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Conserved domains on  [gi|1849801055|gb|KAF5030510|]
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Glycosyl transferases group 1 [anaerobic digester metagenome]

Protein Classification

glycosyltransferase( domain architecture ID 13409205)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
102-194 1.79e-22

Glycosyl transferases group 1;


:

Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 91.51  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055 102 IIPNESI-GFEVNFRLTEGASCGACVLTPDVgPDQDALFDDGHEIVVYADGLDMLEKLRFLLRRPDVAERIGRAAWKRVQ 180
Cdd:pfam13524   1 IVLNPSRrPDSPNMRVFEAAACGAPLLTDRT-PGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVL 79

                          90
                  ....*....|....
gi 1849801055 181 AQHLPDHRAATVLN 194
Cdd:pfam13524  80 AEHTYAHRAEQLLD 93
COG4641 super family cl34798
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
1-198 8.02e-22

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


The actual alignment was detected with superfamily member COG4641:

Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 95.77  E-value: 8.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055   1 MHWHRHYARLFDVLFT---PHLSLFLALPpqWRHPQAVHLAMS-GHARPWQPHAGRGHDVSMVGVLDKHRplRGWLAELL 76
Cdd:COG4641    83 LDRFRELLPLYDLVFTfdgDCVEEYRALG--ARRVFYLPFAADpELHRPVPPEARFRYDVAFVGNYYPDR--RARLEELL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055  77 Q------------------DRFGVQARQGVPFAEMLALYGDTRIIPN----ESIGFEVNFRLTEGASCGACVLTpDVGPD 134
Cdd:COG4641   159 LapaglrlkiygpgwpklaLPANVRRGGHLPGEEHPAAYASSKITLNvnrmAASPDSPTRRTFEAAACGAFLLS-DPWEG 237

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849801055 135 QDALFDDGHEIVVYADGLDMLEKLRFLLRRPDVAERIGRAAWKRVQAQHLPDHRAATVLNAVDK 198
Cdd:COG4641   238 LEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVLAEHTYAHRARELLAILEE 301
 
Name Accession Description Interval E-value
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
102-194 1.79e-22

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 91.51  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055 102 IIPNESI-GFEVNFRLTEGASCGACVLTPDVgPDQDALFDDGHEIVVYADGLDMLEKLRFLLRRPDVAERIGRAAWKRVQ 180
Cdd:pfam13524   1 IVLNPSRrPDSPNMRVFEAAACGAPLLTDRT-PGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVL 79

                          90
                  ....*....|....
gi 1849801055 181 AQHLPDHRAATVLN 194
Cdd:pfam13524  80 AEHTYAHRAEQLLD 93
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
1-198 8.02e-22

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 95.77  E-value: 8.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055   1 MHWHRHYARLFDVLFT---PHLSLFLALPpqWRHPQAVHLAMS-GHARPWQPHAGRGHDVSMVGVLDKHRplRGWLAELL 76
Cdd:COG4641    83 LDRFRELLPLYDLVFTfdgDCVEEYRALG--ARRVFYLPFAADpELHRPVPPEARFRYDVAFVGNYYPDR--RARLEELL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055  77 Q------------------DRFGVQARQGVPFAEMLALYGDTRIIPN----ESIGFEVNFRLTEGASCGACVLTpDVGPD 134
Cdd:COG4641   159 LapaglrlkiygpgwpklaLPANVRRGGHLPGEEHPAAYASSKITLNvnrmAASPDSPTRRTFEAAACGAFLLS-DPWEG 237

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849801055 135 QDALFDDGHEIVVYADGLDMLEKLRFLLRRPDVAERIGRAAWKRVQAQHLPDHRAATVLNAVDK 198
Cdd:COG4641   238 LEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVLAEHTYAHRARELLAILEE 301
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 71-194 4.45e-06

