|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
1-359 |
9.69e-90 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 279.68 E-value: 9.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 1 MELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDF----GLPNaPLSYAPVYGSGLTDQMDFWGRVKNIL 76
Cdd:pfam00201 111 MTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEkvsgGLPS-PPSYVPVILSDLSDHMTFMERVKNML 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 77 M--FFHFtkkrrdIFSQYGNTVQEHFAEGSQ-PV-LSDLLLKAELWFVNSDFALDFARPLFPNTVYVGGLLDKPVQPIPQ 152
Cdd:pfam00201 190 ImlYFDF------WFQCFPRKWDQFASEVLGrPVtLPELMSKASVWLIRSYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 153 DLEDFISQFGDSGFVLVALGSVVSMIqSKEIIKEMNSAFAHLPQGVLWTCKSShwpKDVSLAPNVKIMDWLPQIDLLAHP 232
Cdd:pfam00201 264 EMEAFVQSSGEHGVVVFSLGSMVSNI-PEEKANAIASALAQIPQKVLWRFDGT---KPSTLGNNTRLVKWLPQNDLLGHP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 233 SIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDQRYKTAAMASK 312
Cdd:pfam00201 340 KTRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLTMTSEDLLNALKEVINDPSYKENIMRLS 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568990337 313 VIRQSHPLTPAQRLVGWIDHILQTGGAAHLKPYAFQQPWHEQYMLDV 359
Cdd:pfam00201 420 SIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWYQYHSLDV 466
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
3-315 |
1.15e-61 |
|
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: 203.94 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 3 LLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDFGLPnaplsYAPVYGSGLTDQMDFWGRVKNILMFFHFT 82
Cdd:cd03784 96 LRSSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYLH-----PFGVLNLLLSSLLEPELFLDPLLEVLDRL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 83 KKRRdifsqygntvqeHFAEGSQPVLSDLLLKAELWFVNSDFALDFARPLFPNtVYVGGLLDKPVQPIPQDLEDFISQFG 162
Cdd:cd03784 171 RERL------------GLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPS-VLGGLRIVPKNGPLPDELWEWLDKQP 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 163 DSGFVLVALGSVVSMIqSKEIIKEMNSAFAHLPQGVLWTCKSSHWPKDVSLAPNVKIMDWLPQIDLLAHPSIRLFVTHGG 242
Cdd:cd03784 238 PRSVVYVSFGSMVRDL-PEELLELIAEALASLGQRFLWVVGPDPLGGLERLPDNVLVVKWVPQDELLAHPAVGAFVTHGG 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568990337 243 MNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDQRYKTAAMASKVIR 315
Cdd:cd03784 317 WNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAELLAELR 389
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
106-359 |
2.19e-38 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 144.33 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 106 PVLSDLLLKAELWFVNSDFALDFARPLFPNTVYVGGL-LDKPvqpIPQDLEDFISQFGD---SGFVLVALGSVV---SMi 178
Cdd:PHA03392 237 PTIRELRNRVQLLFVNVHPVFDNNRPVPPSVQYLGGLhLHKK---PPQPLDDYLEEFLNnstNGVVYVSFGSSIdtnDM- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 179 qSKEIIKEMNSAFAHLPQGVLWTCKSSHwpKDVSLAPNVKIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVG 258
Cdd:PHA03392 313 -DNEFLQMLLRTFKKLPYNVLWKYDGEV--EAINLPANVLTQKWFPQRAVLKHKNVKAFVTQGGVQSTDEAIDALVPMVG 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 259 IPFFGDQPENMVRVEakNLGVSIQLQTLKAESFLLTMK--EVIEDQRYKTAAMASKVIRQSHPLTPAQRLVGWIDHIL-Q 335
Cdd:PHA03392 390 LPMMGDQFYNTNKYV--ELGIGRALDTVTVSAAQLVLAivDVIENPKYRKNLKELRHLIRHQPMTPLHKAIWYTEHVIrN 467
|
250 260
....*....|....*....|....
