|
Name |
Accession |
Description |
Interval |
E-value |
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
6-479 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 686.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 6 VLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIAvNNHSDFDYVSSFDVRAGDIQSMANVYSQVVDGV 85
Cdd:COG0297 3 ILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSID-DKLKDLEVVASLEVPLGGRTYYARVLEGPDDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 86 TFYFIEHRDFFERDELYG-----YDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLCRTFYSYREeFRNIK 160
Cdd:COG0297 82 PVYFIDNPELFDRPGPYGdpdrdYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDP-FKRIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 161 HVFTIHNLAFQGIFHKQALWsALGMDYSYYLDGIARFHDeCISFMKLGILYADKVTTVSETYAREILTEEFGENMQHVLE 240
Cdd:COG0297 161 TVFTIHNLAYQGIFPAEILE-LLGLPPELFTPDGLEFYG-QINFLKAGIVYADRVTTVSPTYAREIQTPEFGEGLDGLLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 241 LRKYDLVGIVNGIDYDSWDSQTDQYLVRNYSLETIESKKANKLALQSQFALPQDENVLLIGIVSRLTWQKGFYLLTEVLG 320
Cdd:COG0297 239 ARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 321 HLLQAHVQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLV 400
Cdd:COG0297 319 ELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVPIV 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500275885 401 RETGGLVDTVAPYNMSTKEGTGFSFGGRDAYNMRQVYDLALQTYYDrPDDWYAMVEQAMKRDFSWTASAEKYIWLYREI 479
Cdd:COG0297 399 RRTGGLADTVIDYNEATGEGTGFVFDEYTAEALLAAIRRALALYRD-PEAWRKLQRNAMKQDFSWEKSAKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
6-481 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 647.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 6 VLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIAvnnHSDFDYV-----SSFDVRAGDIQsmanvysq 80
Cdd:PRK00654 3 ILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIR---EKLRDAQvvgrlDLFTVLFGHLE-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 81 vVDGVTFYFIEHRDFFERDELYGYDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLCRTfySYREEFRNIK 160
Cdd:PRK00654 72 -GDGVPVYLIDAPHLFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKE--KYWRGYPDIK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 161 HVFTIHNLAFQGIFHKQALWsALGMDYSYYLDGIARFHDeCISFMKLGILYADKVTTVSETYAREILTEEFGENMQHVLE 240
Cdd:PRK00654 149 TVFTIHNLAYQGLFPAEILG-ELGLPAEAFHLEGLEFYG-QISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLEGLLR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 241 LRKYDLVGIVNGIDYDSWDSQTDQYLVRNYSLETIESKKANKLALQSQFALPqDENVLLIGIVSRLTWQKGFYLLTEVLG 320
Cdd:PRK00654 227 ARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLP-DDDAPLFAMVSRLTEQKGLDLVLEALP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 321 HLLQAHVQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLV 400
Cdd:PRK00654 306 ELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 401 RETGGLVDTVAPYNMSTKEGTGFSFGGRDAYNMRQVYDLALQTYYDRPdDWYAMVEQAMKRDFSWTASAEKYIWLYREIS 480
Cdd:PRK00654 386 RRTGGLADTVIDYNPEDGEATGFVFDDFNAEDLLRALRRALELYRQPP-LWRALQRQAMAQDFSWDKSAEEYLELYRRLL 464
|
.
gi 500275885 481 G 481
Cdd:PRK00654 465 G 465
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
6-478 |
0e+00 |
|
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: 603.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 6 VLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIAvNNHSDFDYVSSFDVRAGDIQSMANVYSQVVDGV 85
Cdd:cd03791 2 VLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIP-DELDGYLRVLGLEVKVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 86 TFYFIEHRDFFERDEL-----YGYDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLCRTFYSYrEEFRNIK 160
Cdd:cd03791 81 DYYFLDNPEFFDRPGLpgppgYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRG-PGFKKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 161 HVFTIHNLAFQGIFHKQALWSALGMDYSYYLDGIArfHDECISFMKLGILYADKVTTVSETYAREILTEEFGENMQHVLE 240
Cdd:cd03791 160 TVFTIHNLAYQGLFPLDTLAELGLPPELFHIDGLE--FYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDGVLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 241 LRKYDLVGIVNGIDYDSWDSQTDQYLVRNYSLETIESKKANKLALQSQFALPQDENVLLIGIVSRLTWQKGFYLLTEVLG 320
Cdd:cd03791 238 ARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 321 HLLQAHVQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLV 400
