: 104.32 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 108 ASVLLLNDLLREEPlPDVVHFHDWHTVFAGALIKKYFKIPAVF-TIHRLN--KSKLPAFYFHEAGLSelapypdidpeht 184
Cdd:cd03807 66 GVLLRLAKLIRKRN-PDVVHTWMYHADLIGGLAAKLAGGVKVIwSVRSSNipQRLTRLVRKLCLLLS------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 185 gGYIADIVTTVSR-GYLIDEWGFFRNfegKITYVFNGIDCSFWNESyltgsrDERKKSLLSKFGMDEGVT-FMFIGRFdR 262
Cdd:cd03807 132 -KFSPATVANSSAvAEFHQEQGYAKN---KIVVIYNGIDLFKLSPD------DASRARARRRLGLAEDRRvIGIVGRL-H 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 263 GQKGVDVLLKAIEILssKKEFQEMRFIIIGKGD--PELEgwaRSLEEKH--GNVKVITEmlsREFVRELYGSVDFVIIPS 338
Cdd:cd03807 201 PVKDHSDLLRAAALL--VETHPDLRLLLVGRGPerPNLE---RLLLELGleDRVHLLGE---RSDVPALLPAMDIFVLSS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 339 YFEPFGLVALEAMCLGaIP-IASAVGGLRDIITNETGILVKAGDPGELANAILKALELsRSDLSKFRENCKKRAMS-FSW 416
Cdd:cd03807 273 RTEGFPNALLEAMACG-LPvVATDVGGAAELVDDGTGFLVPAGDPQALADAIRALLED-PEKRARLGRAARERIANeFSI 350
|
330
....*....|.
3L01_B 417 EKSAERYVKAY 427
Cdd:cd03807 351 DAMVRRYETLY 361
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
1-427 |
4.52e-24 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 104.05 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 1 RHMKVLLLGFEFLP-VKVGGLAEALTAISEALASLGHEVLVFTPSHG-----RFQGEEIgkIRVFGEEV---------QV 65
Cdd:PRK14098 4 RNFKVLYVSGEVSPfVRVSALADFMASFPQALEEEGFEARIMMPKYGtindrKFRLHDV--LRLSDIEVplkektdllHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 66 KVS------------YEERGNLRiyrigGGLLdsEDVY-GPGWDGLIRKAVTFgraSVLLLNDLLREEPLPDVVHFHDWH 132
Cdd:PRK14098 82 KVTalpsskiqtyflYNEKYFKR-----NGLF--TDMSlGGDLKGSAEKVIFF---NVGVLETLQRLGWKPDIIHCHDWY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 133 TVFAGALIK------KYFK-IPAVFTIHRLNKSKLpafyFHEAGLSELAPYPDIDPEH----------TGGYIADIVTTV 195
Cdd:PRK14098 152 AGLVPLLLKtvyadhEFFKdIKTVLTIHNVYRQGV----LPFKVFQKLLPEEVCSGLHregdevnmlyTGVEHADLLTTT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 196 SRGYL-------IDEWGFFRNFEG---KITYVFNGIDCSFWNES--------YLTGSRDER---KKSLLSKFGM--DEGV 252
Cdd:PRK14098 228 SPRYAeeiagdgEEAFGLDKVLEErkmRLHGILNGIDTRQWNPStdklikkrYSIERLDGKlenKKALLEEVGLpfDEET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 253 TFM-FIGRFDRGQkGVDVLLKAIEILSSkkefQEMRFIIIGKGDPELEGWARSLEEKH-GNVKVITEmLSREFVRELYGS 330
Cdd:PRK14098 308 PLVgVIINFDDFQ-GAELLAESLEKLVE----LDIQLVICGSGDKEYEKRFQDFAEEHpEQVSVQTE-FTDAFFHLAIAG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 331 VDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNE-----TGILVKAGDPGELANAILKALELSrSDLSKFRE 405
Cdd:PRK14098 382 LDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVsedkgSGFIFHDYTPEALVAKLGEALALY-HDEERWEE 460
|
490 500
....*....|....*....|....
