NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|500750667|ref|WP_011986586|]
View 

macrolide family glycosyltransferase [Clostridium botulinum]

Protein Classification

glycosyltransferase( domain architecture ID 1004184)

glycosyltransferase catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.40.50.2000
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  12691742|16037492

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MGT super family cl36903
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ...
 7-385 1.46e-99

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]


The actual alignment was detected with superfamily member TIGR01426:

Pssm-ID: 273616 [Multi-domain]  Cd Length: 392  Bit Score: 301.22  E-value: 1.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667    7 FSIPAHGHTNPTIAVVNELVKRGHEVWYYSFYEFQEKIETAGAEFIPCDNYLPEltPD-IEKKIGKDFASLIEMAADMAM 85
Cdd:TIGR01426   1 FNIPAHGHVNPTLGVVEELVARGHRVTYATTEEFAERVEAAGAEFVLYGSALPP--PDnPPENTEEEPIDIIEKLLDEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667   86 SLDEKVCRDLKEFQPHCIVSDSICIWGKLFAIKLNVPYICSTTTFAMNKY----TAKLIKQGLKEIFRMFIGIPRINK-K 160
Cdd:TIGR01426  79 DVLPQLEEAYKGDRPDLIVYDIASWTGRLLARKWDVPVISSFPTFAANEEfeemVSPAGEGSAEEGAIAERGLAEYVArL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  161 IKLLREKGYNVKNFISIIQNDNDTDtIVYASKEFQPMVETFSDKYAFVGPSF----RVPEVEQIKKKYPLIYISLGTVLN 236
Cdd:TIGR01426 159 SALLEEHGITTPPVEFLAAPRRDLN-LVYTPKAFQPAGETFDDSFTFVGPCIgdrkEDGSWERPGDGRPVVLISLGTVFN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  237 QNRHFYENCIKALADVDCQVIMSVGEKADIPSLGKLPDNFKVYPKVEQLKVLQQTDVFITHCGMNSISESLYFGVPSVLF 316
Cdd:TIGR01426 238 NQPSFYRTCVEAFRDLDWHVVLSVGRGVDPADLGELPPNVEVRQWVPQLEILKKADAFITHGGMNSTMEALFNGVPMVAV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500750667  317 PLHSEQAMVANRVAELNAGKILKSDAV--NSIRETVLQVLNDISYKRNAEVISKSLQKAGGASAAANKIEK 385
Cdd:TIGR01426 318 PQGADQPMTARRIAELGLGRHLPPEEVtaEKLREAVLAVLSDPRYAERLRKMRAEIREAGGARRAADEIEG 388
 
Name Accession Description Interval E-value
MGT TIGR01426
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ...
 7-385 1.46e-99

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: 301.22  E-value: 1.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667    7 FSIPAHGHTNPTIAVVNELVKRGHEVWYYSFYEFQEKIETAGAEFIPCDNYLPEltPD-IEKKIGKDFASLIEMAADMAM 85
Cdd:TIGR01426   1 FNIPAHGHVNPTLGVVEELVARGHRVTYATTEEFAERVEAAGAEFVLYGSALPP--PDnPPENTEEEPIDIIEKLLDEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667   86 SLDEKVCRDLKEFQPHCIVSDSICIWGKLFAIKLNVPYICSTTTFAMNKY----TAKLIKQGLKEIFRMFIGIPRINK-K 160
Cdd:TIGR01426  79 DVLPQLEEAYKGDRPDLIVYDIASWTGRLLARKWDVPVISSFPTFAANEEfeemVSPAGEGSAEEGAIAERGLAEYVArL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  161 IKLLREKGYNVKNFISIIQNDNDTDtIVYASKEFQPMVETFSDKYAFVGPSF----RVPEVEQIKKKYPLIYISLGTVLN 236
Cdd:TIGR01426 159 SALLEEHGITTPPVEFLAAPRRDLN-LVYTPKAFQPAGETFDDSFTFVGPCIgdrkEDGSWERPGDGRPVVLISLGTVFN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  237 QNRHFYENCIKALADVDCQVIMSVGEKADIPSLGKLPDNFKVYPKVEQLKVLQQTDVFITHCGMNSISESLYFGVPSVLF 316
Cdd:TIGR01426 238 NQPSFYRTCVEAFRDLDWHVVLSVGRGVDPADLGELPPNVEVRQWVPQLEILKKADAFITHGGMNSTMEALFNGVPMVAV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500750667  317 PLHSEQAMVANRVAELNAGKILKSDAV--NSIRETVLQVLNDISYKRNAEVISKSLQKAGGASAAANKIEK 385
Cdd:TIGR01426 318 PQGADQPMTARRIAELGLGRHLPPEEVtaEKLREAVLAVLSDPRYAERLRKMRAEIREAGGARRAADEIEG 388
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
3-371 4.66e-74

