|
Name |
Accession |
Description |
Interval |
E-value |
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
28-458 |
2.96e-60 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 204.32 E-value: 2.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 28 ANILgIFSYHFSSHNLVVRPLAKALVKRGHNVTLITPVgmptdIEGVRHIRVPKLN-QRVQEMIEGDQILDFFGSKWIAS 106
Cdd:cd03784 1 MRIL-FVPFPGQGHVNPMLPLAKALAARGHEVTVATPP-----FNFADLVEAAGLTfVPVGDDPDELELDSETNLGPDSL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 107 LMVVSMLYNMSSDILSDkgvQKMLQNRNERFDLVMLEPSALEALYgVVEHYNATLMGFSGGnvnwsteevagnfapsind 186
Cdd:cd03784 75 LELLRRLLKAADELLDD---LLAALRSSWKPDLVIADPFAYAGPL-VAEELGIPSVRLFTG------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 187 piSSLGYSRSNSLLSKIYNWVHITEEKLLKHLIFRPSQLRIFKKFFNFSEQKFYNMREKYSVILVNNHISMGRVRSNVPN 266
Cdd:cd03784 132 --PATLLSAYLHPFGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 267 IIEVGGLHLTEPAEPCDSKLQKFMDDA-EHGVIYFSMGQeiMVQFLPEDMQQNLMKSLDQFKQRVVWKTELYNMP---NK 342
Cdd:cd03784 210 PSVLGGLRIVPKNGPLPDELWEWLDKQpPRSVVYVSFGS--MVRDLPEELLELIAEALASLGQRFLWVVGPDPLGgleRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 343 SDNVYVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLEILTS 422
Cdd:cd03784 288 PDNVLVVKWVPQDELLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAK 367
|
410 420 430
....*....|....*....|....*....|....*...
gi 24649339 423 TIRKLLENPRYAlKAKKMSQSFR--DRPMSPLDTAVWW 458
Cdd:cd03784 368 AVREVLEDESYR-RAAELLAELReeDGAPSAADVVERL 404
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
7-466 |
1.18e-58 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 202.88 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 7 WLAVLFCLflqkdlyqDSVQAANILGIF---SYhfsSHNLVVRPLAKALVKRGHNVTLITPvgMPtdiegvRHIRVPKLN 83
Cdd:PHA03392 8 LLLLLLLL--------SGVRAARILAVFptpAY---SHHSVFKVYVEALAERGHNVTVIKP--TL------RVYYASHLC 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 84 QRVQEmIEGDQILDFFG-----SKWIASLMVVS----------M-LYNMSSDILSDKGVQKMLQNRNERFDLVMLEPSAL 147
Cdd:PHA03392 69 GNITE-IDASLSVEYFKklvksSAVFRKRGVVAdsstvtadnyMgLVRMISDQFDLPNVKNLIANKNNKFDLLVTEAFLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 148 EALygVVEH--YNATLMGFSGGNvnwsteEVAGNF----APSINdPI-------SSLGYSRSNSLLSKIY-NWVHITEEK 213
Cdd:PHA03392 148 YPL--VFSHlfGDAPVIQISSGY------GLAENFetmgAVSRH-PVyypnlwrSKFGNLNVWETINEIYtELRLYNEFS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 214 LLKHLifrpsQLRIFKKFFNFSEQKFYNMREKYSVILVNNHISMGRVRSNVPNIIEVGGLHLT-EPAEPCDSKLQKFMDD 292
Cdd:PHA03392 219 LLADE-----QNKLLKQQFGPDTPTIRELRNRVQLLFVNVHPVFDNNRPVPPSVQYLGGLHLHkKPPQPLDDYLEEFLNN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 293 AEHGVIYFSMGQEIMVQFLPEDMQQNLMKSLDQFKQRVVWKTE-LYNMPNKSDNVYVIEQPPQRAVLAHPNTRLFITNGG 371
Cdd:PHA03392 294 STNGVVYVSFGSSIDTNDMDNEFLQMLLRTFKKLPYNVLWKYDgEVEAINLPANVLTQKWFPQRAVLKHKNVKAFVTQGG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 372 LLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLEILTSTIRKLLENPRYALKAKKMSQSFRDRPMSP 451
