|
Name |
Accession |
Description |
Interval |
E-value |
| glgA |
PRK00654 |
glycogen synthase GlgA; |
1-476 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 753.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGIPDAQVVTRRDTFAGRITLLFGHfnGVGIY 80
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVGRLDLFTVLFGHLEGD--GVPVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 81 LIDAPHLYDRPGspyhdtnLFAYTDNVQRFALLGWVGCEMACGLDpfWRPDVVHAHDWHAGLAPAYLAARGHP----AKS 156
Cdd:PRK00654 79 LIDAPHLFDRPS-------GYGYPDNGERFAFFSWAAAEFAEGLD--PRPDIVHAHDWHTGLIPALLKEKYWRgypdIKT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 157 VFTVHNLAYQGMFYAKHMDDIQLPWSFFNVHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLQQRH 236
Cdd:PRK00654 150 VFTIHNLAYQGLFPAEILGELGLPAEAFHLEGLEFYGQISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLEGLLRARS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 237 reGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEEKAENKRQLQIAMGLKvNDKVPLFAVVSRLTSQKGLDLVLEALPG 316
Cdd:PRK00654 230 --GKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLP-DDDAPLFAMVSRLTEQKGLDLVLEALPE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 317 LLEQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVR 396
Cdd:PRK00654 307 LLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 397 RTGGLADTVSDSsleNLADGIASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMTMDFSWQVAAKSYRELYYRL 476
Cdd:PRK00654 387 RTGGLADTVIDY---NPEDGEATGFVFDDFNAEDLLRALRRALELYRQPPLWRALQRQAMAQDFSWDKSAEEYLELYRRL 463
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1-476 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 703.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGIPDAQVVTRRDTFAG----RITLLFGHFNG 76
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDDKLKDLEVVASLEVPLGgrtyYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 77 VGIYLIDAPHLYDRPGsPYHDTNlFAYTDNVQRFALLGWVGCEMACGLDpfWRPDVVHAHDWHAGLAPAYLAARGH---- 152
Cdd:COG0297 81 VPVYFIDNPELFDRPG-PYGDPD-RDYPDNAERFAFFSRAALELLKGLD--WKPDIIHCHDWQTGLIPALLKTRYAddpf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 153 -PAKSVFTVHNLAYQGMFYAKHMDDIQLPWSFFNVHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGL 231
Cdd:COG0297 157 kRIKTVFTIHNLAYQGIFPAEILELLGLPPELFTPDGLEFYGQINFLKAGIVYADRVTTVSPTYAREIQTPEFGEGLDGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 232 LqqRHREGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEEKAENKRQLQIAMGLKVNDKVPLFAVVSRLTSQKGLDLVL 311
Cdd:COG0297 237 L--RARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 312 EALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQLYGLKYGT 391
Cdd:COG0297 315 EALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 392 LPLVRRTGGLADTVSDSsleNLADGIASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMTMDFSWQVAAKSYRE 471
Cdd:COG0297 395 VPIVRRTGGLADTVIDY---NEATGEGTGFVFDEYTAEALLAAIRRALALYRDPEAWRKLQRNAMKQDFSWEKSAKEYLE 471
|
....*
gi 1162548635 472 LYYRL 476
Cdd:COG0297 472 LYREL 476
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1-476 |
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: 653.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRG-IPDAQVVTRRDTFAGRITLLFGHF----N 75
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEvDDQVKVVELVDLSVGPRTLYVKVFegvvE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 76 GVGIYLIDAPHLYDRPGSPYHDtnlfAYTDNVQRFALLGWVGCEMACGLDpfWRPDVVHAHDWHAGLAPAYLAARG--HP 153
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGD----DYPDNAERFAFFSRAAAELLSGLG--WQPDVVHAHDWHTALVPALLKAVYrpNP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 154 AKSVFTVHNLAYQGMFYAKHMDDIQLPWSFFNVHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLQ 233
Cdd:TIGR02095 155 IKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGRVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGLDGVLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 234 QRhrEGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEEKAENKRQLQIAMGLKVNDKVPLFAVVSRLTSQKGLDLVLEA 313
Cdd:TIGR02095 235 AR--SGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 314 LPGLLEQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQLYGLKYGTLP 393
Cdd:TIGR02095 313 LPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 394 LVRRTGGLADTVSDSSLENladGIASGFVFEDSNAWSLLRAIRRAFVLW-SRPSLWRFVQRQAMTMDFSWQVAAKSYREL 472
Cdd:TIGR02095 393 IVRRTGGLADTVVDGDPEA---ESGTGFLFEEYDPGALLAALSRALRLYrQDPSLWEALQKNAMSQDFSWDKSAKQYVEL 469
|
....