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 231.67  E-value: 4.66e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667   3 KIVFFSIPAHGHTNPTIAVVNELVKRGHEVWYYSFYEFQEKIETAGAEFIpcdnylpeltpdiekkigkdfasliemaad 82
Cdd:COG1819    1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFADLVEAAGLEFV------------------------------ 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  83 mamsldekvcrdlkEFQPHCIVSDSICIWGKLFAIKLNVPYICSTttfamnkytaklikqglkeifrmfigiprinkkik 162
Cdd:COG1819   51 --------------DWRPDLVVSDPLALAAALAAEALGIPVVSLT----------------------------------- 81

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 163 llrekgynvknfisiiqndndtdtivyaSKEFQPMVETFSDKYAFVGPSF-----RVPEVEQIKKKYPLIYISLGTVLNQ 237
Cdd:COG1819   82 ----------------------------PPELEYPRPPDPANVRFVGPLLpdgpaELPPWLEEDAGRPLVYVTLGTSAND 133

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 238 NRHFYENCIKALADVDCQVIMSVGEkADIPSLGKLPDNFKVYPKVEQLKVLQQTDVFITHCGMNSISESLYFGVPSVLFP 317
Cdd:COG1819  134 RADLLRAVLEALADLGVRVVVTTGG-LDPAELGPLPDNVRVVDYVPQDALLPRADAVVHHGGAGTTAEALRAGVPQVVVP 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500750667 318 LHSEQAMVANRVAELNAGKILKSDAVN--SIRETVLQVLNDISYKRNAEVISKSLQ 371
Cdd:COG1819  213 FGGDQPLNAARVERLGAGLALPPRRLTaeALRAALRRLLADPSYRERAARLAAEIR 268
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
 3-380 1.79e-72

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: 232.06  E-value: 1.79e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667   3 KIVFFSIPAHGHTNPTIAVVNELVKRGHEVWYYS-FYEFQEKIETAGAEFIPC--DNYLPELTPDIEKKIGKDFASLIEM 79
Cdd:cd03784    2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATpPFNFADLVEAAGLTFVPVgdDPDELELDSETNLGPDSLLELLRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  80 AADMAMSLDEKVCRDLKEFQPHCIVSDSICIWGKLFAIKLNVPYICSTTTFAMN---KYTAKLIKQGLKEIFRMFIGIPR 156
Cdd:cd03784   82 LKAADELLDDLLAALRSSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLlsaYLHPFGVLNLLLSSLLEPELFLD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 157 INKKIKLLREKGYNVKNFISIIQNDNDTD---TIVYASKEFQP--MVETFSDKYAFVGPSFRVPEVE-----QIKKKYPL 226
Cdd:cd03784  162 PLLEVLDRLRERLGLPPFSLVLLLLRLVPplyVIGPTFPSLPPdrPRLPSVLGGLRIVPKNGPLPDElwewlDKQPPRSV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 227 IYISLGTVLNQNR-HFYENCIKALADVDCQVIMSVGeKADIPSLGKLPDNFKVYPKVEQLKVLQQ--TDVFITHCGMNSI 303
Cdd:cd03784  242 VYVSFGSMVRDLPeELLELIAEALASLGQRFLWVVG-PDPLGGLERLPDNVLVVKWVPQDELLAHpaVGAFVTHGGWNST 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500750667 304 SESLYFGVPSVLFPLHSEQAMVANRVAELNAGKILKSDAVN--SIRETVLQVLNDISYKRNAEVISKSLQKAGGASAAA 380
Cdd:cd03784  321 LEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTaeELAKAVREVLEDESYRRAAELLAELREEDGAPSAAD 399
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
227-367 1.85e-11