Cdd:PHA03392 374 VQSTDEAIDALVPMVGLPMMGDQFYNTNKYVELGIGRALDTVTVSAAQLVLAIVDVIENPKYRKNLKELRHLIRHQPMTP 453
|
490
....*....|....*
gi 24649339 452 LDTAVWWTEYALRNK 466
Cdd:PHA03392 454 LHKAIWYTEHVIRNK 468
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
27-481 |
6.33e-46 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 168.36 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 27 AANILGIF-SYHFSSHNLVV-RPLAKALVKRGH--NVTLIT-PVGMPTDIEGVRhirVPKlnqRVQEMIEGDQILDFFgs 101
Cdd:pfam00201 13 WMNMKGILeELVQRGHEVTVlRPSASISIGPGKpsNLKFETyPTSATKEELENP---FPK---RQMQWFEEASFGTVW-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 102 KWIASLMVVSMLYNMS-SDILSDKGVQKMLQNrnERFDLVMLEP----SALEALYGVVEhYNATLMGFSGGnvnwSTEEV 176
Cdd:pfam00201 85 SYFSALQEYSDGYRVTcKELVGNKKLMTKLQE--SSFDVVLADPvwpcGELLAELLHIP-TVYSLRFVPGY----AAEKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 177 AGNF-APSINDPISSLGYSRSNSLLSKIYNWVHITEEKLLKHLIFRPsQLRIFKKFFNFsEQKFYNMREKYSVILVNNHI 255
Cdd:pfam00201 158 SGGLpSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFPRK-WDQFASEVLGR-PVTLPELMSKASVWLIRSYW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 256 SMGRVRSNVPNIIEVGGLHlTEPAEPCDSKLQKFMD-DAEHGVIYFSMGQeiMVQFLPEDMQQNLMKSLDQFKQRVVWKT 334
Cdd:pfam00201 236 DLEFPRPLLPNMDFIGGLH-CKPAKPLPQEMEAFVQsSGEHGVVVFSLGS--MVSNIPEEKANAIASALAQIPQKVLWRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 335 ELYNMPNKSDNVYVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANE 414
Cdd:pfam00201 313 DGTKPSTLGNNTRLVKWLPQNDLLGHPKTRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24649339 415 MTLEILTSTIRKLLENPRYALKAKKMSQSFRDRPMSPLDTAVWWTEYALRNKDASHMRLNTEDVPLY 481
Cdd:pfam00201 393 MTSEDLLNALKEVINDPSYKENIMRLSSIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWY 459
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
265-445 |
7.04e-27 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 109.56 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 265 PNIIEVGGLHLTEPAEPcDSKLQkfmDDAEHGVIYFSMGqeiMVQFLPEDMQQNLMKSLDQFKQRVVW------KTELYN 338
Cdd:COG1819 94 ANVRFVGPLLPDGPAEL-PPWLE---EDAGRPLVYVTLG---TSANDRADLLRAVLEALADLGVRVVVttggldPAELGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 339 MPnksDNVYVIEQPPQRAVLAHpnTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLE 418
Cdd:COG1819 167 LP---DNVRVVDYVPQDALLPR--ADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRRLTAE 241
|
170 180
....*....|....*....|....*..
gi 24649339 419 ILTSTIRKLLENPRYALKAKKMSQSFR 445
Cdd:COG1819 242 ALRAALRRLLADPSYRERAARLAAEIR 268
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
344-445 |
3.37e-15 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 77.42 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 344 DNVYVIEQPPQRAVLAHpnTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLEILTST 423
Cdd:TIGR01426 275 PNVEVRQWVPQLEILKK--ADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREA 352
|
90 100
....*....|....*....|..