3L01_B 406 nCKKRAMS--FSWEKSAERYVKAY 427
Cdd:PRK14098 461 -LVLEAMErdFSWKNSAEEYAQLY 483
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
18-424 |
3.04e-22 |
|
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: 97.44 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 18 GGLAEALTAISEALASLGHEVLVFT--PSHGRFQGEEIGKIRVfGEEVQVKVSYEERGNLRIyriggglldsedVYGPGw 95
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIVStgDGYESLVVEENGRYIP-PQDGFASIPLLRQGAGRT------------DFSPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 96 dglirkavtfgrasvlLLNDLLREEPLPDVVHFHDWHTVFAGALIK--KYFKIPAVFTIHrlnkSKLPAFYFHEAGLSEL 173
Cdd:cd03821 80 ----------------LPNWLRRNLREYDVVHIHGVWTYTSLAACKlaRRRGIPYVVSPH----GMLDPWALQQKHWKKR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 174 APYPDIDPEHTGGYIADIVTTVSrgylIDEWGFFRNFEGKITYVFNGIDCSFWNesylTGSRDERKKSLLskfgmDEGVT 253
Cdd:cd03821 140 IALHLIERRNLNNAALVHFTSEQ----EADELRRFGLEPPIAVIPNGVDIPEFD----PGLRDRRKHNGL-----EDRRI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 254 FMFIGRFDRgQKGVDVLLKAIEILSskKEFQEMRFIIIGKGDPELEGWARSLEEKHGNVKV-ITEMLSREFVRELYGSVD 332
Cdd:cd03821 207 ILFLGRIHP-KKGLDLLIRAARKLA--EQGRDWHLVIAGPDDGAYPAFLQLQSSLGLGDRVtFTGPLYGEAKWALYASAD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 333 FVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAgDPGELANAILKALELsRSDLSKFREN---CKK 409
Cdd:cd03821 284 LFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDP-NVSSLAEALAEALRD-PADRKRLGEMarrARQ 361
|
410
....*....|....*
3L01_B 410 RAMSFSWEKSAERYV 424
Cdd:cd03821 362 VEENFSWEAVAGQLG 376
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
4-409 |
6.85e-22 |
|
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: 96.27 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 4 KVLLLGFEFlpvKVGGLAEALTAISEALASLGHEVLVFtpshgrfqgeeigkirvfgeevqvkvSYEERGNLRIyriggg 83
Cdd:cd03811 1 KILFVIPSL---SGGGAERVLLNLANALDKRGYDVTLV--------------------------LLRDEGDLDK------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 84 LLDSEDVYGPGWDGLIRKAVTFGRASVLLLNDLLREEPlPDVVH-FHDWHTVFAGALIKkyFKIPAVFTIHrlnksklpa 162
Cdd:cd03811 46 QLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILKRAK-PDVVIsFLGFATYIVAKLAA--ARSKVIAWIH--------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 163 FYFHEAGLSELAPYPDIDpehtGGYIADIVTTVSRGylIDEW--GFFRNFEGKITYVFNGIDCSfwnesyltgsrDERKK 240
Cdd:cd03811 114 SSLSKLYYLKKKLLLKLK----LYKKADKIVCVSKG--IKEDliRLGPSPPEKIEVIYNPIDID-----------RIRAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 241 SLLSKFGMDEGV-TFMFIGRFDRgQKGVDVLLKAIEILssKKEFQEMRFIIIGKGDP--ELEGWARSLEEKHgnvKVIte 317
Cdd:cd03811 177 AKEPILNEPEDGpVILAVGRLDP-QKGHDLLIEAFAKL--RKKYPDVKLVILGDGPLreELEKLAKELGLAE---RVI-- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 318 mlsreF------VRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELAnAIL 390
Cdd:cd03811 249 -----FlgfqsnPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDgENGLLVPDGDAAALA-GIL 322
|
410
....*....|....*....
3L01_B 391 KALELSRSDLsKFRENCKK 409
Cdd:cd03811 323 AALLQKKLDA-ALRERLAK 340
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
229-377 |
1.37e-20 |
|
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: 90.16 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 229 SYLTGSRDERKKSLLSKFGMDEGVTFMFIGRFDrGQKGVDVLLKAIEILssKKEFQEMRFIIIGKGDPELEGWARSLEEK 308
Cdd:cd01635 88 PDSLESTRSELLALARLLVSLPLADKVSVGRLV-PEKGIDLLLEALALL--KARLPDLVLVLVGGGGEREEEEALAAALG 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3L01_B 309 HG-NVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIIT-NETGILV 377
Cdd:cd01635 165 LLeRVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVdGENGLLV 235
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
3-427 |
7.95e-20 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 92.24 E-value: 7.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 3 MKVLLLGFEFLPV-KVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIgkirvfgEEVQVKVSYEeRGNLRIyRIG 81
Cdd:PLN02316 588 MHIVHIAVEMAPIaKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHV-------KDLHYQRSYS-WGGTEI-KVW 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 82 GGLLDSEDVY------GPGWDGLI----RKAVTFGRASVLLLNDLLREEPLPDVVHFHDWHTVFAGALIKKYFKIPA--- 148
Cdd:PLN02316 659 FGKVEGLSVYflepqnGMFWAGCVygcrNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGlsk 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 149 ---VFTIHRLNksklpafyFHEAGLSELAPYpdidpehtggyiADIVTTVSRGYLIDEWG------FFRNFEGkityVFN 219
Cdd:PLN02316 739 arvVFTIHNLE--------FGANHIGKAMAY------------ADKATTVSPTYSREVSGnsaiapHLYKFHG----ILN 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 220 GIDCSFWN-------------ESYLTGSRdERKKSLLSKFGMDEgVTFMFIGRFDR--GQKGVDVLLKAI-EILSSKKEF 283
