|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
26-493 |
9.71e-106 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 337.46 E-value: 9.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 26 AKIVGYPMmGGSQYIGMKRIAQELAARGHEVTLLVSSIQ-KIKPTEG--ITHAVYQAPVDKNYME--------QMVSRVI 94
Cdd:pfam00201 1 GKVLVWPM-DGSHWMNMKGILEELVQRGHEVTVLRPSASiSIGPGKPsnLKFETYPTSATKEELEnpfpkrqmQWFEEAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 95 QNGVKEIFSKT-GLLGVMPSFCEATLNSTDIIDLMKE--FDIMISDTSMPCGPVLAEYLNItRVDY----CPGSpripLL 167
Cdd:pfam00201 80 FGTVWSYFSALqEYSDGYRVTCKELVGNKKLMTKLQEssFDVVLADPVWPCGELLAELLHI-PTVYslrfVPGY----AA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 168 YQYHA--PTFPSYVPLLLAGNPARMNFLQRVKNTLVYLAgQTMMRLVMFPKYDNIKQRYNINPeLSFSESLGRAEMVLFL 245
Cdd:pfam00201 155 EKVSGglPSPPSYVPVILSDLSDHMTFMERVKNMLIMLY-FDFWFQCFPRKWDQFASEVLGRP-VTLPELMSKASVWLIR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 246 ADHALDYPFPLLPAHKLIGPVNIQPPRPLSPEFQQIVNKS--DGVIIVSFGSNIAAIADKEVDVLAEAFGRLKETVFWRQ 323
Cdd:pfam00201 233 SYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQEMEAFVQSSgeHGVVVFSLGSMVSNIPEEKANAIASALAQIPQKVLWRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 324 KGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHT 403
Cdd:pfam00201 313 DGTKPSTLGNNTRLVKWLPQNDLLGHPKTRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 404 VTADELYRTIRRVIDEPRFKENAARISRLMQDRRRSPTEEAADWIEYTLRHKRLTHLRPASVHLTWYQYFLLDVILFMGA 483
Cdd:pfam00201 393 MTSEDLLNALKEVINDPSYKENIMRLSSIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWYQYHSLDVIGFLLA 472
|
490
....*....|
gi 2257898537 484 VLLSVAMVTI 493
Cdd:pfam00201 473 CVATVAFITF 482
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
505-946 |
1.47e-94 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 307.80 E-value: 1.47e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 505 TGIAHAVYKVPVEENFMENLVTQSMKNGLMYMFSEKGMFGSQKLFCECALNASDILEPLK--KFDLVLADNSRLCGVVLA 582
Cdd:pfam00201 56 TSATKEELENPFPKRQMQWFEEASFGTVWSYFSALQEYSDGYRVTCKELVGNKKLMTKLQesSFDVVLADPVWPCGELLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 583 EYLNVPRVdYSPVAPRSPVIYQAHG--PSFPSYVPLILSRNPARMNFLQRLKNTLVFVVEQMMtrFLIFP-----LFDDI 655
Cdd:pfam00201 136 ELLHIPTV-YSLRFVPGYAAEKVSGglPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFW--FQCFPrkwdqFASEV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 656 KQRyninpEMSYGESFGNAEMTLFLADHALDYAFPLLPGHKLIGGINIEPARPLSPEFQHIVNKS--DGVIVVSFGSNFA 733
Cdd:pfam00201 213 LGR-----PVTLPELMSKASVWLIRSYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQEMEAFVQSSgeHGVVVFSLGSMVS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 734 AIADKEVDVLARAFGRLKETVIWRQKGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVP 813
Cdd:pfam00201 288 NIPEEKANAIASALAQIPQKVLWRFDGTKPSTLGNNTRLVKWLPQNDLLGHPKTRAFITHAGSNGVYEAICHGVPMVGMP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 814 LFGDQPDNAVLVEDKGLGLAVDIHTVTADKLYRTIRRVIDEPRFKENAVRISRLMQDRRRSPTEEAADWIEYTLRHGRLT 893
Cdd:pfam00201 368 LFGDQMDNAKHMEAKGAAVTLNVLTMTSEDLLNALKEVINDPSYKENIMRLSSIHHDQPVKPLDRAVFWIEFVMRHKGAK 447
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2257898537 894 HLRPASIHLTWYQYFLLDVMLFMgvvLLSVAMVIRLVLKlVCSCFCRKRTKTK 946
Cdd:pfam00201 448 HLRPAAHDLTWYQYHSLDVIGFL---LACVATVAFITFK-CCLFGYRKFVGKK 496
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
26-450 |
2.44e-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: 211.64 E-value: 2.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 26 AKIVGYPMMGGSQYIGMKRIAQELAARGHEVTLLVSSIQKIKPTE--GITHAVYQAPVDKNYMEQMVSRVIQNGVKEIFS 103
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFADLVEaaGLTFVPVGDDPDELELDSETNLGPDSLLELLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 104 ktgLLGVMPSFCEATLnstDIIDLMKEFDIMISDTSMPCGPVLAEYLNItrvdycpgsPRIPLLYQYHAPTFPSYVPLll 183
Cdd:cd03784 81 ---LLKAADELLDDLL---AALRSSWKPDLVIADPFAYAGPLVAEELGI---------PSVRLFTGPATLLSAYLHPF-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 184 agnparmnflqRVKNTLVYLAGQTMMRLVMFPK-YDNIKQRYNINPELSFSESLGRAEMVLFLADHALDYPFPLLPAHKL 262
Cdd:cd03784 144 -----------GVLNLLLSSLLEPELFLDPLLEvLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 263 IGPVNIQP-PRPLSPEFQQIVNK--SDGVIIVSFGSNIAAIADKEVDVLAEAFGRLKETVFW---RQKGYIPANLSPNIK 336
Cdd:cd03784 213 LGGLRIVPkNGPLPDELWEWLDKqpPRSVVYVSFGSMVRDLPEELLELIAEALASLGQRFLWvvgPDPLGGLERLPDNVL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 337 TVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRV 416
Cdd:cd03784 293 VVKWVPQDELLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREV 372
|
410 420 430
....*....|....*....|....*....|....
gi 2257898537 417 IDEPRFKENAARISRLmqdRRRSPTEEAADWIEY 450
Cdd:cd03784 373 LEDESYRRAAELLAEL---REEDGAPSAADVVER 403
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
491-885 |
4.94e-50 |
|
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: 182.37 E-value: 4.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 491 VTILVSSIQKTKPTT--GIAHAVYKVPVEENFMENLVTQSMKNGLMYMFsekgmfgsqKLFCECALNASDILEPLK---K 565
Cdd:cd03784 31 VTVATPPFNFADLVEaaGLTFVPVGDDPDELELDSETNLGPDSLLELLR---------RLLKAADELLDDLLAALRsswK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 566 FDLVLADNSRLCGVVLAEYLNVPRVdYSPVAPRSPVIYQAHGPSFPSYVPLILsrnparmnflqrlkntlvfvVEQMMTR 645
Cdd:cd03784 102 PDLVIADPFAYAGPLVAEELGIPSV-RLFTGPATLLSAYLHPFGVLNLLLSSL--------------------LEPELFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 646 FLIFPLFDDIKQRYNINPEmsygeSFGNAEMTLFLADHALDYAFPLLPG------HKLIGGINIEPARPLSPEFQHIVNK 719
Cdd:cd03784 161 DPLLEVLDRLRERLGLPPF-----SLVLLLLRLVPPLYVIGPTFPSLPPdrprlpSVLGGLRIVPKNGPLPDELWEWLDK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 720 --SDGVIVVSFGSNFAAIADKEVDVLARAFGRLKETVIW---RQKGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHL 794
Cdd:cd03784 236 qpPRSVVYVSFGSMVRDLPEELLELIAEALASLGQRFLWvvgPDPLGGLERLPDNVLVVKWVPQDELLAHPAVGAFVTHG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 795 GQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGLGLAVDIHTVTADKLYRTIRRVIDEPRFKENAVRISRLmqdRRRS 874
Cdd:cd03784 316 GWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAELLAEL---REED 392
|
410
....*....|.