gi 1162548635 473 YYRL 476
Cdd:TIGR02095 470 YRSL 473
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
2-475 |
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: 648.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 2 QVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGIPDAQVVTRRDTFAG----RITLLFGHFNGV 77
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKVGgrgeEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 78 GIYLIDAPHLYDRPGSPYhdTNLFAYTDNVQRFALLGWVGCEMACGLDpfWRPDVVHAHDWHAGLAPAYLAARGHP---- 153
Cdd:cd03791 81 DYYFLDNPEFFDRPGLPG--PPGYDYPDNAERFAFFSRAALELLRRLG--FQPDIIHANDWHTALVPAYLKTRYRGpgfk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 154 -AKSVFTVHNLAYQGMFYAKHMDDIQLPWSFFNVHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLL 232
Cdd:cd03791 157 kIKTVFTIHNLAYQGLFPLDTLAELGLPPELFHIDGLEFYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDGVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 233 qqRHREGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEEKAENKRQLQIAMGLKVNDKVPLFAVVSRLTSQKGLDLVLE 312
Cdd:cd03791 237 --RARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 313 ALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQLYGLKYGTL 392
Cdd:cd03791 315 ALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 393 PLVRRTGGLADTVSDSsleNLADGIASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMTMDFSWQVAAKSYREL 472
Cdd:cd03791 395 PIVRRTGGLADTVFDY---DPETGEGTGFVFEDYDAEALLAALRRALALYRNPELWRKLQKNAMKQDFSWDKSAKEYLEL 471
|
...
gi 1162548635 473 YYR 475
Cdd:cd03791 472 YRS 474
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
1-476 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 554.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGIPDAQVVTR-RDTFAGRITLLFGHFNGVGI 79
Cdd:PRK14099 4 LRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAGIEDAEQVHSfPDLFGGPARLLAARAGGLDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 80 YLIDAPHLYDRPGSPYHDTNLFAYTDNVQRFALLGWVGCEMACGLDPFWRPDVVHAHDWHAGLAPAYLAARGHPA-KSVF 158
Cdd:PRK14099 84 FVLDAPHLYDRPGNPYVGPDGKDWPDNAQRFAALARAAAAIGQGLVPGFVPDIVHAHDWQAGLAPAYLHYSGRPApGTVF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 159 TVHNLAYQGMFYAKHMDDIQLPWSFFNVHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLQQRhrE 238
Cdd:PRK14099 164 TIHNLAFQGQFPRELLGALGLPPSAFSLDGVEYYGGIGYLKAGLQLADRITTVSPTYALEIQGPEAGMGLDGLLRQR--A 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 239 GRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEEKAENKRQLQIAMGLKVNDKVPLFAVVSRLTSQKGLDLVLEALPGLL 318
Cdd:PRK14099 242 DRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 319 EQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVRRT 398
Cdd:PRK14099 322 GEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162548635 399 GGLADTVSDSSLENLADGIASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMTMDFSWQVAAKSYRELYYRL 476
Cdd:PRK14099 402 GGLADTVVDANEMAIATGVATGVQFSPVTADALAAALRKTAALFADPVAWRRLQRNGMTTDVSWRNPAQHYAALYRSL 479
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
3-234 |
1.02e-97 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 293.85 E-value: 1.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 3 VLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGIPDAQVVTRRDTFAG------RITLLFGHFNG 76
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGvpvrplTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 77 VGIYLIDAPHLYDRPGsPYHDTNlFAYTDNVQRFALLGWVGCEMACGLDpfWRPDVVHAHDWHAGLAPAYLAARGHP--- 153
Cdd:pfam08323 81 VDVYFLDNPDYFDRPG-LYGDDG-RDYEDNAERFAFFSRAALELAKKLG--WIPDIIHCHDWHTALVPAYLKEAYADdpf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 154 --AKSVFTVHNLAYQGMFYAKHMDDIQLPWSFFNVHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGL 231
Cdd:pfam08323 157 knIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFNLDGLEFYGQINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGLDGL 236
|
...