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: 48.69  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055  71 WLAELLQDRFGVQAR----QGVPFAEMLALYGDTRII----PNESIGFevnfRLTEGASCGACVLTPDVGPDQDALFDDG 142
Cdd:cd03801   235 LRAELEELELGLGDRvrflGFVPDEELPALYAAADVFvlpsRYEGFGL----VVLEAMAAGLPVVATDVGGLPEVVEDGE 310

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1849801055 143 HEIVVYADGLDML-EKLRFLLRRPDVAERIGRAAWKRVQAQHLPDHRAATVLN 194
Cdd:cd03801   311 GGLVVPPDDVEALaDALLRLLADPELRARLGRAARERVAERFSWERVAERLLD 363
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 116-198 9.55e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 44.98  E-value: 9.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055 116 LTEGASCGACVLTPDVGPDQDALFDDGHEIVVYA-DGLDMLEKLRFLLRRPDVAERIGRAAWKRVQAQHLPDHRAATVLN 194
Cdd:COG0438    37 LLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLA 116


                  ....
gi 1849801055 195 AVDK 198
Cdd:COG0438   117 LYEE 120
 
Name Accession Description Interval E-value
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
102-194 1.79e-22

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 91.51  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055 102 IIPNESI-GFEVNFRLTEGASCGACVLTPDVgPDQDALFDDGHEIVVYADGLDMLEKLRFLLRRPDVAERIGRAAWKRVQ 180
Cdd:pfam13524   1 IVLNPSRrPDSPNMRVFEAAACGAPLLTDRT-PGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVL 79

                          90
                  ....*....|....
gi 1849801055 181 AQHLPDHRAATVLN 194
Cdd:pfam13524  80 AEHTYAHRAEQLLD 93
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
1-198 8.02e-22

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 95.77  E-value: 8.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055   1 MHWHRHYARLFDVLFT---PHLSLFLALPpqWRHPQAVHLAMS-GHARPWQPHAGRGHDVSMVGVLDKHRplRGWLAELL 76
Cdd:COG4641    83 LDRFRELLPLYDLVFTfdgDCVEEYRALG--ARRVFYLPFAADpELHRPVPPEARFRYDVAFVGNYYPDR--RARLEELL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055  77 Q------------------DRFGVQARQGVPFAEMLALYGDTRIIPN----ESIGFEVNFRLTEGASCGACVLTpDVGPD 134
Cdd:COG4641   159 LapaglrlkiygpgwpklaLPANVRRGGHLPGEEHPAAYASSKITLNvnrmAASPDSPTRRTFEAAACGAFLLS-DPWEG 237

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849801055 135 QDALFDDGHEIVVYADGLDMLEKLRFLLRRPDVAERIGRAAWKRVQAQHLPDHRAATVLNAVDK 198
Cdd:COG4641   238 LEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVLAEHTYAHRARELLAILEE 301
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 71-194 4.45e-06

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: 48.69  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055  71 WLAELLQDRFGVQAR----QGVPFAEMLALYGDTRII----PNESIGFevnfRLTEGASCGACVLTPDVGPDQDALFDDG 142
Cdd:cd03801   235 LRAELEELELGLGDRvrflGFVPDEELPALYAAADVFvlpsRYEGFGL----VVLEAMAAGLPVVATDVGGLPEVVEDGE 310

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1849801055 143 HEIVVYADGLDML-EKLRFLLRRPDVAERIGRAAWKRVQAQHLPDHRAATVLN 194
Cdd:cd03801   311 GGLVVPPDDVEALaDALLRLLADPELRARLGRAARERVAERFSWERVAERLLD 363
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 116-198 9.55e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 44.98  E-value: 9.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849801055 116 LTEGASCGACVLTPDVGPDQDALFDDGHEIVVYA-DGLDMLEKLRFLLRRPDVAERIGRAAWKRVQAQHLPDHRAATVLN 194
Cdd:COG0438    37 LLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLA 116


                  ....
gi 1849801055 195 AVDK 198
Cdd:COG0438   117 LYEE 120
 
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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