|
Name |
Accession |
Description |
Interval |
E-value |
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
86-584 |
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: 553.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 86 VIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDQYKDAWDTCVVVQ---IKVGDKVENVRFFHCYKRGVD 162
Cdd:cd03791 2 VLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLgleVKVGGRGEEVGVFELPVDGVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 163 RVFVDHPIFLAKVVGKtgskiygPITGVDYNDNQLRFSLLCQAALEAPQVLnlnsskyfsgpYGEDVVFVANDWHTALLP 242
Cdd:cd03791 82 YYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-----------GFQPDIIHANDWHTALVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 243 CYLKSMYQSRGvYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPisfkSSFDFMDGYEKPvkgRKINWMKAAILEAHRVLTV 322
Cdd:cd03791 144 AYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLP----PELFHIDGLEFY---GQINFLKAGIVYADRVTTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 323 SPYYAQELISGvDRGVELHKYLRM--KTVSGIINGMDVQEWNPSTDKYIDIKYDITTVTDaKPLIKEALQAAVGLPVDRD 400
Cdd:cd03791 216 SPTYAKEILTP-EYGEGLDGVLRAraGKLSGILNGIDYDEWNPATDKLIPANYSANDLEG-KAENKAALQKELGLPVDPD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 401 VPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHMITAGADFII 480
Cdd:cd03791 294 APLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 481 VPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGY------TGFHIGRFNvkcevvdPDDVIAtakAVTRAVAVYGT 554
Cdd:cd03791 374 MPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDpetgegTGFVFEDYD-------AEALLA---ALRRALALYRN 443
|
490 500 510
....*....|....*....|....*....|.
gi 15223331 555 -SAMQEMVKNCMDQDFSWKGPARLWEKVLLS 584
Cdd:cd03791 444 pELWRKLQKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
84-585 |
4.86e-174 |
|
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: 502.57 E-value: 4.86e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 84 MSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDQYKDAW----DTCVVVQIKVGDKVENVRFFHCYKR 159
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVddqvKVVELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 160 GVDRVFVDHPIFLakvvgKTGSKIYGPitgvDYNDNQLRFSLLCQAALEAPQVLNlnsskyfsgpYGEDVVfVANDWHTA 239
Cdd:TIGR02095 81 GVPVYFIDNPSLF-----DRPGGIYGD----DYPDNAERFAFFSRAAAELLSGLG----------WQPDVV-HAHDWHTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 240 LLPCYLKSMYqsrgVYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPISFKSSFDFMDGyekpvkgRKINWMKAAILEAHRV 319
Cdd:TIGR02095 141 LVPALLKAVY----RPNPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFY-------GRVNFLKGGIVYADRV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 320 LTVSPYYAQELISGvDRGVELHKYLRMKT--VSGIINGMDVQEWNPSTDKYIDIKYDITTVTDAKPLiKEALQAAVGLPV 397
Cdd:TIGR02095 210 TTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAEN-KEALQEELGLPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 398 DRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHMITAGAD 477
Cdd:TIGR02095 288 DDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGAD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 478 FIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDG------YTGFHIGRfnvkcevVDPDDVIAtakAVTRAVAV 551
Cdd:TIGR02095 368 FILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGdpeaesGTGFLFEE-------YDPGALLA---ALSRALRL 437
|
490 500 510
....*....|....*....|....*....|....*.
gi 15223331 552 YGT--SAMQEMVKNCMDQDFSWKGPARLWEKVLLSL 585
Cdd:TIGR02095 438 YRQdpSLWEALQKNAMSQDFSWDKSAKQYVELYRSL 473
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
84-576 |
3.24e-156 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 456.86 E-value: 3.24e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 84 MSVIFIGAEVGPWSKTgglgdvlgglPPALAARGHRVMTICPRYDQYKDAWDTCVVV---QIKVGDKVENVRFFHCYKRG 160
Cdd:COG0297 1 MKILFVASEAAPFAKTggladvvgalPKALAKLGHDVRVVLPGYPSIDDKLKDLEVVaslEVPLGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 161 VDRVFVDHPIFLAkvvgktGSKIYGPITGvDYNDNQLRFSLLCQAALEAPQVLNLNsskyfsgPygeDVVFvANDWHTAL 240
Cdd:COG0297 81 VPVYFIDNPELFD------RPGPYGDPDR-DYPDNAERFAFFSRAALELLKGLDWK-------P---DIIH-CHDWQTGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 241 LPCYLKSMYQSRGvYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPisfkSSFDFMDGYEKPvkGrKINWMKAAILEAHRVL 320
Cdd:COG0297 143 IPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLP----PELFTPDGLEFY--G-QINFLKAGIVYADRVT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 321 TVSPYYAQELISGvDRGVELHKYLRMK--TVSGIINGMDVQEWNPSTDKYIDIKYDITTVtDAKPLIKEALQAAVGLPVD 398
Cdd:COG0297 215 TVSPTYAREIQTP-EFGEGLDGLLRARsgKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPVD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 399 RDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHMITAGADF 478
Cdd:COG0297 293 PDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 479 IIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKD------GYTGFhigrfnvkceVVDPDDVIATAKAVTRAVAVY 552
