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Conserved domains on  [gi|1860102248|gb|QKW32554|]
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DUF1205 domain-containing protein (plasmid) [Nocardiopsis flavescens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
1-399 3.03e-116

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member TIGR04516:

Pssm-ID: 471961  Cd Length: 418  Bit Score: 345.01  E-value: 3.03e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   1 MRVLFTAWGWPTHFQPGVPLAWAFQAAGHDVLVASQPSLAAAATEAGLTMAPVGGEVDVDtlrtnpilrEVRDTLRDPMV 80
Cdd:TIGR04516   1 MRVLFTSFAHNTHFHGLVPLAWALRAAGHEVRVASQPALTDAITGAGLTAVPVGEDHDLD---------ELLAEVGGDLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  81 CYMREGELPQGERDKW-----LAMHT------HFGLVAEAMVDDLVALAAAWRPDLIVWEQTTLAGAVTARVHKIPDVRL 149
Cdd:TIGR04516  72 PYHRDFDFTEKRPERLtweylLGMETvltsafYALINNDSMIDDLVAFARSWRPDLVIWEPFTFAGAVAARATGAAHARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 150 VISPDVLGD-RPEAIERQTRSHDVSR----------LFERFG------VLDGHnqarWTLDQCPPSLRLPSATHRMPMRY 212
Cdd:TIGR04516 152 LWGPDLIGRaRRAFLALLAGQPPEHRedplaewltwTLERYGctfdeeLVTGQ----WTIDPMPASLRLDLGLPTVPMRY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 213 TPYAGGALVPDWVHTQPERPRVCLSAGLTTAGFAAQETVSLPELLEYVRELDVEVIMPGAAREFPQLAEqTPPNVRVLDY 292
Cdd:TIGR04516 228 VPYNGPSVVPDWLREPPERPRVCLTLGVSARETMGGDGVSVGELLDALADLDAEVVATLDAAQRELLGP-VPDNVRLVDF 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 293 VPLSLILPSCAAIVHHGGGGTMLTAASHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLLSNTAF 372
Cdd:TIGR04516 307 VPLDALLPTCAAIVHHGGAGTWATAAAHGVPQIILPDLWDAVVRAQRLEALGAGLALPPAELTAERLRDAVVRVLDEPSF 386
                         410       420
                  ....*....|....*....|....*..
gi 1860102248 373 QEAADRVAQENHHQPTAAAVVDVLGRL 399
Cdd:TIGR04516 387 RAGAARLRAEMLAEPSPAEVVPVLERL 413
 
Name Accession Description Interval E-value
glycosyl_450act TIGR04516
glycosyltransferase, activator-dependent family; Many biosynthesis clusters for secondary ...
1-399 3.03e-116

glycosyltransferase, activator-dependent family; Many biosynthesis clusters for secondary metabolites feature a glycosyltransferase gene next to a P450 homolog, often with the P450 lacking a critical heme-binding Cys. These P540-derived sequences seem to be allosteric activators of glycosyltransferases such as the member of this family. This model describes a set of related glycosyltransferases, many of which can be recognized as activator-dependent from genomic context.


Pssm-ID: 275309  Cd Length: 418  Bit Score: 345.01  E-value: 3.03e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   1 MRVLFTAWGWPTHFQPGVPLAWAFQAAGHDVLVASQPSLAAAATEAGLTMAPVGGEVDVDtlrtnpilrEVRDTLRDPMV 80
Cdd:TIGR04516   1 MRVLFTSFAHNTHFHGLVPLAWALRAAGHEVRVASQPALTDAITGAGLTAVPVGEDHDLD---------ELLAEVGGDLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  81 CYMREGELPQGERDKW-----LAMHT------HFGLVAEAMVDDLVALAAAWRPDLIVWEQTTLAGAVTARVHKIPDVRL 149
Cdd:TIGR04516  72 PYHRDFDFTEKRPERLtweylLGMETvltsafYALINNDSMIDDLVAFARSWRPDLVIWEPFTFAGAVAARATGAAHARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 150 VISPDVLGD-RPEAIERQTRSHDVSR----------LFERFG------VLDGHnqarWTLDQCPPSLRLPSATHRMPMRY 212
Cdd:TIGR04516 152 LWGPDLIGRaRRAFLALLAGQPPEHRedplaewltwTLERYGctfdeeLVTGQ----WTIDPMPASLRLDLGLPTVPMRY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 213 TPYAGGALVPDWVHTQPERPRVCLSAGLTTAGFAAQETVSLPELLEYVRELDVEVIMPGAAREFPQLAEqTPPNVRVLDY 292
Cdd:TIGR04516 228 VPYNGPSVVPDWLREPPERPRVCLTLGVSARETMGGDGVSVGELLDALADLDAEVVATLDAAQRELLGP-VPDNVRLVDF 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 293 VPLSLILPSCAAIVHHGGGGTMLTAASHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLLSNTAF 372
Cdd:TIGR04516 307 VPLDALLPTCAAIVHHGGAGTWATAAAHGVPQIILPDLWDAVVRAQRLEALGAGLALPPAELTAERLRDAVVRVLDEPSF 386
                         410       420
                  ....*....|....*....|....*..
gi 1860102248 373 QEAADRVAQENHHQPTAAAVVDVLGRL 399
Cdd:TIGR04516 387 RAGAARLRAEMLAEPSPAEVVPVLERL 413
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
1-396 5.57e-62

