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Conserved domains on  [gi|499282074|ref|WP_010975134|]
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glycosyltransferase [Sinorhizobium meliloti]

Protein Classification

DUF3880 and Glyco_trans_1_2 domain-containing protein; glycosyltransferase; glycosyltransferase; glycosyltransferase family 1 protein; glycosyltransferase; glycosyltransferase family 1 protein; glycosyltransferase; glycosyltransferase family 1 protein; glycosyltransferase; glycosyltransferase family 1 protein; glycosyltransferase; glycosyltransferase family 4 protein; glycosyltransferase; glycosyltransferase family 4 protein; glycosyltransferase; glycosyltransferase family 4 protein; glycosyltransferase; glycosyltransferase family 1 protein; glycosyltransferase; glycosyltransferase family 4 protein; glycosyltransferase; glycosyltransferase; glycosyltransferase family 1 protein; glycosyltransferase; glycosyltransferase; glycosyltransferase family 4 protein( domain architecture ID 11468646)

DUF3880 and Glyco_trans_1_2 domain-containing protein; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Aquifex aeolicus uncharacterized protein aq_271; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Actinobacillus pleuropneumoniae alpha-1,6-glucosyltransferase and Xanthomonas campestris UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferase; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Actinobacillus pleuropneumoniae alpha-1,6-glucosyltransferase and Xanthomonas campestris UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferase; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Aquifex aeolicus uncharacterized protein aq_271; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; such as mycobacterial phosphatidyl-myo-inositol mannosyltransferase (PimA) that catalyzes the addition of a mannosyl residue from GDP-D-mannose to the position 2 of the carrier lipid phosphatidyl-myo-inositol; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Aquifex aeolicus uncharacterized protein aq_271; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Actinobacillus pleuropneumoniae alpha-1,6-glucosyltransferase; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Aquifex aeolicus uncharacterized protein aq_271; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Actinobacillus pleuropneumoniae alpha-1,6-glucosyltransferase; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Aquifex aeolicus uncharacterized protein aq_271; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; such as mycobacterial phosphatidyl-myo-inositol mannosyltransferase (PimA) that catalyzes the addition of a mannosyl residue from GDP-D-mannose to the position 2 of the carrier lipid phosphatidyl-myo-inositol; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Staphylococcus aureus Protein CapJ which is involved in the biosynthesis of type 1 capsular polysaccharide; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Aquifex aeolicus uncharacterized protein aq_271; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; such as mycobacterial phosphatidyl-myo-inositol mannosyltransferase (PimA) that catalyzes the addition of a mannosyl residue from GDP-D-mannose to the position 2 of the carrier lipid phosphatidyl-myo-inositol; glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; with similarity to Bacillus subtilis protein CgeB that may be involved in spore maturation; glycosyltransferase family 1 (GT1) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Aquifex aeolicus uncharacterized protein aq_271

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
15-361 3.49e-80

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 247.92  E-value: 3.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  15 NHGNAHFLRGIMRELIRRGHEAVALEPGDSWSRRnlivdqgngaiaafrkafpdlrvgIYGTDFEHEAaacEADMVIVHE 94
Cdd:COG4641    5 WNGHATYYRGLLRALAALGHEVTFLEPDDPWHDP------------------------LYAAELLDAF---RPDLVLVIS 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  95 WtdPALVAelgriRLKGGRFTLAFHDTHHravSAERDIARLDLSGYDFVLAFGEALRERYLQAGWgRHVHTWHEAADTSL 174
Cdd:COG4641   58 G--VELVA-----ALRARGIPTVFWDTDD---PVTLDRFRELLPLYDLVFTFDGDCVEEYRALGA-RRVFYLPFAADPEL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 175 FHPM-PEVEKRGELIWIGNWgDDERSSEIMSFLVEPAKklkLRTTVRGVRYPKAALRAlrsaKIDYGGWLANAAVPRAFA 253
Cdd:COG4641  127 HRPVpPEARFRYDVAFVGNY-YPDRRARLEELLLAPAG---LRLKIYGPGWPKLALPA----NVRRGGHLPGEEHPAAYA 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 254 EHRVTVHIPRrpyVEALPGIPTIRVFEALACGIPLISAPWTDAEGLFRPGKDFCLAKDGKEMTRLLRQLLAEPDFAAEMT 333
Cdd:COG4641  199 SSKITLNVNR---MAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIA 275
                        330       340
                 ....*....|....*....|....*...
gi 499282074 334 ACGLETVRARHTCSHRVDELLAIVASYR 361
Cdd:COG4641  276 EAGRRRVLAEHTYAHRARELLAILEELG 303
 