Cdd:COG0297 373 FLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDyneatgEGTGF----------VFDEYTAEALLAAIRRALALY 442
|
490 500
....*....|....*....|....*
gi 15223331 553 G-TSAMQEMVKNCMDQDFSWKGPAR 576
Cdd:COG0297 443 RdPEAWRKLQRNAMKQDFSWEKSAK 467
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
84-576 |
6.74e-135 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 402.19 E-value: 6.74e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 84 MSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDQYKDA-WDTCVVVQIkvgDKVeNVRFFHCYKRGVD 162
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKlRDAQVVGRL---DLF-TVLFGHLEGDGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 163 RVFVDHPIFlakvvgktgskiYGPITGVDYNDNQLRFSLLCQAALEAPQVLNLNsskyfsgPygeDVVFvANDWHTALLP 242
Cdd:PRK00654 77 VYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPR-------P---DIVH-AHDWHTGLIP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 243 CYLKSMYQSRgvYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPISFkssFDfMDGYEKPvkgRKINWMKAAILEAHRVLTV 322
Cdd:PRK00654 134 ALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEA---FH-LEGLEFY---GQISFLKAGLYYADRVTTV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 323 SPYYAQElISGVDRGVELHKYLRMKT--VSGIINGMDVQEWNPSTDKYIDIKYDITTVtDAKPLIKEALQAAVGLPVDrD 400
Cdd:PRK00654 205 SPTYARE-ITTPEFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPDD-D 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 401 VPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKaVGVA-KFNVPLAHMITAGADFI 479
Cdd:PRK00654 282 APLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGK-VGVQiGYDEALAHRIYAGADMF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 480 IVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGY------TGFHigrFnvkcevvDPDDVIATAKAVTRAVAVYG 553
Cdd:PRK00654 361 LMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYNpedgeaTGFV---F-------DDFNAEDLLRALRRALELYR 430
|
490 500
....*....|....*....|....
gi 15223331 554 T-SAMQEMVKNCMDQDFSWKGPAR 576
Cdd:PRK00654 431 QpPLWRALQRQAMAQDFSWDKSAE 454
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
84-585 |
6.88e-93 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 294.32 E-value: 6.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 84 MSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYdqykdawdTCVVVQIKVGDKVE--------NVRFFH 155
Cdd:PRK14099 4 LRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGY--------PAVLAGIEDAEQVHsfpdlfggPARLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 156 CYKRGVDRVFVDHPIFLAKvvgkTGSKIYGPiTGVDYNDNQLRFSLLCQAALEAPQVLnlnsskyfSGPYGEDVVFvAND 235
Cdd:PRK14099 76 ARAGGLDLFVLDAPHLYDR----PGNPYVGP-DGKDWPDNAQRFAALARAAAAIGQGL--------VPGFVPDIVH-AHD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 236 WHTALLPCYLKsmYQSRGvymNAKVVFCIHNIAYQGRFAFDDYSLLNLPisfKSSFDfMDGYEkpVKGrKINWMKAAILE 315
Cdd:PRK14099 142 WQAGLAPAYLH--YSGRP---APGTVFTIHNLAFQGQFPRELLGALGLP---PSAFS-LDGVE--YYG-GIGYLKAGLQL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 316 AHRVLTVSPYYAQElISGVDRGVELHKYLRMKT--VSGIINGMDVQEWNPSTDKYIDIKYDITTVTdAKPLIKEALQAAV 393
Cdd:PRK14099 210 ADRITTVSPTYALE-IQGPEAGMGLDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVETLA-ARAANKAALQARF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 394 GLPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHMIT 473
Cdd:PRK14099 288 GLDPDPDALLLGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 474 AGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDG-----YTGFHIGrfnVKCEVVDPDdviATAKAVTRA 548
Cdd:PRK14099 368 AGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDAnemaiATGVATG---VQFSPVTAD---ALAAALRKT 441
|
490 500 510
....*....|....*....|....*....|....*...
gi 15223331 549 VAVYG-TSAMQEMVKNCMDQDFSWKGPARLWEKVLLSL 585
Cdd:PRK14099 442 AALFAdPVAWRRLQRNGMTTDVSWRNPAQHYAALYRSL 479
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
234-575 |
6.78e-66 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 223.46 E-value: 6.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 234 NDWHTALLPCYLKSMYQSRGVYMNAKVVFCIHNIAYQGRFAFDDYSLLnLPISFKSSFDfmdgyekpVKGRKINWMKAAI 313
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCSGLH--------REGDEVNMLYTGV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 314 LEAHRVLTVSPYYAQELISGVDRGVELHKYL--RMKTVSGIINGMDVQEWNPSTDKYIDIKYDITTVtDAKPLIKEALQA 391
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERL-DGKLENKKALLE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 392 AVGLPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHM 471
Cdd:PRK14098 298 EVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 472 ITAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVK----DGYTGFHIGRFNVKcevvdpddviATAKAVTR 547
Cdd:PRK14098 378 AIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEevseDKGSGFIFHDYTPE----------ALVAKLGE 447
|
330 340
....*....|....*....|....*....