gi 24649339 424 IRKLLENPRYALKAKKMSQSFR 445
Cdd:TIGR01426 353 VLAVLSDPRYAERLRKMRAEIR 374
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
28-458 |
2.96e-60 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 204.32 E-value: 2.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 28 ANILgIFSYHFSSHNLVVRPLAKALVKRGHNVTLITPVgmptdIEGVRHIRVPKLN-QRVQEMIEGDQILDFFGSKWIAS 106
Cdd:cd03784 1 MRIL-FVPFPGQGHVNPMLPLAKALAARGHEVTVATPP-----FNFADLVEAAGLTfVPVGDDPDELELDSETNLGPDSL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 107 LMVVSMLYNMSSDILSDkgvQKMLQNRNERFDLVMLEPSALEALYgVVEHYNATLMGFSGGnvnwsteevagnfapsind 186
Cdd:cd03784 75 LELLRRLLKAADELLDD---LLAALRSSWKPDLVIADPFAYAGPL-VAEELGIPSVRLFTG------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 187 piSSLGYSRSNSLLSKIYNWVHITEEKLLKHLIFRPSQLRIFKKFFNFSEQKFYNMREKYSVILVNNHISMGRVRSNVPN 266
Cdd:cd03784 132 --PATLLSAYLHPFGVLNLLLSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 267 IIEVGGLHLTEPAEPCDSKLQKFMDDA-EHGVIYFSMGQeiMVQFLPEDMQQNLMKSLDQFKQRVVWKTELYNMP---NK 342
Cdd:cd03784 210 PSVLGGLRIVPKNGPLPDELWEWLDKQpPRSVVYVSFGS--MVRDLPEELLELIAEALASLGQRFLWVVGPDPLGgleRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 343 SDNVYVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLEILTS 422
Cdd:cd03784 288 PDNVLVVKWVPQDELLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAK 367
|
410 420 430
....*....|....*....|....*....|....*...
gi 24649339 423 TIRKLLENPRYAlKAKKMSQSFR--DRPMSPLDTAVWW 458
Cdd:cd03784 368 AVREVLEDESYR-RAAELLAELReeDGAPSAADVVERL 404
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
7-466 |
1.18e-58 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 202.88 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 7 WLAVLFCLflqkdlyqDSVQAANILGIF---SYhfsSHNLVVRPLAKALVKRGHNVTLITPvgMPtdiegvRHIRVPKLN 83
Cdd:PHA03392 8 LLLLLLLL--------SGVRAARILAVFptpAY---SHHSVFKVYVEALAERGHNVTVIKP--TL------RVYYASHLC 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 84 QRVQEmIEGDQILDFFG-----SKWIASLMVVS----------M-LYNMSSDILSDKGVQKMLQNRNERFDLVMLEPSAL 147
Cdd:PHA03392 69 GNITE-IDASLSVEYFKklvksSAVFRKRGVVAdsstvtadnyMgLVRMISDQFDLPNVKNLIANKNNKFDLLVTEAFLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 148 EALygVVEH--YNATLMGFSGGNvnwsteEVAGNF----APSINdPI-------SSLGYSRSNSLLSKIY-NWVHITEEK 213
Cdd:PHA03392 148 YPL--VFSHlfGDAPVIQISSGY------GLAENFetmgAVSRH-PVyypnlwrSKFGNLNVWETINEIYtELRLYNEFS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 214 LLKHLifrpsQLRIFKKFFNFSEQKFYNMREKYSVILVNNHISMGRVRSNVPNIIEVGGLHLT-EPAEPCDSKLQKFMDD 292
Cdd:PHA03392 219 LLADE-----QNKLLKQQFGPDTPTIRELRNRVQLLFVNVHPVFDNNRPVPPSVQYLGGLHLHkKPPQPLDDYLEEFLNN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 293 AEHGVIYFSMGQEIMVQFLPEDMQQNLMKSLDQFKQRVVWKTE-LYNMPNKSDNVYVIEQPPQRAVLAHPNTRLFITNGG 371
Cdd:PHA03392 294 STNGVVYVSFGSSIDTNDMDNEFLQMLLRTFKKLPYNVLWKYDgEVEAINLPANVLTQKWFPQRAVLKHKNVKAFVTQGG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 372 LLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLEILTSTIRKLLENPRYALKAKKMSQSFRDRPMSP 451