Cdd:cd03791 318 ELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIV 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500275885 401 RETGGLVDTVAPYNMSTKEGTGFSFGGRDAYNMRQVYDLALqTYYDRPDDWYAMVEQAMKRDFSWTASAEKYIWLYRE 478
Cdd:cd03791 398 RRTGGLADTVFDYDPETGEGTGFVFEDYDAEALLAALRRAL-ALYRNPELWRKLQKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
6-479 |
0e+00 |
|
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: 567.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 6 VLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIAVNNHSDFDYVSSFDVRAGDIQSMANVYSQVVDGV 85
Cdd:TIGR02095 3 VLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTLYVKVFEGVVEGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 86 TFYFIEHRDFFERDE-LYG--YDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLcrtfYSYREEFRNIKHV 162
Cdd:TIGR02095 83 PVYFIDNPSLFDRPGgIYGddYPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPAL----LKAVYRPNPIKTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 163 FTIHNLAFQGIFHKQALwSALGMDYSYYLDGIARFHDeCISFMKLGILYADKVTTVSETYAREILTEEFGENMQHVLELR 242
Cdd:TIGR02095 159 FTIHNLAYQGVFPADDF-SELGLPPEYFHMEGLEFYG-RVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGLDGVLKAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 243 KYDLVGIVNGIDYDSWDSQTDQYLVRNYSLETIESKKANKLALQSQFALPQDENVLLIGIVSRLTWQKGFYLLTEVLGHL 322
Cdd:TIGR02095 237 SGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 323 LQAHVQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRE 402
Cdd:TIGR02095 317 LELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVPIVRR 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500275885 403 TGGLVDTVAPYNMSTKEGTGFSFGGRDAYNMRQVYDLALQTYYDRPDDWYAMVEQAMKRDFSWTASAEKYIWLYREI 479
Cdd:TIGR02095 397 TGGLADTVVDGDPEAESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAKQYVELYRSL 473
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
1-479 |
9.18e-116 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 349.02 E-value: 9.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 1 MTKKSVLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIAVNnHSDFDYVSSFDVRAGdiqSMANVYSQ 80
Cdd:PRK14099 1 MTPLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAG-IEDAEQVHSFPDLFG---GPARLLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 81 VVDGVTFYFIEHRDFFERD-ELY----GYD--DDAMRFGyfqhATCRLLEAL------HFFPDVMHTHDWHTAALPFLCR 147
Cdd:PRK14099 77 RAGGLDLFVLDAPHLYDRPgNPYvgpdGKDwpDNAQRFA----ALARAAAAIgqglvpGFVPDIVHAHDWQAGLAPAYLH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 148 tfYSYREEfrnIKHVFTIHNLAFQGIFHKQALwSALGM-DYSYYLDGIARFHDecISFMKLGILYADKVTTVSETYAREI 226
Cdd:PRK14099 153 --YSGRPA---PGTVFTIHNLAFQGQFPRELL-GALGLpPSAFSLDGVEYYGG--IGYLKAGLQLADRITTVSPTYALEI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 227 LTEEFGENMQHVLELRKYDLVGIVNGIDYDSWDSQTDQYLVRNYSLETIESKKANKLALQSQFALPQDENVLLIGIVSRL 306
Cdd:PRK14099 225 QGPEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLDPDPDALLLGVISRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 307 TWQKGFYLLTEVLGHLLQAHVQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGI 386
Cdd:PRK14099 305 SWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 387 SQLISMHYGTLPLVRETGGLVDTVAPYN---MSTKEGTGFSFGGRDAYNMRQVYDLALQTYYDrPDDWYAMVEQAMKRDF 463
Cdd:PRK14099 385 TQLCALRYGAVPVVARVGGLADTVVDANemaIATGVATGVQFSPVTADALAAALRKTAALFAD-PVAWRRLQRNGMTTDV 463
|
490
....*....|....*.
gi 500275885 464 SWTASAEKYIWLYREI 479
Cdd:PRK14099 464 SWRNPAQHYAALYRSL 479
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
6-239 |
1.21e-94 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 286.15 E-value: 1.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 6 VLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIAvNNHSDFDYVSSFDVRAG--DIQSMANVYSQVVD 83
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIP-EERNQLEDVIRLSVAAGvpVRPLTVGVARLELD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 84 GVTFYFIEHRDFFERDELYG-----YDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLCRTFYSYReEFRN 158
Cdd:pfam08323 80 GVDVYFLDNPDYFDRPGLYGddgrdYEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADD-PFKN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 159 IKHVFTIHNLAFQGIFHKQALwSALGMDYSYYLDGIARFHDeCISFMKLGILYADKVTTVSETYAREILTEEFGENMQHV 238
Cdd:pfam08323 159 IKTVFTIHNLAYQGRFPADLL-DLLGLPPEDFNLDGLEFYG-QINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGLDGL 236
|
.