gi 15223331 548 AVAVYGTSAM-QEMVKNCMDQDFSWKGPA 575
Cdd:PRK14098 448 ALALYHDEERwEELVLEAMERDFSWKNSA 476
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
86-345 |
1.43e-65 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 214.50 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 86 VIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYD-------QYKDAWDTCVVVQIKVGDkvENVRFFHCYK 158
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGnipeernQLEDVIRLSVAAGVPVRP--LTVGVARLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 159 RGVDRVFVDHPIFLAKvvgktgSKIYGPiTGVDYNDNQLRFSLLCQAALEAPQVLNlnsskyfsgpYGEDVVfVANDWHT 238
Cdd:pfam08323 79 DGVDVYFLDNPDYFDR------PGLYGD-DGRDYEDNAERFAFFSRAALELAKKLG----------WIPDII-HCHDWHT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 239 ALLPCYLKSMYQSRGVYmNAKVVFCIHNIAYQGRFAFDDYSLLNLPISFKSsfdfMDGYEKPvkgRKINWMKAAILEAHR 318
Cdd:pfam08323 141 ALVPAYLKEAYADDPFK-NIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY---GQINFLKAGIVYADA 212
|
250 260
....*....|....*....|....*..
gi 15223331 319 VLTVSPYYAQELISGVDrGVELHKYLR 345
Cdd:pfam08323 213 VTTVSPTYAEEIQTPEF-GGGLDGLLR 238
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
83-584 |
1.15e-54 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 200.51 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 83 GMSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYD--QYKDAWDTC---VVVQIKVGDKVENVRFFHCY 157
Cdd:PLN02939 481 GLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDcmQYDQIRNLKvldVVVESYFDGNLFKNKIWTGT 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 158 KRGVDRVFVD--HPiflAKVVGKtgSKIYGPitgvdyNDNQLRFSLLCQAALEapqvLNLNSSKYFsgpygeDVVFvAND 235
Cdd:PLN02939 561 VEGLPVYFIEpqHP---SKFFWR--AQYYGE------HDDFKRFSYFSRAALE----LLYQSGKKP------DIIH-CHD 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 236 WHTALL-PCYLkSMYQSRGvYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPISfksSFDFMDGYEKPVKGRkINWMKAAIL 314
Cdd:PLN02939 619 WQTAFVaPLYW-DLYAPKG-FNSARICFTCHNFEYQGTAPASDLASCGLDVH---QLDRPDRMQDNAHGR-INVVKGAIV 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 315 EAHRVLTVSPYYAQELISGVDRGveLHKYLRM--KTVSGIINGMDVQEWNPSTDKYIDIKYDITTVtDAKPLIKEALQAA 392
Cdd:PLN02939 693 YSNIVTTVSPTYAQEVRSEGGRG--LQDTLKFhsKKFVGILNGIDTDTWNPSTDRFLKVQYNANDL-QGKAANKAALRKQ 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 393 VGLP-VDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTgkkkmeAQILELEEKFPGKAVG---------VA 462
Cdd:PLN02939 770 LGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGS------SPVPHIQREFEGIADQfqsnnnirlIL 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 463 KFNVPLAHMITAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKD------------GYTgfhigrfnvkc 530
Cdd:PLN02939 844 KYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDfddetipvelrnGFT----------- 912
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15223331 531 eVVDPDDViATAKAVTRAVAVYGTSAM--QEMVKNCMDQDFSWKGPARLWEKVLLS 584
Cdd:PLN02939 913 -FLTPDEQ-GLNSALERAFNYYKRKPEvwKQLVQKDMNIDFSWDSSASQYEELYQR 966
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
76-575 |
1.11e-53 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 197.79 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 76 GKIVCEKGMSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDqykdawdtCVvvqikvgdKVENVRFFH 155
Cdd:PLN02316 580 GGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYD--------CL--------NLSHVKDLH 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 156 cYKRGVDRVFVDHPIFLAKVVG--------KTGSKIYGPITGVDyNDNQlRFSLLCQAALEAPQvlnlnsskyfSGPYGE 227
Cdd:PLN02316 644 -YQRSYSWGGTEIKVWFGKVEGlsvyflepQNGMFWAGCVYGCR-NDGE-RFGFFCHAALEFLL----------QSGFHP 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 228 DVVFvANDWHTALLPCYLKSMYQSRGVyMNAKVVFCIHNIAYqgrfafddysllnlpisfkssfdfmdgyekpvkgrKIN 307