gi 1162548635 232 LQQ 234
Cdd:pfam08323 237 LRE 239
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
2-476 |
1.11e-82 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 263.90 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 2 QVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFP----------DIRRgIPDAQVVTRRDTF-------- 63
Cdd:PRK14098 7 KVLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGtindrkfrlhDVLR-LSDIEVPLKEKTDllhvkvta 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 64 --AGRITLLF----GHFNGVGIYlIDAPHLYDRPGSpyhdtnlfayTDNVQRFAL--------LGWvgcemacgldpfwR 129
Cdd:PRK14098 86 lpSSKIQTYFlyneKYFKRNGLF-TDMSLGGDLKGS----------AEKVIFFNVgvletlqrLGW-------------K 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 130 PDVVHAHDWHAGLAPAYLAAR--GHP----AKSVFTVHNLAYQGMFYAKHMDDIqLPWSFFNvhGLEF-NGQISFLKAGL 202
Cdd:PRK14098 142 PDIIHCHDWYAGLVPLLLKTVyaDHEffkdIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCS--GLHReGDEVNMLYTGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 203 YYADHITAVSPTYAREIT-EPQFAYGMEGLLQQRhrEGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEEKAENKRQLQ 281
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAgDGEEAFGLDKVLEER--KMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 282 IAMGLKVNDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGYHEAFSH 361
Cdd:PRK14098 297 EEVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 362 RIMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVsdsslENLADGIASGFVFEDSNAWSLLRAIRRAFVL 441
Cdd:PRK14098 377 LAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETI-----EEVSEDKGSGFIFHDYTPEALVAKLGEALAL 451
|
490 500 510
....*....|....*....|....*....|....*
gi 1162548635 442 WSRPSLWRFVQRQAMTMDFSWQVAAKSYRELYYRL 476
Cdd:PRK14098 452 YHDEERWEELVLEAMERDFSWKNSAEEYAQLYREL 486
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1-475 |
1.95e-76 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 257.91 E-value: 1.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRG-IPDAQV--VTRRDTFAGRI---TLLFGHF 74
Cdd:PLN02939 482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDqIRNLKVldVVVESYFDGNLfknKIWTGTV 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 75 NGVGIYLIDAPHlydrPGSPYHDTNLFAYTDNVQRFALLGWVGCEMAcgLDPFWRPDVVHAHDWH-AGLAPAY---LAAR 150
Cdd:PLN02939 562 EGLPVYFIEPQH----PSKFFWRAQYYGEHDDFKRFSYFSRAALELL--YQSGKKPDIIHCHDWQtAFVAPLYwdlYAPK 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 151 G-HPAKSVFTVHNLAYQGMFYAKHMDDIQLpwsffNVHGLE--------FNGQISFLKAGLYYADHITAVSPTYAREItE 221
Cdd:PLN02939 636 GfNSARICFTCHNFEYQGTAPASDLASCGL-----DVHQLDrpdrmqdnAHGRINVVKGAIVYSNIVTTVSPTYAQEV-R 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 222 PQFAYGMEGLLQQRHRegRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEEKAENKRQLQIAMGLKVND-KVPLFAVVSR 300
Cdd:PLN02939 710 SEGGRGLQDTLKFHSK--KFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLSSADaSQPLVGCITR 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 301 LTSQKGLDLVLEALPGLLEQGGQLALLGAgDPV--LQEGFLAAAAEHPGQVGVQI--GYHEAFSHRIMGGADVILVPSRF 376
Cdd:PLN02939 788 LVPQKGVHLIRHAIYKTAELGGQFVLLGS-SPVphIQREFEGIADQFQSNNNIRLilKYDEALSHSIYAASDMFIIPSMF 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 377 EPCGLTQLYGLKYGTLPLVRRTGGLADTVSDSSLENLADGIASGFVFEDSNAWSLLRAIRRAFVLWSR-PSLWRFVQRQA 455
Cdd:PLN02939 867 EPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDDETIPVELRNGFTFLTPDEQGLNSALERAFNYYKRkPEVWKQLVQKD 946
|
490 500
....*....|....*....|
gi 1162548635 456 MTMDFSWQVAAKSYRELYYR 475
Cdd:PLN02939 947 MNIDFSWDSSASQYEELYQR 966
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1-474 |
8.93e-68 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 234.38 E-value: 8.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIR-RGIPDAQVvTRRDTFAG-RITLLFGHFNGVG 78
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNlSHVKDLHY-QRSYSWGGtEIKVWFGKVEGLS 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 79 IYLIDAPHLYDRPGSPYhdtnlfAYTDNVQRFALLgwvgCEMACG--LDPFWRPDVVHAHDWHAglAPAYLAARGH---- 152
Cdd:PLN02316 667 VYFLEPQNGMFWAGCVY------GCRNDGERFGFF----CHAALEflLQSGFHPDIIHCHDWSS--APVAWLFKDHyahy 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 153 ---PAKSVFTVHNLAYQGMFYAKHMDdiqlpwsffnvhglefngqisflkaglyYADHITAVSPTYAREITepqfayGME 229