Cdd:PLN02316 795 GIDPDIWDpyndnfipvpytsENVVEGKR-AAKEALQQRLGLKQ-ADLPLVGIITRltHQKGIHLIKHAIwRTLERNGQV 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 284 qemrfIIIGKG-DPELEG----WARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPI 358
Cdd:PLN02316 873 -----VLLGSApDPRIQNdfvnLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPV 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 359 ASAVGGLRDIITN--------------ETGILVKAGDPGELANAILKALELSRSDLSKFRENCkKRAMS--FSWEKSAER 422
Cdd:PLN02316 948 VRKTGGLFDTVFDvdhdkeraqaqglePNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLC-KRVMEqdWSWNRPALD 1026
|
....*
3L01_B 423 YVKAY 427
Cdd:PLN02316 1027 YMELY 1031
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
211-427 |
1.16e-19 |
|
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: 89.70 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 211 EGKITYVFNGIDCSFWNEsylTGSRDERKKSLLSK------FGmDEGVTFMFigrfdrgqKGVDVLLKAIEILSSKKEFQ 284
Cdd:cd03825 160 GLPVVVIPNGIDTEIFAP---VDKAKARKRLGIPQdkkvilFG-AESVTKPR--------KGFDELIEALKLLATKDDLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 285 emrFIIIGKGDPELegwaRSLEEKHGNVKVITEMLSrefVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGG 364
Cdd:cd03825 228 ---LVVFGKNDPQI----VILPFDIISLGYIDDDEQ---LVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGG 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3L01_B 365 LRDIITN-ETGILVKAGDPGELANAIlKALELSRSDLSKFRENCKKRAM-SFSWEKSAERYVKAY 427
Cdd:cd03825 298 SPEIVQHgVTGYLVPPGDVQALAEAI-EWLLANPKERESLGERARALAEnHFDQRVQAQRYLELY 361
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
189-425 |
3.17e-19 |
|
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: 88.45 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 189 ADIVTTVSRGYLIDEWGFFRNfegKITYVFNgidcsfwnesYLTGSRDERKKSLLSKfgmdegvTFMFIGRFDRgQKGVD 268
Cdd:cd03820 139 ADKIVVLTEADKLKKYKQPNS---NVVVIPN----------PLSFPSEEPSTNLKSK-------RILAVGRLTY-QKGFD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 269 VLLKAIEILssKKEFQEMRFIIIGKGD--PELEGWARS--LEEK---HGNVKVItemlsrefvRELYGSVDFVIIPSYFE 341
Cdd:cd03820 198 LLIEAWALI--AKKHPDWKLRIYGDGPerEELEKLIDKlgLEDRvklLGPTKNI---------AEEYANSSIFVLSSRYE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 342 PFGLVALEAMCLGAIPIASA-VGGLRDIITN-ETGILVKAGDPGELANAILKALElSRSDLSKFRENCKKRAMSFSWEKS 419
Cdd:cd03820 267 GFPMVLLEAMAYGLPIISFDcPTGPSEIIEDgENGLLVPNGDVDALAEALLRLME-DEELRKKMGKNARKNAERFSIEKI 345
|
....*.
3L01_B 420 AERYVK 425
Cdd:cd03820 346 IKQWEE 351
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
190-428 |
2.85e-17 |
|
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: 82.78 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 190 DIVTTVSrGYLIDEwgFFRNFE--GKITYVFNGIDCSFWnesyltgSRDERKKSLLSKFGMDEGVTFMFIGRFDRGQKGV 267
Cdd:cd04962 143 DRVTAVS-SSLRQE--TYELFDvdKDIEVIHNFIDEDVF-------KRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRID 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 268 DVllkaIEILSSKKEFQEMRFIIIGKGdPELEGwARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVA 347
Cdd:cd04962 213 DV----VRVFARVRRKIPAKLLLVGDG-PERVP-AEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 348 LEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKALELSRSdLSKFRENCKKRAMS-FSWEKSAERYVK 425
Cdd:cd04962 287 LEAMACGVPVVSSNAGGIPEVVKHgETGFLSDVGDVDAMAKSALSILEDDEL-YNRMGRAARKRAAErFDPERIVPQYEA 365
|
...
3L01_B 426 AYA 428
Cdd:cd04962 366 YYR 368
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
4-428 |
1.33e-16 |
|
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: 80.41 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 4 KVLLLG--FEFLPVKVGGLAEA-LTAISEALASLGHEVLVFTP--SHGRFQGEE-IGKIRVFGEEVQVKVSYEERGNLRI 77
Cdd:cd03802 1 RIAQVSppRGPVPPGKYGGTELvVSALTEGLVRRGHEVTLFAPgdSHTSAPLVAvIPRALRLDPIPQESKLAELLEALEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 78 YriggglLDSEDVygpgwdglirkavtfgrasvlllndllreeplpDVVHFH--DWHTVFAGaLIKKyfkiPAVFTIHrl 155
Cdd:cd03802 81 Q------LRASDF---------------------------------DVIHNHsyDWLPPFAP-LIGT----PFVTTLH-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 156 nksklpafyfheaGLSELAPYPDIDPEHTGGYIAdiVTTVSRgyliDEWGFFRnfegKITYVFNGIDCSFWnesyltGSR 235
Cdd:cd03802 115 -------------GPSIPPSLAIYAAEPPVNYVS--ISDAQR----AATPPID----YLTVVHNGLDPADY------RFQ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 236 DERKKSLLskfgmdegvtfmFIGRFDRgQKGVDVllkAIEILSSKKefqeMRFIIIGKGDPELEgwARSLEEKH--GNVK 313
Cdd:cd03802 166 PDPEDYLA------------FLGRIAP-EKGLED---AIRVARRAG----LPLKIAGKVRDEDY--FYYLQEPLpgPRIE 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 314 VITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIIT-NETGILVKagDPGELANAILKA 392
Cdd:cd03802 224 FIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQhGETGFLVD--SVEEMAEAIANI 301
|
410 420 430
....*....|....*....|....*....|....*..