gi 500275885 239 L 239
Cdd:pfam08323 237 L 237
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
5-476 |
1.45e-93 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 304.52 E-value: 1.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 5 SVLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIA---VNNHSDFDYV--SSFDvraGDIQSmANVYS 79
Cdd:PLN02939 483 HIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQydqIRNLKVLDVVveSYFD---GNLFK-NKIWT 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 80 QVVDGVTFYFIEHR---DFFERDELYGYDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLCRTFYSYREeF 156
Cdd:PLN02939 559 GTVEGLPVYFIEPQhpsKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKG-F 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 157 RNIKHVFTIHNLAFQGIFHKQALwSALGMDYSYyLDGIARFHDEC---ISFMKLGILYADKVTTVSETYAREILTEEfGE 233
Cdd:PLN02939 638 NSARICFTCHNFEYQGTAPASDL-ASCGLDVHQ-LDRPDRMQDNAhgrINVVKGAIVYSNIVTTVSPTYAQEVRSEG-GR 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 234 NMQHVLELRKYDLVGIVNGIDYDSWDSQTDQYLVRNYSLETIESKKANKLALQSQFALP-QDENVLLIGIVSRLTWQKGF 312
Cdd:PLN02939 715 GLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGV 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 313 YLLTEVLGHLLQAHVQFVILGNG-----EEDIENAFNHFKHAypDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGIS 387
Cdd:PLN02939 795 HLIRHAIYKTAELGGQFVLLGSSpvphiQREFEGIADQFQSN--NNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLT 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 388 QLISMHYGTLPLVRETGGLVDTVAPYNMST---KEGTGFSFGGRDAYNMRQVYDLALQTYYDRPDDWYAMVEQAMKRDFS 464
Cdd:PLN02939 873 QMIAMRYGSVPIVRKTGGLNDSVFDFDDETipvELRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFS 952
|
490
....*....|..
gi 500275885 465 WTASAEKYIWLY 476
Cdd:PLN02939 953 WDSSASQYEELY 964
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
6-481 |
3.50e-92 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 288.56 E-value: 3.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 6 VLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIavNNHS----DFDYVSSFDVRAGDIQSMANVYSQV 81
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTI--NDRKfrlhDVLRLSDIEVPLKEKTDLLHVKVTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 82 VDG--VTFYFIEHRDFFERDELYG-------YDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLCRTFYSY 152
Cdd:PRK14098 86 LPSskIQTYFLYNEKYFKRNGLFTdmslggdLKGSAEKVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPLLLKTVYAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 153 REEFRNIKHVFTIHNLAFQGIFHKQALWSALGMDYSyylDGIARFHDEcISFMKLGILYADKVTTVSETYAREILTEE-- 230
Cdd:PRK14098 166 HEFFKDIKTVLTIHNVYRQGVLPFKVFQKLLPEEVC---SGLHREGDE-VNMLYTGVEHADLLTTTSPRYAEEIAGDGee 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 231 -FGenMQHVLELRKYDLVGIVNGIDYDSWDSQTDQYLVRNYSLETIESKKANKLALQSQFALPQDENVLLIGIVSRLTWQ 309
Cdd:PRK14098 242 aFG--LDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALLEEVGLPFDEETPLVGVIINFDDF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 310 KGFYLLTEVLGHLLQAHVQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGISQL 389
Cdd:PRK14098 320 QGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIESCGMLQM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 390 ISMHYGTLPLVRETGGLVDTVAPYnmSTKEGTGFSFGGRDAYNMRQVYDLALQTYYDRpDDWYAMVEQAMKRDFSWTASA 469
Cdd:PRK14098 400 FAMSYGTIPVAYAGGGIVETIEEV--SEDKGSGFIFHDYTPEALVAKLGEALALYHDE-ERWEELVLEAMERDFSWKNSA 476
|
490
....*....|..
gi 500275885 470 EKYIWLYREISG 481
Cdd:PRK14098 477 EEYAQLYRELLG 488
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
5-477 |
1.47e-88 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 291.77 E-value: 1.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 5 SVLFVASEGLPFIKTGGLADVIGSLPKELVKQGLDVRVVLPLYKKIAVNNHSDFDYVSSFDVRAGDIQsmanVYSQVVDG 84
Cdd:PLN02316 589 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRSYSWGGTEIK----VWFGKVEG 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 85 VTFYFIEHRD-FFERDELYGYDDDAMRFGYFQHATCRLLEALHFFPDVMHTHDWHTAALPFLCRTFYSYREeFRNIKHVF 163
Cdd:PLN02316 665 LSVYFLEPQNgMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYG-LSKARVVF 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 164 TIHNLAFqGIFHkqalwsalgmdysyyldgIARfhdecisfmklGILYADKVTTVSETYAREIlteefgeNMQHVLELRK 243
Cdd:PLN02316 744 TIHNLEF-GANH------------------IGK-----------AMAYADKATTVSPTYSREV-------SGNSAIAPHL 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 244 YDLVGIVNGIDYDSWDSQTDQYLVRNYSLE-TIESKKANKLALQSQFALpQDENVLLIGIVSRLTWQKGFYLLTEVLGHL 322
Cdd:PLN02316 787 YKFHGILNGIDPDIWDPYNDNFIPVPYTSEnVVEGKRAAKEALQQRLGL-KQADLPLVGIITRLTHQKGIHLIKHAIWRT 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 323 LQAHVQFVILGNG-----EEDIENAFNHFKHAYPDKFAFYRGYNEPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTL 397
Cdd:PLN02316 866 LERNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSI 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 398 PLVRETGGLVDTVAPYNMSTK-------EGTGFSFGGRDAYNMRQVYDLALQTYYDRPDDWYAMVEQAMKRDFSWTASAE 470
Cdd:PLN02316 946 PVVRKTGGLFDTVFDVDHDKEraqaqglEPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPAL 1025
|
....*..