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: 205.09  E-value: 5.57e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   1 MRVLFTAWGWPTHFQPGVPLAWAFQAAGHDVLVASQPS-LAAAATEAGLTMAPVGGEVDvdtlrtnpilrevrdtlrdpm 79
Cdd:cd03784     1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFnFADLVEAAGLTFVPVGDDPD--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  80 vcYMREGELPQGERDKWLAMHTHFGLVAEAMVDDLVALAA-AWRPDLIVWEQTTLAGAVTARVHKIPDVRLVISPD---- 154
Cdd:cd03784    60 --ELELDSETNLGPDSLLELLRRLLKAADELLDDLLAALRsSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPAtlls 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 155 -----------VLGDRPEAIERQTRSHDVS-RLFERFGV--------LDGHNQARWTLDQCPPSLRLPSATHRM---PMR 211
Cdd:cd03784   138 aylhpfgvlnlLLSSLLEPELFLDPLLEVLdRLRERLGLppfslvllLLRLVPPLYVIGPTFPSLPPDRPRLPSvlgGLR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 212 YTPYAGGALVPDWVH--TQPERPRVCLSAGLTTAGFAAQETVslpELLEYVRELDVEVIMpGAAREFPQLAEQTPPNVRV 289
Cdd:cd03784   218 IVPKNGPLPDELWEWldKQPPRSVVYVSFGSMVRDLPEELLE---LIAEALASLGQRFLW-VVGPDPLGGLERLPDNVLV 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 290 LDYVPLSLIL--PSCAAIVHHGGGGTMLTAASHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLL 367
Cdd:cd03784   294 VKWVPQDELLahPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREVL 373
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1860102248 368 SNTAFQEAADRVAQ--ENHHQPTAAAVVDVL 396
Cdd:cd03784   374 EDESYRRAAELLAElrEEDGAPSAADVVERL 404
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
2-382 3.29e-60

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


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 196.23  E-value: 3.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   2 RVLFTAWGWPTHFQPGVPLAWAFQAAGHDVLVASQPSLAAAATEAGLTmapvggevdvdtlrtnpilrevrdtlrdpmvc 81
Cdd:COG1819     1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFADLVEAAGLE-------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  82 ymregelpqgerdkwlamhthfglvaeamvddlvalAAAWRPDLIVWEQTTLAGAVTARVHKIPDVRLvispdvlgdrpe 161
Cdd:COG1819    49 ------------------------------------FVDWRPDLVVSDPLALAAALAAEALGIPVVSL------------ 80
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 162 aierqtrshdvsrlferfgvldghnqarwtldqCPPSLRLPSATHRMPMRYTPY---AGGALVPDWVHTQPERPRVCLSA 238
Cdd:COG1819    81 ---------------------------------TPPELEYPRPPDPANVRFVGPllpDGPAELPPWLEEDAGRPLVYVTL 127
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 239 GLTTAGFAAQetvsLPELLEYVRELDVEVIMPGAAREFPQLAEQtPPNVRVLDYVPLSLILPSCAAIVHHGGGGTMLTAA 318
Cdd:COG1819   128 GTSANDRADL----LRAVLEALADLGVRVVVTTGGLDPAELGPL-PDNVRVVDYVPQDALLPRADAVVHHGGAGTTAEAL 202
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860102248 319 SHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLLSNTAFQEAADRVAQE 382
Cdd:COG1819   203 RAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRRLTAEALRAALRRLLADPSYRERAARLAAE 266
DUF1205 pfam06722
Protein of unknown function (DUF1205); This family represents a conserved region of unknown ...
192-288 2.95e-22

Protein of unknown function (DUF1205); This family represents a conserved region of unknown function within bacterial glycosyl transferases. Many family members contain pfam03033.