gi 568990337 336 TGGAAHLKPYAFQQPWHEQYMLDV 359
Cdd:PHA03392 468 KHGNTSLKTKAANVSYSDYFMSYI 491
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
125-308 |
3.90e-36 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 132.67 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 125 ALDFARPLFP-NTVYVGGLLDKPVQPIPqdleDFISQFGDSGFVLVALGSVVSmiQSKEIIKEMNSAFAHLPQGVLWTCK 203
Cdd:COG1819 84 ELEYPRPPDPaNVRFVGPLLPDGPAELP----PWLEEDAGRPLVYVTLGTSAN--DRADLLRAVLEALADLGVRVVVTTG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 204 SSHWPKDVSLAPNVKIMDWLPQIDLLAHpsIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQL 283
Cdd:COG1819 158 GLDPAELGPLPDNVRVVDYVPQDALLPR--ADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPP 235
|
170 180
....*....|....*....|....*
gi 568990337 284 QTLKAESFLLTMKEVIEDQRYKTAA 308
Cdd:COG1819 236 RRLTAEALRAALRRLLADPSYRERA 260
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
2-317 |
1.50e-23 |
|
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: 100.91 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 2 ELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDFGLPNAPLS--YAPVYGSGLTDQMDFWGRVKNILmff 79
Cdd:TIGR01426 86 EAYKGDRPDLIVYDIASWTGRLLARKWDVPVISSFPTFAANEEFEEMVSPAGegSAEEGAIAERGLAEYVARLSALL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 80 hftkkrrdifsqygntvQEHFAEGsqPVLSDLLlkaelwFVNSDFALDF-ARPLFPNTVYVGgllDK-----PVQPIPQD 153
Cdd:TIGR01426 163 -----------------EEHGITT--PPVEFLA------APRRDLNLVYtPKAFQPAGETFD---DSftfvgPCIGDRKE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 154 LEDFISQFGDSGFVLVALGSVVSmiQSKEIIKEMNSAFAHLPQGVLWTCKSSHWPKDV-SLAPNVKIMDWLPQIDLLAHP 232
Cdd:TIGR01426 215 DGSWERPGDGRPVVLISLGTVFN--NQPSFYRTCVEAFRDLDWHVVLSVGRGVDPADLgELPPNVEVRQWVPQLEILKKA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 233 SirLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDQRY--KTAAMa 310
Cdd:TIGR01426 293 D--AFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVLSDPRYaeRLRKM- 369
|
....*..
gi 568990337 311 SKVIRQS 317
Cdd:TIGR01426 370 RAEIREA 376
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
1-359 |
9.69e-90 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 279.68 E-value: 9.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 1 MELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDF----GLPNaPLSYAPVYGSGLTDQMDFWGRVKNIL 76
Cdd:pfam00201 111 MTKLQESSFDVVLADPVWPCGELLAELLHIPTVYSLRFVPGYAAEkvsgGLPS-PPSYVPVILSDLSDHMTFMERVKNML 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 77 M--FFHFtkkrrdIFSQYGNTVQEHFAEGSQ-PV-LSDLLLKAELWFVNSDFALDFARPLFPNTVYVGGLLDKPVQPIPQ 152
Cdd:pfam00201 190 ImlYFDF------WFQCFPRKWDQFASEVLGrPVtLPELMSKASVWLIRSYWDLEFPRPLLPNMDFIGGLHCKPAKPLPQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 153 DLEDFISQFGDSGFVLVALGSVVSMIqSKEIIKEMNSAFAHLPQGVLWTCKSShwpKDVSLAPNVKIMDWLPQIDLLAHP 232
Cdd:pfam00201 264 EMEAFVQSSGEHGVVVFSLGSMVSNI-PEEKANAIASALAQIPQKVLWRFDGT---KPSTLGNNTRLVKWLPQNDLLGHP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 233 SIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDQRYKTAAMASK 312
Cdd:pfam00201 340 KTRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLTMTSEDLLNALKEVINDPSYKENIMRLS 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568990337 313 VIRQSHPLTPAQRLVGWIDHILQTGGAAHLKPYAFQQPWHEQYMLDV 359
Cdd:pfam00201 420 SIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWYQYHSLDV 466
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
3-315 |
1.15e-61 |
|
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: 203.94 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 3 LLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDFGLPnaplsYAPVYGSGLTDQMDFWGRVKNILMFFHFT 82