Name Accession Description Interval E-value
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
15-361 3.49e-80

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 247.92  E-value: 3.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  15 NHGNAHFLRGIMRELIRRGHEAVALEPGDSWSRRnlivdqgngaiaafrkafpdlrvgIYGTDFEHEAaacEADMVIVHE 94
Cdd:COG4641    5 WNGHATYYRGLLRALAALGHEVTFLEPDDPWHDP------------------------LYAAELLDAF---RPDLVLVIS 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  95 WtdPALVAelgriRLKGGRFTLAFHDTHHravSAERDIARLDLSGYDFVLAFGEALRERYLQAGWgRHVHTWHEAADTSL 174
Cdd:COG4641   58 G--VELVA-----ALRARGIPTVFWDTDD---PVTLDRFRELLPLYDLVFTFDGDCVEEYRALGA-RRVFYLPFAADPEL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 175 FHPM-PEVEKRGELIWIGNWgDDERSSEIMSFLVEPAKklkLRTTVRGVRYPKAALRAlrsaKIDYGGWLANAAVPRAFA 253
Cdd:COG4641  127 HRPVpPEARFRYDVAFVGNY-YPDRRARLEELLLAPAG---LRLKIYGPGWPKLALPA----NVRRGGHLPGEEHPAAYA 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 254 EHRVTVHIPRrpyVEALPGIPTIRVFEALACGIPLISAPWTDAEGLFRPGKDFCLAKDGKEMTRLLRQLLAEPDFAAEMT 333
Cdd:COG4641  199 SSKITLNVNR---MAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIA 275
                        330       340
                 ....*....|....*....|....*...
gi 499282074 334 ACGLETVRARHTCSHRVDELLAIVASYR 361
Cdd:COG4641  276 EAGRRRVLAEHTYAHRARELLAILEELG 303
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
257-355 9.30e-25

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 96.52  E-value: 9.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  257 VTVHIPRRPyvealpGIPTIRVFEALACGIPLISAPWTDAEGLFRPGKDFCLAKDGKEMTRLLRQLLAEPDFAAEMTACG 336
Cdd:pfam13524   1 IVLNPSRRP------DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAG 74
                          90
                  ....*....|....*....
gi 499282074  337 LETVRARHTCSHRVDELLA 355
Cdd:pfam13524  75 RERVLAEHTYAHRAEQLLD 93
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-356 6.95e-20

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 89.90  E-value: 6.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074   2 RFLFYTHSLVSDWNhGNAHFLRGIMRELIRRGHEAVALEPGDSWSRRNLIVDQGNGAIAAFRKAFPDLRVGIygTDFEHE 81
Cdd:cd03801    1 KILLLSPELPPPVG-GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLL--RELRPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  82 AAACEADMVIVHEWtdPALVAELGRIRLKGGRFTLAFHDTHHRAVSAERDIAR-------LDLSGYDFVLAFGEALRERY 154
Cdd:cd03801   78 LRLRKFDVVHAHGL--LAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrllaraeALLRRADAVIAVSEALRDEL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 155 LQAGW--GRHVHTWHEAADTSLFHPMPEVEKRGE-----LIWIGNWGDD---ERSSEIMSFLVEPAKKLKLRttVRGVRY 224
Cdd:cd03801  156 RALGGipPEKIVVIPNGVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRkgvDLLLEALAKLLRRGPDVRLV--IVGGDG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 225 P-KAALRALR---SAKIDYGGWLANAAVPRAFAEHRVTVHiPRRPyvEALPgiptIRVFEALACGIPLISAPWTDAEGLF 300
Cdd:cd03801  234 PlRAELEELElglGDRVRFLGFVPDEELPALYAAADVFVL-PSRY--EGFG----LVVLEAMAAGLPVVATDVGGLPEVV 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499282074 301 RPGKDFCLAKDG--KEMTRLLRQLLAEPDFAAEMTACGLETVRARHTCSHRVDELLAI 356
Cdd:cd03801  307 EDGEGGLVVPPDdvEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
 