Cdd:PLN02316 711 DIIH-CHDWSSAPVAWLFKDHYAHYGL-SKARVVFTIHNLEF-----------------------------------GAN 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 308 WMKAAILEAHRVLTVSPYYAQELISGVDRGVELHKYlrmktvSGIINGMDVQEWNPSTDKYIDIKYDITTVTDAKPLIKE 387
Cdd:PLN02316 754 HIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKF------HGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKE 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 388 ALQAAVGLPvDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTG-KKKMEAQILELEEKFPGKAVGVAK--- 463
Cdd:PLN02316 828 ALQQRLGLK-QADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSApDPRIQNDFVNLANQLHSSHHDRARlcl 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 464 -FNVPLAHMITAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVkdgytgfhigrFNV-------KCEVVDP 535
Cdd:PLN02316 907 tYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTV-----------FDVdhdkeraQAQGLEP 975
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15223331 536 D-------DVIATAKAVTRAVAVY--GTSAMQEMVKNCMDQDFSWKGPA 575
Cdd:PLN02316 976 NgfsfdgaDAAGVDYALNRAISAWydGRDWFNSLCKRVMEQDWSWNRPA 1024
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
219-582 |
1.17e-25 |
|
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: 108.78 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 219 KYFSGPYGEDVVfVANDWHTALLPCYLKSMYqsrgvymNAKVVFCIHNIAYQGRFAFDDYSLlnlpisfkssfdfmdgye 298
Cdd:cd03801 75 RPLLRLRKFDVV-HAHGLLAALLAALLALLL-------GAPLVVTLHGAEPGRLLLLLAAER------------------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 299 kpvkgRKINWMKAAILEAHRVLTVSPYYAQELISGVDRGVELHKYLRmktvsgiiNGMDVQEWNPSTDKyidikydittv 378
Cdd:cd03801 129 -----RLLARAEALLRRADAVIAVSEALRDELRALGGIPPEKIVVIP--------NGVDLERFSPPLRR----------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 379 tdakplikealqaavGLPVDRDVPVIGFIGRLEEQKGSDILVEAISKF--MGLNVQMVILGTGKKKMEaqilELEEKFPG 456
Cdd:cd03801 185 ---------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLlrRGPDVRLVIVGGDGPLRA----ELEELELG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 457 KAVGVaKF--NVPLAHM--ITAGADFIIVPSRFEPCGLIQLHAMRYGTvPIVAS-TGGLVDTVKDGYTGFhigrfnvkce 531
Cdd:cd03801 246 LGDRV-RFlgFVPDEELpaLYAAADVFVLPSRYEGFGLVVLEAMAAGL-PVVATdVGGLPEVVEDGEGGL---------- 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15223331 532 VVDPDDVIATAKAVTRAVAvyGTSAMQEMVKN---CMDQDFSWKGPARLWEKVL 582
Cdd:cd03801 314 VVPPDDVEALADALLRLLA--DPELRARLGRAareRVAERFSWERVAERLLDLY 365
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
293-576 |
9.47e-19 |
|
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: 88.84 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 293 FMDGYEKPVKGRKINWMKAAILEAHRVLTVSPYYAQELIS--GVDRGvelhkylRMKTVSgiiNGMDVQEWNPSTDKyid 370
Cdd:cd03800 141 HLGAQDTYHPSLRITAEEQILEAADRVIASTPQEADELISlyGADPS-------RINVVP---PGVDLERFFPVDRA--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 371 ikydittvtdakplikEALQAAVGLPVDRdvPVIGFIGRLEEQKGSDILVEAI--SKFMGLNVQMVILG---TGKKKME- 444
Cdd:cd03800 208 ----------------EARRARLLLPPDK--PVVLALGRLDPRKGIDTLVRAFaqLPELRELANLVLVGgpsDDPLSMDr 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 445 ------AQILELEEK--FPGkavGVAKFNVPLahmITAGADFIIVPSRFEPCGLIQLHAMRYGTvPIVAS-TGGLVDTVK 515
Cdd:cd03800 270 eelaelAEELGLIDRvrFPG---RVSRDDLPE---LYRAADVFVVPSLYEPFGLTAIEAMACGT-PVVATaVGGLQDIVR 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15223331 516 DGYTGFHigrfnvkcevVDPDDVIATAKAVTRAVAvyGTSAMQEMVKNCMD---QDFSWKGPAR 576
Cdd:cd03800 343 DGRTGLL----------VDPHDPEALAAALRRLLD--DPALWQRLSRAGLErarAHYTWESVAD 394
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
400-548 |
5.95e-18 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 81.17 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 400 DVPVIGFIGRLEEQKGSDILVEAISKF--MGLNVQMVILGTG--KKKMEAQILELEekfPGKAVGVAKF--NVPLAHMIT 473