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 65.51  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  227 IYISLGTVLNQNRHFYENCI-KALADVDCQVIMSVGEKAdiPSLgkLPDNFKVYPKVEQLKVLQ--QTDVFITHCGMNSI 303
Cdd:pfam00201 278 VVFSLGSMVSNIPEEKANAIaSALAQIPQKVLWRFDGTK--PST--LGNNTRLVKWLPQNDLLGhpKTRAFITHAGSNGV 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  304 SESLYFGVPSVLFPLHSEQAMVANRVA------ELNAGKILKSDAVNSIREtvlqVLNDISYKRNAEVIS 367
Cdd:pfam00201 354 YEAICHGVPMVGMPLFGDQMDNAKHMEakgaavTLNVLTMTSEDLLNALKE----VINDPSYKENIMRLS 419
PLN02207 PLN02207
UDP-glycosyltransferase
 284-385 1.29e-10

UDP-glycosyltransferase


Pssm-ID: 177857 [Multi-domain]  Cd Length: 468  Bit Score: 62.75  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 284 QLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVAN-RVAEL------------NAGKILKSDAVNSIRE 348
Cdd:PLN02207 342 QVEILAHKAVggFVSHCGWNSIVESLWFGVPIVTWPMYAEQQLNAFlMVKELklavelkldyrvHSDEIVNANEIETAIR 421

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 500750667 349 TVLQVLNDISYKRNAEvISKSLQKA---GGASAAAnkIEK 385
Cdd:PLN02207 422 CVMNKDNNVVRKRVMD-ISQMIQRAtknGGSSFAA--IEK 458
 
Name Accession Description Interval E-value
MGT TIGR01426
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ...
 7-385 1.46e-99

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: 301.22  E-value: 1.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667    7 FSIPAHGHTNPTIAVVNELVKRGHEVWYYSFYEFQEKIETAGAEFIPCDNYLPEltPD-IEKKIGKDFASLIEMAADMAM 85
Cdd:TIGR01426   1 FNIPAHGHVNPTLGVVEELVARGHRVTYATTEEFAERVEAAGAEFVLYGSALPP--PDnPPENTEEEPIDIIEKLLDEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667   86 SLDEKVCRDLKEFQPHCIVSDSICIWGKLFAIKLNVPYICSTTTFAMNKY----TAKLIKQGLKEIFRMFIGIPRINK-K 160
Cdd:TIGR01426  79 DVLPQLEEAYKGDRPDLIVYDIASWTGRLLARKWDVPVISSFPTFAANEEfeemVSPAGEGSAEEGAIAERGLAEYVArL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  161 IKLLREKGYNVKNFISIIQNDNDTDtIVYASKEFQPMVETFSDKYAFVGPSF----RVPEVEQIKKKYPLIYISLGTVLN 236
Cdd:TIGR01426 159 SALLEEHGITTPPVEFLAAPRRDLN-LVYTPKAFQPAGETFDDSFTFVGPCIgdrkEDGSWERPGDGRPVVLISLGTVFN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  237 QNRHFYENCIKALADVDCQVIMSVGEKADIPSLGKLPDNFKVYPKVEQLKVLQQTDVFITHCGMNSISESLYFGVPSVLF 316
Cdd:TIGR01426 238 NQPSFYRTCVEAFRDLDWHVVLSVGRGVDPADLGELPPNVEVRQWVPQLEILKKADAFITHGGMNSTMEALFNGVPMVAV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500750667  317 PLHSEQAMVANRVAELNAGKILKSDAV--NSIRETVLQVLNDISYKRNAEVISKSLQKAGGASAAANKIEK 385
Cdd:TIGR01426 318 PQGADQPMTARRIAELGLGRHLPPEEVtaEKLREAVLAVLSDPRYAERLRKMRAEIREAGGARRAADEIEG 388
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
3-371 4.66e-74

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 231.67  E-value: 4.66e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667   3 KIVFFSIPAHGHTNPTIAVVNELVKRGHEVWYYSFYEFQEKIETAGAEFIpcdnylpeltpdiekkigkdfasliemaad 82
Cdd:COG1819    1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFADLVEAAGLEFV------------------------------ 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  83 mamsldekvcrdlkEFQPHCIVSDSICIWGKLFAIKLNVPYICSTttfamnkytaklikqglkeifrmfigiprinkkik 162
Cdd:COG1819   51 --------------DWRPDLVVSDPLALAAALAAEALGIPVVSLT----------------------------------- 81

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 163 llrekgynvknfisiiqndndtdtivyaSKEFQPMVETFSDKYAFVGPSF-----RVPEVEQIKKKYPLIYISLGTVLNQ 237
Cdd:COG1819   82 ----------------------------PPELEYPRPPDPANVRFVGPLLpdgpaELPPWLEEDAGRPLVYVTLGTSAND 133