Name Accession Description Interval E-value
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
15-361 3.49e-80

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 247.92  E-value: 3.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  15 NHGNAHFLRGIMRELIRRGHEAVALEPGDSWSRRnlivdqgngaiaafrkafpdlrvgIYGTDFEHEAaacEADMVIVHE 94
Cdd:COG4641    5 WNGHATYYRGLLRALAALGHEVTFLEPDDPWHDP------------------------LYAAELLDAF---RPDLVLVIS 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  95 WtdPALVAelgriRLKGGRFTLAFHDTHHravSAERDIARLDLSGYDFVLAFGEALRERYLQAGWgRHVHTWHEAADTSL 174
Cdd:COG4641   58 G--VELVA-----ALRARGIPTVFWDTDD---PVTLDRFRELLPLYDLVFTFDGDCVEEYRALGA-RRVFYLPFAADPEL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 175 FHPM-PEVEKRGELIWIGNWgDDERSSEIMSFLVEPAKklkLRTTVRGVRYPKAALRAlrsaKIDYGGWLANAAVPRAFA 253
Cdd:COG4641  127 HRPVpPEARFRYDVAFVGNY-YPDRRARLEELLLAPAG---LRLKIYGPGWPKLALPA----NVRRGGHLPGEEHPAAYA 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 254 EHRVTVHIPRrpyVEALPGIPTIRVFEALACGIPLISAPWTDAEGLFRPGKDFCLAKDGKEMTRLLRQLLAEPDFAAEMT 333
Cdd:COG4641  199 SSKITLNVNR---MAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIA 275
                        330       340
                 ....*....|....*....|....*...
gi 499282074 334 ACGLETVRARHTCSHRVDELLAIVASYR 361
Cdd:COG4641  276 EAGRRRVLAEHTYAHRARELLAILEELG 303
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
257-355 9.30e-25

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 96.52  E-value: 9.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  257 VTVHIPRRPyvealpGIPTIRVFEALACGIPLISAPWTDAEGLFRPGKDFCLAKDGKEMTRLLRQLLAEPDFAAEMTACG 336
Cdd:pfam13524   1 IVLNPSRRP------DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAG 74
                          90
                  ....*....|....*....
gi 499282074  337 LETVRARHTCSHRVDELLA 355
Cdd:pfam13524  75 RERVLAEHTYAHRAEQLLD 93
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-356 6.95e-20

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 89.90  E-value: 6.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074   2 RFLFYTHSLVSDWNhGNAHFLRGIMRELIRRGHEAVALEPGDSWSRRNLIVDQGNGAIAAFRKAFPDLRVGIygTDFEHE 81
Cdd:cd03801    1 KILLLSPELPPPVG-GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLL--RELRPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  82 AAACEADMVIVHEWtdPALVAELGRIRLKGGRFTLAFHDTHHRAVSAERDIAR-------LDLSGYDFVLAFGEALRERY 154
Cdd:cd03801   78 LRLRKFDVVHAHGL--LAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrllaraeALLRRADAVIAVSEALRDEL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 155 LQAGW--GRHVHTWHEAADTSLFHPMPEVEKRGE-----LIWIGNWGDD---ERSSEIMSFLVEPAKKLKLRttVRGVRY 224
Cdd:cd03801  156 RALGGipPEKIVVIPNGVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRkgvDLLLEALAKLLRRGPDVRLV--IVGGDG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 225 P-KAALRALR---SAKIDYGGWLANAAVPRAFAEHRVTVHiPRRPyvEALPgiptIRVFEALACGIPLISAPWTDAEGLF 300
Cdd:cd03801  234 PlRAELEELElglGDRVRFLGFVPDEELPALYAAADVFVL-PSRY--EGFG----LVVLEAMAAGLPVVATDVGGLPEVV 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499282074 301 RPGKDFCLAKDG--KEMTRLLRQLLAEPDFAAEMTACGLETVRARHTCSHRVDELLAI 356
Cdd:cd03801  307 EDGEGGLVVPPDdvEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
25-332 3.09e-08