Cdd:cd03784 96 LRSSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYLH-----PFGVLNLLLSSLLEPELFLDPLLEVLDRL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 83 KKRRdifsqygntvqeHFAEGSQPVLSDLLLKAELWFVNSDFALDFARPLFPNtVYVGGLLDKPVQPIPQDLEDFISQFG 162
Cdd:cd03784 171 RERL------------GLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPS-VLGGLRIVPKNGPLPDELWEWLDKQP 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 163 DSGFVLVALGSVVSMIqSKEIIKEMNSAFAHLPQGVLWTCKSSHWPKDVSLAPNVKIMDWLPQIDLLAHPSIRLFVTHGG 242
Cdd:cd03784 238 PRSVVYVSFGSMVRDL-PEELLELIAEALASLGQRFLWVVGPDPLGGLERLPDNVLVVKWVPQDELLAHPAVGAFVTHGG 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568990337 243 MNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDQRYKTAAMASKVIR 315
Cdd:cd03784 317 WNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAELLAELR 389
|
|
| egt |
PHA03392 |
ecdysteroid UDP-glucosyltransferase; Provisional |
106-359 |
2.19e-38 |
|
ecdysteroid UDP-glucosyltransferase; Provisional
Pssm-ID: 223071 [Multi-domain] Cd Length: 507 Bit Score: 144.33 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 106 PVLSDLLLKAELWFVNSDFALDFARPLFPNTVYVGGL-LDKPvqpIPQDLEDFISQFGD---SGFVLVALGSVV---SMi 178
Cdd:PHA03392 237 PTIRELRNRVQLLFVNVHPVFDNNRPVPPSVQYLGGLhLHKK---PPQPLDDYLEEFLNnstNGVVYVSFGSSIdtnDM- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 179 qSKEIIKEMNSAFAHLPQGVLWTCKSSHwpKDVSLAPNVKIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVG 258
Cdd:PHA03392 313 -DNEFLQMLLRTFKKLPYNVLWKYDGEV--EAINLPANVLTQKWFPQRAVLKHKNVKAFVTQGGVQSTDEAIDALVPMVG 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 259 IPFFGDQPENMVRVEakNLGVSIQLQTLKAESFLLTMK--EVIEDQRYKTAAMASKVIRQSHPLTPAQRLVGWIDHIL-Q 335
Cdd:PHA03392 390 LPMMGDQFYNTNKYV--ELGIGRALDTVTVSAAQLVLAivDVIENPKYRKNLKELRHLIRHQPMTPLHKAIWYTEHVIrN 467
|
250 260
....*....|....*....|....
gi 568990337 336 TGGAAHLKPYAFQQPWHEQYMLDV 359
Cdd:PHA03392 468 KHGNTSLKTKAANVSYSDYFMSYI 491
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
125-308 |
3.90e-36 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 132.67 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 125 ALDFARPLFP-NTVYVGGLLDKPVQPIPqdleDFISQFGDSGFVLVALGSVVSmiQSKEIIKEMNSAFAHLPQGVLWTCK 203
Cdd:COG1819 84 ELEYPRPPDPaNVRFVGPLLPDGPAELP----PWLEEDAGRPLVYVTLGTSAN--DRADLLRAVLEALADLGVRVVVTTG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 204 SSHWPKDVSLAPNVKIMDWLPQIDLLAHpsIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQL 283
Cdd:COG1819 158 GLDPAELGPLPDNVRVVDYVPQDALLPR--ADAVVHHGGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPP 235
|
170 180
....*....|....*....|....*
gi 568990337 284 QTLKAESFLLTMKEVIEDQRYKTAA 308
Cdd:COG1819 236 RRLTAEALRAALRRLLADPSYRERA 260
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
2-317 |
1.50e-23 |
|
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: 100.91 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 2 ELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDFGLPNAPLS--YAPVYGSGLTDQMDFWGRVKNILmff 79
Cdd:TIGR01426 86 EAYKGDRPDLIVYDIASWTGRLLARKWDVPVISSFPTFAANEEFEEMVSPAGegSAEEGAIAERGLAEYVARLSALL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 80 hftkkrrdifsqygntvQEHFAEGsqPVLSDLLlkaelwFVNSDFALDF-ARPLFPNTVYVGgllDK-----PVQPIPQD 153
Cdd:TIGR01426 163 -----------------EEHGITT--PPVEFLA------APRRDLNLVYtPKAFQPAGETFD---DSftfvgPCIGDRKE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 154 LEDFISQFGDSGFVLVALGSVVSmiQSKEIIKEMNSAFAHLPQGVLWTCKSSHWPKDV-SLAPNVKIMDWLPQIDLLAHP 232
Cdd:TIGR01426 215 DGSWERPGDGRPVVLISLGTVFN--NQPSFYRTCVEAFRDLDWHVVLSVGRGVDPADLgELPPNVEVRQWVPQLEILKKA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 233 SirLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDQRY--KTAAMa 310
Cdd:TIGR01426 293 D--AFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVLSDPRYaeRLRKM- 369
|
....*..