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLkeKNPNLKLVIAGDGeeEKRLKKLAEKLG---LGDNVIFLGFvsDEDLPELLK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15223331 474 AgADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKAVTRA 548
Cdd:pfam00534 78 I-ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF----------LVKPNNAEALAEAIDKL 141
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
402-547 |
1.47e-16 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 76.40 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 402 PVIGFIGRL-EEQKGSDILVEAISKFM--GLNVQMVILGTGK-KKMEAQILELEEK--FPGKAVGVAKFnvpLAHmitag 475
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRkrDNDVRLVIVGDGPeEELEELAAGLEDRviFTGFVEDLAEL---LAA----- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15223331 476 ADFIIVPSRFEPCGLIQLHAMRYGtVPIVAST-GGLVDTVkDGYTGFhigrfnvkceVVDPDDVIATAKAVTR 547
Cdd:pfam13692 74 ADVFVLPSLYEGFGLKLLEAMAAG-LPVVATDvGGIPELV-DGENGL----------LVPPGDPEALAEAILR 134
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
400-550 |
1.11e-14 |
|
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: 75.88 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 400 DVPVIGFIGRLEEQKGSDILVEAISKFM--GLNVQMVILGTG--KKKMEAQI--LELEEKFpgKAVGVAKFNVPLAHMit 473
Cdd:cd03798 199 DAFVILFVGRLIPRKGIDLLLEAFARLAkaRPDVVLLIVGDGplREALRALAedLGLGDRV--TFTGRLPHEQVPAYY-- 274
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15223331 474 AGADFIIVPSRFEPCGLIQLHAMRYGTvPIVAS-TGGLVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKAVTRAVA 550
Cdd:cd03798 275 RACDVFVLPSRHEGFGLVLLEAMACGL-PVVATdVGGIPEVVGDPETGL----------LVPPGDADALAAALRRALA 341
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
304-544 |
1.83e-14 |
|
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: 75.32 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 304 RKINWMKAAILE------AHRVLTVSPYYAQELIsgvdrgvELHKYLRMKTVSGIINGMDVQEWNPSTDKYIDikyditt 377
Cdd:cd03808 122 GKLLRLLYLLLEklallfTDKVIFVNEDDRDLAI-------KKGIIKKKKTVLIPGSGVDLDRFQYSPESLPS------- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 378 vtdakplikealqaavglpvdrDVPVIGFIGRLEEQKGSDILVEAIS--KFMGLNVQMVILGTGKKKMEAQI----LELE 451
Cdd:cd03808 188 ----------------------EKVVFLFVARLLKDKGIDELIEAAKilKKKGPNVRFLLVGDGELENPSEIliekLGLE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 452 E--KFPGKAVGVAKFnvpLAHmitagADFIIVPSRFEPCGLIQLHAMRYGtVPIVAS-TGGLVDTVKDGYTGFhigrfnv 528
Cdd:cd03808 246 GriEFLGFRSDVPEL---LAE-----SDVFVLPSYREGLPRSLLEAMAAG-RPVITTdVPGCRELVIDGVNGF------- 309
|
250
....*....|....*.
gi 15223331 529 kceVVDPDDVIATAKA 544
Cdd:cd03808 310 ---LVPPGDVEALADA 322
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
228-545 |
2.06e-14 |
|
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: 75.09 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 228 DVVFvandWHTALLPCYLKSMYQSRgvymnAKVVFCIHNiayqgrFAFDDYSLLNLPISFKSSFDFMDgyekpvkgrkin 307
Cdd:cd03811 85 DVVI----SFLGFATYIVAKLAAAR-----SKVIAWIHS------SLSKLYYLKKKLLLKLKLYKKAD------------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 308 wmkaaileahRVLTVSPYYAQELISgvdrgvelHKYLRMKTVSGIINGmdvqewnpstdkyIDIkydittvtdakPLIKE 387
Cdd:cd03811 138 ----------KIVCVSKGIKEDLIR--------LGPSPPEKIEVIYNP-------------IDI-----------DRIRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 388 ALQAAVGLPvDRDVPVIGFIGRLEEQKGSDILVEAISKF--MGLNVQMVILGTGKKKME----AQILELEEK--FPGKav 459
Cdd:cd03811 176 LAKEPILNE-PEDGPVILAVGRLDPQKGHDLLIEAFAKLrkKYPDVKLVILGDGPLREEleklAKELGLAERviFLGF-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 460 gvaKFNvPLAHMitAGADFIIVPSRFEPCGLIQLHAMRYGTvPIVAS-TGGLVDTVKDGYTGFhigrfnvkceVVDPDDV 538
Cdd:cd03811 253 ---QSN-PYPYL--KKADLFVLSSRYEGFPNVLLEAMALGT-PVVSTdCPGPREILDDGENGL----------LVPDGDA 315
|
....*..
gi 15223331 539 IATAKAV 545
Cdd:cd03811 316 AALAGIL 322
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
406-523 |
6.04e-13 |
|
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: 68.58 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 406 FIGRLEEQKGSDILVEAISKF--MGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKF-NVPLAHMITAGADFIIVP 482
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLkaRLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLvDDEVLELLLAAADVFVLP 194
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15223331 483 SRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFHI 523
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
468-585 |
1.35e-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: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 468 LAHMITAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKAVTR 547
Cdd:COG0438 13 LLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGL----------LVPPGDPEALAEAILR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15223331 548 AVAVYgtSAMQEMVKNCMD---QDFSWKGPARLWEKVLLSL 585
Cdd:COG0438 83 LLEDP--ELRRRLGEAAREraeERFSWEAIAERLLALYEEL 121
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
403-549 |
1.03e-11 |
|
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: 66.58 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 403 VIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQI-----LELEEKFPGKAVGvakfnvplAHMitAGAD 477
Cdd:cd03823 193 RFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGPLSDERQIeggrrIAFLGRVPTDDIK--------DFY--EKID 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15223331 478 FIIVPSRF-EPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFHIgrfnvkcevvDPDDVIATAKAVTRAV 549
Cdd:cd03823 263 VLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLF----------APGDAEDLAAAMRRLL 325
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
395-582 |
1.15e-11 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 66.74 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 395 LPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGL--NVQMVILG--TGKKKMEA-----QILELEEKFPGKAVGVAKFN 465
Cdd:PRK15484 187 LNISPDETVLLYAGRISPDKGILLLMQAFEKLATAhsNLKLVVVGdpTASSKGEKaayqkKVLEAAKRIGDRCIMLGGQP 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 466 VPLAHMITAGADFIIVPSRF-EPCGLIQLHAMRYGTvPIVAST-GGLVDTVKDGYTGFHIGrfnvkcEVVDPDDVIATak 543
Cdd:PRK15484 267 PEKMHNYYPLADLVVVPSQVeEAFCMVAVEAMAAGK-PVLASTkGGITEFVLEGITGYHLA------EPMTSDSIISD-- 337
|
170 180 190
....*....|....*....|....*....|....*....
gi 15223331 544 aVTRAVAVYGTSAMQEMVKNCMDQDFSWKGPARLWEKVL 582
Cdd:PRK15484 338 -INRTLADPELTQIAEQAKDFVFSKYSWEGVTQRFEEQI 375
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
397-550 |
2.73e-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: 62.37 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 397 VDRDVPVIGFIGRLEEQKGSDILVEAISKF-MGLNVQMVILGTG--KKKMEAQILELeekfpGKA--VGVAKFNVPLAHM 471
Cdd:cd03819 178 LPEGKPVVGYVGRLSPEKGWLLLVDAAAELkDEPDFRLLVAGDGpeRDEIRRLVERL-----GLRdrVTFTGFREDVPAA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 472 ITAgADFIIVPSRFEPCGLIQLHAMRYGTvPIVAST-GGLVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKAVTRAVA 550
Cdd:cd03819 253 LAA-SDVVVLPSLHEEFGRVALEAMACGT-PVVATDvGGAREIVVHGRTGL----------LVPPGDAEALADAIRAAKL 320
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
407-544 |
9.31e-10 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 60.71 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 407 IGRLEEQKGSDILVEAIS----KFMGLnvQMVILGTG--KKKMEAQI--LELEE--KFPGKAVGVAKfnvplahmITAGA 476
Cdd:cd03820 187 VGRLTYQKGFDLLIEAWAliakKHPDW--KLRIYGDGpeREELEKLIdkLGLEDrvKLLGPTKNIAE--------EYANS 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 477 DFIIVPSRFEPCGLIQLHAMRYGtVPIVAS--TGGLVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKA 544
Cdd:cd03820 257 SIFVLSSRYEGFPMVLLEAMAYG-LPIISFdcPTGPSEIIEDGENGL----------LVPNGDVDALAEA 315
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
400-572 |
2.92e-09 |
|
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: 59.30 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 400 DVPVIGFIGRLEEQKGSDILVEAISKF--MGLNVQMVILGTG----KKKMEAQI-LELEEK--FPGKAVGVAKfnvpLAH 470
Cdd:cd03821 203 DRRIILFLGRIHPKKGLDLLIRAARKLaeQGRDWHLVIAGPDdgayPAFLQLQSsLGLGDRvtFTGPLYGEAK----WAL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 471 MitAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGytgfhIGRfnvkceVVDPDDViATAKAVTRAVA 550
Cdd:cd03821 279 Y--ASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-----CGV------VVDPNVS-SLAEALAEALR 344
|
170 180
....*....|....*....|....*
gi 15223331 551 VYG-TSAMQEMVKNC--MDQDFSWK 572