Pssm-ID: 369050  Cd Length: 95  Bit Score: 90.26  E-value: 2.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 192 LDQCPPSLRLPSATHRMPMRYTPYAGGALVPDWVHTQPERPRVCLSAGLTTAGFAAQEtVSLPELLEYVRELDVEVIMPG 271
Cdd:pfam06722   1 IDVAPPSLRPDDGKGTVPMRYVPYNGPSVVPEWLYTGSARRRICVTLGTSVPNGYNQA-DLIQAVLDQVATLDAEIVVAV 79
                          90
                  ....*....|....*..
gi 1860102248 272 AAREFPQLAEqTPPNVR 288
Cdd:pfam06722  80 DEDARSELRE-LPDNVR 95
 
Name Accession Description Interval E-value
glycosyl_450act TIGR04516
glycosyltransferase, activator-dependent family; Many biosynthesis clusters for secondary ...
1-399 3.03e-116

glycosyltransferase, activator-dependent family; Many biosynthesis clusters for secondary metabolites feature a glycosyltransferase gene next to a P450 homolog, often with the P450 lacking a critical heme-binding Cys. These P540-derived sequences seem to be allosteric activators of glycosyltransferases such as the member of this family. This model describes a set of related glycosyltransferases, many of which can be recognized as activator-dependent from genomic context.


Pssm-ID: 275309  Cd Length: 418  Bit Score: 345.01  E-value: 3.03e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   1 MRVLFTAWGWPTHFQPGVPLAWAFQAAGHDVLVASQPSLAAAATEAGLTMAPVGGEVDVDtlrtnpilrEVRDTLRDPMV 80
Cdd:TIGR04516   1 MRVLFTSFAHNTHFHGLVPLAWALRAAGHEVRVASQPALTDAITGAGLTAVPVGEDHDLD---------ELLAEVGGDLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  81 CYMREGELPQGERDKW-----LAMHT------HFGLVAEAMVDDLVALAAAWRPDLIVWEQTTLAGAVTARVHKIPDVRL 149
Cdd:TIGR04516  72 PYHRDFDFTEKRPERLtweylLGMETvltsafYALINNDSMIDDLVAFARSWRPDLVIWEPFTFAGAVAARATGAAHARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 150 VISPDVLGD-RPEAIERQTRSHDVSR----------LFERFG------VLDGHnqarWTLDQCPPSLRLPSATHRMPMRY 212
Cdd:TIGR04516 152 LWGPDLIGRaRRAFLALLAGQPPEHRedplaewltwTLERYGctfdeeLVTGQ----WTIDPMPASLRLDLGLPTVPMRY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 213 TPYAGGALVPDWVHTQPERPRVCLSAGLTTAGFAAQETVSLPELLEYVRELDVEVIMPGAAREFPQLAEqTPPNVRVLDY 292
Cdd:TIGR04516 228 VPYNGPSVVPDWLREPPERPRVCLTLGVSARETMGGDGVSVGELLDALADLDAEVVATLDAAQRELLGP-VPDNVRLVDF 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 293 VPLSLILPSCAAIVHHGGGGTMLTAASHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLLSNTAF 372
Cdd:TIGR04516 307 VPLDALLPTCAAIVHHGGAGTWATAAAHGVPQIILPDLWDAVVRAQRLEALGAGLALPPAELTAERLRDAVVRVLDEPSF 386
                         410       420
                  ....*....|....*....|....*..
gi 1860102248 373 QEAADRVAQENHHQPTAAAVVDVLGRL 399
Cdd:TIGR04516 387 RAGAARLRAEMLAEPSPAEVVPVLERL 413
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
1-396 5.57e-62