3L01_B 393 LELSrsdlskfRENCKKRAM-SFSWEKSAERYVKAYA 428
Cdd:cd03802 302 DRID-------RAACRRYAEdRFSAARMADRYEALYR 331
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
189-424 |
2.75e-15 |
|
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: 76.54 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 189 ADIVTTVSRGYLiDEWGFFRNFEGKITYVFNGIDCSFWNESYLTGSRDERKKsllsKFGMDegvtFMFIGRFdRGQKGVD 268
Cdd:cd03795 138 ADRIIATSPNYV-ETSPTLREFKNKVRVIPLGIDKNVYNIPRVDFENIKREK----KGKKI----FLFIGRL-VYYKGLD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 269 VLLKAIEILsskkefqEMRFIIIGKGD--PELEgwARSLEEKHGNVKVITEMLSREFVrELYGSVDFVIIPSYF--EPFG 344
Cdd:cd03795 208 YLIEAAQYL-------NYPIVIGGEGPlkPDLE--AQIELNLLDNVKFLGRVDDEEKV-IYLHLCDVFVFPSVLrsEAFG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 345 LVALEAMCLGAIPIASAVGGLRDIITN--ETGILVKAGDPGELANAILKALElSRSDLSKFRENCKKRamsFSWEKSAER 422
Cdd:cd03795 278 IVLLEAMMCGKPVISTNIGTGVPYVNNngETGLVVPPKDPDALAEAIDKLLS-DEELRESYGENAKKR---FEELFTAEK 353
|
..
3L01_B 423 YV 424
Cdd:cd03795 354 MK 355
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
123-410 |
4.41e-15 |
|
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: 76.33 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 123 PDVVHFHDWHT-VFAGALIKKYFKIPAVFTIHRLNksklpafyfhEAGLSELAPYPDIDpehtggYIADIVTTVSR---G 198
Cdd:cd04951 80 PDVVHSHMFHAnIFARFLRMLYPIPLLICTAHNKN----------EGGRIRMFIYRLTD------FLCDITTNVSRealD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 199 YLIDEWGFFRNfegKITYVFNGIDCSFWNESyltgsrDERKKSLLSKFGM--DEGVtFMFIGRFDRGQKGVDVLLKAIEI 276
Cdd:cd04951 144 EFIAKKAFSKN---KSVPVYNGIDLNKFKKD------INVRLKIRNKLNLknDEFV-ILNVGRLTEAKDYPNLLLAISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 277 LSSKKEFqemRFIIIGkgdpelEGWARS-LEEKHGNVKVITEML---SREFVRELYGSVDFVIIPSYFEPFGLVALEAMC 352
Cdd:cd04951 214 ILSKNDF---KLLIAG------DGPLRNeLERLICNLNLVDRVIllgQISNISEYYNAADLFVLSSEWEGFGLVVAEAMA 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
3L01_B 353 LGAIPIASAVGGLRDIITNETGIlVKAGDPGELANAILKALELS---RSDLSKFRENCKKR 410
Cdd:cd04951 285 CERPVVATDAGGVAEVVGDHNYV-VPVSDPQLLAEKIKEIFDMSdeeRDILGNKNEYIAKN 344
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
18-224 |
5.11e-15 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 72.57 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 18 GGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIGKIRVFgeevqvkvsyeergnlriyriggglldsedvygPGWDG 97
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRV---------------------------------PRVPL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 98 LIRKAVTFGRASVLLLNDLLREEPlPDVVHFHDWHTVFAGAL-IKKYFKIPAVFTIHRLNKSKLPAFYFHEAGLSELAPY 176
Cdd:pfam13439 48 PLPPRLLRSLAFLRRLRRLLRRER-PDVVHAHSPFPLGLAALaARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
3L01_B 177 pdidpEHTGGYIADIVTTVS---RGYLIDEWGFFRnfeGKITYVFNGIDCS 224
Cdd:pfam13439 127 -----ERRLLRRADRVIAVSeavADELRRLYGVPP---EKIRVIPNGVDLE 169
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
18-428 |
1.64e-14 |
|
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: 74.36 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 18 GGLAEALtAISEALASLGHEVLVFTPSHGRFQGEEIGKIRVfgeeVQVKVSYEERGNLRIyrIGGGLLDSEDVYGPGWDg 97
Cdd:TIGR04047 13 GGVVHTL-ELAEALTALGHDVTVWALAADGFGFFRDPPCAV----RLVPVAPAPGDTDAM--VEQRIARSIDHLRAHFA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 98 lirkavtfgrasvlllndllreePLPDVVHFHDWHTVFAGALIKKYFKIP-AVFTIHRLNKSKLPAFY-FHEAGLSElap 175
Cdd:TIGR04047 85 -----------------------RGFDVVHAQDCISGNALATLRAEGLIPgFVRTVHHLDDFDDPRLAaCQERAIVE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 176 ypdidpehtggyiADIVTTVSRGY---LIDEWGFfrnfegKITYVFNGIDCSFWNESyltgsRDERKKSLLSKFGMDEGV 252
Cdd:TIGR04047 139 -------------ADAVLCVSAAWaaeLRAEWGI------DATVVPNGVDAARFSPA-----ADAADAALRRRLGLRGGP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 253 TFMFIGRFDRgQKGVDVLLKAIEILssKKEFQEMRFIIIGKG-----DP---ELEGWARSLEEKHGNVkVITEMLSREFV 324
Cdd:TIGR04047 195 YVLAVGGIEP-RKNTIDLLEAFALL--RARRPQAQLVIAGGAtlfdyDAyrrEFRARAAELGVDPGPV-VITGPVPDADL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 325 RELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAGDPGELANAILKALElsRSDLSKFR 404
Cdd:TIGR04047 271 PALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRFDAAWADPSDPDSIADALALALD--PARRPALR 348
|
410 420
....*....|....*....|....