gi 2257898537 875 PTEEAADWIEY 885
Cdd:cd03784 393 GAPSAADVVER 403
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
270-493 |
8.15e-39 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 152.03 E-value: 8.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 270 PPRPLSPEFQQIVNKS-DGVIIVSFGSNI--AAIADKEVDVLAEAFGRLKETVFWRQKGYIPA-NLSPNIKTVEWLPQND 345
Cdd:PHA03392 279 PPQPLDDYLEEFLNNStNGVVYVSFGSSIdtNDMDNEFLQMLLRTFKKLPYNVLWKYDGEVEAiNLPANVLTQKWFPQRA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 346 LLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRVIDEPRFKEN 425
Cdd:PHA03392 359 VLKHKNVKAFVTQGGVQSTDEAIDALVPMVGLPMMGDQFYNTNKYVELGIGRALDTVTVSAAQLVLAIVDVIENPKYRKN 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2257898537 426 AARISRLMQDRRRSPTEEAADWIEYTLRHKR-LTHLRPASVHLTWYQYflldvilFMGAVLLSVAMVTI 493
Cdd:PHA03392 439 LKELRHLIRHQPMTPLHKAIWYTEHVIRNKHgNTSLKTKAANVSYSDY-------FMSYILVPLVTFTV 500
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
678-914 |
4.43e-37 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 146.64 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 678 LFLADHAL-DYAFPLLPGHKLIGGI--NIEPARPLSPEFQHIVNKS-DGVIVVSFGS--NFAAIADKEVDVLARAFGRLK 751
Cdd:PHA03392 249 LFVNVHPVfDNNRPVPPSVQYLGGLhlHKKPPQPLDDYLEEFLNNStNGVVYVSFGSsiDTNDMDNEFLQMLLRTFKKLP 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 752 ETVIWRQKGYIPA-NLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGL 830
Cdd:PHA03392 329 YNVLWKYDGEVEAiNLPANVLTQKWFPQRAVLKHKNVKAFVTQGGVQSTDEAIDALVPMVGLPMMGDQFYNTNKYVELGI 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 831 GLAVDIHTVTADKLYRTIRRVIDEPRFKENAVRISRLMQDRRRSPTEEAADWIEYTLRHGR-LTHLRPASIHLTWYQYFL 909
Cdd:PHA03392 409 GRALDTVTVSAAQLVLAIVDVIENPKYRKNLKELRHLIRHQPMTPLHKAIWYTEHVIRNKHgNTSLKTKAANVSYSDYFM 488
|
....*
gi 2257898537 910 LDVML 914
Cdd:PHA03392 489 SYILV 493
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
249-434 |
8.76e-31 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 122.27 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 249 ALDYPFPLLPAH-KLIGPVNIQPPRPLSPEFQQivNKSDGVIIVSFGSnIAAIADKEVDVLAEAFGRLKETVFWRQKGYI 327
Cdd:COG1819 84 ELEYPRPPDPANvRFVGPLLPDGPAELPPWLEE--DAGRPLVYVTLGT-SANDRADLLRAVLEALADLGVRVVVTTGGLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 328 PA---NLSPNIKTVEWLPQNDLLAneKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTV 404
Cdd:COG1819 161 PAelgPLPDNVRVVDYVPQDALLP--RADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRRL 238
|
170 180 190
....*....|....*....|....*....|
gi 2257898537 405 TADELYRTIRRVIDEPRFKENAARISRLMQ 434
Cdd:COG1819 239 TAEALRAALRRLLADPSYRERAARLAAEIR 268
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
684-869 |
1.45e-29 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 118.81 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 684 ALDYAFPLLP-GHKLIGGINIEPARPLSPefqhIVNKSDG--VIVVSFGSnFAAIADKEVDVLARAFGRLKETVIWRQKG 760
Cdd:COG1819 84 ELEYPRPPDPaNVRFVGPLLPDGPAELPP----WLEEDAGrpLVYVTLGT-SANDRADLLRAVLEALADLGVRVVVTTGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 761 YIPA---NLSPNIKTVEWLPQNDLLAneKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGLGLAVDIH 837
Cdd:COG1819 159 LDPAelgPLPDNVRVVDYVPQDALLP--RADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPR 236
|
170 180 190
....*....|....*....|....*....|..
gi 2257898537 838 TVTADKLYRTIRRVIDEPRFKENAVRISRLMQ 869
Cdd:COG1819 237 RLTAEALRAALRRLLADPSYRERAARLAAEIR 268
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
45-453 |
2.66e-22 |
|
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: 100.14 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 45 IAQELAARGHEVT-----LLVSSIQKIkpteGITHAVYQAPVDKNYMEQMVSRVIQNGVKEIFSKTGLlGVMPSFCEATl 119
Cdd:TIGR01426 15 VVEELVARGHRVTyatteEFAERVEAA----GAEFVLYGSALPPPDNPPENTEEEPIDIIEKLLDEAE-DVLPQLEEAY- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 120 nSTDiidlmkEFDIMISDTSMPCGPVLAEYLNITRVDYCPgsprIPLLYQYHAPTFPSYVPLLLAGNPARMNFLQRvknt 199
Cdd:TIGR01426 89 -KGD------RPDLIVYDIASWTGRLLARKWDVPVISSFP----TFAANEEFEEMVSPAGEGSAEEGAIAERGLAE---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 200 lvylagqtmmrlvMFPKYDNIKQRYNIN-PELSFsesLGRAEmvlflADHALDY-PFPLLPA-------HKLIGPVniQP 270
Cdd:TIGR01426 154 -------------YVARLSALLEEHGITtPPVEF---LAAPR-----RDLNLVYtPKAFQPAgetfddsFTFVGPC--IG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 271 PRPLSPEFQqIVNKSDGVIIVSFGSniaaIADKEVDVL---AEAFGRL-KETVFWRQKGYIPANLSPNIKTVE---WLPQ 343
Cdd:TIGR01426 211 DRKEDGSWE-RPGDGRPVVLISLGT----VFNNQPSFYrtcVEAFRDLdWHVVLSVGRGVDPADLGELPPNVEvrqWVPQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 344 NDLLanEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRVIDEPRFK 423
Cdd:TIGR01426 286 LEIL--KKADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVLSDPRYA 363
|
410 420 430
....*....|....*....|....*....|
gi 2257898537 424 ENAARISRLMqdRRRSPTEEAADWIEYTLR 453
Cdd:TIGR01426 364 ERLRKMRAEI--REAGGARRAADEIEGFLA 391
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
550-888 |
2.52e-21 |
|
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: 97.45 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 550 CECALnaSDILEPLK--KFDLVLADNSRLCGVVLAEYLNVPRVDYSP--VAPRSpvIYQAHGPSFPSY--VPLILSRNPA 623
Cdd:TIGR01426 77 AEDVL--PQLEEAYKgdRPDLIVYDIASWTGRLLARKWDVPVISSFPtfAANEE--FEEMVSPAGEGSaeEGAIAERGLA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 624 RmnFLQRLKNTLV-FVVEQMMTRFLIFPlfddiKQRYNI----NPEMSYGESFGNAemtlfladhaldYAF--PLLPGHK 696
Cdd:TIGR01426 153 E--YVARLSALLEeHGITTPPVEFLAAP-----RRDLNLvytpKAFQPAGETFDDS------------FTFvgPCIGDRK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 697 LIGginiEPARPLspefqhivnKSDGVIVVSFGSNFAAiADKEVDVLARAFGRL-KETVIWRQKGYIPANLSPNIKTVE- 774
Cdd:TIGR01426 214 EDG----SWERPG---------DGRPVVLISLGTVFNN-QPSFYRTCVEAFRDLdWHVVLSVGRGVDPADLGELPPNVEv 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 775 --WLPQNDLLanEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGLGLAVDIHTVTADKLYRTIRRVI 852
Cdd:TIGR01426 280 rqWVPQLEIL--KKADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVL 357
|
330 340 350
....*....|....*....|....*....|....*..