gi 500275885 471 KYIWLYR 477
Cdd:PLN02316 1026 DYMELYH 1032
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
85-477 |
2.24e-26 |
|
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: 109.93 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 85 VTFYFIEHRDFFERDELYGYDDDAMRFGYFQHATCRLLEALHFF-----PDVMHTHDWHTAAlpflcrtFYSYREEFRNI 159
Cdd:cd03801 34 VTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLlrlrkFDVVHAHGLLAAL-------LAALLALLLGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 160 KHVFTIHNLAFQgifhkqalwsalgmDYSYYLDGIARFhdecISFMKLGILYADKVTTVSEtYAREILTEEFGEnmqhvl 239
Cdd:cd03801 107 PLVVTLHGAEPG--------------RLLLLLAAERRL----LARAEALLRRADAVIAVSE-ALRDELRALGGI------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 240 elRKYDLVGIVNGIDYDSWDSQTDQylvrnysletieskkanklalqsqfALPQDENVLLIGIVSRLTWQKGFYLLTEVL 319
Cdd:cd03801 162 --PPEKIVVIPNGVDLERFSPPLRR-------------------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 320 GHLLQAH--VQFVILGNGEEDIENAFNHFKHAYPD-KFAFYRGYNEplAHQIYAASDLFLMPSMFEPCGISQLISMHYGT 396
Cdd:cd03801 215 AKLLRRGpdVRLVIVGGDGPLRAELEELELGLGDRvRFLGFVPDEE--LPALYAAADVFVLPSRYEGFGLVVLEAMAAGL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 397 LPLVRETGGLVDTVAPynmstkEGTGFSFGGRDAYNMRQvydlALQTYYDRPDDWYAMVEQAMKR---DFSWTASAEKYI 473
Cdd:cd03801 293 PVVATDVGGLPEVVED------GEGGLVVPPDDVEALAD----ALLRLLADPELRARLGRAARERvaeRFSWERVAERLL 362
|
....
gi 500275885 474 WLYR 477
Cdd:cd03801 363 DLYR 366
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
362-479 |
1.26e-12 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 64.63 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 362 EPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVAPynmstkEGTGFSFGGRDAYNMRQvydlAL 441
Cdd:COG0438 11 DLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED------GETGLLVPPGDPEALAE----AI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 500275885 442 QTYYDRPDDWYAMVEQAMKR---DFSWTASAEKYIWLYREI 479
Cdd:COG0438 81 LRLLEDPELRRRLGEAARERaeeRFSWEAIAERLLALYEEL 121
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
294-413 |
2.89e-11 |
|
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: 61.52 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 294 DENVLLIgiVSRLTWQKGFYLLTEVLGHLLQAH--VQFVILGNGEED------IENAFNHFKHaypdKFAFYRGYNEPla 365
Cdd:pfam00534 1 KKKIILF--VGRLEPEKGLDLLIKAFALLKEKNpnLKLVIAGDGEEEkrlkklAEKLGLGDNV----IFLGFVSDEDL-- 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 500275885 366 HQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVAPY 413
Cdd:pfam00534 73 PELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDG 120
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
269-479 |
2.24e-10 |
|
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: 61.96 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 269 NYSLETIESKKANKLALQSQFALPQDENVLLIGIVSRLTWQKGFYLLTEVLGHLLQ-AHVQFVILGNGEEDIENA-FNHF 346
Cdd:cd03825 167 PNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEALKLLATkDDLLLVVFGKNDPQIVILpFDII 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 347 KHAYPDkfafyrgyNEPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDtvapynMSTKEGTGFSFG 426
Cdd:cd03825 247 SLGYID--------DDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPE------IVQHGVTGYLVP 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500275885 427 GRDAYNMRQvydlALQTYYDRPDDWYAMVEQAMK---RDFSWTASAEKYIWLYREI 479
Cdd:cd03825 313 PGDVQALAE----AIEWLLANPKERESLGERARAlaeNHFDQRVQAQRYLELYKDL 364
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
187-462 |
6.38e-10 |
|
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: 60.45 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 187 YSYYLDGIARFHDEciSFMKLGILYADKVTTVSEtYAREILTEEFGenmqhVLELRkydLVGIVNGIDYDSWDSQTDQYL 266