Cdd:cd03821 345 DPAdRKRLGEMARRArqVEENFSWE 369
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
402-546 |
3.60e-09 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 58.82 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 402 PVIGFIGRLEEQKGSDILVEAISkfmGLNVQMVILGTG--KKKMEAQILELEE---KFPGKAVGVAKfnVPLAHMitagA 476
Cdd:cd03795 192 KIFLFIGRLVYYKGLDYLIEAAQ---YLNYPIVIGGEGplKPDLEAQIELNLLdnvKFLGRVDDEEK--VIYLHL----C 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15223331 477 DFIIVPS--RFEPCGLIQLHAMRYGtVPIVAST--GGLVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKAVT 546
Cdd:cd03795 263 DVFVFPSvlRSEAFGIVLLEAMMCG-KPVISTNigTGVPYVNNNGETGL----------VVPPKDPDALAEAID 325
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
385-550 |
9.49e-09 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 57.46 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 385 IKEALqAAVGLPVDR--------------------DVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQ--MVILGTG--K 440
Cdd:cd05844 154 IRDRL-LARGLPAERihvhyigidpakfaprdpaeRAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTarLVIAGDGplR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 441 KKMEAQileleekfpGKAVGVAKFN--VPLAHMIT--AGADFIIVPSRF------EPCGLIQLHAMRYGtVPIVAST-GG 509
Cdd:cd05844 233 PALQAL---------AAALGRVRFLgaLPHAEVQDwmRRAEIFCLPSVTaasgdsEGLGIVLLEAAACG-VPVVSSRhGG 302
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15223331 510 LVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKAVTRAVA 550
Cdd:cd05844 303 IPEAILDGETGF----------LVPEGDVDALADALQALLA 333
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
352-557 |
2.43e-08 |
|
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: 56.17 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 352 IINGMDVQEWNPSTDKyidikydittvtdakplikeALQAAVGLPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNV 431
Cdd:cd03807 161 IYNGIDLFKLSPDDAS--------------------RARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 432 QMVIL----GTGKKKMEAQILE--LEEK--FPGKAVGVAKFnvpLAHMitagaDFIIVPSRFEPCGLIQLHAMRYGtVPI 503
Cdd:cd03807 221 DLRLLlvgrGPERPNLERLLLElgLEDRvhLLGERSDVPAL---LPAM-----DIFVLSSRTEGFPNALLEAMACG-LPV 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15223331 504 VAS-TGGLVDTVKDGyTGFhigrfnvkceVVDPDDVIATAKAVTRAVAVYGTSAM 557
Cdd:cd03807 292 VATdVGGAAELVDDG-TGF----------LVPAGDPQALADAIRALLEDPEKRAR 335
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
402-571 |
4.65e-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: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 402 PVIGFIGRLEEQKGSDILVEAISKFMGLN-VQMVILGTG--KKKMEAQILELeeKFPGkavgvAKFNVPLAHmITAGADF 478
Cdd:cd03814 199 PLLLYVGRLAPEKNLEALLDADLPLAASPpVRLVVVGDGpaRAELEARGPDV--IFTG-----FLTGEELAR-AYASADV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 479 IIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFhigrfnvkceVVDPDDVIATAKAVT------RAVAVY 552
Cdd:cd03814 271 FVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGA----------LVEPGDAAAFAAALRalledpELRRRM 340
|
170
....*....|....*....
gi 15223331 553 GTSAMQEMVkncmdqDFSW 571
Cdd:cd03814 341 AARARAEAE------RYSW 353
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
382-523 |
1.13e-07 |
|
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: 54.21 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 382 KPLIKEALQAavgLPVDRDVPVIGFIGRLEEQKGSDILVEAISKF-MGLNVQMVILGTG--KKKMEAQI--LELEEK--F 454
Cdd:cd03817 185 KPLNTEERRK---LGLPPDEPILLYVGRLAKEKNIDFLLRAFAELkKEPNIKLVIVGDGpeREELKELAreLGLADKviF 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15223331 455 pgkaVGVAKFN-VPLAHmitAGADFIIVPSRFEPCGLIQLHAMRYGtVPIVA-STGGLVDTVKDGYTGFHI 523
Cdd:cd03817 262 ----TGFVPREeLPEYY---KAADLFVFASTTETQGLVYLEAMAAG-LPVVAaKDPAASELVEDGENGFLF 324
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
296-543 |
4.17e-07 |
|
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: 52.35 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 296 GYEKPVKGrKINWmkaAILEAHRVLTVSPYYAQELIS--GVDRGVELhkylrmktvsgIINGMDVQEWnpstdkyidiky 373
Cdd:cd04962 126 GYDPSLQP-AVRF---SINKSDRVTAVSSSLRQETYElfDVDKDIEV-----------IHNFIDEDVF------------ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 374 dittVTDAKPLIKEALQAAvglpvdRDVPVIGFIGRLEEQKGSDILVEAISKFM-GLNVQMVILGTGKKKMEAQILELEE 452
Cdd:cd04962 179 ----KRKPAGALKRRLLAP------PDEKVVIHVSNFRPVKRIDDVVRVFARVRrKIPAKLLLVGDGPERVPAEELAREL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 453 KFPGKAVGVAKFNvPLAHMITAgADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFhigrfnvkceV 532
Cdd:cd04962 249 GVEDRVLFLGKQD-DVEELLSI-ADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGF----------L 316
|
250
....*....|.
