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Conserved domains on  [gi|1059842862|ref|NP_001317433|]
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chitobiosyldiphosphodolichol beta-mannosyltransferase isoform 2 [Homo sapiens]

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 ...
1-350 0e+00

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 cd03816:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 411  Bit Score: 554.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862   1 MYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHL 80
Cdd:cd03816    83 LSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADA 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  81 NLCVTNAMREDLA--DNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGL 158
Cdd:cd03816   163 HLCVTKAMQRDLQqfENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGA 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 159 VTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWL 237
Cdd:cd03816   221 VSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWL 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 238 EAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFp 317
Cdd:cd03816   301 SAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDF- 379
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1059842862 318 dPAGKLNQFRKNLRESQQLRWDESWVQTVLPLV 350
Cdd:cd03816   380 -DRGKLNVLKKGAQEESENRWDENWDRVAGPLF 411
 
Name Accession Description Interval E-value
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-350 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 554.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862   1 MYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHL 80
Cdd:cd03816    83 LSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADA 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  81 NLCVTNAMREDLA--DNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGL 158
Cdd:cd03816   163 HLCVTKAMQRDLQqfENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGA 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 159 VTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWL 237
Cdd:cd03816   221 VSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWL 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 238 EAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFp 317
Cdd:cd03816   301 SAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDF- 379
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1059842862 318 dPAGKLNQFRKNLRESQQLRWDESWVQTVLPLV 350
Cdd:cd03816   380 -DRGKLNVLKKGAQEESENRWDENWDRVAGPLF 411
PLN02275 PLN02275
transferase, transferring glycosyl groups
3-313 2.86e-127

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 369.39  E-value: 2.86e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862   3 LLWKLMWREPGAYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLN 81
Cdd:PLN02275   90 LLWFLCVKIPRPDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGH 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  82 LCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLdlqhrlfmklgsmhspfrarsepedpvtersafterdagsglVTR 161
Cdd:PLN02275  170 LCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASL------------------------------------------EIR 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 162 LRE-RPALLVSSTSWTEDEDFSILLAALEKFEQL---TLDGHN--------LPSLVCVITGKGPLREYYSRLIHQKHFQH 229
Cdd:PLN02275  208 LRPnRPALVVSSTSWTPDEDFGILLEAAVMYDRRvaaRLNESDsasgkqslYPRLLFIITGKGPQKAMYEEKISRLNLRH 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 230 IQVCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQL 309
Cdd:PLN02275  288 VAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELADQL 367

                  ....
gi 1059842862 310 QMLF 313
Cdd:PLN02275  368 LELL 371
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
219-339 1.46e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 52.30  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 219 SRLIHQKHFQHIqvctpwLEAedyplLLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 298
Cdd:COG0438     2 GRLVPRKGLDLL------LEA-----LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLL 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1059842862 299 FE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRESQQLRWD 339
Cdd:COG0438    68 VPpgDPEALAEAILRLLED----PELRRRLGEAARERAEERFS 106
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
184-332 1.68e-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: 53.05  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 184 LLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgld 263
Cdd:pfam00534  20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG--- 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1059842862 264 LPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRE 332
Cdd:pfam00534  91 FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED----EELRERLGENARK 157
 
Name Accession Description Interval E-value
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-350 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 554.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862   1 MYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHL 80
Cdd:cd03816    83 LSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADA 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  81 NLCVTNAMREDLA--DNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGL 158
Cdd:cd03816   163 HLCVTKAMQRDLQqfENWNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGA 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 159 VTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWL 237
Cdd:cd03816   221 VSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWL 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 238 EAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFp 317
Cdd:cd03816   301 SAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDF- 379
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1059842862 318 dPAGKLNQFRKNLRESQQLRWDESWVQTVLPLV 350
Cdd:cd03816   380 -DRGKLNVLKKGAQEESENRWDENWDRVAGPLF 411
PLN02275 PLN02275
transferase, transferring glycosyl groups
3-313 2.86e-127