Cdd:cd03819 104 TTVHGSYLATYHPK--DFALAVRARGDRVIAVSE-LVRDHLIEALG-----VDPER---IRVIPNGVDTDRFPPEAEAEE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 267 VRNYSLetieskkanklalqsqfalpqDENVLLIGIVSRLTWQKGFYLLTEVLGHL-LQAHVQFVILGNGEED--IENAF 343
Cdd:cd03819 173 RAQLGL---------------------PEGKPVVGYVGRLSPEKGWLLLVDAAAELkDEPDFRLLVAGDGPERdeIRRLV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 344 NhfKHAYPDKFAFYrGYNEPLAHqIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVAPYNmstkEGTGF 423
Cdd:cd03819 232 E--RLGLRDRVTFT-GFREDVPA-ALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGR----TGLLV 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 500275885 424 SFGGRDAynMRQvydlALQTYYDRPDDWYAMVEQAMKRD 462
Cdd:cd03819 304 PPGDAEA--LAD----AIRAAKLLPEAREKLQAAAALTE 336
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
299-410 |
5.28e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 54.44 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 299 LIGIVSRLT-WQKGFYLLTEVLGHLLQAH--VQFVILGNGEEDienAFNHFKHAYPDKFAFyRGYNEPLAhQIYAASDLF 375
Cdd:pfam13692 3 VILFVGRLHpNVKGVDYLLEAVPLLRKRDndVRLVIVGDGPEE---ELEELAAGLEDRVIF-TGFVEDLA-ELLAAADVF 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 500275885 376 LMPSMFEPCGISQLISMHYGtLPLV-RETGGLVDTV 410
Cdd:pfam13692 78 VLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELV 112
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
157-473 |
5.93e-09 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 57.76 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 157 RNIKHVFTIHNLAFqgIFHKQalwsalgmdysYYLDGIARFHDeciSFMKLGILYADKVTTVSETYAREILtEEFGENMQ 236
Cdd:cd03809 100 KGCPQVVTIHDLIP--LRYPE-----------FFPKRFRLYYR---LLLPISLRRADAIITVSEATRDDII-KFYGVPPE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 237 HVlelrkydlVGIVNGIDYDSWDSQTDQYLVRNYsletieskkanklalqsqfalPQDENVLLIgiVSRLTWQKGFYLLT 316
Cdd:cd03809 163 KI--------VVIPLGVDPSFFPPESAAVLIAKY---------------------LLPEPYFLY--VGTLEPRKNHERLL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 317 EVLGHLLQAH--VQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGY-NEPLAHQIYAASDLFLMPSMFEPCGISQLISMH 393
Cdd:cd03809 212 KAFALLKKQGgdLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYvSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 394 YGT------LPLVRE-TGGLVDTVAPYnmstkegtgfsfggrDAYNMRQvydlALQTYYDRPDDWYAMVEQAMKRD--FS 464
Cdd:cd03809 292 CGTpviasnISVLPEvAGDAALYFDPL---------------DPESIAD----AILRLLEDPSLREELIRKGLERAkkFS 352
|
....*....
gi 500275885 465 WTASAEKYI 473
Cdd:cd03809 353 WEKTAEKTL 361
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
299-412 |
3.21e-08 |
|
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: 55.38 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 299 LIGIVSRLTWQKGFYLLTEVLGHLLQAH-VQFVILGNGEEDIEnafnhFKHAYPD-KFAFYRGyNEPLAhQIYAASDLFL 376
Cdd:cd03814 200 LLLYVGRLAPEKNLEALLDADLPLAASPpVRLVVVGDGPARAE-----LEARGPDvIFTGFLT-GEELA-RAYASADVFV 272
|
90 100 110
....*....|....*....|....*....|....*..
gi 500275885 377 MPSMFEPCGISQLISMHYGtLPLV-RETGGLVDTVAP 412
Cdd:cd03814 273 FPSRTETFGLVVLEAMASG-LPVVaADAGGPRDIVRP 308
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
288-472 |
6.23e-08 |
|
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: 54.55 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 288 QFALPQDENVLLIgiVSRLTWQKGFYLLTEVLGHL--LQAHVQFVILGNGEEDI----ENAFNHFKHAY--PDKFAFYRG 359
Cdd:cd03800 213 RLLLPPDKPVVLA--LGRLDPRKGIDTLVRAFAQLpeLRELANLVLVGGPSDDPlsmdREELAELAEELglIDRVRFPGR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 360 YNEPLAHQIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVAPynmstkEGTGFSFGGRDAynmrQVYDL 439
Cdd:cd03800 291 VSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRD------GRTGLLVDPHDP----EALAA 360
|
170 180 190
....*....|....*....|....*....|....*.