gi 2257898537 853 DEPRFKEnavRISRLMQDRRRS-PTEEAADWIEYTLR 888
Cdd:TIGR01426 358 SDPRYAE---RLRKMRAEIREAgGARRAADEIEGFLA 391
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
26-493 |
9.71e-106 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 337.46 E-value: 9.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 26 AKIVGYPMmGGSQYIGMKRIAQELAARGHEVTLLVSSIQ-KIKPTEG--ITHAVYQAPVDKNYME--------QMVSRVI 94
Cdd:pfam00201 1 GKVLVWPM-DGSHWMNMKGILEELVQRGHEVTVLRPSASiSIGPGKPsnLKFETYPTSATKEELEnpfpkrqmQWFEEAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 95 QNGVKEIFSKT-GLLGVMPSFCEATLNSTDIIDLMKE--FDIMISDTSMPCGPVLAEYLNItRVDY----CPGSpripLL 167
Cdd:pfam00201 80 FGTVWSYFSALqEYSDGYRVTCKELVGNKKLMTKLQEssFDVVLADPVWPCGELLAELLHI-PTVYslrfVPGY----AA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 168 YQYHA--PTFPSYVPLLLAGNPARMNFLQRVKNTLVYLAgQTMMRLVMFPKYDNIKQRYNINPeLSFSESLGRAEMVLFL 245
Cdd:pfam00201 155 EKVSGglPSPPSYVPVILSDLSDHMTFMERVKNMLIMLY-FDFWFQCFPRKWDQFASEVLGRP-VTLPELMSKASVWLIR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 246 ADHALDYPFPLLPAHKLIGPVNIQPPRPLSPEFQQIVNKS--DGVIIVSFGSNIAAIADKEVDVLAEAFGRLKETVFWRQ 323
Cdd:pfam00201 233 SYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQEMEAFVQSSgeHGVVVFSLGSMVSNIPEEKANAIASALAQIPQKVLWRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 324 KGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHT 403
Cdd:pfam00201 313 DGTKPSTLGNNTRLVKWLPQNDLLGHPKTRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 404 VTADELYRTIRRVIDEPRFKENAARISRLMQDRRRSPTEEAADWIEYTLRHKRLTHLRPASVHLTWYQYFLLDVILFMGA 483
Cdd:pfam00201 393 MTSEDLLNALKEVINDPSYKENIMRLSSIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWYQYHSLDVIGFLLA 472
|
490
....*....|
gi 2257898537 484 VLLSVAMVTI 493
Cdd:pfam00201 473 CVATVAFITF 482
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
505-946 |
1.47e-94 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 307.80 E-value: 1.47e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 505 TGIAHAVYKVPVEENFMENLVTQSMKNGLMYMFSEKGMFGSQKLFCECALNASDILEPLK--KFDLVLADNSRLCGVVLA 582
Cdd:pfam00201 56 TSATKEELENPFPKRQMQWFEEASFGTVWSYFSALQEYSDGYRVTCKELVGNKKLMTKLQesSFDVVLADPVWPCGELLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 583 EYLNVPRVdYSPVAPRSPVIYQAHG--PSFPSYVPLILSRNPARMNFLQRLKNTLVFVVEQMMtrFLIFP-----LFDDI 655
Cdd:pfam00201 136 ELLHIPTV-YSLRFVPGYAAEKVSGglPSPPSYVPVILSDLSDHMTFMERVKNMLIMLYFDFW--FQCFPrkwdqFASEV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 656 KQRyninpEMSYGESFGNAEMTLFLADHALDYAFPLLPGHKLIGGINIEPARPLSPEFQHIVNKS--DGVIVVSFGSNFA 733
Cdd:pfam00201 213 LGR-----PVTLPELMSKASVWLIRSYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQEMEAFVQSSgeHGVVVFSLGSMVS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 734 AIADKEVDVLARAFGRLKETVIWRQKGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVP 813
Cdd:pfam00201 288 NIPEEKANAIASALAQIPQKVLWRFDGTKPSTLGNNTRLVKWLPQNDLLGHPKTRAFITHAGSNGVYEAICHGVPMVGMP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 814 LFGDQPDNAVLVEDKGLGLAVDIHTVTADKLYRTIRRVIDEPRFKENAVRISRLMQDRRRSPTEEAADWIEYTLRHGRLT 893
Cdd:pfam00201 368 LFGDQMDNAKHMEAKGAAVTLNVLTMTSEDLLNALKEVINDPSYKENIMRLSSIHHDQPVKPLDRAVFWIEFVMRHKGAK 447
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2257898537 894 HLRPASIHLTWYQYFLLDVMLFMgvvLLSVAMVIRLVLKlVCSCFCRKRTKTK 946
Cdd:pfam00201 448 HLRPAAHDLTWYQYHSLDVIGFL---LACVATVAFITFK-CCLFGYRKFVGKK 496
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
26-450 |
2.44e-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: 211.64 E-value: 2.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 26 AKIVGYPMMGGSQYIGMKRIAQELAARGHEVTLLVSSIQKIKPTE--GITHAVYQAPVDKNYMEQMVSRVIQNGVKEIFS 103
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFADLVEaaGLTFVPVGDDPDELELDSETNLGPDSLLELLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 104 ktgLLGVMPSFCEATLnstDIIDLMKEFDIMISDTSMPCGPVLAEYLNItrvdycpgsPRIPLLYQYHAPTFPSYVPLll 183
Cdd:cd03784 81 ---LLKAADELLDDLL---AALRSSWKPDLVIADPFAYAGPLVAEELGI---------PSVRLFTGPATLLSAYLHPF-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 184 agnparmnflqRVKNTLVYLAGQTMMRLVMFPK-YDNIKQRYNINPELSFSESLGRAEMVLFLADHALDYPFPLLPAHKL 262
Cdd:cd03784 144 -----------GVLNLLLSSLLEPELFLDPLLEvLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 263 IGPVNIQP-PRPLSPEFQQIVNK--SDGVIIVSFGSNIAAIADKEVDVLAEAFGRLKETVFW---RQKGYIPANLSPNIK 336
Cdd:cd03784 213 LGGLRIVPkNGPLPDELWEWLDKqpPRSVVYVSFGSMVRDLPEELLELIAEALASLGQRFLWvvgPDPLGGLERLPDNVL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 337 TVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRV 416
Cdd:cd03784 293 VVKWVPQDELLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREV 372
|
410 420 430
....*....|....*....|....*....|....
gi 2257898537 417 IDEPRFKENAARISRLmqdRRRSPTEEAADWIEY 450
Cdd:cd03784 373 LEDESYRRAAELLAEL---REEDGAPSAADVVER 403
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
491-885 |
4.94e-50 |
|
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: 182.37 E-value: 4.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 491 VTILVSSIQKTKPTT--GIAHAVYKVPVEENFMENLVTQSMKNGLMYMFsekgmfgsqKLFCECALNASDILEPLK---K 565
Cdd:cd03784 31 VTVATPPFNFADLVEaaGLTFVPVGDDPDELELDSETNLGPDSLLELLR---------RLLKAADELLDDLLAALRsswK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 566 FDLVLADNSRLCGVVLAEYLNVPRVdYSPVAPRSPVIYQAHGPSFPSYVPLILsrnparmnflqrlkntlvfvVEQMMTR 645
Cdd:cd03784 102 PDLVIADPFAYAGPLVAEELGIPSV-RLFTGPATLLSAYLHPFGVLNLLLSSL--------------------LEPELFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 646 FLIFPLFDDIKQRYNINPEmsygeSFGNAEMTLFLADHALDYAFPLLPG------HKLIGGINIEPARPLSPEFQHIVNK 719
Cdd:cd03784 161 DPLLEVLDRLRERLGLPPF-----SLVLLLLRLVPPLYVIGPTFPSLPPdrprlpSVLGGLRIVPKNGPLPDELWEWLDK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 720 --SDGVIVVSFGSNFAAIADKEVDVLARAFGRLKETVIW---RQKGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHL 794
Cdd:cd03784 236 qpPRSVVYVSFGSMVRDLPEELLELIAEALASLGQRFLWvvgPDPLGGLERLPDNVLVVKWVPQDELLAHPAVGAFVTHG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 795 GQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGLGLAVDIHTVTADKLYRTIRRVIDEPRFKENAVRISRLmqdRRRS 874
Cdd:cd03784 316 GWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAELLAEL---REED 392
|
410
....*....|.