3L01_B 405 ENCKKRAMSFSWEKSAERYVKAYA 428
Cdd:TIGR04047 349 AAGPELAARYTWDASARAHLEFYR 372
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
213-427 |
2.61e-14 |
|
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: 74.29 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 213 KITYVFNGIDCSFWnesylTGSRDERKKSllskfgmdEGVTFMFIGRFDRgQKGVDVLLKAIEILSSKKEfqEMRFIIIG 292
Cdd:cd03813 268 KTRVIPNGIDIQRF-----APAREERPEK--------EPPVVGLVGRVVP-IKDVKTFIRAFKLVRRAMP--DAEGWLIG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 293 --KGDPELE----GWARSLEEKhGNVKviteMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLR 366
Cdd:cd03813 332 peDEDPEYAqeckRLVASLGLE-NKVK----FLGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCR 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3L01_B 367 DII------TNETGILVKAGDPGELANAILKALElSRSDLSKFRENCKKRAMS-FSWEKSAERYVKAY 427
Cdd:cd03813 407 ELIygaddaLGQAGLVVPPADPEALAEALIKLLR-DPELRQAFGEAGRKRVEKyYTLEGMIDSYRKLY 473
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
247-428 |
1.33e-12 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 69.35 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 247 GMDEGVTFMFIGRFDRgQKGVDVLLKAIEILSskkefqEMRFIIIGKGdPElegwaRSLEEKH--GNVKVITEMLSREFV 324
Cdd:PLN02871 259 GEPEKPLIVYVGRLGA-EKNLDFLKRVMERLP------GARLAFVGDG-PY-----REELEKMfaGTPTVFTGMLQGDEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 325 RELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNE----TGILVkagDPGELANAILKALELSRSDl 400
Cdd:PLN02871 326 SQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDqegkTGFLY---TPGDVDDCVEKLETLLADP- 401
|
170 180 190
....*....|....*....|....*....|....*..
3L01_B 401 sKFRENCKKRAMS----FSWEKSA-----ERYVKAYA 428
Cdd:PLN02871 402 -ELRERMGAAAREevekWDWRAATrklrnEQYSAAIW 437
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
206-425 |
7.25e-12 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 66.35 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 206 FFRNF--EGKITYVFNGIDcsfwNESYltgsRDERKKSLLSKFGMDEGVTFMFI-GRFDRgQKGVDVLLKAIEILssKKE 282
Cdd:PRK15484 153 FYEERlpNADISIVPNGFC----LETY----QSNPQPNLRQQLNISPDETVLLYaGRISP-DKGILLLMQAFEKL--ATA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 283 FQEMRFIIIGkgDPelegWARSLEEKHGNVKVITEMLSR-------------EFVRELYGSVDFVIIPSYF-EPFGLVAL 348
Cdd:PRK15484 222 HSNLKLVVVG--DP----TASSKGEKAAYQKKVLEAAKRigdrcimlggqppEKMHNYYPLADLVVVPSQVeEAFCMVAV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 349 EAMCLGAIPIASAVGGLRD-IITNETGI-LVKAGDPGELANAILKAleLSRSDLSKFRENCKKRAMS-FSWEKSAERYVK 425
Cdd:PRK15484 296 EAMAAGKPVLASTKGGITEfVLEGITGYhLAEPMTSDSIISDINRT--LADPELTQIAEQAKDFVFSkYSWEGVTQRFEE 373
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
123-427 |
1.15e-11 |
|
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: 65.87 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 123 PDVVHFHDWHTVFAGALI------KKYFKIPAVFTIHRlnksklpafYFHEAGLSELAPYpdidpehtggYIADIVTTVS 196
Cdd:cd03822 76 PDVVHIQHEFGIFGGKYGlyalglLLHLRIPVITTLHT---------VLDLSDPGKQALK----------VLFRIATLSE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 197 RgyLIDEWGFFRNFEGKItYVFNGIDCSFWN---ESYLTGSRDERKKSLLSKfgmDEGVTFMFiGRFDRGqKGVDVLLKA 273
Cdd:cd03822 137 R--VVVMAPISRFLLVRI-KLIPAVNIEVIPhgvPEVPQDPTTALKRLLLPE---GKKVILTF-GFIGPG-KGLEILLEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 274 IEILssKKEFQEMRFIIIGKGDPELEG------WARSLEEK--HGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGL 345
Cdd:cd03822 209 LPEL--KAEFPDVRLVIAGELHPSLARyegeryRKAAIEELglQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 346 --VALEAMCLGAIPIASAVGGLRDIITNETGILVKAGDPGELANAILKALELSRSdLSKFRENCKKRAMSFSWEKSAERY 423
Cdd:cd03822 287 sgTLSYAIACGKPVISTPLRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDER-RQAIAERAYAYARAMTWESIADRY 365
|
....
3L01_B 424 VKAY 427
Cdd:cd03822 366 LRLF 369
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
18-155 |
2.11e-11 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 62.03 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 18 GGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEigkirvfgeevqvkvsyeERGNLRIYRIGgglldsedvYGPGWDG 97
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPEL------------------VGDGVRVHRLP---------VPPRPSP 53
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
3L01_B 98 LirkavtFGRASVLLLNDLLREEPlPDVVHFHDWHTVFAGALIKKYFKIPAVFTIHRL 155
Cdd:pfam13579 54 L------ADLAALRRLRRLLRAER-PDVVHAHSPTAGLAARLARRRRGVPLVVTVHGL 104
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
203-376 |
2.25e-11 |
|
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: 65.00 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 203 EWGFFRNFEGKITYVFNGIDCSfwNESYLTGSRDERKKSLLSkfgmDEGVTFMFIGRFDRgQKGVDVLLKAIEILssKKE 282
Cdd:cd03812 149 EWLFGEVENGKFKVIPNGIDIE--KYKFNKEKRRKRRKLLIL----EDKLVLGHVGRFNE-QKNHSFLIDIFEEL--KKK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 283 FQEMRFIIIGKGdpELEGWARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASav 362
Cdd:cd03812 220 NPNVKLVLVGEG--ELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLS-- 295
|
170
....*....|....
