NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17531359|ref|NP_496426|]
View 

GPI mannosyltransferase 1 [Caenorhabditis elegans]

Protein Classification

glycosyltransferase family protein; YfhO family protein( domain architecture ID 10523334)

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| YfhO family protein is an integral membrane protein similar to Bacillus subtilis YfhO that is essential to lipoteichoic acid (LTA) glycosylation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Mannosyl_trans pfam05007
Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many ...
 146-405 1.53e-117

Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many glycosyltransferases that utilize nucleotide sugars. It is thought that the motif is involved in the binding of a manganese ion that is required for association of the enzymes with nucleotide sugar substrates.


:

Pssm-ID: 252941  Cd Length: 259  Bit Score: 343.24  E-value: 1.53e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   146 ISARGNAESIVAAVVLLNIVLLQKGYWKSAALVHGaLAIQLKIYPLIYLPSVFLSLSTIGEQsCVVNKFKSLVSnWKGFA 225
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLG-FAVHFKIYPIIYALPIALSLSTVREQ-SVAAKLNSLLS-IAVLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   226 YMLVTLTSFAAVVLFFFQIYGQLFLDEYLIYHVKRRDLAHNFSPYFYLLYLYEANPTM-SQIIGLGAFIPQIVLIVFFAF 304
Cdd:pfam05007  78 SILGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLYSASKHApSQILGLVAFAPQFVLLSFVSL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   305 KHYDDLPFCWFITTFAFVTYNKVCTSQYFVWYIVLLPLLAHKIMM-SRQLALSLMAAWFATQGIWLLAAYLFEFQGWNTF 383
Cdd:pfam05007 158 KFRRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMlSWKKALGLLLLWFATQALWLLPAYLLEFHGKNTF 237

                         250       260
                  ....*....|....*....|..
gi 17531359   384 FLMFLASCLFLIANSFILKQII 405
Cdd:pfam05007 238 YPLWLASCLFFLANVYILKQIL 259
 
Name Accession Description Interval E-value
Mannosyl_trans pfam05007
Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many ...
 146-405 1.53e-117

Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many glycosyltransferases that utilize nucleotide sugars. It is thought that the motif is involved in the binding of a manganese ion that is required for association of the enzymes with nucleotide sugar substrates.


Pssm-ID: 252941  Cd Length: 259  Bit Score: 343.24  E-value: 1.53e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   146 ISARGNAESIVAAVVLLNIVLLQKGYWKSAALVHGaLAIQLKIYPLIYLPSVFLSLSTIGEQsCVVNKFKSLVSnWKGFA 225
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLG-FAVHFKIYPIIYALPIALSLSTVREQ-SVAAKLNSLLS-IAVLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   226 YMLVTLTSFAAVVLFFFQIYGQLFLDEYLIYHVKRRDLAHNFSPYFYLLYLYEANPTM-SQIIGLGAFIPQIVLIVFFAF 304
Cdd:pfam05007  78 SILGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLYSASKHApSQILGLVAFAPQFVLLSFVSL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   305 KHYDDLPFCWFITTFAFVTYNKVCTSQYFVWYIVLLPLLAHKIMM-SRQLALSLMAAWFATQGIWLLAAYLFEFQGWNTF 383
Cdd:pfam05007 158 KFRRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMlSWKKALGLLLLWFATQALWLLPAYLLEFHGKNTF 237

                         250       260
                  ....*....|....*....|..
gi 17531359   384 FLMFLASCLFLIANSFILKQII 405
Cdd:pfam05007 238 YPLWLASCLFFLANVYILKQIL 259
PLN02841 PLN02841
GPI mannosyltransferase
 17-408 1.36e-77

GPI mannosyltransferase


Pssm-ID: 178434  Cd Length: 440  Bit Score: 247.01  E-value: 1.36e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   17 KILLVAFVARIILVFYAHIHDYLFKVNFTDIDYHVFSDAAKHVSNGGSPFDRATYRYTPALAWILLPVVHF-PDFGKILF 95
Cdd:PLN02841  10 SLLLASALLRVALIVYGEWQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLLALLLVPNSLLhRSWGKFLF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   96 CIFDILVAILYFKIMEKdlnetksetrEEMKDDQTMNVVIYWLANPLTAIISARGNAESIVAAVVLLNIVLLQKGYWKSA 175
Cdd:PLN02841  90 SAADLLVGLFIHTILRL----------RGVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIVCAVILWILICLMNGRLLQA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359  176 ALVHGaLAIQLKIYPLIY-LPSVFL-----------------------SLSTIGEQSCVVNKFKSLVSNWKGFAYMLVTL 231
Cdd:PLN02841 160 AFWYG-LVVHFRIYPIIYaLPIILVldkqyfgpggrpaltkwnskqnkTPSSNTEATSFLFNLWTFLTSLFSRERIMFGL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359  232 TS---FAAVVLFFFQIYGQLFLDEYLIYHVKRRDLAHNFSPYFYLLYLYEANpTMSQIIGLGAFIPQIVLIVFFAFKHYD 308
Cdd:PLN02841 239 ISggvFFALTGVSFYLYGWEFLNEALLYHLTRTDPRHNFSIYFYHIYLHHEQ-GFSLVERLASFLPQFLVQLALILCFSQ 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359  309 DLPFCWFITTFAFVTYNKVCTSQYFVWYIVLLPL-LAHKIMMSRQLALSLMAAWFATQGIWLLAAYLFEFQGWNTFFLMF 387
Cdd:PLN02841 318 DLPFCLFLQTVAFVAFNKVITAQYFVWFFCLLPLiLPWSRMKLKWKGLLCILVWMGSQLHWLMWAYLLEFKGRNVFLQLW 397