gi 2257898537 875 PTEEAADWIEY 885
Cdd:cd03784 393 GAPSAADVVER 403
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
270-493 |
8.15e-39 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 152.03 E-value: 8.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 270 PPRPLSPEFQQIVNKS-DGVIIVSFGSNI--AAIADKEVDVLAEAFGRLKETVFWRQKGYIPA-NLSPNIKTVEWLPQND 345
Cdd:PHA03392 279 PPQPLDDYLEEFLNNStNGVVYVSFGSSIdtNDMDNEFLQMLLRTFKKLPYNVLWKYDGEVEAiNLPANVLTQKWFPQRA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 346 LLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRVIDEPRFKEN 425
Cdd:PHA03392 359 VLKHKNVKAFVTQGGVQSTDEAIDALVPMVGLPMMGDQFYNTNKYVELGIGRALDTVTVSAAQLVLAIVDVIENPKYRKN 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2257898537 426 AARISRLMQDRRRSPTEEAADWIEYTLRHKR-LTHLRPASVHLTWYQYflldvilFMGAVLLSVAMVTI 493
Cdd:PHA03392 439 LKELRHLIRHQPMTPLHKAIWYTEHVIRNKHgNTSLKTKAANVSYSDY-------FMSYILVPLVTFTV 500
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
678-914 |
4.43e-37 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 146.64 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 678 LFLADHAL-DYAFPLLPGHKLIGGI--NIEPARPLSPEFQHIVNKS-DGVIVVSFGS--NFAAIADKEVDVLARAFGRLK 751
Cdd:PHA03392 249 LFVNVHPVfDNNRPVPPSVQYLGGLhlHKKPPQPLDDYLEEFLNNStNGVVYVSFGSsiDTNDMDNEFLQMLLRTFKKLP 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 752 ETVIWRQKGYIPA-NLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGL 830
Cdd:PHA03392 329 YNVLWKYDGEVEAiNLPANVLTQKWFPQRAVLKHKNVKAFVTQGGVQSTDEAIDALVPMVGLPMMGDQFYNTNKYVELGI 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 831 GLAVDIHTVTADKLYRTIRRVIDEPRFKENAVRISRLMQDRRRSPTEEAADWIEYTLRHGR-LTHLRPASIHLTWYQYFL 909
Cdd:PHA03392 409 GRALDTVTVSAAQLVLAIVDVIENPKYRKNLKELRHLIRHQPMTPLHKAIWYTEHVIRNKHgNTSLKTKAANVSYSDYFM 488
|
....*
gi 2257898537 910 LDVML 914
Cdd:PHA03392 489 SYILV 493
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
249-434 |
8.76e-31 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 122.27 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 249 ALDYPFPLLPAH-KLIGPVNIQPPRPLSPEFQQivNKSDGVIIVSFGSnIAAIADKEVDVLAEAFGRLKETVFWRQKGYI 327
Cdd:COG1819 84 ELEYPRPPDPANvRFVGPLLPDGPAELPPWLEE--DAGRPLVYVTLGT-SANDRADLLRAVLEALADLGVRVVVTTGGLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 328 PA---NLSPNIKTVEWLPQNDLLAneKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTV 404
Cdd:COG1819 161 PAelgPLPDNVRVVDYVPQDALLP--RADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRRL 238
|
170 180 190
....*....|....*....|....*....|
gi 2257898537 405 TADELYRTIRRVIDEPRFKENAARISRLMQ 434
Cdd:COG1819 239 TAEALRAALRRLLADPSYRERAARLAAEIR 268
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
684-869 |
1.45e-29 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 118.81 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 684 ALDYAFPLLP-GHKLIGGINIEPARPLSPefqhIVNKSDG--VIVVSFGSnFAAIADKEVDVLARAFGRLKETVIWRQKG 760
Cdd:COG1819 84 ELEYPRPPDPaNVRFVGPLLPDGPAELPP----WLEEDAGrpLVYVTLGT-SANDRADLLRAVLEALADLGVRVVVTTGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 761 YIPA---NLSPNIKTVEWLPQNDLLAneKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGLGLAVDIH 837
Cdd:COG1819 159 LDPAelgPLPDNVRVVDYVPQDALLP--RADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPR 236
|
170 180 190
....*....|....*....|....*....|..
gi 2257898537 838 TVTADKLYRTIRRVIDEPRFKENAVRISRLMQ 869
Cdd:COG1819 237 RLTAEALRAALRRLLADPSYRERAARLAAEIR 268
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
45-453 |
2.66e-22 |
|
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: 100.14 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 45 IAQELAARGHEVT-----LLVSSIQKIkpteGITHAVYQAPVDKNYMEQMVSRVIQNGVKEIFSKTGLlGVMPSFCEATl 119
Cdd:TIGR01426 15 VVEELVARGHRVTyatteEFAERVEAA----GAEFVLYGSALPPPDNPPENTEEEPIDIIEKLLDEAE-DVLPQLEEAY- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 120 nSTDiidlmkEFDIMISDTSMPCGPVLAEYLNITRVDYCPgsprIPLLYQYHAPTFPSYVPLLLAGNPARMNFLQRvknt 199
Cdd:TIGR01426 89 -KGD------RPDLIVYDIASWTGRLLARKWDVPVISSFP----TFAANEEFEEMVSPAGEGSAEEGAIAERGLAE---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 200 lvylagqtmmrlvMFPKYDNIKQRYNIN-PELSFsesLGRAEmvlflADHALDY-PFPLLPA-------HKLIGPVniQP 270
Cdd:TIGR01426 154 -------------YVARLSALLEEHGITtPPVEF---LAAPR-----RDLNLVYtPKAFQPAgetfddsFTFVGPC--IG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 271 PRPLSPEFQqIVNKSDGVIIVSFGSniaaIADKEVDVL---AEAFGRL-KETVFWRQKGYIPANLSPNIKTVE---WLPQ 343
Cdd:TIGR01426 211 DRKEDGSWE-RPGDGRPVVLISLGT----VFNNQPSFYrtcVEAFRDLdWHVVLSVGRGVDPADLGELPPNVEvrqWVPQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 344 NDLLanEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRVIDEPRFK 423
Cdd:TIGR01426 286 LEIL--KKADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVLSDPRYA 363
|
410 420 430
....*....|....*....|....*....|
gi 2257898537 424 ENAARISRLMqdRRRSPTEEAADWIEYTLR 453
Cdd:TIGR01426 364 ERLRKMRAEI--REAGGARRAADEIEGFLA 391
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
550-888 |
2.52e-21 |
|
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: 97.45 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 550 CECALnaSDILEPLK--KFDLVLADNSRLCGVVLAEYLNVPRVDYSP--VAPRSpvIYQAHGPSFPSY--VPLILSRNPA 623
Cdd:TIGR01426 77 AEDVL--PQLEEAYKgdRPDLIVYDIASWTGRLLARKWDVPVISSFPtfAANEE--FEEMVSPAGEGSaeEGAIAERGLA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 624 RmnFLQRLKNTLV-FVVEQMMTRFLIFPlfddiKQRYNI----NPEMSYGESFGNAemtlfladhaldYAF--PLLPGHK 696
Cdd:TIGR01426 153 E--YVARLSALLEeHGITTPPVEFLAAP-----RRDLNLvytpKAFQPAGETFDDS------------FTFvgPCIGDRK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 697 LIGginiEPARPLspefqhivnKSDGVIVVSFGSNFAAiADKEVDVLARAFGRL-KETVIWRQKGYIPANLSPNIKTVE- 774
Cdd:TIGR01426 214 EDG----SWERPG---------DGRPVVLISLGTVFNN-QPSFYRTCVEAFRDLdWHVVLSVGRGVDPADLGELPPNVEv 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 775 --WLPQNDLLanEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGLGLAVDIHTVTADKLYRTIRRVI 852
Cdd:TIGR01426 280 rqWVPQLEIL--KKADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVL 357
|
330 340 350
....*....|....*....|....*....|....*..
gi 2257898537 853 DEPRFKEnavRISRLMQDRRRS-PTEEAADWIEYTLR 888
Cdd:TIGR01426 358 SDPRYAE---RLRKMRAEIREAgGARRAADEIEGFLA 391
|
|
| PLN02554 |
PLN02554 |
UDP-glycosyltransferase family protein |
336-419 |
1.08e-11 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215304 Cd Length: 481 Bit Score: 68.27 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 336 KTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENA-VLVEDkgLGLAVDIH------------ 402
Cdd:PLN02554 345 KVIGWAPQVAVLAKPAIGGFVTHCGWNSILESLWFGVPMAAWPLYAEQKFNAfEMVEE--LGLAVEIRkywrgdllagem 422
|
90
....*....|....*...
gi 2257898537 403 -TVTADELYRTIRRVIDE 419
Cdd:PLN02554 423 eTVTAEEIERGIRCLMEQ 440
|
|
| PLN02554 |
PLN02554 |
UDP-glycosyltransferase family protein |
771-854 |
8.88e-11 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215304 Cd Length: 481 Bit Score: 65.19 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 771 KTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNA-VLVEDkgLGLAVDIH------------ 837
Cdd:PLN02554 345 KVIGWAPQVAVLAKPAIGGFVTHCGWNSILESLWFGVPMAAWPLYAEQKFNAfEMVEE--LGLAVEIRkywrgdllagem 422
|
90
....*....|....*...