gi 568990337 311 SKVIRQS 317
Cdd:TIGR01426 370 RAEIREA 376
|
|
| PLN02173 |
PLN02173 |
UDP-glucosyl transferase family protein |
167-305 |
1.17e-15 |
|
UDP-glucosyl transferase family protein
Pssm-ID: 177830 [Multi-domain] Cd Length: 449 Bit Score: 78.15 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 167 VLVALGSVVSMiqSKEIIKEMNSAFAHLpqGVLWTCKSSH---WP--------KDVSLapnvkIMDWLPQIDLLAHPSIR 235
Cdd:PLN02173 267 VYIAFGSMAKL--SSEQMEEIASAISNF--SYLWVVRASEeskLPpgfletvdKDKSL-----VLKWSPQLQVLSNKAIG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 236 LFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENM----------VRVEA-KNLGVSiqlqtlKAESFLLTMKEVIEDQRY 304
Cdd:PLN02173 338 CFMTHCGWNSTMEGLSLGVPMVAMPQWTDQPMNAkyiqdvwkvgVRVKAeKESGIA------KREEIEFSIKEVMEGEKS 411
|
.
gi 568990337 305 K 305
Cdd:PLN02173 412 K 412
|
|
| PLN02555 |
PLN02555 |
limonoid glucosyltransferase |
164-300 |
1.87e-15 |
|
limonoid glucosyltransferase
Pssm-ID: 178170 [Multi-domain] Cd Length: 480 Bit Score: 77.53 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 164 SGFVLVALGSVVSMIQskEIIKEMnsAFAHLPQGV--LWTCKSSHwpKDVSLAPNV-------------KIMDWLPQIDL 228
Cdd:PLN02555 277 SSVVYISFGTVVYLKQ--EQIDEI--AYGVLNSGVsfLWVMRPPH--KDSGVEPHVlpeeflekagdkgKIVQWCPQEKV 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568990337 229 LAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVR-VEAKNLGVsiQLQTLKAESFLLTMKEVIE 300
Cdd:PLN02555 351 LAHPSVACFVTHCGWNSTMEALSSGVPVVCFPQWGDQVTDAVYlVDVFKTGV--RLCRGEAENKLITREEVAE 421
|
|
| PLN00164 |
PLN00164 |
glucosyltransferase; Provisional |
194-284 |
5.20e-14 |
|
glucosyltransferase; Provisional
Pssm-ID: 215084 [Multi-domain] Cd Length: 480 Bit Score: 73.17 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 194 LPQGVLWTCKSSH--WPKdvslapnvkimdWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPEN--- 268
Cdd:PLN00164 328 LPEGFLERTKGRGlvWPT------------WAPQKEILAHAAVGGFVTHCGWNSVLESLWHGVPMAPWPLYAEQHLNafe 395
|
90
....*....|....*.