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 238 NRHFYENCIKALADVDCQVIMSVGEkADIPSLGKLPDNFKVYPKVEQLKVLQQTDVFITHCGMNSISESLYFGVPSVLFP 317
Cdd:COG1819  134 RADLLRAVLEALADLGVRVVVTTGG-LDPAELGPLPDNVRVVDYVPQDALLPRADAVVHHGGAGTTAEALRAGVPQVVVP 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500750667 318 LHSEQAMVANRVAELNAGKILKSDAVN--SIRETVLQVLNDISYKRNAEVISKSLQ 371
Cdd:COG1819  213 FGGDQPLNAARVERLGAGLALPPRRLTaeALRAALRRLLADPSYRERAARLAAEIR 268
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
 3-380 1.79e-72

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: 232.06  E-value: 1.79e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667   3 KIVFFSIPAHGHTNPTIAVVNELVKRGHEVWYYS-FYEFQEKIETAGAEFIPC--DNYLPELTPDIEKKIGKDFASLIEM 79
Cdd:cd03784    2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATpPFNFADLVEAAGLTFVPVgdDPDELELDSETNLGPDSLLELLRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  80 AADMAMSLDEKVCRDLKEFQPHCIVSDSICIWGKLFAIKLNVPYICSTTTFAMN---KYTAKLIKQGLKEIFRMFIGIPR 156
Cdd:cd03784   82 LKAADELLDDLLAALRSSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLlsaYLHPFGVLNLLLSSLLEPELFLD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 157 INKKIKLLREKGYNVKNFISIIQNDNDTD---TIVYASKEFQP--MVETFSDKYAFVGPSFRVPEVE-----QIKKKYPL 226
Cdd:cd03784  162 PLLEVLDRLRERLGLPPFSLVLLLLRLVPplyVIGPTFPSLPPdrPRLPSVLGGLRIVPKNGPLPDElwewlDKQPPRSV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 227 IYISLGTVLNQNR-HFYENCIKALADVDCQVIMSVGeKADIPSLGKLPDNFKVYPKVEQLKVLQQ--TDVFITHCGMNSI 303
Cdd:cd03784  242 VYVSFGSMVRDLPeELLELIAEALASLGQRFLWVVG-PDPLGGLERLPDNVLVVKWVPQDELLAHpaVGAFVTHGGWNST 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500750667 304 SESLYFGVPSVLFPLHSEQAMVANRVAELNAGKILKSDAVN--SIRETVLQVLNDISYKRNAEVISKSLQKAGGASAAA 380
Cdd:cd03784  321 LEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTaeELAKAVREVLEDESYRRAAELLAELREEDGAPSAAD 399
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 13-379 1.36e-14

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: 74.17  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  13 GHTNPTIAVVNELVKRGHEVwyySFYEFQEKIEtagAEFIPCDNYlPELTPDIEKKIGKDFASLIEMAADMAMSLDEKVc 92
Cdd:cd03785   11 GHIFPALALAEELRKRGAEI---LFIGTKRGLE---AKLVPEAGI-PFHTIPISGLRRKGSLKNLKAPFKLLKGLRQAR- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  93 RDLKEFQPHCIVSDS------ICIWgklfAIKLNVPYI---CSTTTFAMNKYTAKLIK---QGLKEIFRMFIGiprinKK 160
Cdd:cd03785   83 KILRKFKPDVVIGFGgyvsgpVVLA----ARLLGIPLIiheQNAVPGLANRLLSRFADkvaVSFPETKKYFPA-----AK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 161 IKL----LREKGYNVKNFISIIQNDNDTDTIVyaskefqpmvetfsdkyAFVGpsfrvpeveqikkkypliyiSLG-TVL 235
Cdd:cd03785  154 VVVtgnpVREEILNLRKELKRFGLPPDKPTLL-----------------VFGG--------------------SQGaRAI 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 236 NQnrhFYENCIKALADVDCQVIMSVGEK--ADIPSL-GKLPDNFKVYPKVEQL-KVLQQTDVFITHCGMNSISESLYFGV 311
Cdd:cd03785  197 NR---AVPKALPKLLERGIQVIHQTGKGdyDEVKKLyEDLGINVKVFPFIDDMaAAYAAADLVISRAGASTIAELTAAGK 273