gi 2257898537 838 -TVTADKLYRTIRRVIDE 854
Cdd:PLN02554 423 eTVTAEEIERGIRCLMEQ 440
|
|
| PLN02210 |
PLN02210 |
UDP-glucosyl transferase |
723-877 |
1.44e-10 |
|
UDP-glucosyl transferase
Pssm-ID: 215127 [Multi-domain] Cd Length: 456 Bit Score: 64.67 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 723 VIVVSFGSNFAAIaDKEVDVLARAFGRLKETVIW----RQKGYIPANLSPNIK-----TVEWLPQNDLLANEKTRVFVSH 793
Cdd:PLN02210 271 VVYISFGSMLESL-ENQVETIAKALKNRGVPFLWvirpKEKAQNVQVLQEMVKegqgvVLEWSPQEKILSHMAISCFVTH 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 794 LGQNSLYEAGYHGIPLVGVPLFGDQPDNA-VLVEDKGLGLAVDIHTVTADKLYRTIRRVIDeprfkenAVRISRLMQDRR 872
Cdd:PLN02210 350 CGWNSTIETVVAGVPVVAYPSWTDQPIDArLLVDVFGIGVRMRNDAVDGELKVEEVERCIE-------AVTEGPAAADIR 422
|
....*
gi 2257898537 873 RSPTE 877
Cdd:PLN02210 423 RRAAE 427
|
|
| PLN00164 |
PLN00164 |
glucosyltransferase; Provisional |
340-443 |
9.09e-10 |
|
glucosyltransferase; Provisional
Pssm-ID: 215084 [Multi-domain] Cd Length: 480 Bit Score: 62.00 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 340 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENA-VLVEDKGLGLAVDIHT-----VTADELYRTI 413
Cdd:PLN00164 346 WAPQKEILAHAAVGGFVTHCGWNSVLESLWHGVPMAPWPLYAEQHLNAfELVADMGVAVAMKVDRkrdnfVEAAELERAV 425
|
90 100 110
....*....|....*....|....*....|....*
gi 2257898537 414 RRVIDEP-----RFKENAARisrlMQDRRRSPTEE 443
Cdd:PLN00164 426 RSLMGGGeeegrKAREKAAE----MKAACRKAVEE 456
|
|
| PLN02167 |
PLN02167 |
UDP-glycosyltransferase family protein |
340-423 |
1.46e-09 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215112 [Multi-domain] Cd Length: 475 Bit Score: 61.35 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 340 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEdKGLGLAVDIH---------TVTADELY 410
Cdd:PLN02167 347 WAPQVEILAHKAIGGFVSHCGWNSVLESLWFGVPIATWPMYAEQQLNAFTMV-KELGLAVELRldyvsaygeIVKADEIA 425
|
90
....*....|....*.
gi 2257898537 411 RTIRRVID---EPRFK 423
Cdd:PLN02167 426 GAVRSLMDgedVPRKK 441
|
|
| PLN02210 |
PLN02210 |
UDP-glucosyl transferase |
288-437 |
1.52e-09 |
|
UDP-glucosyl transferase
Pssm-ID: 215127 [Multi-domain] Cd Length: 456 Bit Score: 61.21 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 288 VIIVSFGSNIAAIaDKEVDVLAEAFGRLKETVFW----RQKGYIPANLSPNIK-----TVEWLPQNDLLANEKTRVFVSH 358
Cdd:PLN02210 271 VVYISFGSMLESL-ENQVETIAKALKNRGVPFLWvirpKEKAQNVQVLQEMVKegqgvVLEWSPQEKILSHMAISCFVTH 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 359 LGQNSLYEAGYHGIPLVGVPLFGDQSENA-VLVEDKGLGLAVDIHTVTAD----ELYRTIRRVIDEPRFKENAARISRLM 433
Cdd:PLN02210 350 CGWNSTIETVVAGVPVVAYPSWTDQPIDArLLVDVFGIGVRMRNDAVDGElkveEVERCIEAVTEGPAAADIRRRAAELK 429
|
....
gi 2257898537 434 QDRR 437
Cdd:PLN02210 430 HVAR 433
|
|
| PLN02173 |
PLN02173 |
UDP-glucosyl transferase family protein |
723-827 |
4.65e-09 |
|
UDP-glucosyl transferase family protein
Pssm-ID: 177830 [Multi-domain] Cd Length: 449 Bit Score: 59.66 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 723 VIVVSFGSnFAAIADKEVDVLARAFGRLkeTVIWRQKGYIPANLSPN-IKTV--------EWLPQNDLLANEKTRVFVSH 793
Cdd:PLN02173 266 VVYIAFGS-MAKLSSEQMEEIASAISNF--SYLWVVRASEESKLPPGfLETVdkdkslvlKWSPQLQVLSNKAIGCFMTH 342
|
90 100 110
....*....|....*....|....*....|....
gi 2257898537 794 LGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVED 827
Cdd:PLN02173 343 CGWNSTMEGLSLGVPMVAMPQWTDQPMNAKYIQD 376
|
|
| PLN00164 |
PLN00164 |
glucosyltransferase; Provisional |
775-853 |
5.02e-09 |
|
glucosyltransferase; Provisional
Pssm-ID: 215084 [Multi-domain] Cd Length: 480 Bit Score: 59.69 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 775 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNA-VLVEDKGLGLAVDIHT-----VTADKLYRTI 848
Cdd:PLN00164 346 WAPQKEILAHAAVGGFVTHCGWNSVLESLWHGVPMAPWPLYAEQHLNAfELVADMGVAVAMKVDRkrdnfVEAAELERAV 425
|
....*
gi 2257898537 849 RRVID 853
Cdd:PLN00164 426 RSLMG 430
|
|
| PLN02152 |
PLN02152 |
indole-3-acetate beta-glucosyltransferase |
690-867 |
6.69e-09 |
|
indole-3-acetate beta-glucosyltransferase
Pssm-ID: 177813 [Multi-domain] Cd Length: 455 Bit Score: 59.30 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 690 PLLPGHKLIGGiniEPARPLSPEFQH------IVNKSDG-VIVVSFGSnFAAIADKEVDVLARAFGRLKETVIWrqkgYI 762
Cdd:PLN02152 226 PLLPAEIFTGS---ESGKDLSVRDQSssytlwLDSKTESsVIYVSFGT-MVELSKKQIEELARALIEGKRPFLW----VI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 763 PANLSPNIKT------------------------VEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQ 818
Cdd:PLN02152 298 TDKLNREAKIegeeeteiekiagfrheleevgmiVSWCSQIEVLRHRAVGCFVTHCGWSSSLESLVLGVPVVAFPMWSDQ 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2257898537 819 PDNAVLVEDK-GLGLAVDIHT---VTADKLYRTIRRVIDEP--RFKENAVRISRL 867
Cdd:PLN02152 378 PANAKLLEEIwKTGVRVRENSeglVERGEIRRCLEAVMEEKsvELRESAEKWKRL 432
|
|
| PLN02992 |
PLN02992 |
coniferyl-alcohol glucosyltransferase |
340-432 |
7.52e-09 |
|
coniferyl-alcohol glucosyltransferase
Pssm-ID: 178572 [Multi-domain] Cd Length: 481 Bit Score: 59.22 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 340 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKgLGLAVDI----HTVTADELYRTIRR 415
Cdd:PLN02992 345 WAPQAEILAHQAVGGFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALLSDE-LGIAVRSddpkEVISRSKIEALVRK 423
|
90
....*....|....*..
gi 2257898537 416 VIDEPRFKENAARISRL 432
Cdd:PLN02992 424 VMVEEEGEEMRRKVKKL 440
|
|
| PLN02207 |
PLN02207 |
UDP-glycosyltransferase |
340-433 |
7.67e-09 |
|
UDP-glycosyltransferase
Pssm-ID: 177857 [Multi-domain] Cd Length: 468 Bit Score: 59.28 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 340 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEdKGLGLAVD------IHT---VTADELY 410
Cdd:PLN02207 339 WSPQVEILAHKAVGGFVSHCGWNSIVESLWFGVPIVTWPMYAEQQLNAFLMV-KELKLAVElkldyrVHSdeiVNANEIE 417
|
90 100
....*....|....*....|...