gi 568990337 269 MVRVeaknLGVSIQLQ 284
Cdd:PLN00164 396 LVAD----MGVAVAMK 407
|
|
| PLN02448 |
PLN02448 |
UDP-glycosyltransferase family protein |
125-268 |
6.21e-13 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215247 [Multi-domain] Cd Length: 459 Bit Score: 70.04 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 125 ALDFARPLFPNTVYvgglldkPVQP-IP-QDLEDFISQFGDS---------------GFVL-VALGSVVSM--IQSKEII 184
Cdd:PLN02448 224 AIDALKSKFPFPVY-------PIGPsIPyMELKDNSSSSNNEdnepdyfqwldsqpeGSVLyVSLGSFLSVssAQMDEIA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 185 KEMNSAfahlpqGV--LWTCKSSHWPKDVSLAPNVKIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFF 262
Cdd:PLN02448 297 AGLRDS------GVrfLWVARGEASRLKEICGDMGLVVPWCDQLKVLCHSSVGGFWTHCGWNSTLEAVFAGVPMLTFPLF 370
|
....*.
gi 568990337 263 GDQPEN 268
Cdd:PLN02448 371 WDQPLN 376
|
|
| PLN02207 |
PLN02207 |
UDP-glycosyltransferase |
108-283 |
1.67e-12 |
|
UDP-glycosyltransferase
Pssm-ID: 177857 [Multi-domain] Cd Length: 468 Bit Score: 68.53 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 108 LSDLLLKAELWFVNSDFALD-------FARPLFPNTVYVGGLLDKPVQPIP-QDLE------DFISQFGDSGFVLVALGS 173
Cdd:PLN02207 205 LAILFTKANGILVNSSFDIEpysvnhfLDEQNYPSVYAVGPIFDLKAQPHPeQDLArrdelmKWLDDQPEASVVFLCFGS 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 174 VVSMiqSKEIIKEMNSAFAHLPQGVLWTCKSSHWPKDvSLAPNV---------KIMDWLPQIDLLAHPSIRLFVTHGGMN 244
Cdd:PLN02207 285 MGRL--RGPLVKEIAHGLELCQYRFLWSLRTEEVTND-DLLPEGfldrvsgrgMICGWSPQVEILAHKAVGGFVSHCGWN 361
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568990337 245 SVMEAVHHGVPMVGIPFFGDQPEN-MVRVEAKNLGVSIQL 283
Cdd:PLN02207 362 SIVESLWFGVPIVTWPMYAEQQLNaFLMVKELKLAVELKL 401
|
|
| PLN02410 |
PLN02410 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
167-273 |
4.50e-12 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 178032 [Multi-domain] Cd Length: 451 Bit Score: 67.37 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 167 VLVALGSVvSMIQSKEIIkEMNSAFAHLPQGVLW-----TCKSSHW----PKDVS--LAPNVKIMDWLPQIDLLAHPSIR 235
Cdd:PLN02410 267 IFVSLGSL-ALMEINEVM-ETASGLDSSNQQFLWvirpgSVRGSEWieslPKEFSkiISGRGYIVKWAPQKEVLSHPAVG 344
|
90 100 110
....*....|....*....|....*....|....*...
gi 568990337 236 LFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVE 273
Cdd:PLN02410 345 GFWSHCGWNSTLESIGEGVPMICKPFSSDQKVNARYLE 382
|
|
| PLN02210 |
PLN02210 |
UDP-glucosyl transferase |
164-298 |
1.51e-10 |
|
UDP-glucosyl transferase
Pssm-ID: 215127 [Multi-domain] Cd Length: 456 Bit Score: 62.36 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 164 SGFVLVALGSVVSMIQSKeiIKEMNSAFAHLPQGVLWTCKSSHWPKDVS-LAPNVK-----IMDWLPQIDLLAHPSIRLF 237
Cdd:PLN02210 269 SSVVYISFGSMLESLENQ--VETIAKALKNRGVPFLWVIRPKEKAQNVQvLQEMVKegqgvVLEWSPQEKILSHMAISCF 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568990337 238 VTHGGMNSVMEAVHHGVPMVGIPFFGDQPENM-VRVEAKNLGVSIQLQTLKAEsflLTMKEV 298
Cdd:PLN02210 347 VTHCGWNSTIETVVAGVPVVAYPSWTDQPIDArLLVDVFGIGVRMRNDAVDGE---LKVEEV 405
|
|
| PLN02554 |
PLN02554 |
UDP-glycosyltransferase family protein |
218-282 |
2.31e-10 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215304 Cd Length: 481 Bit Score: 62.11 E-value: 2.31e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568990337 218 KIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPEN-MVRVEAKNLGVSIQ 282
Cdd:PLN02554 345 KVIGWAPQVAVLAKPAIGGFVTHCGWNSILESLWFGVPMAAWPLYAEQKFNaFEMVEELGLAVEIR 410
|
|
| PLN02992 |
PLN02992 |
coniferyl-alcohol glucosyltransferase |
219-314 |
3.96e-10 |
|
coniferyl-alcohol glucosyltransferase
Pssm-ID: 178572 [Multi-domain] Cd Length: 481 Bit Score: 61.15 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 219 IMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVeAKNLGVSIQLQtlkaesfllTMKEV 298
Cdd:PLN02992 342 VPSWAPQAEILAHQAVGGFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALL-SDELGIAVRSD---------DPKEV 411
|
90
....*....|....*.