Cdd:PLN02316 735 glsKARVVFTIHNLEFGANHIGKAMA----------------------------YADKATTVSPTYSREVS------GNS 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 230 GLLQQRHRegrLSGVLNGVDEKIWSPETDLLLASRYTRD-TLEEKAENKRQLQIAMGLKVNDKvPLFAVVSRLTSQKGLD 308
Cdd:PLN02316 781 AIAPHLYK---FHGILNGIDPDIWDPYNDNFIPVPYTSEnVVEGKRAAKEALQQRLGLKQADL-PLVGIITRLTHQKGIH 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 309 LVLEALPGLLEQGGQLALLG-AGDPVLQEGFLAAA----AEHPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQ 383
Cdd:PLN02316 857 LIKHAIWRTLERNGQVVLLGsAPDPRIQNDFVNLAnqlhSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQ 936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 384 LYGLKYGTLPLVRRTGGLADTVSDSSLEN---LADGI-ASGFVFEDSNAWSLLRAIRRAFVLWSRPSLW-RFVQRQAMTM 458
Cdd:PLN02316 937 LTAMRYGSIPVVRKTGGLFDTVFDVDHDKeraQAQGLePNGFSFDGADAAGVDYALNRAISAWYDGRDWfNSLCKRVMEQ 1016
|
490
....*....|....*.
gi 1162548635 459 DFSWQVAAKSYRELYY 474
Cdd:PLN02316 1017 DWSWNRPALDYMELYH 1032
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
127-473 |
1.62e-22 |
|
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: 98.76 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 127 FWRPDVVHAHDWHAGLApAYLAARGHPAKSVFTVHNLAYQGMFYAKHmddIQLPWsffnvhglefngqISFLKAGLYYAD 206
Cdd:cd03801 80 LRKFDVVHAHGLLAALL-AALLALLLGAPLVVTLHGAEPGRLLLLLA---AERRL-------------LARAEALLRRAD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 207 HITAVSPTYAREITEpqfAYGMEgllqqrhrEGRLSGVLNGVDEKIWSPETDLllasrytrdtleekaenkrqlqiamGL 286
Cdd:cd03801 143 AVIAVSEALRDELRA---LGGIP--------PEKIVVIPNGVDLERFSPPLRR-------------------------KL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 287 KVNDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALL--GAGDPVLQEgflaaAAEHPGQVGVQIGYHEAFS---- 360
Cdd:cd03801 187 GIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVivGGDGPLRAE-----LEELELGLGDRVRFLGFVPdeel 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 361 HRIMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVsdsslenlADGIAsGFVFEDSNAWSLLRAIRRAfv 440
Cdd:cd03801 262 PALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV--------EDGEG-GLVVPPDDVEALADALLRL-- 330
|
330 340 350
....*....|....*....|....*....|....*
gi 1162548635 441 LWSRPSLWRFVQ--RQAMTMDFSWQVAAKSYRELY 473
Cdd:cd03801 331 LADPELRARLGRaaRERVAERFSWERVAERLLDLY 365
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
291-438 |
4.14e-14 |
|
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: 69.61 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 291 KVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEHPGQVGVQ-IGY--HEAFsHRIMGGA 367
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIfLGFvsDEDL-PELLKIA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162548635 368 DVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVsdsslenlADGIAsGFVFEDSNAWSLLRAIRRA 438
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV--------KDGET-GFLVKPNNAEALAEAIDKL 141
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
88-475 |
3.09e-13 |
|
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: 70.85 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 88 YDRPGSPYHDTNLFAYTDNVQRFALLGWVgcemacgldpfWRPDVVHAHDWHAGLApAYLAARGHPAKSVFTVHNLAyqg 167
Cdd:cd03819 46 QIGIGLPGLKVPLLRALLGNVRLARLIRR-----------ERIDLIHAHSRAPAWL-GWLASRLTGVPLVTTVHGSY--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 168 mfyakhmddiqlpwsFFNVHGLEFngqisfLKAGLYYADHITAVSPtYAREITEPQFAYGmegllqqrhrEGRLSGVLNG 247
Cdd:cd03819 111 ---------------LATYHPKDF------ALAVRARGDRVIAVSE-LVRDHLIEALGVD----------PERIRVIPNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 248 VDEKIWSPETdlllasrytrdtleeKAENKRQLQIAmglkvnDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALL 327
Cdd:cd03819 159 VDTDRFPPEA---------------EAEERAQLGLP------EGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 328 gAGDPvLQEGFLAAAAEHPG---QVGVqIGYHEAfSHRIMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADT 404