gi 15223331 533 VDPDDVIATAK 543
Cdd:cd04962 317 SDVGDVDAMAK 327
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
382-550 |
1.09e-06 |
|
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: 51.18 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 382 KPLIKEALQAAVGLPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGL-NVQMVILGtgkkKMEAQILeleeKFPGKAVG 460
Cdd:cd03825 176 APVDKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEALKLLATKdDLLLVVFG----KNDPQIV----ILPFDIIS 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 461 VAKF-NVPLAHMITAGADFIIVPSRFEPCGLIQLHAMRYGTvPIVA-STGGLVDTVKDGYTGFhigrfnvkceVVDPDDV 538
Cdd:cd03825 248 LGYIdDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGT-PVVAfDTGGSPEIVQHGVTGY----------LVPPGDV 316
|
170
....*....|..
gi 15223331 539 IATAKAVTRAVA 550
Cdd:cd03825 317 QALAEAIEWLLA 328
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
400-521 |
2.10e-06 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 50.48 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 400 DVPVIGFIGRLEEQKGSDILVEAISKFMGlnVQMVILGTGKKKMEaqileLEEKFPGKavgvakfNVPLAHMIT------ 473
Cdd:PLN02871 262 EKPLIVYVGRLGAEKNLDFLKRVMERLPG--ARLAFVGDGPYREE-----LEKMFAGT-------PTVFTGMLQgdelsq 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15223331 474 --AGADFIIVPSRFEPCGLIQLHAMRYGtVPIVAS-TGGLVDTV---KDGYTGF 521
Cdd:PLN02871 328 ayASGDVFVMPSESETLGFVVLEAMASG-VPVVAArAGGIPDIIppdQEGKTGF 380
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
257-547 |
2.68e-06 |
|
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: 50.05 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 257 NAKVVFCIHNIayqgrfafddysllnLPISFKSSFDFmdgyeKPVKGRKInWMKAAILEAHRVLTVSPYYAQELIsgvdr 336
Cdd:cd03809 101 GCPQVVTIHDL---------------IPLRYPEFFPK-----RFRLYYRL-LLPISLRRADAIITVSEATRDDII----- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 337 gvelhkylrmktvsgiingmdvqewnpstdKYIDIKYDITTVT------DAKPLIKEALQAAVGLPVDrdvPVIGFIGRL 410
Cdd:cd03809 155 ------------------------------KFYGVPPEKIVVIplgvdpSFFPPESAAVLIAKYLLPE---PYFLYVGTL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 411 EEQKGSDILVEAISKF--MGLNVQMVILGTGKKKMEaQILELEEKFPGKavGVAKF--NVP---LAHMItAGADFIIVPS 483
Cdd:cd03809 202 EPRKNHERLLKAFALLkkQGGDLKLVIVGGKGWEDE-ELLDLVKKLGLG--GRVRFlgYVSdedLPALY-RGARAFVFPS 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15223331 484 RFEPCGLIQLHAMRYGTvPIVASTGGLVDTVkdgyTGFHigrfnvkCEVVDPDDVIATAKAVTR 547
Cdd:cd03809 278 LYEGFGLPVLEAMACGT-PVIASNISVLPEV----AGDA-------ALYFDPLDPESIADAILR 329
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
403-506 |
5.29e-06 |
|
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: 48.82 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 403 VIGFIGRLEEQKGSDILVEAISKF--MGLNVQMVILGTG----KKKMEAQILELEEK--FPGKAVGVAKFnvpLAHMita 474
Cdd:cd03812 193 VLGHVGRFNEQKNHSFLIDIFEELkkKNPNVKLVLVGEGelkeKIKEKVKELGLEDKviFLGFRNDVSEI---LSAM--- 266
|
90 100 110
....*....|....*....|....*....|..
gi 15223331 475 gaDFIIVPSRFEPCGLIQLHAMRYGtVPIVAS 506
Cdd:cd03812 267 --DVFLFPSLYEGLPLVAVEAQASG-LPCLLS 295
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
396-521 |
1.74e-04 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 44.20 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 396 PVDRDVPVIGFIGRLEEQKGSDILVEAISKfmgLNVQMVILGTGKKKMEAQilELEEKFPGKA------VGVAKFNVPLA 469
Cdd:cd03802 164 FQPDPEDYLAFLGRIAPEKGLEDAIRVARR---AGLPLKIAGKVRDEDYFY--YLQEPLPGPRiefigeVGHDEKQELLG 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15223331 470 HmitAGAdfIIVPSRF-EPCGLIQLHAMRYGTvPIVAST-GGLVDTVKDGYTGF 521
Cdd:cd03802 239 G---ARA--LLFPINWdEPFGLVMIEAMACGT-PVIAYRrGGLPEVIQHGETGF 286
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
408-530 |
1.78e-03 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 41.12 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223331 408 GRLEEQKGSDILVEAISKfMGLnvQMVILGTGK-----KKMEAQILELeekfpgkaVGVAKFNVPLAHMITAGAdfIIVP 482
Cdd:cd03804 206 SRLVPYKRIDLAVEAFNE-LPK--RLVVIGDGPdldrlRAMASPNVEF--------LGYQPDEVLKELLSKARA--FVFA 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15223331 483 SRfEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFHIGRFNVKC 530
Cdd:cd03804 273 AE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVES 319
|
|
| |