gi 568990337 299 IedQRYKTAAMASKVI 314
Cdd:PLN02992 412 I--SRSKIEALVRKVM 425
|
|
| PLN02152 |
PLN02152 |
indole-3-acetate beta-glucosyltransferase |
131-268 |
4.06e-10 |
|
indole-3-acetate beta-glucosyltransferase
Pssm-ID: 177813 [Multi-domain] Cd Length: 455 Bit Score: 61.22 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 131 PLFPNTVYVGGL--LDKPVQPIPQDLEDFISQFGDSGFVLVALGSVVSMiqSKEIIKEMNSAFAHLPQGVLW--TCKSS- 205
Cdd:PLN02152 226 PLLPAEIFTGSEsgKDLSVRDQSSSYTLWLDSKTESSVIYVSFGTMVEL--SKKQIEELARALIEGKRPFLWviTDKLNr 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 206 -------------------HWPKDVSLapnvkIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQP 266
Cdd:PLN02152 304 eakiegeeeteiekiagfrHELEEVGM-----IVSWCSQIEVLRHRAVGCFVTHCGWSSSLESLVLGVPVVAFPMWSDQP 378
|
..
gi 568990337 267 EN 268
Cdd:PLN02152 379 AN 380
|
|
| PLN02534 |
PLN02534 |
UDP-glycosyltransferase |
167-281 |
3.03e-09 |
|
UDP-glycosyltransferase
Pssm-ID: 215293 [Multi-domain] Cd Length: 491 Bit Score: 58.33 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 167 VLVALGSVVSMIQSKEIikEMNSAFAHLPQGVLWTCKSSH-------WPKDVSLAPNVK-----IMDWLPQIDLLAHPSI 234
Cdd:PLN02534 286 IYACLGSLCRLVPSQLI--ELGLGLEASKKPFIWVIKTGEkhseleeWLVKENFEERIKgrgllIKGWAPQVLILSHPAI 363
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568990337 235 RLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQ--PENMVrVEAKNLGVSI 281
Cdd:PLN02534 364 GGFLTHCGWNSTIEGICSGVPMITWPLFAEQflNEKLI-VEVLRIGVRV 411
|
|
| PLN03015 |
PLN03015 |
UDP-glucosyl transferase |
192-289 |
3.69e-09 |
|
UDP-glucosyl transferase
Pssm-ID: 178589 [Multi-domain] Cd Length: 470 Bit Score: 58.17 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 192 AHLPQGVLwtcksshwpkDVSLAPNVKIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVR 271
Cdd:PLN03015 322 ASLPEGFL----------DRTRGVGLVVTQWAPQVEILSHRSIGGFLSHCGWSSVLESLTKGVPIVAWPLYAEQWMNATL 391
|
90
....*....|....*...