Cdd:cd03819 218 -AGDG-PERDEIRRLVERLGlrdRVTF-TGFRED-VPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREI 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162548635 405 VsdsslENLADGIASgfVFEDSNAwsLLRAIRRAFVLwsrPSLWRFVQRQAMTmdfswqvaAKSYRELYYR 475
Cdd:cd03819 294 V-----VHGRTGLLV--PPGDAEA--LADAIRAAKLL---PEAREKLQAAAAL--------TEAVRELLLR 344
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
66-476 |
1.39e-10 |
|
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: 62.78 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 66 RITLLFGHFNGVGIYLIDAPHLYDRPGSPYHDTNLFAYTDNVQRFALLGWvgcEMACGLDPF--WRPDVVHAH-DWHAGL 142
Cdd:cd03798 33 DVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAP---SLAKLLKRRrrGPPDLIHAHfAYPAGF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 143 APAYLAAR-GHPAksVFTVHnlayqGMFYAKHMddiqlPWSffnvhglefnGQISFLKAGLYYADHITAVSptyaREITE 221
Cdd:cd03798 110 AAALLARLyGVPY--VVTEH-----GSDINVFP-----PRS----------LLRKLLRWALRRAARVIAVS----KALAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 222 PQFAYGMegllqqrhREGRLSGVLNGVDEKIWSPETDlllasrytrdtleekaenkrqlqiamGLKVNDKVPLFAVVSRL 301
Cdd:cd03798 164 ELVALGV--------PRDRVDVIPNGVDPARFQPEDR--------------------------GLGLPLDAFVILFVGRL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 302 TSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEgFLAAAAEHPGqVGVQIGYHEAFSH----RIMGGADVILVPSRFE 377
Cdd:cd03798 210 IPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLRE-ALRALAEDLG-LGDRVTFTGRLPHeqvpAYYRACDVFVLPSRHE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 378 PCGLTQLYGLKYGTLPLVRRTGGLADTVSDSslenladgiASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRfVQRQAMT 457
Cdd:cd03798 288 GFGLVLLEAMACGLPVVATDVGGIPEVVGDP---------ETGLLVPPGDADALAAALRRALAEPYLRELGE-AARARVA 357
|
410
....*....|....*....
gi 1162548635 458 MDFSWQVAAKSYRELYYRL 476
Cdd:cd03798 358 ERFSWVKAADRIAAAYRDV 376
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
363-476 |
1.73e-10 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 58.46 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 363 IMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVSDSslenladgiASGFVFEDSNAWSLLRAIRRafvLW 442
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDG---------ETGLLVPPGDPEALAEAILR---LL 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 1162548635 443 SRPSLWRFVQ---RQAMTMDFSWQVAAKSYRELYYRL 476
Cdd:COG0438 85 EDPELRRRLGeaaRERAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
118-469 |
2.41e-10 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 62.26 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 118 CEMACGLDPFWR-----PDVVHAHDWHAGLApAYLAARGHPAKSVFTVHNLA---YQgmfyakHMDDIqlpWSFFnvhgl 189
Cdd:cd03800 85 EEFADGLLRFIAreggrYDLIHSHYWDSGLV-GALLARRLGVPLVHTFHSLGrvkYR------HLGAQ---DTYH----- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 190 eFNGQISFLKAGLYYADHITAvsptyareiTEPQFAYGMEGLLQQRhrEGRLSGVLNGVDEKIWSPETDlllasrytrdt 269
Cdd:cd03800 150 -PSLRITAEEQILEAADRVIA---------STPQEADELISLYGAD--PSRINVVPPGVDLERFFPVDR----------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 270 leekAENKRqlqIAMGLKVNDKVPLFavVSRLTSQKGLDLVLEALpGLLEQGGQLALL-----GAGDPVLQEGFLAAAAE 344
Cdd:cd03800 207 ----AEARR---ARLLLPPDKPVVLA--LGRLDPRKGIDTLVRAF-AQLPELRELANLvlvggPSDDPLSMDREELAELA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 345 HPGQVGVQIGYHEAFSHRIMG----GADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVsdsslenlADGIaSG 420
Cdd:cd03800 277 EELGLIDRVRFPGRVSRDDLPelyrAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIV--------RDGR-TG 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1162548635 421 FVFEDSNAWSLLRAIRRAFvlwSRPSLWRFVQRQAM---TMDFSWQVAAKSY 469
Cdd:cd03800 348 LLVDPHDPEALAAALRRLL---DDPALWQRLSRAGLeraRAHYTWESVADQL 396
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
297-407 |
5.66e-10 |
|
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: 59.34 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 297 VVSRLTSQKGLDLVLEALPGLLEQGG--QLALLGAGDPVLQEGFLAAAAEHPGQVGVQIGY-HEAFSHRIMGGADVILVP 373
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPdlVLVLVGGGGEREEEEALAAALGLLERVVIIGGLvDDEVLELLLAAADVFVLP 194
|
90 100 110
....*....|....*....|....*....|....