gi 2257898537 411 RTIRRVIDeprfKENAARISRLM 433
Cdd:PLN02207 418 TAIRCVMN----KDNNVVRKRVM 436
|
|
| PLN02173 |
PLN02173 |
UDP-glucosyl transferase family protein |
288-424 |
9.73e-09 |
|
UDP-glucosyl transferase family protein
Pssm-ID: 177830 [Multi-domain] Cd Length: 449 Bit Score: 58.89 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 288 VIIVSFGSnIAAIADKEVDVLAEAFGRLkeTVFWRQKGYIPANLSPN-IKTV--------EWLPQNDLLANEKTRVFVSH 358
Cdd:PLN02173 266 VVYIAFGS-MAKLSSEQMEEIASAISNF--SYLWVVRASEESKLPPGfLETVdkdkslvlKWSPQLQVLSNKAIGCFMTH 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2257898537 359 LGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVED---KGLGLAVDIHTVTA--DELYRTIRRVIDEPRFKE 424
Cdd:PLN02173 343 CGWNSTMEGLSLGVPMVAMPQWTDQPMNAKYIQDvwkVGVRVKAEKESGIAkrEEIEFSIKEVMEGEKSKE 413
|
|
| PLN02167 |
PLN02167 |
UDP-glycosyltransferase family protein |
775-858 |
1.37e-08 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215112 [Multi-domain] Cd Length: 475 Bit Score: 58.27 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 775 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEdKGLGLAVDIH---------TVTADKLY 845
Cdd:PLN02167 347 WAPQVEILAHKAIGGFVSHCGWNSVLESLWFGVPIATWPMYAEQQLNAFTMV-KELGLAVELRldyvsaygeIVKADEIA 425
|
90
....*....|....*.
gi 2257898537 846 RTIRRVID---EPRFK 858
Cdd:PLN02167 426 GAVRSLMDgedVPRKK 441
|
|
| PLN02207 |
PLN02207 |
UDP-glycosyltransferase |
775-868 |
1.42e-08 |
|
UDP-glycosyltransferase
Pssm-ID: 177857 [Multi-domain] Cd Length: 468 Bit Score: 58.13 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 775 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEdKGLGLAVD------IHT---VTADKLY 845
Cdd:PLN02207 339 WSPQVEILAHKAVGGFVSHCGWNSIVESLWFGVPIVTWPMYAEQQLNAFLMV-KELKLAVElkldyrVHSdeiVNANEIE 417
|
90 100
....*....|....*....|...
gi 2257898537 846 RTIRRVIDeprfKENAVRISRLM 868
Cdd:PLN02207 418 TAIRCVMN----KDNNVVRKRVM 436
|
|
| PLN02992 |
PLN02992 |
coniferyl-alcohol glucosyltransferase |
696-867 |
1.50e-08 |
|
coniferyl-alcohol glucosyltransferase
Pssm-ID: 178572 [Multi-domain] Cd Length: 481 Bit Score: 58.07 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 696 KLIGGINIEPARPLSP--------EFQHIV----NK--SDGVIVVSFGSNfAAIADKEVDVLARAFGRLKETVIWRQK-- 759
Cdd:PLN02992 224 KLLGRVARVPVYPIGPlcrpiqssKTDHPVldwlNKqpNESVLYISFGSG-GSLSAKQLTELAWGLEMSQQRFVWVVRpp 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 760 -------GYIPANL------SPNI-------KTVE-------WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGV 812
Cdd:PLN02992 303 vdgsacsAYFSANGgetrdnTPEYlpegfvsRTHDrgfvvpsWAPQAEILAHQAVGGFLTHCGWSSTLESVVGGVPMIAW 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2257898537 813 PLFGDQPDNAVLVEDKgLGLAVDI----HTVTADKLYRTIRRVIDEPRFKENAVRISRL 867
Cdd:PLN02992 383 PLFAEQNMNAALLSDE-LGIAVRSddpkEVISRSKIEALVRKVMVEEEGEEMRRKVKKL 440
|
|
| PLN02152 |
PLN02152 |
indole-3-acetate beta-glucosyltransferase |
255-432 |
3.80e-08 |
|
indole-3-acetate beta-glucosyltransferase
Pssm-ID: 177813 [Multi-domain] Cd Length: 455 Bit Score: 56.99 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 255 PLLPAHKLIGPVNiqpPRPLSPEFQQ------IVNKSDG-VIIVSFGSnIAAIADKEVDVLAEAFGRLKETVFWrqkgYI 327
Cdd:PLN02152 226 PLLPAEIFTGSES---GKDLSVRDQSssytlwLDSKTESsVIYVSFGT-MVELSKKQIEELARALIEGKRPFLW----VI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 328 PANLSPNIKT------------------------VEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQ 383
Cdd:PLN02152 298 TDKLNREAKIegeeeteiekiagfrheleevgmiVSWCSQIEVLRHRAVGCFVTHCGWSSSLESLVLGVPVVAFPMWSDQ 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2257898537 384 SENAVLVEDK-GLGLAVDIHT---VTADELYRTIRRVIDEP--RFKENAARISRL 432
Cdd:PLN02152 378 PANAKLLEEIwKTGVRVRENSeglVERGEIRRCLEAVMEEKsvELRESAEKWKRL 432
|
|
| PLN02555 |
PLN02555 |
limonoid glucosyltransferase |
336-392 |
9.52e-08 |
|
limonoid glucosyltransferase
Pssm-ID: 178170 [Multi-domain] Cd Length: 480 Bit Score: 55.57 E-value: 9.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2257898537 336 KTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVED 392
Cdd:PLN02555 340 KIVQWCPQEKVLAHPSVACFVTHCGWNSTMEALSSGVPVVCFPQWGDQVTDAVYLVD 396
|
|
| PLN02562 |
PLN02562 |
UDP-glycosyltransferase |
719-879 |
9.61e-08 |
|
UDP-glycosyltransferase
Pssm-ID: 215305 Cd Length: 448 Bit Score: 55.66 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 719 KSDGVIVVSFGSNFAAIADKEVDVLARAFGRLKETVIWR-----QKGYIPA---NLSPNIKTVEWLPQNDLLANEKTRVF 790
Cdd:PLN02562 271 KPNSVIYISFGSWVSPIGESNVRTLALALEASGRPFIWVlnpvwREGLPPGyveRVSKQGKVVSWAPQLEVLKHQAVGCY 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 791 VSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKgLGLAVDIHTVTADKLYRTIRRVIDEPRFKEnavrisRLMQD 870
Cdd:PLN02562 351 LTHCGWNSTMEAIQCQKRLLCYPVAGDQFVNCAYIVDV-WKIGVRISGFGQKEVEEGLRKVMEDSGMGE------RLMKL 423
|
....*....
gi 2257898537 871 RRRSPTEEA 879
Cdd:PLN02562 424 RERAMGEEA 432
|
|
| PLN02555 |
PLN02555 |
limonoid glucosyltransferase |
771-827 |
1.24e-07 |
|
limonoid glucosyltransferase
Pssm-ID: 178170 [Multi-domain] Cd Length: 480 Bit Score: 55.19 E-value: 1.24e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2257898537 771 KTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVED 827
Cdd:PLN02555 340 KIVQWCPQEKVLAHPSVACFVTHCGWNSTMEALSSGVPVVCFPQWGDQVTDAVYLVD 396
|
|
| PLN02410 |
PLN02410 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
255-439 |
3.85e-07 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 178032 [Multi-domain] Cd Length: 451 Bit Score: 53.51 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 255 PLLPahklIGPVNI--QPPRPLSPEFQQIV-----NKSDGVIIVSFGSnIAAIADKEVDVLAEAFGRLKETVFWRQK--- 324
Cdd:PLN02410 230 PVYP----IGPLHLvaSAPTSLLEENKSCIewlnkQKKNSVIFVSLGS-LALMEINEVMETASGLDSSNQQFLWVIRpgs 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 325 -------GYIPANLSPNIK----TVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVE-- 391
Cdd:PLN02410 305 vrgsewiESLPKEFSKIISgrgyIVKWAPQKEVLSHPAVGGFWSHCGWNSTLESIGEGVPMICKPFSSDQKVNARYLEcv 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2257898537 392 -DKGLGLAVDIHTVTADelyRTIRRVIDEPRFKENAARISRLMQDRRRS 439
Cdd:PLN02410 385 wKIGIQVEGDLDRGAVE---RAVKRLMVEEEGEEMRKRAISLKEQLRAS 430
|
|
| PLN03015 |
PLN03015 |
UDP-glucosyl transferase |
759-865 |
4.07e-06 |
|
UDP-glucosyl transferase
Pssm-ID: 178589 [Multi-domain] Cd Length: 470 Bit Score: 50.46 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 759 KGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKgLGLAVDIHT 838
Cdd:PLN03015 326 EGFLDRTRGVGLVVTQWAPQVEILSHRSIGGFLSHCGWSSVLESLTKGVPIVAWPLYAEQWMNATLLTEE-IGVAVRTSE 404
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2257898537 839 VTADKLY------RTIRRVIDEP-------RFKENAVRIS 865
Cdd:PLN03015 405 LPSEKVIgreevaSLVRKIVAEEdeegqkiRAKAEEVRVS 444
|
|
| PLN03015 |
PLN03015 |
UDP-glucosyl transferase |
324-419 |
5.55e-06 |
|
UDP-glucosyl transferase
Pssm-ID: 178589 [Multi-domain] Cd Length: 470 Bit Score: 50.08 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 324 KGYIPANLSPNIKTVEWLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKgLGLAVDI-- 401
Cdd:PLN03015 326 EGFLDRTRGVGLVVTQWAPQVEILSHRSIGGFLSHCGWSSVLESLTKGVPIVAWPLYAEQWMNATLLTEE-IGVAVRTse 404
|
90 100
....*....|....*....|..