gi 568990337 272 VeAKNLGVSIQLQTLKAE 289
Cdd:PLN03015 392 L-TEEIGVAVRTSELPSE 408
|
|
| PLN02167 |
PLN02167 |
UDP-glycosyltransferase family protein |
221-284 |
1.86e-08 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215112 [Multi-domain] Cd Length: 475 Bit Score: 55.96 E-value: 1.86e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568990337 221 DWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVeAKNLGVSIQLQ 284
Cdd:PLN02167 346 GWAPQVEILAHKAIGGFVSHCGWNSVLESLWFGVPIATWPMYAEQQLNAFTM-VKELGLAVELR 408
|
|
| PLN03004 |
PLN03004 |
UDP-glycosyltransferase |
180-298 |
3.25e-08 |
|
UDP-glycosyltransferase
Pssm-ID: 178581 Cd Length: 451 Bit Score: 55.08 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 180 SKEIIKEMNSAFAHLPQGVLWTCKSshwPKDV--------SLAPN----------VKIMDWLPQIDLLAHPSIRLFVTHG 241
Cdd:PLN03004 284 SKEQVIEIAVGLEKSGQRFLWVVRN---PPELekteldlkSLLPEgflsrtedkgMVVKSWAPQVPVLNHKAVGGFVTHC 360
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568990337 242 GMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKnlgVSIQLQTLKAESFLLTMKEV 298
Cdd:PLN03004 361 GWNSILEAVCAGVPMVAWPLYAEQRFNRVMIVDE---IKIAISMNESETGFVSSTEV 414
|
|
| PLN02863 |
PLN02863 |
UDP-glucoronosyl/UDP-glucosyl transferase family protein |
219-265 |
1.31e-07 |
|
UDP-glucoronosyl/UDP-glucosyl transferase family protein
Pssm-ID: 215465 Cd Length: 477 Bit Score: 53.34 E-value: 1.31e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568990337 219 IMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQ 265
Cdd:PLN02863 347 IRGWAPQVAILSHRAVGAFLTHCGWNSVLEGLVAGVPMLAWPMAADQ 393
|
|
| PLN02562 |
PLN02562 |
UDP-glycosyltransferase |
218-302 |
5.68e-06 |
|
UDP-glycosyltransferase
Pssm-ID: 215305 Cd Length: 448 Bit Score: 48.34 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 218 KIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVR-VEAKNLGVsiQLQTLKAESFLLTMK 296
Cdd:PLN02562 331 KVVSWAPQLEVLKHQAVGCYLTHCGWNSTMEAIQCQKRLLCYPVAGDQFVNCAYiVDVWKIGV--RISGFGQKEVEEGLR 408
|
....*.
gi 568990337 297 EVIEDQ 302
Cdd:PLN02562 409 KVMEDS 414
|
|
| PLN02670 |
PLN02670 |
transferase, transferring glycosyl groups |
222-281 |
6.47e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 178275 [Multi-domain] Cd Length: 472 Bit Score: 47.98 E-value: 6.47e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 222 WLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSI 281
Cdd:PLN02670 346 WVPQVKILSHESVGGFLTHCGWNSVVEGLGFGRVLILFPVLNEQGLNTRLLHGKKLGLEV 405
|
|
| PLN03007 |
PLN03007 |
UDP-glucosyltransferase family protein |
219-265 |
6.64e-06 |
|
UDP-glucosyltransferase family protein
Pssm-ID: 178584 [Multi-domain] Cd Length: 482 Bit Score: 47.93 E-value: 6.64e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568990337 219 IMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQ 265
Cdd:PLN03007 349 IRGWAPQVLILDHQATGGFVTHCGWNSLLEGVAAGLPMVTWPVGAEQ 395
|
|
| PLN02208 |
PLN02208 |
glycosyltransferase family protein |
222-335 |
6.86e-06 |
|
glycosyltransferase family protein
Pssm-ID: 177858 Cd Length: 442 Bit Score: 47.70 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 222 WLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPEnMVRVEAKNLGVSIQLQTLKA-----ESFLLTMK 296
Cdd:PLN02208 318 WVQQPLILDHPSIGCFVNHCGPGTIWESLVSDCQMVLIPFLSDQVL-FTRLMTEEFEVSVEVSREKTgwfskESLSNAIK 396
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568990337 297 EVIEDQryktaAMASKVIRQSHP-----LTPAQRLVGWIDHILQ 335
Cdd:PLN02208 397 SVMDKD-----SDLGKLVRSNHTklkeiLVSPGLLTGYVDKFVE 435
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
212-313 |
3.15e-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: 43.86 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 212 SLAPNVKIMDWLPQIDLLAHPSIrLFVTHGGMNSVMEAVHHGVPMVGIPF----FGDQPENMVRVEAKNLGVSIQLQTLK 287
Cdd:pfam04101 51 ELGINYEVFPFIDNMAEYIKAAD-LVISRAGAGTIAELLALGKPAILVPNpsaaRGHQDNNAKELVKAGAALVILQKELT 129
|
90 100
....*....|....*....|....*..