Cdd:PHA03392 374 VQSTDEAIDALVPMVGLPMMGDQFYNTNKYVELGIGRALDTVTVSAAQLVLAIVDVIENPKYRKNLKELRHLIRHQPMTP 453
|
490
....*....|....*
gi 24649339 452 LDTAVWWTEYALRNK 466
Cdd:PHA03392 454 LHKAIWYTEHVIRNK 468
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
27-481 |
6.33e-46 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 168.36 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 27 AANILGIF-SYHFSSHNLVV-RPLAKALVKRGH--NVTLIT-PVGMPTDIEGVRhirVPKlnqRVQEMIEGDQILDFFgs 101
Cdd:pfam00201 13 WMNMKGILeELVQRGHEVTVlRPSASISIGPGKpsNLKFETyPTSATKEELENP---FPK---RQMQWFEEASFGTVW-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 102 KWIASLMVVSMLYNMS-SDILSDKGVQKMLQNrnERFDLVMLEP----SALEALYGVVEhYNATLMGFSGGnvnwSTEEV 176
Cdd:pfam00201 85 SYFSALQEYSDGYRVTcKELVGNKKLMTKLQE--SSFDVVLADPvwpcGELLAELLHIP-TVYSLRFVPGY----AAEKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 177 AGNF-APSINDPISSLGYSRSNSLLSKIYNWVHITEEKLLKHLIFRPsQLRIFKKFFNFsEQKFYNMREKYSVILVNNHI 255
Cdd:pfam00201 158 SGGLpSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFWFQCFPRK-WDQFASEVLGR-PVTLPELMSKASVWLIRSYW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 256 SMGRVRSNVPNIIEVGGLHlTEPAEPCDSKLQKFMD-DAEHGVIYFSMGQeiMVQFLPEDMQQNLMKSLDQFKQRVVWKT 334
Cdd:pfam00201 236 DLEFPRPLLPNMDFIGGLH-CKPAKPLPQEMEAFVQsSGEHGVVVFSLGS--MVSNIPEEKANAIASALAQIPQKVLWRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 335 ELYNMPNKSDNVYVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANE 414
Cdd:pfam00201 313 DGTKPSTLGNNTRLVKWLPQNDLLGHPKTRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24649339 415 MTLEILTSTIRKLLENPRYALKAKKMSQSFRDRPMSPLDTAVWWTEYALRNKDASHMRLNTEDVPLY 481
Cdd:pfam00201 393 MTSEDLLNALKEVINDPSYKENIMRLSSIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWY 459
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
265-445 |
7.04e-27 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 109.56 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 265 PNIIEVGGLHLTEPAEPcDSKLQkfmDDAEHGVIYFSMGqeiMVQFLPEDMQQNLMKSLDQFKQRVVW------KTELYN 338
Cdd:COG1819 94 ANVRFVGPLLPDGPAEL-PPWLE---EDAGRPLVYVTLG---TSANDRADLLRAVLEALADLGVRVVVttggldPAELGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 339 MPnksDNVYVIEQPPQRAVLAHpnTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLE 418
Cdd:COG1819 167 LP---DNVRVVDYVPQDALLPR--ADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRRLTAE 241
|
170 180
....*....|....*....|....*..
gi 24649339 419 ILTSTIRKLLENPRYALKAKKMSQSFR 445
Cdd:COG1819 242 ALRAALRRLLADPSYRERAARLAAEIR 268
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
344-445 |
3.37e-15 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 77.42 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 344 DNVYVIEQPPQRAVLAHpnTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNVNLRGMAEVLDANEMTLEILTST 423
Cdd:TIGR01426 275 PNVEVRQWVPQLEILKK--ADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREA 352
|
90 100
....*....|....*....|..