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 369.39  E-value: 2.86e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862   3 LLWKLMWREPGAYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLN 81
Cdd:PLN02275   90 LLWFLCVKIPRPDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGH 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  82 LCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLdlqhrlfmklgsmhspfrarsepedpvtersafterdagsglVTR 161
Cdd:PLN02275  170 LCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASL------------------------------------------EIR 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 162 LRE-RPALLVSSTSWTEDEDFSILLAALEKFEQL---TLDGHN--------LPSLVCVITGKGPLREYYSRLIHQKHFQH 229
Cdd:PLN02275  208 LRPnRPALVVSSTSWTPDEDFGILLEAAVMYDRRvaaRLNESDsasgkqslYPRLLFIITGKGPQKAMYEEKISRLNLRH 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 230 IQVCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQL 309
Cdd:PLN02275  288 VAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELADQL 367

                  ....
gi 1059842862 310 QMLF 313
Cdd:PLN02275  368 LELL 371
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
23-339 2.72e-09

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: 57.93  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  23 GLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLvlLAKWyeKFFGRLSHLNLCVTNAMREDLADNWHI---R 99
Cdd:cd03801    90 GLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL--LARA--EALLRRADAVIAVSEALRDELRALGGIppeK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 100 AVTVYdkpasffkeTPLDLQHrlfmklgsmhSPFRARSEPEDPVTERSAFTerdagsglVTRLRERPALLVsstswtede 179
Cdd:cd03801   166 IVVIP---------NGVDLER----------FSPPLRRKLGIPPDRPVLLF--------VGRLSPRKGVDL--------- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 180 dfsiLLAALEKFEQLtldghnLPSLVCVITGKGPlrEYYSRLIHQKHFQHIQV-CTPWLEAEDYPLLLGSADLGVCLHTS 258
Cdd:cd03801   210 ----LLEALAKLLRR------GPDVRLVIVGGDG--PLRAELEELELGLGDRVrFLGFVPDEELPALYAAADVFVLPSRY 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 259 SSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSnfpDPAgKLNQFRKNLRESQQL 336
Cdd:cd03801   278 EG---FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpdDVEALADALLRLLA---DPE-LRARLGRAARERVAE 350

                  ...
gi 1059842862 337 RWD 339
Cdd:cd03801   351 RFS 353
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
219-339 1.46e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 52.30  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 219 SRLIHQKHFQHIqvctpwLEAedyplLLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 298
Cdd:COG0438     2 GRLVPRKGLDLL------LEA-----LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLL 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1059842862 299 FE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRESQQLRWD 339
Cdd:COG0438    68 VPpgDPEALAEAILRLLED----PELRRRLGEAARERAEERFS 106
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
184-332 1.68e-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: 53.05  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 184 LLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgld 263
Cdd:pfam00534  20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG--- 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1059842862 264 LPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfpdpAGKLNQFRKNLRE 332
Cdd:pfam00534  91 FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED----EELRERLGENARK 157
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
141-299 3.75e-08

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: 53.56  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 141 DPVTERSAFTERDAGSGLVTRLRERPALLVSStsWTEDEDFSILLAALEKFeqltldGHNLPSLVCVITGKGPLREYYSR 220
Cdd:cd01635    87 GPDSLESTRSELLALARLLVSLPLADKVSVGR--LVPEKGIDLLLEALALL------KARLPDLVLVLVGGGGEREEEEA 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 221 LI-HQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVF 299
Cdd:cd01635   159 LAaALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEG---FGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
3-315 2.00e-07