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 55.04  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  25 IMRELIRRGHEAVAL---EPGDSWSRRNLIVDQGNGAIAAFRKAFPDLRVGIYGTDFEHEAAACEA-----------DMV 90
Cdd:cd03794   23 LAKELVRRGHEVTVLtpsPNYPLGRIFAGATETKDGIRVIRVKLGPIKKNGLIRRLLNYLSFALAAllkllvreerpDVI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  91 IVHewTDPALVAELGRI--RLKGGRFTLAFHDTHHRAV---------SAERDIARLDLSGY---DFVLAFGEALRERYLQ 156
Cdd:cd03794  103 IAY--SPPITLGLAALLlkKLRGAPFILDVRDLWPESLialgvlkkgSLLKLLKKLERKLYrlaDAIIVLSPGLKEYLLR 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 157 AG-WGRHVHTWHEAADTSLFHPMPEVEKRGE--------LIWIGNWGDDERsseiMSFLVEPAKKLKLRTTVR----GVR 223
Cdd:cd03794  181 KGvPKEKIIVIPNWADLEEFKPPPKDELRKKlglddkfvVVYAGNIGKAQG----LETLLEAAERLKRRPDIRflfvGDG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 224 YPKAALRALRSAK----IDYGGWLANAAVPRAFAEHRVTVhIPRRPYVEALPGIPTiRVFEALACGIPLISA--PWTD-A 296
Cdd:cd03794  257 DEKERLKELAKARgldnVTFLGRVPKEEVPELLSAADVGL-VPLKDNPANRGSSPS-KLFEYMAAGKPILASddGGSDlA 334
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 499282074 297 EGLFRPGKdFCLAKDGKEMTRLLRQLLAEPDFAAEM 332
Cdd:cd03794  335 VEINGCGL-VVEPGDPEALADAILELLDDPELRRAM 369
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
278-359 2.25e-07

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 49.22  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 278 VFEALACGIPLISAPWTDAEGLFRPGKD--FCLAKDGKEMTRLLRQLLAEPDFAAEMTACGLETVRARHTCSHRVDELLA 355
Cdd:COG0438   37 LLEAMAAGLPVIATDVGGLPEVIEDGETglLVPPGDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLA 116

                 ....
gi 499282074 356 IVAS 359
Cdd:COG0438  117 LYEE 120
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
12-356 3.46e-05

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 45.45  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  12 SDWNHGNAHFLRGIMRELIRRGHEA--VALEPGDSWSRRNLIVDQGNGAIAAFRKAFPDLRVGIYGTD-FEHEAAACE-- 86
Cdd:cd03798   10 NANSPGRGIFVRRQVRALSRRGVDVevLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLApLRAPSLAKLlk 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074  87 ------ADMVIVHeWTDPALVAELGRIRLKGGRFTLAFHDTH---HRAVSAERDIARLDLSGYDFVLAFGEALRERYL-Q 156
Cdd:cd03798   90 rrrrgpPDLIHAH-FAYPAGFAAALLARLYGVPYVVTEHGSDinvFPPRSLLRKLLRWALRRAARVIAVSKALAEELVaL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 157 AGWGRHVHTWHEAADTSLFHPMPEVEKRGE----LIWIGNWGDDERS---SEIMSFLVEPAKKLKLRTTVRGVRypKAAL 229
Cdd:cd03798  169 GVPRDRVDVIPNGVDPARFQPEDRGLGLPLdafvILFVGRLIPRKGIdllLEAFARLAKARPDVVLLIVGDGPL--REAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 230 RALRS-----AKIDYGGWLANAAVPRAFAEHRVTVhIPRRpyVEALPGIptirVFEALACGIPLISAPWTDAEGLFRPGK 304
Cdd:cd03798  247 RALAEdlglgDRVTFTGRLPHEQVPAYYRACDVFV-LPSR--HEGFGLV----LLEAMACGLPVVATDVGGIPEVVGDPE 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499282074 305 DFCLAKDG--KEMTRLLRQLLAEPDFAAEMTAcGLETVRARHTCSHRVDELLAI 356
Cdd:cd03798  320 TGLLVPPGdaDALAAALRRALAEPYLRELGEA-ARARVAERFSWVKAADRIAAA 372
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
205-354 7.63e-04