                        410       420
                 ....*....|....*....|.
gi 17531359  388 LASCLFLIANSFILKQIINHY 408
Cdd:PLN02841 398 IASLLFLAANTFVLLMIIQHH 418
 
Name Accession Description Interval E-value
Mannosyl_trans pfam05007
Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many ...
 146-405 1.53e-117

Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many glycosyltransferases that utilize nucleotide sugars. It is thought that the motif is involved in the binding of a manganese ion that is required for association of the enzymes with nucleotide sugar substrates.


Pssm-ID: 252941  Cd Length: 259  Bit Score: 343.24  E-value: 1.53e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   146 ISARGNAESIVAAVVLLNIVLLQKGYWKSAALVHGaLAIQLKIYPLIYLPSVFLSLSTIGEQsCVVNKFKSLVSnWKGFA 225
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLG-FAVHFKIYPIIYALPIALSLSTVREQ-SVAAKLNSLLS-IAVLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   226 YMLVTLTSFAAVVLFFFQIYGQLFLDEYLIYHVKRRDLAHNFSPYFYLLYLYEANPTM-SQIIGLGAFIPQIVLIVFFAF 304
Cdd:pfam05007  78 SILGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLYSASKHApSQILGLVAFAPQFVLLSFVSL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   305 KHYDDLPFCWFITTFAFVTYNKVCTSQYFVWYIVLLPLLAHKIMM-SRQLALSLMAAWFATQGIWLLAAYLFEFQGWNTF 383
Cdd:pfam05007 158 KFRRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMlSWKKALGLLLLWFATQALWLLPAYLLEFHGKNTF 237

                         250       260
                  ....*....|....*....|..
gi 17531359   384 FLMFLASCLFLIANSFILKQII 405
Cdd:pfam05007 238 YPLWLASCLFFLANVYILKQIL 259
PLN02841 PLN02841
GPI mannosyltransferase
 17-408 1.36e-77

GPI mannosyltransferase


Pssm-ID: 178434  Cd Length: 440  Bit Score: 247.01  E-value: 1.36e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   17 KILLVAFVARIILVFYAHIHDYLFKVNFTDIDYHVFSDAAKHVSNGGSPFDRATYRYTPALAWILLPVVHF-PDFGKILF 95
Cdd:PLN02841  10 SLLLASALLRVALIVYGEWQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLLALLLVPNSLLhRSWGKFLF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359   96 CIFDILVAILYFKIMEKdlnetksetrEEMKDDQTMNVVIYWLANPLTAIISARGNAESIVAAVVLLNIVLLQKGYWKSA 175
Cdd:PLN02841  90 SAADLLVGLFIHTILRL----------RGVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIVCAVILWILICLMNGRLLQA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359  176 ALVHGaLAIQLKIYPLIY-LPSVFL-----------------------SLSTIGEQSCVVNKFKSLVSNWKGFAYMLVTL 231
Cdd:PLN02841 160 AFWYG-LVVHFRIYPIIYaLPIILVldkqyfgpggrpaltkwnskqnkTPSSNTEATSFLFNLWTFLTSLFSRERIMFGL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359  232 TS---FAAVVLFFFQIYGQLFLDEYLIYHVKRRDLAHNFSPYFYLLYLYEANpTMSQIIGLGAFIPQIVLIVFFAFKHYD 308
Cdd:PLN02841 239 ISggvFFALTGVSFYLYGWEFLNEALLYHLTRTDPRHNFSIYFYHIYLHHEQ-GFSLVERLASFLPQFLVQLALILCFSQ 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531359  309 DLPFCWFITTFAFVTYNKVCTSQYFVWYIVLLPL-LAHKIMMSRQLALSLMAAWFATQGIWLLAAYLFEFQGWNTFFLMF 387
Cdd:PLN02841 318 DLPFCLFLQTVAFVAFNKVITAQYFVWFFCLLPLiLPWSRMKLKWKGLLCILVWMGSQLHWLMWAYLLEFKGRNVFLQLW 397

                        410       420
                 ....*....|....*....|.
gi 17531359  388 LASCLFLIANSFILKQIINHY 408
Cdd:PLN02841 398 IASLLFLAANTFVLLMIIQHH 418
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH