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Conserved domains on  [gi|223691483|gb|ACN14766|]
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putative glycosyltransferase [Desulforapulum autotrophicum HRM2]

Protein Classification

DUF3524 and GT4_PimA-like domain-containing protein( domain architecture ID 13777992)

DUF3524 and GT4_PimA-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 2.69e-82

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


:

Pssm-ID: 432280  Cd Length: 165  Bit Score: 247.86  E-value: 2.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483    2 RFLFLESFFGGSHKAFALGLKAHSNHEIDIVTLPDHYWRWRMRGAALLFHERIDNLSAY-DGVIATDMINLSDFMAMA-- 78
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSPHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRpd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483   79 GPNTPpVLAYFHENQLGYPDNPGVPPEVQYGFMNMTTALCADRVFFNSRFQMEQFLAGVEGLLTTMPDLNPSWVGRTIRA 158
Cdd:pfam12038  81 LANCP-KLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRA 159


                  ....*.
gi 223691483  159 RSGVLY 164
Cdd:pfam12038 160 KSRVLY 165
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 20-357 1.59e-18

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: 85.67  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  20 GLKAHSNHEIDIVTLPDHYWRWRMRGAALLFHERIDNLSAYDGVIATDMINLSDFMAMAGPNTPPVLAYFHEnqlGYPDN 99
Cdd:cd03801   43 GEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHG---AEPGR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 100 PGVPPEVQYGFMN--MTTALCADRVFFNSRFQMEQFLAgvegllttmpdlnpswVGRTIRARSGVLYPGCS---FPVGSS 174
Cdd:cd03801  120 LLLLLAAERRLLAraEALLRRADAVIAVSEALRDELRA----------------LGGIPPEKIVVIPNGVDlerFSPPLR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 175 ESLPDKALAPLVIWNHRWEYDKKPERFFRALGEIKRRGIPFRLaLLGGGVSKIPKAFLAAREAFKQEIVVFGHVPSKSVY 254
Cdd:cd03801  184 RKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRL-VIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 255 fDWLSRGHIVVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMPREHHGTIL-YKDHGDLVDKLAGFLLSSDRHEPLG 333
Cdd:cd03801  263 -ALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVpPDDVEALADALLRLLADPELRARLG 341

                        330       340
                 ....*....|....*....|....*
gi 223691483 334 RN-LAQAMEEYAWNHVIKKYDEILN 357
Cdd:cd03801  342 RAaRERVAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 2.69e-82

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 247.86  E-value: 2.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483    2 RFLFLESFFGGSHKAFALGLKAHSNHEIDIVTLPDHYWRWRMRGAALLFHERIDNLSAY-DGVIATDMINLSDFMAMA-- 78
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSPHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRpd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483   79 GPNTPpVLAYFHENQLGYPDNPGVPPEVQYGFMNMTTALCADRVFFNSRFQMEQFLAGVEGLLTTMPDLNPSWVGRTIRA 158
Cdd:pfam12038  81 LANCP-KLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRA 159


                  ....*.
gi 223691483  159 RSGVLY 164
Cdd:pfam12038 160 KSRVLY 165
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 20-357 1.59e-18

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: 85.67  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  20 GLKAHSNHEIDIVTLPDHYWRWRMRGAALLFHERIDNLSAYDGVIATDMINLSDFMAMAGPNTPPVLAYFHEnqlGYPDN 99
Cdd:cd03801   43 GEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHG---AEPGR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 100 PGVPPEVQYGFMN--MTTALCADRVFFNSRFQMEQFLAgvegllttmpdlnpswVGRTIRARSGVLYPGCS---FPVGSS 174
Cdd:cd03801  120 LLLLLAAERRLLAraEALLRRADAVIAVSEALRDELRA----------------LGGIPPEKIVVIPNGVDlerFSPPLR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 175 ESLPDKALAPLVIWNHRWEYDKKPERFFRALGEIKRRGIPFRLaLLGGGVSKIPKAFLAAREAFKQEIVVFGHVPSKSVY 254
Cdd:cd03801  184 RKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRL-VIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 255 fDWLSRGHIVVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMPREHHGTIL-YKDHGDLVDKLAGFLLSSDRHEPLG 333
Cdd:cd03801  263 -ALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVpPDDVEALADALLRLLADPELRARLG 341

                        330       340
                 ....*....|....*....|....*
gi 223691483 334 RN-LAQAMEEYAWNHVIKKYDEILN 357
Cdd:cd03801  342 RAaRERVAERFSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 257-361 1.74e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 58.08  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 257 WLSRGHIVVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMPREHHGTILY-KDHGDLVDKLAGFLLSSDRHEPLGRN 335
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpGDPEALAEAILRLLEDPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*..
gi 223691483 336 -LAQAMEEYAWNHVIKKYDEILNHLAA 361
Cdd:COG0438   97 aRERAEERFSWEAIAERLLALYEELLA 123
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 184-335 7.18e-08

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 51.51  E-value: 7.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  184 PLVIWNHRWEYDKKPERFFRALGEIKRRGIPFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGHVPSKSVYfDWLSRGHI 263
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLP-ELLKIADV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223691483  264 VVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMpREHHGTILYK--DHGDLVDKLAGFLLSSDRHEPLGRN 335
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV-KDGETGFLVKpnNAEALAEAIDKLLEDEELRERLGEN 154
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 2.69e-82

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 247.86  E-value: 2.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483    2 RFLFLESFFGGSHKAFALGLKAHSNHEIDIVTLPDHYWRWRMRGAALLFHERIDNLSAY-DGVIATDMINLSDFMAMA-- 78
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSPHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRpd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483   79 GPNTPpVLAYFHENQLGYPDNPGVPPEVQYGFMNMTTALCADRVFFNSRFQMEQFLAGVEGLLTTMPDLNPSWVGRTIRA 158
Cdd:pfam12038  81 LANCP-KLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRA 159


                  ....*.
gi 223691483  159 RSGVLY 164
Cdd:pfam12038 160 KSRVLY 165
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 20-357 1.59e-18

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: 85.67  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  20 GLKAHSNHEIDIVTLPDHYWRWRMRGAALLFHERIDNLSAYDGVIATDMINLSDFMAMAGPNTPPVLAYFHEnqlGYPDN 99
Cdd:cd03801   43 GEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHG---AEPGR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 100 PGVPPEVQYGFMN--MTTALCADRVFFNSRFQMEQFLAgvegllttmpdlnpswVGRTIRARSGVLYPGCS---FPVGSS 174
Cdd:cd03801  120 LLLLLAAERRLLAraEALLRRADAVIAVSEALRDELRA----------------LGGIPPEKIVVIPNGVDlerFSPPLR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 175 ESLPDKALAPLVIWNHRWEYDKKPERFFRALGEIKRRGIPFRLaLLGGGVSKIPKAFLAAREAFKQEIVVFGHVPSKSVY 254
Cdd:cd03801  184 RKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRL-VIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 255 fDWLSRGHIVVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMPREHHGTIL-YKDHGDLVDKLAGFLLSSDRHEPLG 333
Cdd:cd03801  263 -ALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVpPDDVEALADALLRLLADPELRARLG 341

                        330       340
                 ....*....|....*....|....*
gi 223691483 334 RN-LAQAMEEYAWNHVIKKYDEILN 357
Cdd:cd03801  342 RAaRERVAERFSWERVAERLLDLYR 366
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 191-308 1.30e-11

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 63.96  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 191 RWEYDKKPERFFRALGEIKRRGIPFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGHVPSKSVYFDWLSRGHIVVSTAIQ 270
Cdd:cd01635  118 RLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRS 197

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 223691483 271 ENFGISVVEAVGMGCIPLLPDRLAYPEIMPREHHGTIL 308
Cdd:cd01635  198 EGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 257-361 1.74e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 58.08  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 257 WLSRGHIVVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMPREHHGTILY-KDHGDLVDKLAGFLLSSDRHEPLGRN 335
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpGDPEALAEAILRLLEDPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*..
gi 223691483 336 -LAQAMEEYAWNHVIKKYDEILNHLAA 361
Cdd:COG0438   97 aRERAEERFSWEAIAERLLALYEELLA 123
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 184-335 7.18e-08

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 51.51  E-value: 7.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  184 PLVIWNHRWEYDKKPERFFRALGEIKRRGIPFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGHVPSKSVYfDWLSRGHI 263
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLP-ELLKIADV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223691483  264 VVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMpREHHGTILYK--DHGDLVDKLAGFLLSSDRHEPLGRN 335
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV-KDGETGFLVKpnNAEALAEAIDKLLEDEELRERLGEN 154
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 194-354 2.77e-06

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: 48.75  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 194 YDKKPERFFRALGEIKRRGIPFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGHVpsKSVyFDWLSRGHIVVSTAIQENF 273
Cdd:cd03808  200 KDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFR--SDV-PELLAESDVFVLPSYREGL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 274 GISVVEAVGMGcIPLlpdrLAYPEIMPRE--HHGTILY----KDHGDLVDKLAGFLLSsdrheplgRNLAQAMEEYAWNH 347
Cdd:cd03808  277 PRSLLEAMAAG-RPV----ITTDVPGCRElvIDGVNGFlvppGDVEALADAIEKLIED--------PELRKEMGEAARKR 343


                 ....*..
gi 223691483 348 VIKKYDE 354
Cdd:cd03808  344 VEEKFDE 350
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
192-285 4.88e-06

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 45.58  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  192 WEYDKKPERFFRALGEIKRRGIPFRLALLGGGVskiPKAFLAAREAFKQEIVVFGHVPSKSvyfDWLSRGHIVVSTAIQE 271
Cdd:pfam13692  11 HPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGP---EEELEELAAGLEDRVIFTGFVEDLA---ELLAAADVFVLPSLYE 84

                          90
                  ....*....|....
gi 223691483  272 NFGISVVEAVGMGC 285
Cdd:pfam13692  85 GFGLKLLEAMAAGL 98
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 162-354 2.61e-05

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 45.82  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 162 VLYPGCS---FPVGSSESLPDKALAP---LVIWNHRWEYdKKPERFFRALGEIKRRGIPFRLALLGGGVSKIPKAFLAAR 235
Cdd:cd03809  166 VIPLGVDpsfFPPESAAVLIAKYLLPepyFLYVGTLEPR-KNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVK 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 236 EA-FKQEIVVFGHVPSKSVYfdWLSRG-HIVVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMPrehhGTILY---K 310
Cdd:cd03809  245 KLgLGGRVRFLGYVSDEDLP--ALYRGaRAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAG----DAALYfdpL 318

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 223691483 311 DHGDLVDKLAGFLLSSDRHEPLGRNLAQAMEEYAWNHVIKKYDE 354
Cdd:cd03809  319 DPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 10-352 3.22e-05

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 45.43  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  10 FGGSHKAF---ALGLkAHSNHEIDIVTLP---DHYWRWRMRGAALLFHERIDNLSA------------------YDGVIA 65
Cdd:cd03811   11 GGGAERVLlnlANAL-DKRGYDVTLVLLRdegDLDKQLNGDVKLIRLLIRVLKLIKlgllkailklkrilkrakPDVVIS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483  66 tdMINLSDFMAMAGPNTP-PVLAYFH--ENQLGYPDNPGVPPEVQYGFmnmttalcADRVFFNSRFQMEQFLAgvegllt 142
Cdd:cd03811   90 --FLGFATYIVAKLAAARsKVIAWIHssLSKLYYLKKKLLLKLKLYKK--------ADKIVCVSKGIKEDLIR------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 143 tmpdlnpswVGRTIRARSGVLYPGCSFPvgsseSLPDKALAPLVIWNH---------RWEYDKKPERFFRALGEIKRRGI 213
Cdd:cd03811  153 ---------LGPSPPEKIEVIYNPIDID-----RIRALAKEPILNEPEdgpvilavgRLDPQKGHDLLIEAFAKLRKKYP 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 214 PFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGHVPskSVYfDWLSRGHIVVSTAIQENFGISVVEAVGMGCIPLLPDRL 293
Cdd:cd03811  219 DVKLVILGDGPLREELEKLAKELGLAERVIFLGFQS--NPY-PYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCP 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 223691483 294 AYPEIMPREHHGTILYKDHGDLVDKLAGFLLssdrhEPLGRNLAQAMEEYAWNHVIKKY 352
Cdd:cd03811  296 GPREILDDGENGLLVPDGDAAALAGILAALL-----QKKLDAALRERLAKAQEAVFREY 349
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
 132-288 3.81e-05

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 45.29  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 132 QFLAGVEGLLTTMPDL---NPSWVGRTIRA------RSGVLYPGCSfpVGSSESLPDK---------ALA--------PL 185
Cdd:cd03806  177 RLFAFLYGLAGSFADVvmvNSTWTYNHIRQlwkrniKPSIVYPPCD--TEELTKLPIDektrenqilSIAqfrpeknhPL 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 186 VIwnhrweydKKPERFFRALGEIKRRgiPFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGHVP-SKSVYFD----WLSR 260
Cdd:cd03806  255 QL--------RAFAELLKRLPESIRS--NPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEfVVDAPYEelkeLLST 324

                        170       180
                 ....*....|....*....|....*...
gi 223691483 261 GHIVVSTAIQENFGISVVEAVGMGCIPL 288
Cdd:cd03806  325 ASIGLHTMWNEHFGIGVVEYMAAGLIPL 352
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 195-339 2.57e-04

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 42.73  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 195 DKKPERFFRALGEIKRRGiPFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGH---VPSksvyfdWLSRGHIVVSTAIQE 271
Cdd:cd03819  194 EKGWLLLVDAAAELKDEP-DFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFredVPA------ALAASDVVVLPSLHE 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223691483 272 NFGISVVEAVGMGCIPLLPDRLAYPEIMPREHHGTILYK-DHGDLVDKLAGFLLSSDRHEPLGRNLAQA 339
Cdd:cd03819  267 EFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEAREKLQAAAALT 335
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 115-352 1.88e-03

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 39.88  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 115 TALCADRVFFNSRFQMEQFLagvegllTTMPDLNpswvgrtiRARSGVLYPGCSFPVGSSESLPDKALAPLVIWN----- 189
Cdd:cd03805  151 TTGMADQIVVNSNFTAGVFK-------KTFPSLA--------KNPPEVLYPCVDTDSFDSTSEDPDPGDLIAKSNkkffl 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 190 --HRWEYDKKPERFFRALGEIKRRG---IPFRLALLGGGVSKIPK--------AFLAAREAFKQEIVVFGHVPSKSVYFD 256
Cdd:cd03805  216 siNRFERKKNIALAIEAFAKLKQKLpefENVRLVIAGGYDPRVAEnveyleelQRLAEELLNVEDQVLFLRSISDSQKEQ 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 257 WLSRGHIVVSTAIQENFGISVVEAVGMGCipllpdrlayPEIM-----PREhhgTILYKDHGDLVDKLAGFLLSSDRHEP 331
Cdd:cd03805  296 LLSSALALLYTPSNEHFGIVPLEAMYAGK----------PVIAcnsggPLE---TVVEGVTGFLCEPTPEAFAEAMLKLA 362

                        250       260
                 ....*....|....*....|.
gi 223691483 332 LGRNLAQAMEEYAWNHVIKKY 352
Cdd:cd03805  363 NDPDLADRMGAAGRKRVKEKF 383
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 246-357 3.00e-03

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 39.14  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 246 GHVPSKSVYfDWLSRGHIVVSTAIQENFGISVVEAVGMGCIPLLPDRLAYPEIMPrehHGTILY--KDHGDLVDKL--AG 321
Cdd:cd03796  256 GAVPHEEVR-DVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLP---PDMILLaePDPEDIVRKLeeAI 331

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 223691483 322 FLLSSDRHEPLG-RNLAQAMeeYAWNHVIKK----YDEILN 357
Cdd:cd03796  332 SILRTGKHDPWSfHNRVKKM--YSWEDVARRtekvYDRILS 370
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 170-359 5.74e-03

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: 38.51  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 170 PVGSSESLPDKAlaPLVIWNHRWEYDKKPERFFRALGEIKRRGIPFRLALLGGGVSKIPKAFLAAREAFKQEIVVFGHVP 249
Cdd:cd03798  189 PEDRGLGLPLDA--FVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLP 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223691483 250 SKSVYfDWLSRGHIVVSTAIQENFGISVVEAvgMGC-IPLLPDRLAYPEIMPREHHGTILYKDhGD---LVDKLAGFLLS 325
Cdd:cd03798  267 HEQVP-AYYRACDVFVLPSRHEGFGLVLLEA--MACgLPVVATDVGGIPEVVGDPETGLLVPP-GDadaLAAALRRALAE 342

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 223691483 326 SDRHEpLGRNLAQ-AMEEYAWNHVIKKYDEILNHL 359
Cdd:cd03798  343 PYLRE-LGEAARArVAERFSWVKAADRIAAAYRDV 376
 
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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