gi 24649339 424 IRKLLENPRYALKAKKMSQSFR 445
Cdd:TIGR01426 353 VLAVLSDPRYAERLRKMRAEIR 374
|
|
| PLN02448 |
PLN02448 |
UDP-glycosyltransferase family protein |
354-401 |
5.76e-09 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215247 [Multi-domain] Cd Length: 459 Bit Score: 58.48 E-value: 5.76e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 24649339 354 QRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLRNV 401
Cdd:PLN02448 333 QLKVLCHSSVGGFWTHCGWNSTLEAVFAGVPMLTFPLFWDQPLNSKLI 380
|
|
| PLN02410 |
PLN02410 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
270-399 |
7.44e-08 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 178032 [Multi-domain] Cd Length: 451 Bit Score: 54.66 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 270 VGGLHLTEPA-----EPCDSKLQKFMDDAEHGVIYFSMGQEIMVQfLPEDMQQNLmkSLDQFKQRVVW---------KTE 335
Cdd:PLN02410 234 IGPLHLVASAptsllEENKSCIEWLNKQKKNSVIFVSLGSLALME-INEVMETAS--GLDSSNQQFLWvirpgsvrgSEW 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24649339 336 LYNMPNK-----SDNVYVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLR 399
Cdd:PLN02410 311 IESLPKEfskiiSGRGYIVKWAPQKEVLSHPAVGGFWSHCGWNSTLESIGEGVPMICKPFSSDQKVNAR 379
|
|
| PLN02555 |
PLN02555 |
limonoid glucosyltransferase |
275-443 |
1.53e-07 |
|
limonoid glucosyltransferase
Pssm-ID: 178170 [Multi-domain] Cd Length: 480 Bit Score: 54.03 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 275 LTEPAEPC----DSKlqkfmddAEHGVIYFSMGQeiMVQFLPEDMQQ---NLMKS------------LDQFKQRVVWKTE 335
Cdd:PLN02555 260 ISKPADDCiewlDSK-------PPSSVVYISFGT--VVYLKQEQIDEiayGVLNSgvsflwvmrpphKDSGVEPHVLPEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 336 LynMPNKSDNVYVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLR--------NVNL-RGM 406
Cdd:PLN02555 331 F--LEKAGDKGKIVQWCPQEKVLAHPSVACFVTHCGWNSTMEALSSGVPVVCFPQWGDQVTDAVylvdvfktGVRLcRGE 408
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24649339 407 AE--VLDANEMTLEILTSTI-RKLLENPRYALKAKKMSQS 443
Cdd:PLN02555 409 AEnkLITREEVAECLLEATVgEKAAELKQNALKWKEEAEA 448
|
|
| PLN02210 |
PLN02210 |
UDP-glucosyl transferase |
293-434 |
5.96e-07 |
|
UDP-glucosyl transferase
Pssm-ID: 215127 [Multi-domain] Cd Length: 456 Bit Score: 51.96 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 293 AEHGVIYFSMGQeiMVQFLpEDMQQNLMKSLDQFKQRVVW------KTE----LYNMPNKSDNVyVIEQPPQRAVLAHPN 362
Cdd:PLN02210 267 ARSSVVYISFGS--MLESL-ENQVETIAKALKNRGVPFLWvirpkeKAQnvqvLQEMVKEGQGV-VLEWSPQEKILSHMA 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649339 363 TRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLR------NVNLRGMAEVLDAnEMTLEILTSTIRKLLENPRYA 434
Cdd:PLN02210 343 ISCFVTHCGWNSTIETVVAGVPVVAYPSWTDQPIDARllvdvfGIGVRMRNDAVDG-ELKVEEVERCIEAVTEGPAAA 419
|
|
| PLN02173 |
PLN02173 |
UDP-glucosyl transferase family protein |
273-453 |
8.09e-06 |
|
UDP-glucosyl transferase family protein
Pssm-ID: 177830 [Multi-domain] Cd Length: 449 Bit Score: 48.49 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 273 LHLTEPAEpcDSKLQKFMDDAEHG-VIYFSMGQeiMVQFLPEDMQQnLMKSLDQFKQR-VVWKTELYNMPN------KSD 344