gi 1162548635 374 SRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVSD 407
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
258-473 |
2.51e-09 |
|
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: 58.88 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 258 DLLLA-SRYTRDTLEEK-AENKRQLQIAMGLKVNDKVPL----------FAVVSRLTSQKGLDLVLEALPGLLEQGGQLA 325
Cdd:cd03823 145 DAVLApSRFTANLHEANgLFSARISVIPNAVEPDLAPPPrrrpgterlrFGYIGRLTEEKGIDLLVEAFKRLPREDIELV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 326 LLGAGdPVLQEGFLAAaaehpgqvGVQIGYHEAFSH----RIMGGADVILVPSRF-EPCGLTQLYGLKYGTLPLVRRTGG 400
Cdd:cd03823 225 IAGHG-PLSDERQIEG--------GRRIAFLGRVPTddikDFYEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGG 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162548635 401 LADTVSDSslenladgiASGFVFEDSNAWSLLRAIRRafvLWSRPSLWRFVQRQAMTMDFSWQVAAKsYRELY 473
Cdd:cd03823 296 IAELIQPG---------VNGLLFAPGDAEDLAAAMRR---LLTDPALLERLRAGAEPPRSTESQAEE-YLKLY 355
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
128-249 |
1.83e-08 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 53.69 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 128 WRPDVVHAHDWHAGLAPAYLAARGHPAKSVFTVHNLAYQGMFYAKHMDDIQLPWsffnvhglefngqISFLKAGLYYADH 207
Cdd:pfam13439 70 ERPDVVHAHSPFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLL-------------RRLERRLLRRADR 136
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1162548635 208 ITAVSPTYAREITEpqfAYGMegllqqrhREGRLSGVLNGVD 249
Cdd:pfam13439 137 VIAVSEAVADELRR---LYGV--------PPEKIRVIPNGVD 167
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
129-471 |
4.40e-07 |
|
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: 51.98 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 129 RPDVVHAHDWHAGLapaylaaRGHPAKSVFTVHNLAYqgMFYAKHMddiqlPWSFFNVHGLefngqisFLKAGLYYADHI 208
Cdd:cd03809 84 KPDLLHSPHNTAPL-------LLKGCPQVVTIHDLIP--LRYPEFF-----PKRFRLYYRL-------LLPISLRRADAI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 209 TAVSPTYAREITEpqFaYGMegllqqrhREGRLSGVLNGVDEKIWSPETDLLLASRYtrdtleekaenkrqlqiamglkv 288
Cdd:cd03809 143 ITVSEATRDDIIK--F-YGV--------PPEKIVVIPLGVDPSFFPPESAAVLIAKY----------------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 289 NDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALL---GAGDPVLQEGFLAAAAEHPGQVgVQIGY------HEAF 359
Cdd:cd03809 189 LLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVivgGKGWEDEELLDLVKKLGLGGRV-RFLGYvsdedlPALY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 360 SHrimggADVILVPSRFEPCGLTQLYGLKYGTlPLVrrtggladtVSD-SSLENLADGiaSGFVFEDSNAWSLLRAIRRa 438
Cdd:cd03809 268 RG-----ARAFVFPSLYEGFGLPVLEAMACGT-PVI---------ASNiSVLPEVAGD--AALYFDPLDPESIADAILR- 329
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1162548635 439 fvLWSRPSLwrfvqRQAMTMD-------FSWQVAAKSYRE 471
Cdd:cd03809 330 --LLEDPSL-----REELIRKglerakkFSWEKTAEKTLE 362
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
17-221 |
1.71e-06 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 47.78 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 17 GGLADVIGALPAAQIADGVDARVLLPAFPDIRRGIPDAqvvtrrdtfagritllfghfnGVGIYLIDAPHLYDRPGSPyh 96
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGD---------------------GVRVHRLPVPPRPSPLADL-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 97 dtnlfAYTDNVQRFALLgwvgcemacgldpfWRPDVVHAHDWHAGLApAYLAARGHPAKSVFTVHNLAYQGmfyakhmdd 176
Cdd:pfam13579 58 -----AALRRLRRLLRA--------------ERPDVVHAHSPTAGLA-ARLARRRRGVPLVVTVHGLALDY--------- 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1162548635 177 iQLPWSFFNVHGLEfngqisflKAGLYYADHITAVSPTYAREITE 221
Cdd:pfam13579 109 -GSGWKRRLARALE--------RRLLRRADAVVVVSEAEAELLRA 144
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
127-429 |
5.13e-06 |
|
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: 48.43 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 127 FWRPDVVHAHD-WHAGLApAYLAARGHPAKSVFTVHNLAYQgmfYAKHMddiQLPWSFFNVHGlefngqISFLKAGLYYA 205
Cdd:cd03817 82 ELGPDIIHTHTpFSLGKL-GLRIARKLKIPIVHTYHTMYED---YLHYI---PKGKLLVKAVV------RKLVRRFYNHT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 206 DHITAVSPTYAREitepqfaygmeglLQQRHREGRLSGVLNGVDEKIWSPETDlllasrytrdtleekAENKRQLQIamg 285
Cdd:cd03817 149 DAVIAPSEKIKDT-------------LREYGVKGPIEVIPNGIDLDKFEKPLN---------------TEERRKLGL--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 286 lkvNDKVPLFAVVSRLTSQKGLDLVLEALPGLL-EQGGQLALLGAGD--PVLQEgfLAAAAEHPGQVgVQIGYHEafsHR 362
Cdd:cd03817 198 ---PPDEPILLYVGRLAKEKNIDFLLRAFAELKkEPNIKLVIVGDGPerEELKE--LARELGLADKV-IFTGFVP---RE 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162548635 363 IMG----GADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVSDSSlenladgiaSGFVFEDSNAW 429
Cdd:cd03817 269 ELPeyykAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGE---------NGFLFEPNDET 330
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
293-437 |
1.11e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 44.81 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 293 PLFAVVSRLTS-QKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEgFLAAAAEHPGQVgVQIGYHEAFsHRIMGGADVIL 371
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLEDRV-IFTGFVEDL-AELLAAADVFV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162548635 372 VPSRFEPCGLTQLYGLKYGtLPLV-RRTGGLADTVsdsslenlaDGIAsGFVFEDSNAWSLLRAIRR 437
Cdd:pfam13692 79 LPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELV---------DGEN-GLLVPPGDPEALAEAILR 134
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
293-476 |
6.38e-05 |
|
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: 44.98 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 293 PLFAVVSRLTSQKGLDLVLEA-LPGLLEQGGQLALLGAG--DPVLQEGFLAAaaehpgqvgVQIGYH--EAFShRIMGGA 367
Cdd:cd03814 199 PLLLYVGRLAPEKNLEALLDAdLPLAASPPVRLVVVGDGpaRAELEARGPDV---------IFTGFLtgEELA-RAYASA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 368 DVILVPSRFEPCGLTQLYGLKYGtLPLV-RRTGGLADTVSDSslenladgiASGFVFEDSNAWSLLRAIRRafvLWSRPS 446
Cdd:cd03814 269 DVFVFPSRTETFGLVVLEAMASG-LPVVaADAGGPRDIVRPG---------GTGALVEPGDAAAFAAALRA---LLEDPE 335
|
170 180 190
....*....|....*....|....*....|
gi 1162548635 447 LwrfvqRQAMTMDFSWQVAAKSYRELYYRL 476
Cdd:cd03814 336 L-----RRRMAARARAEAERYSWEAFLDNL 360
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
94-469 |
1.83e-04 |
|
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: 43.87 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 94 PYHDTNLFAYTDNVQRFALLGWVGCemacgLDPFWRPDVVHAHDWHAGLA-PAYLAARGHPAKSVFTVHNLAYQ-----G 167
Cdd:cd03794 68 PIKKNGLIRRLLNYLSFALAALLKL-----LVREERPDVIIAYSPPITLGlAALLLKKLRGAPFILDVRDLWPEslialG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 168 MFYAKHMDDIqlpWSFFNvhglefngqisflKAGLYYADHITAVSPTYAREItepqfaygmeglLQQRHREGRLSGVLNG 247