3L01_B 363 gglrDIITNETGIL 376
Cdd:cd03812 296 ----DTITKECDIT 305
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
253-393 |
5.44e-11 |
|
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: 63.63 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 253 TFMFIGRFDRgQKGVDVLLKAIEILSSKKEfqEMRFIIIGKGD--PELEGWARSLeekhGNVKVITEMLSREFVRELYGS 330
Cdd:cd05844 191 TILFVGRLVE-KKGCDVLIEAFRRLAARHP--TARLVIAGDGPlrPALQALAAAL----GRVRFLGALPHAEVQDWMRRA 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 331 VDFVIiPSYF------EPFGLVALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKAL 393
Cdd:cd05844 264 EIFCL-PSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDgETGFLVPEGDVDALADALQALL 332
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
234-422 |
1.87e-09 |
|
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: 59.16 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 234 SRDERKKSLLSkfgmdegvtfmfIGRFdRGQKGVDVLLKAIEIL---SSKKEFQEMRFIIIG----KGDPE----LEGWA 302
Cdd:cd03806 232 DEKTRENQILS------------IAQF-RPEKNHPLQLRAFAELlkrLPESIRSNPKLVLIGscrnEEDKErveaLKLLA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 303 RSLEEKHgNVKVITEmLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGG-LRDIIT----NETGILv 377
Cdd:cd03806 299 KELILED-SVEFVVD-APYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGpLLDIVVpwdgGPTGFL- 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
3L01_B 378 kAGDPGELANAILKALELSRSDLSKFRENCKKRAMSFSWEKSAER 422
Cdd:cd03806 376 -ASTPEEYAEAIEKILTLSEEERLQRREAARSSAERFSDEEFERD 419
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
250-422 |
9.37e-09 |
|
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: 56.83 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 250 EGVTFMFIGRFDRgQKGVDVLLKAIEILSSK-KEFQEMRFIIIGKGDP----------ELegwaRSLEEKHGNVKVITEM 318
Cdd:cd03805 210 NKKFFLSINRFER-KKNIALAIEAFAKLKQKlPEFENVRLVIAGGYDPrvaenveyleEL----QRLAEELLNVEDQVLF 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 319 L---SREFVRELYGSVDFVI-IPSYfEPFGLVALEAMCLGAIPIASAVGG-LRDIITNETGILVKAgDPGELANAILKAL 393
Cdd:cd03805 285 LrsiSDSQKEQLLSSALALLyTPSN-EHFGIVPLEAMYAGKPVIACNSGGpLETVVEGVTGFLCEP-TPEAFAEAMLKLA 362
|
170 180 190
....*....|....*....|....*....|
3L01_B 394 ElSRSDLSKFRENCKKRAMS-FSWEKSAER 422
Cdd:cd03805 363 N-DPDLADRMGAAGRKRVKEkFSREAFAER 391
|
|
| PHA01633 |
PHA01633 |
putative glycosyl transferase group 1 |
245-421 |
1.41e-08 |
|
putative glycosyl transferase group 1
Pssm-ID: 107050 [Multi-domain] Cd Length: 335 Bit Score: 56.14 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 245 KFGMDEGVTfmfigrfdrGQKGVDVLLKAIEILSSK--KEFQEMRFIIIGKGDpelegwaRSLEEKHGNVKVITEM--LS 320
Cdd:PHA01633 150 KFGIVSGLT---------KRKNMDLMLQVFNELNTKypDIAKKIHFFVISHKQ-------FTQLEVPANVHFVAEFghNS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 321 REFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAG-------------------D 381
Cdd:PHA01633 214 REYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMGTPVIHQLMPPLDEFTSWQWNLLIKSSkveeyydkehgqkwkihkfQ 293
|
170 180 190 200
....*....|....*....|....*....|....*....|..
3L01_B 382 PGELANAILKALELS-RSDLS-KFRENCKKRAMSFSWEKSAE 421
Cdd:PHA01633 294 IEDMANAIILAFELQdREERSmKLKELAKKYDIRNLYTRFLE 335
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
211-427 |
3.64e-08 |
|
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: 55.11 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 211 EGKITYVFNGIDcsfwnESYLTGSRDERKKSLLSKFGMDEGVTFMFIGRFDRGQKGVDVLLKAIEILSSKKEFQE-MRFI 289
Cdd:TIGR03088 159 PAKIHQIYNGVD-----TERFHPSRGDRSPILPPDFFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGAErLRLV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 290 IIGKGD--PELEGWARSleekHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRD 367
Cdd:TIGR03088 234 IVGDGParGACEQMVRA----AGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPE 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3L01_B 368 -IITNETGILVKAGDPGELANAILKALElsrSDLSKFRENCKKRA---MSFSWEKSAERYVKAY 427
Cdd:TIGR03088 310 lVQHGVTGALVPPGDAVALARALQPYVS---DPAARRAHGAAGRAraeQQFSINAMVAAYAGLY 370
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
254-426 |
6.34e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 51.28 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 254 FMFIGRFdRGQKGVDVLLKA----IEILSSkkEFQEMRFIIIG----KGDPE----LEGWARSLEEKhGNVKVITEMLSR 321
Cdd:PLN02949 271 IISVAQF-RPEKAHALQLEAfalaLEKLDA--DVPRPKLQFVGscrnKEDEErlqkLKDRAKELGLD-GDVEFHKNVSYR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 322 EFVRELYGSV-------DfviipsyfEPFGLVALEAMCLGAIPIASAVGGLR-DIITNE----TGILvkAGDPGELANAI 389
Cdd:PLN02949 347 DLVRLLGGAVaglhsmiD--------EHFGISVVEYMAAGAVPIAHNSAGPKmDIVLDEdgqqTGFL--ATTVEEYADAI 416
|
170 180 190
....*....|....*....|....*....|....*..