gi 2257898537 402 ----HTVTADELYRTIRRVIDE 419
Cdd:PLN03015 405 lpseKVIGREEVASLVRKIVAE 426
|
|
| PLN02670 |
PLN02670 |
transferase, transferring glycosyl groups |
284-439 |
7.60e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 178275 [Multi-domain] Cd Length: 472 Bit Score: 49.52 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 284 KSDGVIIVSFGSNiAAIADKEVDVLAEAFGRLKETVFW----------RQKGYIPANLSPNIKT-----VEWLPQNDLLA 348
Cdd:PLN02670 276 RVNSVVYVALGTE-ASLRREEVTELALGLEKSETPFFWvlrnepgttqNALEMLPDGFEERVKGrgmihVGWVPQVKILS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 349 NEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKGLGLAVDIH----TVTADELYRTIRRV-IDEP--R 421
Cdd:PLN02670 355 HESVGGFLTHCGWNSVVEGLGFGRVLILFPVLNEQGLNTRLLHGKKLGLEVPRDerdgSFTSDSVAESVRLAmVDDAgeE 434
|
170
....*....|....*...
gi 2257898537 422 FKENAARISRLMQDRRRS 439
Cdd:PLN02670 435 IRDKAKEMRNLFGDMDRN 452
|
|
| PLN02410 |
PLN02410 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
719-826 |
9.21e-06 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 178032 [Multi-domain] Cd Length: 451 Bit Score: 49.27 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 719 KSDGVIVVSFGSnFAAIADKEVDVLARAFGRLKETVIWRQK----------GYIPANLSPNIK----TVEWLPQNDLLAN 784
Cdd:PLN02410 262 KKNSVIFVSLGS-LALMEINEVMETASGLDSSNQQFLWVIRpgsvrgsewiESLPKEFSKIISgrgyIVKWAPQKEVLSH 340
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2257898537 785 EKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVE 826
Cdd:PLN02410 341 PAVGGFWSHCGWNSTLESIGEGVPMICKPFSSDQKVNARYLE 382
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
329-436 |
1.33e-05 |
|
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: 46.55 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 329 ANLSPNIKTVEWLPQNDLLAnEKTRVFVSHLGQNSLYEAGYHGIPLVGVPL----FGDQSENAVLVEDKGLGLAVDIHTV 404
Cdd:pfam04101 50 AELGINYEVFPFIDNMAEYI-KAADLVISRAGAGTIAELLALGKPAILVPNpsaaRGHQDNNAKELVKAGAALVILQKEL 128
|
90 100 110
....*....|....*....|....*....|..
gi 2257898537 405 TADELYRTIRRVIDEPRFKENAARISRLMQDR 436
Cdd:pfam04101 129 TPEKLIEALLKLLLNPLRLAEMAKASKASGFK 160
|
|
| PLN03004 |
PLN03004 |
UDP-glycosyltransferase |
340-430 |
1.70e-05 |
|
UDP-glycosyltransferase
Pssm-ID: 178581 Cd Length: 451 Bit Score: 48.53 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 340 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKgLGLAVDIHT-----VTADELYRTIR 414
Cdd:PLN03004 341 WAPQVPVLNHKAVGGFVTHCGWNSILEAVCAGVPMVAWPLYAEQRFNRVMIVDE-IKIAISMNEsetgfVSSTEVEKRVQ 419
|
90 100
....*....|....*....|..
gi 2257898537 415 RVIDEPRFKE------NAARIS 430
Cdd:PLN03004 420 EIIGECPVRErtmamkNAAELA 441
|
|
| PLN02670 |
PLN02670 |
transferase, transferring glycosyl groups |
719-874 |
5.86e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 178275 [Multi-domain] Cd Length: 472 Bit Score: 46.82 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 719 KSDGVIVVSFGSNfAAIADKEVDVLARAFGRLKETVIW----------RQKGYIPANLSPNIKT-----VEWLPQNDLLA 783
Cdd:PLN02670 276 RVNSVVYVALGTE-ASLRREEVTELALGLEKSETPFFWvlrnepgttqNALEMLPDGFEERVKGrgmihVGWVPQVKILS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 784 NEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKGLGLAVDIH----TVTADKLYRTIRRV-IDEP--R 856
Cdd:PLN02670 355 HESVGGFLTHCGWNSVVEGLGFGRVLILFPVLNEQGLNTRLLHGKKLGLEVPRDerdgSFTSDSVAESVRLAmVDDAgeE 434
|
170
....*....|....*...
gi 2257898537 857 FKENAVRISRLMQDRRRS 874
Cdd:PLN02670 435 IRDKAKEMRNLFGDMDRN 452
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
764-855 |
6.12e-05 |
|
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: 44.63 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 764 ANLSPNIKTVEWLPQNDLLAnEKTRVFVSHLGQNSLYEAGYHGIPLVGVPL----FGDQPDNAVLVEDKGLGLAVDIHTV 839
Cdd:pfam04101 50 AELGINYEVFPFIDNMAEYI-KAADLVISRAGAGTIAELLALGKPAILVPNpsaaRGHQDNNAKELVKAGAALVILQKEL 128
|
90
....*....|....*.
gi 2257898537 840 TADKLYRTIRRVIDEP 855
Cdd:pfam04101 129 TPEKLIEALLKLLLNP 144
|
|
| PLN03004 |
PLN03004 |
UDP-glycosyltransferase |
775-862 |
9.99e-05 |
|
UDP-glycosyltransferase
Pssm-ID: 178581 Cd Length: 451 Bit Score: 45.84 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 775 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKgLGLAVDIHT-----VTADKLYRTIR 849
Cdd:PLN03004 341 WAPQVPVLNHKAVGGFVTHCGWNSILEAVCAGVPMVAWPLYAEQRFNRVMIVDE-IKIAISMNEsetgfVSSTEVEKRVQ 419
|
90
....*....|...
gi 2257898537 850 RVIDEPRFKENAV 862
Cdd:PLN03004 420 EIIGECPVRERTM 432
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
32-449 |
1.62e-04 |
|
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: 45.22 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 32 PMMGGSQYIgMKRIAQELAARGHEVTLLVSSIQKIKPTEGITHAVYQAPVDKNYMEQMVSRVIQNGvkeifsktgllgvm 111
Cdd:cd03801 11 PPVGGAERH-VRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 112 psfceatlnstdIIDLMKEFDIMISDTSMPCGPVLaeylnitrvdYCPGSPRIPLLYQYHAPTFPSYVPLLlagnPARMN 191
Cdd:cd03801 76 ------------PLLRLRKFDVVHAHGLLAALLAA----------LLALLLGAPLVVTLHGAEPGRLLLLL----AAERR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 192 FLQRVKNTLvylagqtmmrlvmfPKYDNIkqryninpeLSFSEslgraemvlFLADHALDYPFPLLPAHKLIgPVNIQPP 271
Cdd:cd03801 130 LLARAEALL--------------RRADAV---------IAVSE---------ALRDELRALGGIPPEKIVVI-PNGVDLE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 272 RPLSPEFQQIVNKSDGVIIVSFGSNIAaiaDKEVDVLAEAFGRLKETVFWRQ------KGYIPANL-------SPNIKTV 338
Cdd:cd03801 177 RFSPPLRRKLGIPPDRPVLLFVGRLSP---RKGVDLLLEALAKLLRRGPDVRlvivggDGPLRAELeelelglGDRVRFL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 339 EWLPQND---LLANekTRVFVS-----HLGqNSLYEAGYHGIPLVGvplfGDQSENAVLVEDKGLGLAVDIHTVtaDELY 410
Cdd:cd03801 254 GFVPDEElpaLYAA--ADVFVLpsryeGFG-LVVLEAMAAGLPVVA----TDVGGLPEVVEDGEGGLVVPPDDV--EALA 324
|
410 420 430
....*....|....*....|....*....|....*....