gi 500275885 440 ALQTYYDRPDDWYAMVEQAMKR---DFSWTASAEKY 472
Cdd:cd03800 361 ALRRLLDDPALWQRLSRAGLERaraHYTWESVADQL 396
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
303-414 |
5.64e-07 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 50.48 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 303 VSRLTWQKGFYLLTEVLGHLLQAH--VQFVILGNGEEDIENAFNHFKHAYPDKFAFYRGY-NEPLAHQIYAASDLFLMPS 379
Cdd:cd01635 116 VGRLVPEKGIDLLLEALALLKARLpdLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLvDDEVLELLLAAADVFVLPS 195
|
90 100 110
....*....|....*....|....*....|....*
gi 500275885 380 MFEPCGISQLISMHYGTLPLVRETGGLVDTVAPYN 414
Cdd:cd01635 196 RSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGE 230
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
129-477 |
7.98e-07 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 51.16 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 129 PDVMHTHDWHTAALPFLCRTFYsyreefRNIKHVFTIHNlafqgifhkqalwsalgMDYSYYLDGIARFHDECISFMKLG 208
Cdd:cd03807 80 PDVVHTWMYHADLIGGLAAKLA------GGVKVIWSVRS-----------------SNIPQRLTRLVRKLCLLLSKFSPA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 209 ILYadkvttVSETYAREILTEEFgenmqhvlelRKYDLVGIVNGIDYDSWDsqtdqylvrnysletIESKKANKLALqsq 288
Cdd:cd03807 137 TVA------NSSAVAEFHQEQGY----------AKNKIVVIYNGIDLFKLS---------------PDDASRARARR--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 289 fALPQDENVLLIGIVSRLTWQKGFYLLTEVLGHLLQAHVQ--FVILGNGEEDIENAFNHFKHAYPDKFAFyRGYNEPLAh 366
Cdd:cd03807 183 -RLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDlrLLLVGRGPERPNLERLLLELGLEDRVHL-LGERSDVP- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 367 QIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVAPynmstkeGTGFSFGGRDAYNMRQvydlALQTYYD 446
Cdd:cd03807 260 ALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDD-------GTGFLVPAGDPQALAD----AIRALLE 328
|
330 340 350
....*....|....*....|....*....|....
gi 500275885 447 RPDDWYAMVEQAMKR---DFSWTASAEKYIWLYR 477
Cdd:cd03807 329 DPEKRARLGRAARERianEFSIDAMVRRYETLYY 362
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
295-479 |
6.44e-06 |
|
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: 48.14 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 295 ENVLLIGIVSRLTWQKGFYLLTEVLGHLLQA--HVQFVILGNGE---------EDIENAFNHfkhaypdKFAFYRGYNEP 363
Cdd:cd03798 198 LDAFVILFVGRLIPRKGIDLLLEAFARLAKArpDVVLLIVGDGPlrealralaEDLGLGDRV-------TFTGRLPHEQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 364 LAHqiYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVapynmsTKEGTGFSFGGRDAynmrQVYDLALQT 443
Cdd:cd03798 271 PAY--YRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVV------GDPETGLLVPPGDA----DALAAALRR 338
|
170 180 190
....*....|....*....|....*....|....*...
gi 500275885 444 YYDRPDDWYAMVEQAMK--RDFSWTASAEKYIWLYREI 479
Cdd:cd03798 339 ALAEPYLRELGEAARARvaERFSWVKAADRIAAAYRDV 376
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
292-461 |
7.35e-06 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 47.98 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 292 PQDENVLLIGIVSRLTWQKGFYLLTEVLGHLLQAHVQ--FVILGNGEEDIENAFNHFKHAYPDKFAFYrGYNEPLAHqIY 369
Cdd:cd03808 184 SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNvrFLLVGDGELENPSEILIEKLGLEGRIEFL-GFRSDVPE-LL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 370 AASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVAPYNmstkegTGFSFGGRDaynmrqVYDLA--LQTYYDR 447
Cdd:cd03808 262 AESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGV------NGFLVPPGD------VEALAdaIEKLIED 329
|
170
....*....|....
gi 500275885 448 PDDWYAMVEQAMKR 461
Cdd:cd03808 330 PELRKEMGEAARKR 343
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
120-232 |
1.29e-05 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 45.60 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 120 RLLEALHFF-PDVMHTHDWHTAALPFLcrtfysYREEFRNIKHVFTIHNLAFQGIFHKQALWsalgmdysyyldgiaRFH 198
Cdd:pfam13439 62 RLRRLLRRErPDVVHAHSPFPLGLAAL------AARLRLGIPLVVTYHGLFPDYKRLGARLS---------------PLR 120
|
90 100 110
....*....|....*....|....*....|....