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: 205.09  E-value: 5.57e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   1 MRVLFTAWGWPTHFQPGVPLAWAFQAAGHDVLVASQPS-LAAAATEAGLTMAPVGGEVDvdtlrtnpilrevrdtlrdpm 79
Cdd:cd03784     1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFnFADLVEAAGLTFVPVGDDPD--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  80 vcYMREGELPQGERDKWLAMHTHFGLVAEAMVDDLVALAA-AWRPDLIVWEQTTLAGAVTARVHKIPDVRLVISPD---- 154
Cdd:cd03784    60 --ELELDSETNLGPDSLLELLRRLLKAADELLDDLLAALRsSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPAtlls 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 155 -----------VLGDRPEAIERQTRSHDVS-RLFERFGV--------LDGHNQARWTLDQCPPSLRLPSATHRM---PMR 211
Cdd:cd03784   138 aylhpfgvlnlLLSSLLEPELFLDPLLEVLdRLRERLGLppfslvllLLRLVPPLYVIGPTFPSLPPDRPRLPSvlgGLR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 212 YTPYAGGALVPDWVH--TQPERPRVCLSAGLTTAGFAAQETVslpELLEYVRELDVEVIMpGAAREFPQLAEQTPPNVRV 289
Cdd:cd03784   218 IVPKNGPLPDELWEWldKQPPRSVVYVSFGSMVRDLPEELLE---LIAEALASLGQRFLW-VVGPDPLGGLERLPDNVLV 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 290 LDYVPLSLIL--PSCAAIVHHGGGGTMLTAASHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLL 367
Cdd:cd03784   294 VKWVPQDELLahPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVEELGAGVELDKDELTAEELAKAVREVL 373
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1860102248 368 SNTAFQEAADRVAQ--ENHHQPTAAAVVDVL 396
Cdd:cd03784   374 EDESYRRAAELLAElrEEDGAPSAADVVERL 404
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
2-382 3.29e-60

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


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 196.23  E-value: 3.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   2 RVLFTAWGWPTHFQPGVPLAWAFQAAGHDVLVASQPSLAAAATEAGLTmapvggevdvdtlrtnpilrevrdtlrdpmvc 81
Cdd:COG1819     1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFADLVEAAGLE-------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  82 ymregelpqgerdkwlamhthfglvaeamvddlvalAAAWRPDLIVWEQTTLAGAVTARVHKIPDVRLvispdvlgdrpe 161
Cdd:COG1819    49 ------------------------------------FVDWRPDLVVSDPLALAAALAAEALGIPVVSL------------ 80
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 162 aierqtrshdvsrlferfgvldghnqarwtldqCPPSLRLPSATHRMPMRYTPY---AGGALVPDWVHTQPERPRVCLSA 238
Cdd:COG1819    81 ---------------------------------TPPELEYPRPPDPANVRFVGPllpDGPAELPPWLEEDAGRPLVYVTL 127
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 239 GLTTAGFAAQetvsLPELLEYVRELDVEVIMPGAAREFPQLAEQtPPNVRVLDYVPLSLILPSCAAIVHHGGGGTMLTAA 318
Cdd:COG1819   128 GTSANDRADL----LRAVLEALADLGVRVVVTTGGLDPAELGPL-PDNVRVVDYVPQDALLPRADAVVHHGGAGTTAEAL 202
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860102248 319 SHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLLSNTAFQEAADRVAQE 382
Cdd:COG1819   203 RAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRRLTAEALRAALRRLLADPSYRERAARLAAE 266
DUF1205 pfam06722
Protein of unknown function (DUF1205); This family represents a conserved region of unknown ...
192-288 2.95e-22

Protein of unknown function (DUF1205); This family represents a conserved region of unknown function within bacterial glycosyl transferases. Many family members contain pfam03033.


Pssm-ID: 369050  Cd Length: 95  Bit Score: 90.26  E-value: 2.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 192 LDQCPPSLRLPSATHRMPMRYTPYAGGALVPDWVHTQPERPRVCLSAGLTTAGFAAQEtVSLPELLEYVRELDVEVIMPG 271
Cdd:pfam06722   1 IDVAPPSLRPDDGKGTVPMRYVPYNGPSVVPEWLYTGSARRRICVTLGTSVPNGYNQA-DLIQAVLDQVATLDAEIVVAV 79
                          90
                  ....*....|....*..
gi 1860102248 272 AAREFPQLAEqTPPNVR 288
Cdd:pfam06722  80 DEDARSELRE-LPDNVR 95
MGT TIGR01426
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ...
5-399 9.88e-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: 95.91  E-value: 9.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248   5 FTAWGwptHFQPGVPLAWAFQAAGHDVLVASQPSLAAAATEAGLTMAPVGGEVDVDTLRtNPILREvrdTLRDPMVCYMR 84
Cdd:TIGR01426   3 IPAHG---HVNPTLGVVEELVARGHRVTYATTEEFAERVEAAGAEFVLYGSALPPPDNP-PENTEE---EPIDIIEKLLD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248  85 EGE--LPQgerdkwlamhthfglVAEAMVDDlvalaaawRPDLIVWEQTTLAGAVTARVHKIPDVRL------------- 149
Cdd:TIGR01426  76 EAEdvLPQ---------------LEEAYKGD--------RPDLIVYDIASWTGRLLARKWDVPVISSfptfaaneefeem 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 150 --VISPDVLGDRPEAIERQTR-SHDVSRLFERFGVLD------GHNQARWTLDQCPPSLRlpSATHRMPMRYT----PYA 216
Cdd:TIGR01426 133 vsPAGEGSAEEGAIAERGLAEyVARLSALLEEHGITTppveflAAPRRDLNLVYTPKAFQ--PAGETFDDSFTfvgpCIG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 217 GGALVPDWVHTQPERPRVCLSAGltTAgFAAQETVsLPELLEYVRELDVEVIMPGAAREFPQLAEQTPPNVRVLDYVPLS 296
Cdd:TIGR01426 211 DRKEDGSWERPGDGRPVVLISLG--TV-FNNQPSF-YRTCVEAFRDLDWHVVLSVGRGVDPADLGELPPNVEVRQWVPQL 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 297 LILPSCAAIVHHGGGGTMLTAASHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRETLDQLLSNTAFQEAA 376
Cdd:TIGR01426 287 EILKKADAFITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVLSDPRYAERL 366
                         410       420
                  ....*....|....*....|...
gi 1860102248 377 DRVAQENHHQPTAAAVVDVLGRL 399
Cdd:TIGR01426 367 RKMRAEIREAGGARRAADEIEGF 389
UDPGT pfam00201
UDP-glucoronosyl and UDP-glucosyl transferase;
285-388 1.32e-07