gi 2257898537 411 RTIRRVIDEPRFKENAARISRLMQDRRRSPTEEAADWIE 449
Cdd:cd03801 325 DALLRLLADPELRARLGRAARERVAERFSWERVAERLLD 363
|
|
| PLN02863 |
PLN02863 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
340-439 |
1.73e-04 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 215465 Cd Length: 477 Bit Score: 45.25 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 340 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENAVLVEDKgLGLAVDI----HTVT-ADELYRTIR 414
Cdd:PLN02863 350 WAPQVAILSHRAVGAFLTHCGWNSVLEGLVAGVPMLAWPMAADQFVNASLLVDE-LKVAVRVcegaDTVPdSDELARVFM 428
|
90 100 110
....*....|....*....|....*....|
gi 2257898537 415 RVIDEPRF-KENAARISRL----MQDRRRS 439
Cdd:PLN02863 429 ESVSENQVeRERAKELRRAaldaIKERGSS 458
|
|
| PLN02863 |
PLN02863 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
775-874 |
2.68e-04 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 215465 Cd Length: 477 Bit Score: 44.48 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 775 WLPQNDLLANEKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEDKgLGLAVDI----HTVT-ADKLYRTIR 849
Cdd:PLN02863 350 WAPQVAILSHRAVGAFLTHCGWNSVLEGLVAGVPMLAWPMAADQFVNASLLVDE-LKVAVRVcegaDTVPdSDELARVFM 428
|
90 100 110
....*....|....*....|....*....|
gi 2257898537 850 RVIDEPRF-KENAVRISRL----MQDRRRS 874
Cdd:PLN02863 429 ESVSENQVeRERAKELRRAaldaIKERGSS 458
|
|
| PLN02448 |
PLN02448 |
UDP-glycosyltransferase family protein |
723-827 |
3.57e-04 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215247 [Multi-domain] Cd Length: 459 Bit Score: 44.23 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 723 VIVVSFGSnFAAIADKEVD---------------VLARAFGRLKEtvIWRQKGYIpanlspniktVEWLPQNDLLANEKT 787
Cdd:PLN02448 276 VLYVSLGS-FLSVSSAQMDeiaaglrdsgvrflwVARGEASRLKE--ICGDMGLV----------VPWCDQLKVLCHSSV 342
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2257898537 788 RVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNA-VLVED 827
Cdd:PLN02448 343 GGFWTHCGWNSTLEAVFAGVPMLTFPLFWDQPLNSkLIVED 383
|
|
| PLN02448 |
PLN02448 |
UDP-glycosyltransferase family protein |
288-418 |
6.58e-04 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215247 [Multi-domain] Cd Length: 459 Bit Score: 43.46 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 288 VIIVSFGS----------NIAA-IADKEVD---VLAEAFGRLKETVfwRQKGYIpanlspniktVEWLPQNDLLANEKTR 353
Cdd:PLN02448 276 VLYVSLGSflsvssaqmdEIAAgLRDSGVRflwVARGEASRLKEIC--GDMGLV----------VPWCDQLKVLCHSSVG 343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2257898537 354 VFVSHLGQNSLYEAGYHGIPLVGVPLFGDQSENA-VLVEDKGLGLAVD-----IHTVTADELYRTIRRVID 418
Cdd:PLN02448 344 GFWTHCGWNSTLEAVFAGVPMLTFPLFWDQPLNSkLIVEDWKIGWRVKrevgeETLVGREEIAELVKRFMD 414
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
356-454 |
1.32e-03 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 42.04 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 356 VSHLGQNSLYEAGYHGIPLVGVPL-F---GDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRVI-DEPRFKENAARIS 430
Cdd:COG0707 263 ISRAGASTVAELAALGKPAILVPLpHaadDHQTKNARALVEAGAAVLIPQSELTPEKLAEALEELLeDPERLAKMAEAAR 342
|
90 100
....*....|....*....|....
gi 2257898537 431 RLMqdrRRSPTEEAADWIEYTLRH 454
Cdd:COG0707 343 ALA---RPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
356-431 |
1.71e-03 |
|
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: 41.82 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 356 VSHLGQNSLYEAGYHGIPLVGVPLF----GDQSENAVLVEDKGLGLAVDIHTVTADELYRTIRRVIDEP----RFKENAA 427
Cdd:cd03785 257 ISRAGASTIAELTAAGKPAILIPYPyaadDHQEANARALEKAGAAIVIDQEELTPEVLAEAILDLLNDPerlkKMAEAAK 336
|
....
gi 2257898537 428 RISR 431
Cdd:cd03785 337 KLAK 340
|
|
| PLN03007 |
PLN03007 |
UDP-glucosyltransferase family protein |
719-880 |
2.21e-03 |
|
UDP-glucosyltransferase family protein
Pssm-ID: 178584 [Multi-domain] Cd Length: 482 Bit Score: 41.77 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 719 KSDGVIVVSFGSnFAAIADKEVDVLARAFGRLKETVIW--RQKG-------YIPANLSPNIK-----TVEWLPQNDLLAN 784
Cdd:PLN03007 283 KPDSVIYLSFGS-VASFKNEQLFEIAAGLEGSGQNFIWvvRKNEnqgekeeWLPEGFEERTKgkgliIRGWAPQVLILDH 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 785 EKTRVFVSHLGQNSLYEAGYHGIPLVGVPLFGDQPDNAVLVEdKGLGLAVdihTVTADKLYRTIRRVIDEPRFkENAVR- 863
Cdd:PLN03007 362 QATGGFVTHCGWNSLLEGVAAGLPMVTWPVGAEQFYNEKLVT-QVLRTGV---SVGAKKLVKVKGDFISREKV-EKAVRe 436
|
170
....*....|....*....
gi 2257898537 864 --ISRLMQDRRRSPTEEAA 880
Cdd:PLN03007 437 viVGEEAEERRLRAKKLAE 455
|
|
| SDR_a1 |
cd05265 |
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ... |
34-74 |
2.55e-03 |
|
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187575 [Multi-domain] Cd Length: 250 Bit Score: 40.74 E-value: 2.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2257898537 34 MGGSQYIGmKRIAQELAARGHEVTLLVSSIQKIKPTEGITH 74
Cdd:cd05265 6 IGGTRFIG-KALVEELLAAGHDVTVFNRGRTKPDLPEGVEH 45
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
791-889 |
5.93e-03 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 40.11 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257898537 791 VSHLGQNSLYEAGYHGIPLVGVPL-F---GDQPDNAVLVEDKGLGLAVDIHTVTADKLYRTIRRVI-DEPRFKENAVRIS 865
Cdd:COG0707 263 ISRAGASTVAELAALGKPAILVPLpHaadDHQTKNARALVEAGAAVLIPQSELTPEKLAEALEELLeDPERLAKMAEAAR 342
|
90 100
....*....|....*....|....
gi 2257898537 866 RLMqdrRRSPTEEAADWIEYTLRH 889
Cdd:COG0707 343 ALA---RPDAAERIADLILELAKG 363
|
|
| YwnB |
COG2910 |
Putative NADH-flavin reductase [General function prediction only]; |
35-73 |
8.45e-03 |
|
Putative NADH-flavin reductase [General function prediction only];
Pssm-ID: 442154 [Multi-domain] Cd Length: 205 Bit Score: 38.68 E-value: 8.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2257898537 35 GGSQYIGmKRIAQELAARGHEVTLLVSSIQKIKPT-EGIT 73
Cdd:COG2910 6 GATGRVG-SLIVREALARGHEVTALVRNPEKLPDEhPGLT 44
|
|
| |