gi 500275885 199 DECISFMKLGILYADKVTTVSEtYAREILTEEFG 232
Cdd:pfam13439 121 RLLRRLERRLLRRADRVIAVSE-AVADELRRLYG 153
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
299-425 |
7.55e-05 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 45.09 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 299 LIGIVSRLTWQKGFYLLTEVLGHLLQAHVQFVILGNGEEDIENafnHFKhaypDKFAFYRGY--NEPLAhQIYAASDLFL 376
Cdd:PLN02871 265 LIVYVGRLGAEKNLDFLKRVMERLPGARLAFVGDGPYREELEK---MFA----GTPTVFTGMlqGDELS-QAYASGDVFV 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 500275885 377 MPSMFEPCGISQLISMHYGtLPLVR-ETGGLVDTVAPynmsTKEG-TGFSF 425
Cdd:PLN02871 337 MPSESETLGFVVLEAMASG-VPVVAaRAGGIPDIIPP----DQEGkTGFLY 382
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
20-226 |
1.31e-04 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 42.39 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 20 GGLADVIGSLPKELVKQGLDVRVVLPLykkiavnnhsdfDYVSSFDVRAgdiqsmanvysqvvDGVTFYfiehrdffeRD 99
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPG------------GPPGRPELVG--------------DGVRVH---------RL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 100 ELYGYDDDAMRFGYfqhaTCRLLEALHFF-PDVMHTHDWHTAALPFLCRTfysyreeFRNIKHVFTIHNLAF-QGIFHKQ 177
Cdd:pfam13579 46 PVPPRPSPLADLAA----LRRLRRLLRAErPDVVHAHSPTAGLAARLARR-------RRGVPLVVTVHGLALdYGSGWKR 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500275885 178 ALWSALgmdysyyldgiarfhdecisfMKLGILYADKVTTVSETYAREI 226
Cdd:pfam13579 115 RLARAL---------------------ERRLLRRADAVVVVSEAEAELL 142
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
92-477 |
1.49e-04 |
|
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: 43.86 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 92 HRDFFERDElygYDDDAMRFGYFqhatcRLLEAlhFFPDVMHTHDW--HTAALPFLCRTfysyreefRNIKHVFTIHNla 169
Cdd:cd03823 70 KRRGYELFE---TYNPGLRRLLA-----RLLED--FRPDVVHTHNLsgLGASLLDAARD--------LGIPVVHTLHD-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 170 fqgifhkqalwsalgmdysYYLdgiarfhdECI--SFMKLGIlyaDKVTTVSEtYAREILTEEFGEN-MQHVlelrkydl 246
Cdd:cd03823 130 -------------------YWL--------LCPrqFLFKKGG---DAVLAPSR-FTANLHEANGLFSaRISV-------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 247 vgIVNGIDYDswdsqtdqylvrnysletieskkanKLALQSQFALPQDENVLLIGivsRLTWQKGFYLLTEVLGHLLQAH 326
Cdd:cd03823 171 --IPNAVEPD-------------------------LAPPPRRRPGTERLRFGYIG---RLTEEKGIDLLVEAFKRLPRED 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 327 VQFVILGNGEEDIEnafnhfKHAYPDKFAFYRGY--NEPLAHQiYAASDLFLMPSMF-EPCGISQLISMHYGTLPLVRET 403
Cdd:cd03823 221 IELVIAGHGPLSDE------RQIEGGRRIAFLGRvpTDDIKDF-YEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDL 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500275885 404 GGLVDTVAPynmsTKEGTGFSFGGRDAynmrqvYDLALQTYYDRPDDWYAMVEQAMKRDFSwTASAEKYIWLYR 477
Cdd:cd03823 294 GGIAELIQP----GVNGLLFAPGDAED------LAAAMRRLLTDPALLERLRAGAEPPRST-ESQAEEYLKLYR 356
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
206-479 |
1.79e-04 |
|
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: 43.49 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 206 KLGILYADKVTTVSETYAREILTeefgenmqhVLELRKyDLVGIVNGIDYDSWdsqtdqylvrnysletiesKKANKLAL 285
Cdd:cd04962 136 RFSINKSDRVTAVSSSLRQETYE---------LFDVDK-DIEVIHNFIDEDVF-------------------KRKPAGAL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 286 QSQFALPQDENVLLIgiVSRLTWQKGFYLLTEVLgHLLQAHV--QFVILGNGEEdIENAFNHFKHAYPDKFAFYRGYNEP 363
Cdd:cd04962 187 KRRLLAPPDEKVVIH--VSNFRPVKRIDDVVRVF-ARVRRKIpaKLLLVGDGPE-RVPAEELARELGVEDRVLFLGKQDD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 364 LAHqIYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVapynmstKEG-TGFSFGGRDAYNMRqvyDLALQ 442
Cdd:cd04962 263 VEE-LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVV-------KHGeTGFLSDVGDVDAMA---KSALS 331
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 500275885 443 TYYDrpDDWYAMVEQAMKRDFSWTASAEK----YIWLYREI 479