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: 52.34  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862   3 LLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGcLCGSKLVID----WHNygySIMGLVHGPNHPLVLLAKWYEKFFGRLS 78
Cdd:cd03794    89 LLKLLVREERPDVIIAYSPPITLGLAALLLKK-LRGAPFILDvrdlWPE---SLIALGVLKKGSLLKLLKKLERKLYRLA 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  79 HLNLCVTNAMREdladnwHIRAVTVYDKPASFFKEtpldlqhrlfmklGSMHSPFRarsePEDPVTERSAFTERDagsgl 158
Cdd:cd03794   165 DAIIVLSPGLKE------YLLRKGVPKEKIIVIPN-------------WADLEEFK----PPPKDELRKKLGLDD----- 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 159 vtrlrerPALLVSSTSWTEDEDFSILLAALEKFEQLtldghnlPSLVCVITGKGPLREYYSRLIHQKHfqhIQVCT--PW 236
Cdd:cd03794   217 -------KFVVVYAGNIGKAQGLETLLEAAERLKRR-------PDIRFLFVGDGDEKERLKELAKARG---LDNVTflGR 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 237 LEAEDYPLLLGSADLG-VCLHTS-SSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQML 312
Cdd:cd03794   280 VPKEEVPELLSAADVGlVPLKDNpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEpgDPEALADAILEL 359

                  ...
gi 1059842862 313 FSN 315
Cdd:cd03794   360 LDD 362
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
41-335 5.58e-07

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: 50.82  E-value: 5.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862  41 LVIDWHNYGYSIMGLV-----------HGP---NHPLVLLAKWYEKFFGRLSHLnLCVTNAMREDLADNWHI---RAVTV 103
Cdd:cd03811    86 VVISFLGFATYIVAKLaaarskviawiHSSlskLYYLKKKLLLKLKLYKKADKI-VCVSKGIKEDLIRLGPSppeKIEVI 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 104 YDkpasffketPLDLQHrlfmklgsmhspFRARSEPEDPVTERSAFTerdagsgLVT--RLrerpallvsstswTEDEDF 181
Cdd:cd03811   165 YN---------PIDIDR------------IRALAKEPILNEPEDGPV-------ILAvgRL-------------DPQKGH 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 182 SILLAAlekFEQLTLDGHNLPslvCVITGKGPLREYYSRLIHQkhfqhiqvctpwLEAEDYPLLLG----------SADL 251
Cdd:cd03811   204 DLLIEA---FAKLRKKYPDVK---LVILGDGPLREELEKLAKE------------LGLAERVIFLGfqsnpypylkKADL 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 252 GVclHTSSS-GLdlPMKVVDMFGCCLPVCAVNFKCLHELVKHEENG-LVFEDSEELAAQLQMLFSNFPDPAGKLNQFRKN 329
Cdd:cd03811   266 FV--LSSRYeGF--PNVLLEAMALGTPVVSTDCPGPREILDDGENGlLVPDGDAAALAGILAALLQKKLDAALRERLAKA 341

                  ....*.
gi 1059842862 330 LRESQQ 335
Cdd:cd03811   342 QEAVFR 347
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
181-307 2.77e-04

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 42.27  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 181 FSILLAALEKFeqltldgHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVclHTSSS 260
Cdd:cd03817   216 IDFLLRAFAEL-------KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFV--FASTT 286
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1059842862 261 GLdLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAA 307
Cdd:cd03817   287 ET-QGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLA 332
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
177-315 5.86e-03

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: 38.35  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 177 EDEDFSILLAA-----------LEKFEQLTLDGhnlPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEaeDYPLL 245
Cdd:cd03808   186 PSEKVVFLFVArllkdkgidelIEAAKILKKKG---PNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRS--DVPEL 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059842862 246 LGSADLgVCLHTSSSGLdlPMKVV------------DMFGCClpvcavnfkclhELVKHEENGLVFE--DSEELAAQLQM 311
Cdd:cd03808   261 LAESDV-FVLPSYREGL--PRSLLeamaagrpvittDVPGCR------------ELVIDGVNGFLVPpgDVEALADAIEK 325

                  ....
gi 1059842862 312 LFSN 315
Cdd:cd03808   326 LIED 329
 
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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