Cdd:PLN02173 243 LNLFDLKE--AALCTDWLDKRPQGsVVYIAFGS--MAKLSSEQMEE-IASAISNFSYLwVVRASEESKLPPgfletvDKD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 345 NVYVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLR------NVNLRGMAEVlDANEMTLE 418
Cdd:PLN02173 318 KSLVLKWSPQLQVLSNKAIGCFMTHCGWNSTMEGLSLGVPMVAMPQWTDQPMNAKyiqdvwKVGVRVKAEK-ESGIAKRE 396
|
170 180 190
....*....|....*....|....*....|....*
gi 24649339 419 ILTSTIRKLLENPRyALKAKKMSQSFRDRPMSPLD 453
Cdd:PLN02173 397 EIEFSIKEVMEGEK-SKEMKENAGKWRDLAVKSLS 430
|
|
| PLN00164 |
PLN00164 |
glucosyltransferase; Provisional |
353-397 |
1.60e-05 |
|
glucosyltransferase; Provisional
Pssm-ID: 215084 [Multi-domain] Cd Length: 480 Bit Score: 47.36 E-value: 1.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 24649339 353 PQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFIN 397
Cdd:PLN00164 348 PQKEILAHAAVGGFVTHCGWNSVLESLWHGVPMAPWPLYAEQHLN 392
|
|
| PLN02863 |
PLN02863 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
294-399 |
1.84e-05 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 215465 Cd Length: 477 Bit Score: 47.17 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 294 EHGVIYFSMGQEIMvqfLPEDMQQNLMKSLDQFKQRVVW-------KTELYNM--PNKSDNV----YVIEQ-PPQRAVLA 359
Cdd:PLN02863 282 DHKVVYVCFGSQVV---LTKEQMEALASGLEKSGVHFIWcvkepvnEESDYSNipSGFEDRVagrgLVIRGwAPQVAILS 358
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 24649339 360 HPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFINLR 399
Cdd:PLN02863 359 HRAVGAFLTHCGWNSVLEGLVAGVPMLAWPMAADQFVNAS 398
|
|
| PLN02534 |
PLN02534 |
UDP-glycosyltransferase |
353-397 |
7.54e-05 |
|
UDP-glycosyltransferase
Pssm-ID: 215293 [Multi-domain] Cd Length: 491 Bit Score: 45.24 E-value: 7.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 24649339 353 PQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFIN 397
Cdd:PLN02534 353 PQVLILSHPAIGGFLTHCGWNSTIEGICSGVPMITWPLFAEQFLN 397
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
365-444 |
5.13e-04 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340818 [Multi-domain] Cd Length: 350 Bit Score: 42.20 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 365 LFITNGGLLSVMEAVYSGVPILGLPVFF----DQFINLRNVNLRGMAEVLDANEMTLEILTSTIRKLLENPRYALKAKKM 440
Cdd:cd03785 255 LVISRAGASTIAELTAAGKPAILIPYPYaaddHQEANARALEKAGAAIVIDQEELTPEVLAEAILDLLNDPERLKKMAEA 334
|
....
gi 24649339 441 SQSF 444
Cdd:cd03785 335 AKKL 338
|
|
| PLN02992 |
PLN02992 |
coniferyl-alcohol glucosyltransferase |
353-443 |
6.05e-04 |
|
coniferyl-alcohol glucosyltransferase
Pssm-ID: 178572 [Multi-domain] Cd Length: 481 Bit Score: 42.27 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 353 PQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFIN--LRNVNLrGMAEVLDANE--MTLEILTSTIRKLL 428
Cdd:PLN02992 347 PQAEILAHQAVGGFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNaaLLSDEL-GIAVRSDDPKevISRSKIEALVRKVM 425
|
90
....*....|....*...