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 41.04  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 205 FLVEPAKKLKLRttvrgvrYPKAALRAL-----------------RSAKIDYGGWLANaaVPRAFAEHRVTVHIPRRpyv 267
Cdd:cd03808  206 ELIEAAKILKKK-------GPNVRFLLVgdgelenpseilieklgLEGRIEFLGFRSD--VPELLAESDVFVLPSYR--- 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 268 EALPgiptiRVF-EALACGIPLISapwTDAEG---LFRPGKDFCLA--KDGKEMTRLLRQLLAEPDFAAEMTACGLETVR 341
Cdd:cd03808  274 EGLP-----RSLlEAMAAGRPVIT---TDVPGcreLVIDGVNGFLVppGDVEALADAIEKLIEDPELRKEMGEAARKRVE 345
                        170
                 ....*....|...
gi 499282074 342 ARHTCSHRVDELL 354
Cdd:cd03808  346 EKFDEEKVVNKLL 358
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
140-332 5.17e-03

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 38.43  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 140 YDFVLAFGEALRERYLQAGwGRHVHTWHEAADTSLFHPmpevEKRGELIWIGnWGDDER---------SSEI-MSFLVEP 209
Cdd:cd03814  146 FDTTLVPSPSIARELEGHG-FERVRLWPRGVDTELFHP----SRRDAALRRR-LGPPGRplllyvgrlAPEKnLEALLDA 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 210 AKKLKLRTTVR----GVRYPKAALRAlRSAKIDYGGWLANAAVPRAFAEHRVTVHiprrpyvealpgiPTIR------VF 279
Cdd:cd03814  220 DLPLAASPPVRlvvvGDGPARAELEA-RGPDVIFTGFLTGEELARAYASADVFVF-------------PSRTetfglvVL 285
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499282074 280 EALACGIPLISAPWTDAEGLFRPGKDFCLAKDG--KEMTRLLRQLLAEPDFAAEM 332
Cdd:cd03814  286 EAMASGLPVVAADAGGPRDIVRPGGTGALVEPGdaAAFAAALRALLEDPELRRRM 340
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
144-344 8.14e-03

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 37.82  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 144 LAFGEALRERYLQAGW-GRHVHTWHEAADTSLFHPMPEVEKRGELIWIGNWGDDERsseiMSFLVEPAKKLKLR-TTVRG 221
Cdd:cd05844  148 VAVSGFIRDRLLARGLpAERIHVHYIGIDPAKFAPRDPAERAPTILFVGRLVEKKG----CDVLIEAFRRLAARhPTARL 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282074 222 VRYPKAALR------ALRSAKIDYGGWLANAAVPRAFAEHRVTV---HIPRRPYVEALPgiptIRVFEALACGIPLISAP 292
Cdd:cd05844  224 VIAGDGPLRpalqalAAALGRVRFLGALPHAEVQDWMRRAEIFClpsVTAASGDSEGLG----IVLLEAAACGVPVVSSR 299
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499282074 293 WTDAEGLFRPGKDFCLAKDGKEM--TRLLRQLLAEPDFAAEMTACGLETVRARH 344
Cdd:cd05844  300 HGGIPEAILDGETGFLVPEGDVDalADALQALLADRALADRMGGAARAFVCEQF 353
 
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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