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500750667 312 PSVLFPL----HSEQAMVANRVAELNAGKILKSDAVNSirETVLQVLNDI-SYKRNAEVISKSLQKAGGASAA 379
Cdd:cd03785  274 PAILIPYpyaaDDHQEANARALEKAGAAIVIDQEELTP--EVLAEAILDLlNDPERLKKMAEAAKKLAKPDAA 344
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
227-367 1.85e-11

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 65.51  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  227 IYISLGTVLNQNRHFYENCI-KALADVDCQVIMSVGEKAdiPSLgkLPDNFKVYPKVEQLKVLQ--QTDVFITHCGMNSI 303
Cdd:pfam00201 278 VVFSLGSMVSNIPEEKANAIaSALAQIPQKVLWRFDGTK--PST--LGNNTRLVKWLPQNDLLGhpKTRAFITHAGSNGV 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  304 SESLYFGVPSVLFPLHSEQAMVANRVA------ELNAGKILKSDAVNSIREtvlqVLNDISYKRNAEVIS 367
Cdd:pfam00201 354 YEAICHGVPMVGMPLFGDQMDNAKHMEakgaavTLNVLTMTSEDLLNALKE----VINDPSYKENIMRLS 419
PLN02207 PLN02207
UDP-glycosyltransferase
 284-385 1.29e-10

UDP-glycosyltransferase


Pssm-ID: 177857 [Multi-domain]  Cd Length: 468  Bit Score: 62.75  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 284 QLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVAN-RVAEL------------NAGKILKSDAVNSIRE 348
Cdd:PLN02207 342 QVEILAHKAVggFVSHCGWNSIVESLWFGVPIVTWPMYAEQQLNAFlMVKELklavelkldyrvHSDEIVNANEIETAIR 421

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 500750667 349 TVLQVLNDISYKRNAEvISKSLQKA---GGASAAAnkIEK 385
Cdd:PLN02207 422 CVMNKDNNVVRKRVMD-ISQMIQRAtknGGSSFAA--IEK 458
PLN02554 PLN02554
UDP-glycosyltransferase family protein
 272-331 4.47e-08

UDP-glycosyltransferase family protein


Pssm-ID: 215304  Cd Length: 481  Bit Score: 54.79  E-value: 4.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 272 LPDNF--------KVYPKVEQLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVANRVAE 331
Cdd:PLN02554 332 LPEGFldrtkdigKVIGWAPQVAVLAKPAIggFVTHCGWNSILESLWFGVPMAAWPLYAEQKFNAFEMVE 401
PLN00164 PLN00164
glucosyltransferase; Provisional
 278-326 4.88e-08

glucosyltransferase; Provisional


Pssm-ID: 215084 [Multi-domain]  Cd Length: 480  Bit Score: 54.68  E-value: 4.88e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500750667 278 VYPK-VEQLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVA 326
Cdd:PLN00164 342 VWPTwAPQKEILAHAAVggFVTHCGWNSVLESLWHGVPMAPWPLYAEQHLNA 393
egt PHA03392
ecdysteroid UDP-glucosyltransferase; Provisional
 227-362 6.76e-08

ecdysteroid UDP-glucosyltransferase; Provisional


Pssm-ID: 223071 [Multi-domain]  Cd Length: 507  Bit Score: 54.19  E-value: 6.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 227 IYISLGT---VLNQNRHFYENCIKALADVDCQVIMSVGekaDIPSLGKLPDNFKVYPKVEQLKVLQQTDV--FITHCGMN 301
Cdd:PHA03392 299 VYVSFGSsidTNDMDNEFLQMLLRTFKKLPYNVLWKYD---GEVEAINLPANVLTQKWFPQRAVLKHKNVkaFVTQGGVQ 375

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500750667 302 SISESLYFGVPSVLFPLHSEQAMVANRVAELNAGKILKSDAVNSIR--ETVLQVLNDISYKRN 362
Cdd:PHA03392 376 STDEAIDALVPMVGLPMMGDQFYNTNKYVELGIGRALDTVTVSAAQlvLAIVDVIENPKYRKN 438
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 244-389 7.36e-08

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: 53.59  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 244 NCIKALADVDCQVIMSVGeKADIPSL-----GKLPDNFKVYPKVEQL-KVLQQTDVFITHCGMNSISESLYFGVPSVLFP 317
Cdd:COG0707  207 AALAALLEARLQVVHQTG-KGDYEEVraayaAAIRPNAEVFPFIDDMaDAYAAADLVISRAGASTVAELAALGKPAILVP 285