gi 568990337 288 AESFLLTMKEVI-EDQRYKTAAMASKV 313
Cdd:pfam04101 130 PEKLIEALLKLLlNPLRLAEMAKASKA 156
|
|
| PLN00414 |
PLN00414 |
glycosyltransferase family protein |
222-300 |
3.14e-04 |
|
glycosyltransferase family protein
Pssm-ID: 177807 [Multi-domain] Cd Length: 446 Bit Score: 42.70 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 222 WLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPEnMVRVEAKNLGVSIQLQT-----LKAESFLLTMK 296
Cdd:PLN00414 319 WVEQPLILSHPSVGCFVNHCGFGSMWESLVSDCQIVFIPQLADQVL-ITRLLTEELEVSVKVQRedsgwFSKESLRDTVK 397
|
....
gi 568990337 297 EVIE 300
Cdd:PLN00414 398 SVMD 401
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
124-319 |
3.24e-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: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 124 FALDFARPLFPNTVYVGGLLDKPVQPIPQDLEDFisQFGDSGFVLVAL-GSvvsmiQ-SKEIIKEMNSAFAHLPQG---V 198
Cdd:cd03785 142 FPETKKYFPAAKVVVTGNPVREEILNLRKELKRF--GLPPDKPTLLVFgGS-----QgARAINRAVPKALPKLLERgiqV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 199 LWTCKSSHWPKDVS----LAPNVKIMDWLPQIDLL---AHpsirLFVTHGGMNSVMEAVHHGVPMVGIPFF----GDQPE 267
Cdd:cd03785 215 IHQTGKGDYDEVKKlyedLGINVKVFPFIDDMAAAyaaAD----LVISRAGASTIAELTAAGKPAILIPYPyaadDHQEA 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568990337 268 NMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDqRYKTAAMASKVIRQSHP 319
Cdd:cd03785 291 NARALEKAGAAIVIDQEELTPEVLAEAILDLLND-PERLKKMAEAAKKLAKP 341
|
|
| PLN02764 |
PLN02764 |
glycosyltransferase family protein |
221-336 |
4.77e-04 |
|
glycosyltransferase family protein
Pssm-ID: 178364 Cd Length: 453 Bit Score: 41.97 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 221 DWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENmVRVEAKNLGVSIQLQTLKAESFlltMKEVIE 300
Cdd:PLN02764 323 GWVQQPLILSHPSVGCFVSHCGFGSMWESLLSDCQIVLVPQLGDQVLN-TRLLSDELKVSVEVAREETGWF---SKESLR 398
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568990337 301 DQRYKTAAMASKV---IRQSH-----PLTPAQRLVGWIDHILQT 336
Cdd:PLN02764 399 DAINSVMKRDSEIgnlVKKNHtkwreTLASPGLLTGYVDNFIES 442
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
213-335 |
9.73e-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: 37.80 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990337 213 LAPNVKIMDWLPQIDLL---AHpsirLFVTHGGMNSVMEAVHHGVPMVGIPF-F---GDQPENMVRVEAKNLGVSIQLQT 285
Cdd:COG0707 239 IRPNAEVFPFIDDMADAyaaAD----LVISRAGASTVAELAALGKPAILVPLpHaadDHQTKNARALVEAGAAVLIPQSE 314
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568990337 286 LKAESFLLTMKEVIEDqRYKTAAMASKvIRQSHPLTPAQRLVGWIDHILQ 335
Cdd:COG0707 315 LTPEKLAEALEELLED-PERLAKMAEA-ARALARPDAAERIADLILELAK 362
|
|
|