Cdd:cd04962 332 ILED--DELYNRMGRAARKRAAERFDPERivpqYEAYYRRL 370
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
272-414 |
3.01e-04 |
|
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: 42.82 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 272 LETIESKKANKLALQSQFALPQDENVLLIgiVSRLTWQKGFYLLTEVLGHLLQAHVQF--VILGNGE--EDIENAFNHFK 347
Cdd:cd04951 165 LNKFKKDINVRLKIRNKLNLKNDEFVILN--VGRLTEAKDYPNLLLAISELILSKNDFklLIAGDGPlrNELERLICNLN 242
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500275885 348 HAYPDKFAFYRGYNEPLahqiYAASDLFLMPSMFEPCGISQLISMHYGTLPLVRETGGLVDTVAPYN 414
Cdd:cd04951 243 LVDRVILLGQISNISEY----YNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN 305
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
18-400 |
6.16e-04 |
|
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: 41.97 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 18 KTGGLADVIGSLPKELVKQGLDVRVVlplykkiavnnhsdfdyvssfdvragdiqSMANVYSQVVDGVTFYFIEHRDFFE 97
Cdd:cd03821 12 KAGGPVKVVLRLAAALAALGHEVTIV-----------------------------STGDGYESLVVEENGRYIPPQDGFA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 98 RDELYGYDDDAMRFGYF--QHATCRLLEalhffPDVMHTHD-WHTAALPF--LCRTfysyreefRNIKHVFTIHN----L 168
Cdd:cd03821 63 SIPLLRQGAGRTDFSPGlpNWLRRNLRE-----YDVVHIHGvWTYTSLAAckLARR--------RGIPYVVSPHGmldpW 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 169 AFQgifHKQALWSALGMDysyyldgIARFHDECisfmklgilyADKVTTVSETYAREilteefgenmQHVLELRKYDLVg 248
Cdd:cd03821 130 ALQ---QKHWKKRIALHL-------IERRNLNN----------AALVHFTSEQEADE----------LRRFGLEPPIAV- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 249 IVNGIDYDSWDSQtdqylvrnysletieskkankLALQSQFALPQDENVLLIgiVSRLTWQKGFYLLTEVLGHLLQAH-- 326
Cdd:cd03821 179 IPNGVDIPEFDPG---------------------LRDRRKHNGLEDRRIILF--LGRIHPKKGLDLLIRAARKLAEQGrd 235
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500275885 327 VQFVILGNGEEDiENAFNHFKHAY--PDKFAFYRG-YNEPLAhQIYAASDLFLMPSMFEPCGISQLISMHYGtLPLV 400
Cdd:cd03821 236 WHLVIAGPDDGA-YPAFLQLQSSLglGDRVTFTGPlYGEAKW-ALYASADLFVLPSYSENFGNVVAEALACG-LPVV 309
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
129-383 |
3.93e-03 |
|
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: 39.26 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 129 PDVMHTHDWHTAALPFLCRTfysyreefRNIKHVFTIHNLafqgifhkqalwsalgMDYSYYLDGIarfhdecISFMKLG 208
Cdd:cd03811 84 PDVVISFLGFATYIVAKLAA--------ARSKVIAWIHSS----------------LSKLYYLKKK-------LLLKLKL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 209 ILYADKVTTVSETyAREILTEEFGENMQHVLelrkydlVgIVNGIDydswdsqtdqylvrnysLETIEsKKANKLALQsq 288
Cdd:cd03811 133 YKKADKIVCVSKG-IKEDLIRLGPSPPEKIE-------V-IYNPID-----------------IDRIR-ALAKEPILN-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 289 falpQDENVLLIGIVSRLTWQKGFYLLTEVLGHLL--QAHVQFVILGNGEE-----------DIENAFnHFKHAYPDKFA 355
Cdd:cd03811 184 ----EPEDGPVILAVGRLDPQKGHDLLIEAFAKLRkkYPDVKLVILGDGPLreeleklakelGLAERV-IFLGFQSNPYP 258
|
250 260
....*....|....*....|....*...
gi 500275885 356 FYRgyneplahqiyaASDLFLMPSMFEP 383
Cdd:cd03811 259 YLK------------KADLFVLSSRYEG 274
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
203-400 |
4.44e-03 |
|
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: 39.19 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 203 SFMKLGILYADKVTTVSEtyareilteEFGENMQHVLELRKYDLVGivNGIDYDSWdsqtdqylvrNYSLETIESKKANK 282
Cdd:cd03812 128 VLKKLIERLSTKYLACSE---------DAGEWLFGEVENGKFKVIP--NGIDIEKY----------KFNKEKRRKRRKLL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275885 283 LAlqsqfalpqdENVLLIGIVSRLTWQKGFYLLTEVLGHLL--QAHVQFVILGNGE--EDIENAFNHFKHAypDKFAFYR 358
Cdd:cd03812 187 IL----------EDKLVLGHVGRFNEQKNHSFLIDIFEELKkkNPNVKLVLVGEGElkEKIKEKVKELGLE--DKVIFLG 254
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500275885 359 GYNEPlaHQIYAASDLFLMPSMFEPCGISqLISMHYGTLPLV 400
Cdd:cd03812 255 FRNDV--SEILSAMDVFLFPSLYEGLPLV-AVEAQASGLPCL 293
|
|
| |