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500750667 318 L----HSEQAMVANRVAELNAGKILKSDAVN--SIRETVLQVLNDISYKRNAEVISKSLQKAGGASAAANKIEKVCNK 389
Cdd:COG0707  286 LphaaDDHQTKNARALVEAGAAVLIPQSELTpeKLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
PLN02448 PLN02448
UDP-glycosyltransferase family protein
 278-331 9.00e-08

UDP-glycosyltransferase family protein


Pssm-ID: 215247 [Multi-domain]  Cd Length: 459  Bit Score: 53.86  E-value: 9.00e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500750667 278 VYPKVEQLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVANRVAE 331
Cdd:PLN02448 327 VVPWCDQLKVLCHSSVggFWTHCGWNSTLEAVFAGVPMLTFPLFWDQPLNSKLIVE 382
PLN02173 PLN02173
UDP-glucosyl transferase family protein
 178-374 1.15e-07

UDP-glucosyl transferase family protein


Pssm-ID: 177830 [Multi-domain]  Cd Length: 449  Bit Score: 53.50  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 178 IQNDNDTDTIVYASKEfqpmvETFSDKYAFVGPSFRVpeveqikkkyplIYISLGTVLNQNRHFYENCIKALADVDCQVI 257
Cdd:PLN02173 235 IKSDNDYDLNLFDLKE-----AALCTDWLDKRPQGSV------------VYIAFGSMAKLSSEQMEEIASAISNFSYLWV 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 258 MSVGEKADIPSlGKL----PDNFKVYPKVEQLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVAN---- 327
Cdd:PLN02173 298 VRASEESKLPP-GFLetvdKDKSLVLKWSPQLQVLSNKAIgcFMTHCGWNSTMEGLSLGVPMVAMPQWTDQPMNAKyiqd 376

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500750667 328 ------RVAELNAGKILKSDAVN-SIREtVLQVLNDISYKRNA----EVISKSLQKAG 374
Cdd:PLN02173 377 vwkvgvRVKAEKESGIAKREEIEfSIKE-VMEGEKSKEMKENAgkwrDLAVKSLSEGG 433
PLN02167 PLN02167
UDP-glycosyltransferase family protein
 247-350 5.39e-07

UDP-glycosyltransferase family protein


Pssm-ID: 215112 [Multi-domain]  Cd Length: 475  Bit Score: 51.34  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 247 KALADVDCQVIMSV----GEKADIPSLgkLPDNFK--------VYPKVEQLKVLQQTDV--FITHCGMNSISESLYFGVP 312
Cdd:PLN02167 303 QALELVGCRFLWSIrtnpAEYASPYEP--LPEGFMdrvmgrglVCGWAPQVEILAHKAIggFVSHCGWNSVLESLWFGVP 380

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500750667 313 SVLFPLHSEQAMVA-NRVAELNAGKILKSDAVNSIRETV 350
Cdd:PLN02167 381 IATWPMYAEQQLNAfTMVKELGLAVELRLDYVSAYGEIV 419
PLN02152 PLN02152
indole-3-acetate beta-glucosyltransferase
 284-387 7.52e-07

indole-3-acetate beta-glucosyltransferase


Pssm-ID: 177813 [Multi-domain]  Cd Length: 455  Bit Score: 50.82  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 284 QLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVAN----------RVAELNAGKILKSDavnsIRETVL 351
Cdd:PLN02152 337 QIEVLRHRAVgcFVTHCGWSSSLESLVLGVPVVAFPMWSDQPANAKlleeiwktgvRVRENSEGLVERGE----IRRCLE 412

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 500750667 352 QVLNDIS--YKRNAEVISKSLQKAGGASAAANK-----IEKVC 387
Cdd:PLN02152 413 AVMEEKSveLRESAEKWKRLAIEAGGEGGSSDKnveafVKTLC 455
PLN03015 PLN03015
UDP-glucosyl transferase
 284-351 1.53e-06

UDP-glucosyl transferase


Pssm-ID: 178589 [Multi-domain]  Cd Length: 470  Bit Score: 50.08  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 284 QLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAM----------VANRVAELNAGKILKSDAVNSIRETVL 351
Cdd:PLN03015 345 QVEILSHRSIggFLSHCGWSSVLESLTKGVPIVAWPLYAEQWMnatllteeigVAVRTSELPSEKVIGREEVASLVRKIV 424
PLN02210 PLN02210
UDP-glucosyl transferase
 226-344 3.07e-06