UDP-glucoronosyl and UDP-glucosyl transferase;


Pssm-ID: 278624 [Multi-domain]  Cd Length: 499  Bit Score: 53.57  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 285 PNVRVLDYVPLSLIL--PSCAAIVHHGGGGTMLTAASHGVPQVVLPQILDQGINAHQITRTGAGLTVSRDQASARSVRET 362
Cdd:pfam00201 322 NNTRLVKWLPQNDLLghPKTRAFITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLTMTSEDLLNA 401
                          90       100
                  ....*....|....*....|....*.
gi 1860102248 363 LDQLLSNTAFQEAADRVAQENHHQPT 388
Cdd:pfam00201 402 LKEVINDPSYKENIMRLSSIHHDQPV 427
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
228-400 7.98e-07

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: 50.78  E-value: 7.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 228 QPERPRVCLSAGLTTAGFAaQETVSlpELLEyvRELDVEVIMP----GAAREFPQLAEQTPPNVRVLDYV-PLSLILPSC 302
Cdd:cd17507   194 SPDKPTVLLMGGGGGMGPV-KETVE--ALLD--SLRAGQVLVVcgknKKLYEKLSGLEEDYINVRVLGYVdDMNELMAAS 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 303 AAIVHHGGGGTMLTAASHGVPQVVLPQILDQGI-NAHQITRTGAGLTVSRDQAsarsVRETLDQLLSNTAFQEAADRVAQ 381
Cdd:cd17507   269 DLVITKPGGLTISEALARGLPVIIYDPIPGQEEeNADFLENNGAGIIARDPEE----LLEIVARLIDPPSLLRMMSEAAK 344
                         170
                  ....*....|....*....
gi 1860102248 382 ENHHQPTAAAVVDVLGRLG 400
Cdd:cd17507   345 ELKPPAAAKVIADILSLLI 363
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
253-383 1.62e-05

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: 46.44  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 253 LPELLEYVRELDVEVIM---PGAAREFPQLAEQTPPNVRVLDYV-PLSLILPSCAAIVHHGGGGTMLTAASHGVPQVVLP 328
Cdd:cd03785   200 VPKALPKLLERGIQVIHqtgKGDYDEVKKLYEDLGINVKVFPFIdDMAAAYAAADLVISRAGASTIAELTAAGKPAILIP 279
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860102248 329 QIL----DQGINAHQITRTGAGLTVSRDQASARSVRETLDQLLSNT----AFQEAADRVAQEN 383
Cdd:cd03785   280 YPYaaddHQEANARALEKAGAAIVIDQEELTPEVLAEAILDLLNDPerlkKMAEAAKKLAKPD 342
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
270-378 4.55e-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: 37.69  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860102248 270 PGAAREFPQLAEQTPPNVRVLDYVP-LSLILPSCAAIVHHGGGGTMLTAASHGVPQVVLP----QILDQGINAHQITRTG 344
Cdd:pfam04101  39 KGDLEEVKIDYAELGINYEVFPFIDnMAEYIKAADLVISRAGAGTIAELLALGKPAILVPnpsaARGHQDNNAKELVKAG 118
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1860102248 345 AGLTVSRDQASARSVRETLDQLLSNTAFQEAADR 378
Cdd:pfam04101 119 AALVILQKELTPEKLIEALLKLLLNPLRLAEMAK 152
 
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.
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