Cdd:cd03794 143 VLKKGSLLKL---LKKLE-------------RKLYRLADAIIVLSPGLKEYL------------LRKGVPKEKIIVIPNW 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 248 VDEKIWSPetdlllasrytrdtleekaeNKRQLQIAMGLKVNDKVPLFAVVsrLTSQKGLDLVLEALPGLLEQGG-QLAL 326
Cdd:cd03794 195 ADLEEFKP--------------------PPKDELRKKLGLDDKFVVVYAGN--IGKAQGLETLLEAAERLKRRPDiRFLF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 327 LGAGDPVlqEGFLAAAAEHPGQVGVQIGY--HEAFSHrIMGGADVILVPSRFEPCGL----TQLYG-LKYGtLPLVrrtg 399
Cdd:cd03794 253 VGDGDEK--ERLKELAKARGLDNVTFLGRvpKEEVPE-LLSAADVGLVPLKDNPANRgsspSKLFEyMAAG-KPIL---- 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162548635 400 GLADTVSDSSLEnlaDGIAsGFVFEDSNAWSLLRAIRRAfvLWSrPSLWRFV---QRQAMTMDFSWQVAAKSY 469
Cdd:cd03794 325 ASDDGGSDLAVE---INGC-GLVVEPGDPEALADAILEL--LDD-PELRRAMgenGRELAEEKFSREKLADRL 390
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
246-476 |
9.46e-04 |
|
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: 41.55 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 246 NGVDEKIWSPEtdlllasrytrdtleEKAENKRQLqiamGLKVNDKVPLFAVVSRLTSQKGLDLVLEALPGLL-EQGGQL 324
Cdd:cd03825 168 NGIDTEIFAPV---------------DKAKARKRL----GIPQDKKVILFGAESVTKPRKGFDELIEALKLLAtKDDLLL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 325 ALLGAGDPVLQEGflaaaaehPGQVgVQIGY--HEAFSHRIMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLA 402
Cdd:cd03825 229 VVFGKNDPQIVIL--------PFDI-ISLGYidDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSP 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162548635 403 DTVSDSSlenlaDGIASGfvFEDSNAwsLLRAIRRafVLWSRPSLWRFVQRQ--AMTMDFSWQVAAKSYRELYYRL 476
Cdd:cd03825 300 EIVQHGV-----TGYLVP--PGDVQA--LAEAIEW--LLANPKERESLGERAraLAENHFDQRVQAQRYLELYKDL 364
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
271-409 |
3.01e-03 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 39.77 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 271 EEKAENKRQlqiAMGLKVNDKVPLFAvvSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPV-LQEGFLAAAAEHPGQV 349
Cdd:PRK15484 177 SNPQPNLRQ---QLNISPDETVLLYA--GRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTaSSKGEKAAYQKKVLEA 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162548635 350 GVQIGyheafSHRIMGG-------------ADVILVPSRF-EPCGLTQLYGLKYGTLPLVRRTGGLADTVSDSS 409
Cdd:PRK15484 252 AKRIG-----DRCIMLGgqppekmhnyyplADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGI 320
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
293-471 |
5.16e-03 |
|
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: 38.89 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 293 PLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAG-DPVLQEGFLAAAAEHPGQVGVQIG---YHEAFShRIMGGAD 368
Cdd:cd03821 205 RIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTgplYGEAKW-ALYASAD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162548635 369 VILVPSRFEPCGLTQLYGLKYGtLPLVrrtggladtVSDSSleNLADGI--ASGFVFeDSNAWSLLRAIRRAFVLWSRPS 446
Cdd:cd03821 284 LFVLPSYSENFGNVVAEALACG-LPVV---------ITDKC--GLSELVeaGCGVVV-DPNVSSLAEALAEALRDPADRK 350
|
170 180
....*....|....*....|....*..
gi 1162548635 447 LWRFVQRQAMTMD--FSWQVAAKSYRE 471
Cdd:cd03821 351 RLGEMARRARQVEenFSWEAVAGQLGE 377
|
|
| |