UDP-glucosyl transferase


Pssm-ID: 215127 [Multi-domain]  Cd Length: 456  Bit Score: 48.88  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 226 LIYISLGTVLNQNRHFYENCIKALADVDCQVIMSVGEKADIPSLGKLPDNFK-----VYPKVEQLKVLQQTDV--FITHC 298
Cdd:PLN02210 271 VVYISFGSMLESLENQVETIAKALKNRGVPFLWVIRPKEKAQNVQVLQEMVKegqgvVLEWSPQEKILSHMAIscFVTHC 350

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 500750667 299 GMNSISESLYFGVPSVLFPLHSEQAMVANRVAEL-NAGKILKSDAVN 344
Cdd:PLN02210 351 GWNSTIETVVAGVPVVAYPSWTDQPIDARLLVDVfGIGVRMRNDAVD 397
PLN02670 PLN02670
transferase, transferring glycosyl groups
 268-324 3.53e-06

transferase, transferring glycosyl groups


Pssm-ID: 178275 [Multi-domain]  Cd Length: 472  Bit Score: 48.75  E-value: 3.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500750667 268 SLGKLPDNFKVYPK---------VEQLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAM 324
Cdd:PLN02670 324 ALEMLPDGFEERVKgrgmihvgwVPQVKILSHESVggFLTHCGWNSVVEGLGFGRVLILFPVLNEQGL 391
PLN02555 PLN02555
limonoid glucosyltransferase
 208-322 1.07e-05

limonoid glucosyltransferase


Pssm-ID: 178170 [Multi-domain]  Cd Length: 480  Bit Score: 47.49  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 208 VGPSFRVPEV-----------------EQIKKKYP--LIYISLGTVLNQNRHFYENCIKAL--ADVDCQVIM------SV 260
Cdd:PLN02555 242 VGPLFKMAKTpnsdvkgdiskpaddciEWLDSKPPssVVYISFGTVVYLKQEQIDEIAYGVlnSGVSFLWVMrpphkdSG 321

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500750667 261 GEKADIPS--LGKLPDNFKVYPKVEQLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQ 322
Cdd:PLN02555 322 VEPHVLPEefLEKAGDKGKIVQWCPQEKVLAHPSVacFVTHCGWNSTMEALSSGVPVVCFPQWGDQ 387
PLN02992 PLN02992
coniferyl-alcohol glucosyltransferase
 284-331 6.02e-05

coniferyl-alcohol glucosyltransferase


Pssm-ID: 178572 [Multi-domain]  Cd Length: 481  Bit Score: 44.97  E-value: 6.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 500750667 284 QLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVANRVAE 331
Cdd:PLN02992 348 QAEILAHQAVggFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALLSD 397
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
 208-384 1.88e-04

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 43.08  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 208 VGPSF-RVPEVEQIKKKY------PLIYISLGTVlnQNRHFYENCiKALADVDC--QVIMSVGE----KADIPSLGKLPD 274
Cdd:cd17507  174 VRPSFaEVRDKDEARNELnlspdkPTVLLMGGGG--GMGPVKETV-EALLDSLRagQVLVVCGKnkklYEKLSGLEEDYI 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 275 NFKVYPKVEQL-KVLQQTDVFITHCGMNSISESLYFGVPSVLF---PLHSEQAmvANRVAELNAGKILKSDAVnsIRETV 350
Cdd:cd17507  251 NVRVLGYVDDMnELMAASDLVITKPGGLTISEALARGLPVIIYdpiPGQEEEN--ADFLENNGAGIIARDPEE--LLEIV 326

                        170       180       190
                 ....*....|....*....|....*....|....
gi 500750667 351 LQVLNDISYKRnaevISKSLQKAGGASAAANKIE 384
Cdd:cd17507  327 ARLIDPPSLLR----MMSEAAKELKPPAAAKVIA 356
PLN03004 PLN03004
UDP-glycosyltransferase
 284-337 2.20e-04

UDP-glycosyltransferase


Pssm-ID: 178581  Cd Length: 451  Bit Score: 43.14  E-value: 2.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500750667 284 QLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMvaNRVAELNAGKI 337
Cdd:PLN03004 344 QVPVLNHKAVggFVTHCGWNSILEAVCAGVPMVAWPLYAEQRF--NRVMIVDEIKI 397
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 230-389 3.40e-04