3L01_B 390 LKALELSRSDLSKFRENCKKRAMSFSWEKSAERYVKA 426
Cdd:PLN02949 417 LEVLRMRETERLEIAAAARKRANRFSEQRFNEDFKDA 453
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
254-418 |
9.52e-07 |
|
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: 50.38 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 254 FMFIGRFDRgQKGVDVLLKAIEILssKKEFQEMRFIIIGKGDpELEGWARSLEEKHGNVKVITEMLSREfVRELYGSVDF 333
Cdd:cd04949 163 IITISRLAP-EKQLDHLIEAVAKA--VKKVPEITLDIYGYGE-EREKLKKLIEELHLEDNVFLKGYHSN-LDQEYQDAYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 334 VIIPSYFEPFGLVALEAMCLGAIPIASAVG-GLRDIITN-ETGILVKAGDPGELANAILKALElSRSDLSKFRENCKKRA 411
Cdd:cd04949 238 SLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDgENGYLIEKNNIDALADKIIELLN-DPEKLQQFSEESYKIA 316
|
....*..
3L01_B 412 MSFSWEK 418
Cdd:cd04949 317 EKYSTEN 323
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
265-409 |
9.96e-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: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 265 KGVDVLLKAIEILSSKKEFQEMRFIIIGKGdPELEGWARSLEEKHGNVKVI-TEMLSREFVRELY--GSVDFVIIPSYFE 341
Cdd:cd04946 237 KRIDLIIETLNSLCVAHPSICISWTHIGGG-PLKERLEKLAENKLENVKVNfTGEVSNKEVKQLYkeNDVDVFVNVSESE 315
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 342 PFGLVALEAMCLGAIPIASAVGGLRDIITNETG--ILVKAGDPGELANAILKaLELSRSDLSKFRENCKK 409
Cdd:cd04946 316 GIPVSIMEAISFGIPVIATNVGGTREIVENETNglLLDKDPTPNEIVSSIMK-FYLDGGDYKTMKISARE 384
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
250-427 |
1.70e-06 |
|
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: 49.93 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 250 EGVTFMFIGR-FDRgqKGVDVLLKAIEILSSKkeFQEMRFIIIGKGdP---ELEGwarsLEEKH---GNVKVITeMLSRE 322
Cdd:cd03796 192 NKITIVVISRlVYR--KGIDLLVGIIPRICKK--HPNVRFIIGGDG-PkriELEE----MREKYqlqDRVELLG-AVPHE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 323 FVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAgDPGELANAILKALELSRS---D 399
Cdd:cd03796 262 EVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEP-DPEDIVRKLEEAISILRTgkhD 340
|
170 180
....*....|....*....|....*...
3L01_B 400 LSKFRENCKKramSFSWEKSAERYVKAY 427
Cdd:cd03796 341 PWSFHNRVKK---MYSWEDVARRTEKVY 365
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
123-423 |
2.57e-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: 46.70 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 123 PDVVHFHDWHTVFAGALIKKYFKIPAVFTIHRLNKSKLPAFyFHEAGLSElapyPDID----------PEHTGGYIADIV 192
Cdd:TIGR02468 311 PYVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQL-LKQGRMSK----EEINstykimrrieAEELSLDASEIV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 193 TTVSRGYLIDEWGFFRNFEGKITYVFNgidcsfwnesyltgSRDERKKSLLSKF---------GMDegvtFMFIgrfDRG 263
Cdd:TIGR02468 386 ITSTRQEIEEQWGLYDGFDVILERKLR--------------ARARRGVSCYGRFmprmavippGME----FSHI---VPH 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 264 QKGVDVLLKAIEILSSKKE----FQEMRF---------IIIGKGDPELE--------GWARSLEE--------------- 307
Cdd:TIGR02468 445 DGDMDGETEGNEEHPAKPDppiwSEIMRFftnprkpmiLALARPDPKKNittlvkafGECRPLRElanltlimgnrddid 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 308 --KHGNVKVITEMLSREFVRELYGSVDF---------------------VII-PSYFEPFGLVALEAMCLGAIPIASAVG 363
Cdd:TIGR02468 525 emSSGSSSVLTSVLKLIDKYDLYGQVAYpkhhkqsdvpdiyrlaaktkgVFInPAFIEPFGLTLIEAAAHGLPMVATKNG 604
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
3L01_B 364 GLRDIITN-ETGILVKAGDPGELANAILKAleLSRSDL-SKFRENCKKRAMSFSWEKSAERY 423
Cdd:TIGR02468 605 GPVDIHRVlDNGLLVDPHDQQAIADALLKL--VADKQLwAECRQNGLKNIHLFSWPEHCKTY 664
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
102-428 |
3.37e-05 |
|
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: 45.82 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 102 AVTFGRASVLLLNDLLREEPLPDVVHFH-DW-HTVFAGALIkkyfkiPAVFTIHRLNksklpaFYFHEAGLSELAPYPDI 179
Cdd:cd03818 69 GVLRGQAVLRALLALKREGFRPDVVVGHpGWgEALFVKDVF------PDVPLIGYCE------YYYRAEGADVGFDPEFP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 180 DPEHTGGYIADIVTTVSRGYLIDEWG----------FFRNFEGKITYVFNGIDCSFwnesyLTGSRDERKKSL-LSKF-G 247
Cdd:cd03818 137 LDLMIRCRLRNRNIALLLSLEQADLGvtptrwqrslFPAAYRDRISVIHDGVDTDR-----LAPDPAARLRLLnGTELkA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 248 MDEGVTFmfIGRFDRGQKGVDVLLKAIEILssKKEFQEMRFIIIGKGD-------PELEGW-ARSLEEKHGNVKVI--TE 317
Cdd:cd03818 212 GDPVITY--VARNLEPYRGFHVFMRALPRI--QARRPDARVVVVGGDGvsygsppPDGGSWkQKMLAELGVDLERVhfVG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 318 MLSR-EFVRELYGSvDFVIIPSYfePFGLV--ALEAMCLGAIPIASAVGGLRDIITN-ETGILVKAGDPGELANAILKAL 393
Cdd:cd03818 288 KVPYdQYVRLLQLS-DAHVYLTY--PFVLSwsLLEAMACGCPVIGSDTAPVREVIRDgRNGLLVDFFDPDALAAAVLELL 364
|
330 340 350
....*....|....*....|....*....|....*
3L01_B 394 ElSRSDLSKFRENCKKRAMSFSwekSAERYVKAYA 428
Cdd:cd03818 365 E-DPDRAAALRRAARRTVERSD---SLDVCLARYL 395
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
265-415 |
5.05e-05 |
|
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: 44.97 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 265 KGVDVLLKAieilsskkeFQEM--RFIIIGKGdPELEgwarSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYfEP 342
Cdd:cd03804 212 KRIDLAVEA---------FNELpkRLVVIGDG-PDLD----RLRAMASPNVEFLGYQPDEVLKELLSKARAFVFAAE-ED 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3L01_B 343 FGLVALEAMCLGAIPIASAVGGLRD-IITNETGILVKAGDPGELaNAILKALELSRSDLSKfrENCKKRAMSFS 415
Cdd:cd03804 277 FGIVPVEAQACGTPVIAFGKGGALEtVRPGPTGILFGEQTVESL-KAAVEEFEQNFDRFKP--QAIRANAERFS 347
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
257-398 |
5.84e-05 |
|
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: 45.00 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 257 IGRFDRgQKGVDVLLKAIEILssKKEFQEMRFIIIGKG---DPEleGW-----ARSLEEKHGNVKVITEMLSREFVRELY 328
Cdd:cd03792 203 VARFDP-SKDPLGVIDAYKLF--KRRAEEPQLVICGHGavdDPE--GSvvyeeVMEYAGDDHDIHVLRLPPSDQEINALQ 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3L01_B 329 GSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLR-DIITNETGILVKAGDpgELANAILKAL---ELSRS 398
Cdd:cd03792 278 RAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPlQVIDGETGFLVNSVE--GAAVRILRLLtdpELRRK 349
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
249-394 |
1.09e-04 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 43.93 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 249 DEGVTFMFIGR--FDrGQKGVDVLLKAIEILSSKKEFQemrfiIIGKGDPE--LEGWARSLEEK-----HGNVKVITEml 319
Cdd:PRK09922 178 DKPAVFLYVGRlkFE-GQKNVKELFDGLSQTTGEWQLH-----IIGDGSDFekCKAYSRELGIEqriiwHGWQSQPWE-- 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3L01_B 320 sreFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGaIPIASA--VGGLRDII-TNETGILVKAGDPGELANAILKALE 394
Cdd:PRK09922 250 ---VVQQKIKNVSALLLTSKFEGFPMTLLEAMSYG-IPCISSdcMSGPRDIIkPGLNGELYTPGNIDEFVGKLNKVIS 323
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
3-217 |
4.65e-03 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 39.07 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 3 MKVLLLGFEFlpvkvGGLAEALTAISEALASLGHEVLVFTPSHGrfqgeeigkirvfgeevqvKVSYEERGNLRIYRIGG 82
Cdd:cd03784 1 MRILFVPFPG-----QGHVNPMLPLAKALAARGHEVTVATPPFN-------------------FADLVEAAGLTFVPVGD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 83 GLLDSE--DVYGPGWDGLIRKAVTFGRASVLLLNDLLREEPL---PDVVhFHDWHTvFAGALIKKYFKIPAVftIHRLNK 157
Cdd:cd03784 57 DPDELEldSETNLGPDSLLELLRRLLKAADELLDDLLAALRSswkPDLV-IADPFA-YAGPLVAEELGIPSV--RLFTGP 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
3L01_B 158 SKLPAFYFHEAGLSELAPYPDIDPEHTGGYIADIVTTVSRGYLIDEWGFFRNFEGKITYV 217
Cdd:cd03784 133 ATLLSAYLHPFGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPL 192
|
|
| |