gi 24649339 429 ---ENPRYALKAKKMSQS 443
Cdd:PLN02992 426 veeEGEEMRRKVKKLRDT 443
|
|
| PLN02207 |
PLN02207 |
UDP-glycosyltransferase |
244-397 |
7.51e-04 |
|
UDP-glycosyltransferase
Pssm-ID: 177857 [Multi-domain] Cd Length: 468 Bit Score: 41.95 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 244 EKYSVilvnNHISMGRvrsNVPNIIEVGGL-------HLTEPAEPCDsKLQKFMDDAEHGVIYF----SMGQeimvqfLP 312
Cdd:PLN02207 224 EPYSV----NHFLDEQ---NYPSVYAVGPIfdlkaqpHPEQDLARRD-ELMKWLDDQPEASVVFlcfgSMGR------LR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 313 EDMQQNLMKSLDQFKQRVVWKTELYNMPNKS-------DNV----YVIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYS 381
Cdd:PLN02207 290 GPLVKEIAHGLELCQYRFLWSLRTEEVTNDDllpegflDRVsgrgMICGWSPQVEILAHKAVGGFVSHCGWNSIVESLWF 369
|
170
....*....|....*.
gi 24649339 382 GVPILGLPVFFDQFIN 397
Cdd:PLN02207 370 GVPIVTWPMYAEQQLN 385
|
|
| PLN03015 |
PLN03015 |
UDP-glucosyl transferase |
348-397 |
7.64e-04 |
|
UDP-glucosyl transferase
Pssm-ID: 178589 [Multi-domain] Cd Length: 470 Bit Score: 41.99 E-value: 7.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24649339 348 VIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFIN 397
Cdd:PLN03015 339 VTQWAPQVEILSHRSIGGFLSHCGWSSVLESLTKGVPIVAWPLYAEQWMN 388
|
|
| PLN02554 |
PLN02554 |
UDP-glycosyltransferase family protein |
348-397 |
8.90e-04 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215304 Cd Length: 481 Bit Score: 42.08 E-value: 8.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24649339 348 VIEQPPQRAVLAHPNTRLFITNGGLLSVMEAVYSGVPILGLPVFFDQFIN 397
Cdd:PLN02554 346 VIGWAPQVAVLAKPAIGGFVTHCGWNSILESLWFGVPMAAWPLYAEQKFN 395
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
365-446 |
3.56e-03 |
|
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.
Pssm-ID: 427711 [Multi-domain] Cd Length: 166 Bit Score: 38.46 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 365 LFITNGGLLSVMEAVYSGVPILGLPvFFDQFINLRNVNLR-----GMAEVLDANEMTLEILTSTIRKLLENP--RYALKA 437
Cdd:pfam04101 74 LVISRAGAGTIAELLALGKPAILVP-NPSAARGHQDNNAKelvkaGAALVILQKELTPEKLIEALLKLLLNPlrLAEMAK 152
|
....*....
gi 24649339 438 KKMSQSFRD 446
Cdd:pfam04101 153 ASKASGFKD 161
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
313-446 |
6.17e-03 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). 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: 340861 [Multi-domain] Cd Length: 364 Bit Score: 38.84 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649339 313 EDMQQNLMKSLDQFKQRVV------WKTELYNMPNKSDNVYV---IEQPPQ--RAvlahpnTRLFITNGGLLSVMEAVYS 381
Cdd:cd17507 213 KETVEALLDSLRAGQVLVVcgknkkLYEKLSGLEEDYINVRVlgyVDDMNElmAA------SDLVITKPGGLTISEALAR 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649339 382 GVPILGLPVFFDQFI-NLRNVNLRGMAEVLDANEMTLEILTSTI--RKLLENPRYALKAKKMSQSFRD 446
Cdd:cd17507 287 GLPVIIYDPIPGQEEeNADFLENNGAGIIARDPEELLEIVARLIdpPSLLRMMSEAAKELKPPAAAKV 354
|
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