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 42.43  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 230 SLG-TVLNQnrhFYENCIKALADvDCQVIMSVGEK--ADIPSLGKLPDNFKVYPKVEQL-KVLQQTDVFITHCGMNSISE 305
Cdd:PRK00726 192 SQGaRVLNE---AVPEALALLPE-ALQVIHQTGKGdlEEVRAAYAAGINAEVVPFIDDMaAAYAAADLVICRAGASTVAE 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 306 SLYFGVPSVLFPL----HSEQAMVANRVAELNAGKILKSDAVN--SIRETVLQVLNDISYKRNAEVISKSLQKAGGASAA 379
Cdd:PRK00726 268 LAAAGLPAILVPLphaaDDHQTANARALVDAGAALLIPQSDLTpeKLAEKLLELLSDPERLEAMAEAARALGKPDAAERL 347

                        170
                 ....*....|
gi 500750667 380 ANKIEKVCNK 389
Cdd:PRK00726 348 ADLIEELARK 357
PLN02534 PLN02534
UDP-glycosyltransferase
 294-322 1.18e-03

UDP-glycosyltransferase


Pssm-ID: 215293 [Multi-domain]  Cd Length: 491  Bit Score: 41.00  E-value: 1.18e-03
                         10        20
                 ....*....|....*....|....*....
gi 500750667 294 FITHCGMNSISESLYFGVPSVLFPLHSEQ 322
Cdd:PLN02534 366 FLTHCGWNSTIEGICSGVPMITWPLFAEQ 394
COG5017 COG5017
UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism];
273-317 5.50e-03

UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism];


Pssm-ID: 444041 [Multi-domain]  Cd Length: 164  Bit Score: 37.21  E-value: 5.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 500750667 273 PDNFKVYPKV---EQLKVLQQTDVFITHCGMNSISESLYFGVPSVLFP 317
Cdd:COG5017   44 PRNAEAVPFLppdEFQKLIAQARLVISHAGMGSILTALKLGKPFILVP 91
PLN03007 PLN03007
UDP-glucosyltransferase family protein
 221-322 5.93e-03

UDP-glucosyltransferase family protein


Pssm-ID: 178584 [Multi-domain]  Cd Length: 482  Bit Score: 38.69  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 221 KKKYPLIYISLGTVLN-QNRHFYEncIKALADVDCQVIMSV-------GEKADIpslgkLPDNFKVYPKVEQL------- 285
Cdd:PLN03007 282 KKPDSVIYLSFGSVASfKNEQLFE--IAAGLEGSGQNFIWVvrknenqGEKEEW-----LPEGFEERTKGKGLiirgwap 354

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 500750667 286 KVL----QQTDVFITHCGMNSISESLYFGVPSVLFPLHSEQ 322
Cdd:PLN03007 355 QVLildhQATGGFVTHCGWNSLLEGVAAGLPMVTWPVGAEQ 395
PLN02863 PLN02863
UDP-glucoronosyl/UDP-glucosyl transferase family protein
 282-373 6.50e-03

UDP-glucoronosyl/UDP-glucosyl transferase family protein


Pssm-ID: 215465  Cd Length: 477  Bit Score: 38.70  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667 282 VEQLKVLQQTDV--FITHCGMNSISESLYFGVPSVLFPLHSEQAMVANR-VAELNAGKIL--KSDAVNSIRETVLQVLND 356
Cdd:PLN02863 351 APQVAILSHRAVgaFLTHCGWNSVLEGLVAGVPMLAWPMAADQFVNASLlVDELKVAVRVceGADTVPDSDELARVFMES 430

                         90
                 ....*....|....*..
gi 500750667 357 ISYKRNAEVISKSLQKA 373
Cdd:PLN02863 431 VSENQVERERAKELRRA 447
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 255-373 8.57e-03

Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.


Pssm-ID: 427711 [Multi-domain]  Cd Length: 166  Bit Score: 36.92  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500750667  255 QVIMSVGEKAD---IPSLGKLPDNFKVYPKVEQLK-VLQQTDVFITHCGMNSISESLYFGVPSVLFPL--HSEQAMVANR 328
Cdd:pfam04101  32 QVLHQTGKGDLeevKIDYAELGINYEVFPFIDNMAeYIKAADLVISRAGAGTIAELLALGKPAILVPNpsAARGHQDNNA 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 500750667  329 --VAELNAGKILKSDAVN--SIRETVLQVLNDIsyKRNAEVISKSLQKA 373
Cdd:pfam04101 112 keLVKAGAALVILQKELTpeKLIEALLKLLLNP--LRLAEMAKASKASG 158
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH