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Conserved domains on  [gi|42742257|ref|NP_012547|]
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glycosylphosphatidylinositol-alpha 1,4 mannosyltransferase I [Saccharomyces cerevisiae S288C]

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

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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 ...
 127-386 1.07e-106

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: 315.12  E-value: 1.07e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   127 ISTRGNAESVLCCLIMFTLFFLQKSRYTLAGILYGLSIHFKIYPIIYCIPIAIFIYyNKRNQGPRTQLTSLLNI-----G 201
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLGFAVHFKIYPIIYALPIALSLS-TVREQSVAAKLNSLLSIavlvsI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   202 LSTLTTLLGCGWAMYKIYGYEFLDQAYLYHLYRTDHRHNFSVWNMLLYLDSANKENGESNLSRYAFVPQLLLVLVTgCLE 281
Cdd:pfam05007  80 LGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLYSASKHAPSQILGLVAFAPQFVLLSFV-SLK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   282 WwnptFDNLLRVLFVQTFAFVTYNKVCTSQYFVWYLIFLPFYLSRTHI-GWKKGLLMATLWVGTQGIWLSQGYYLEFEGK 360
Cdd:pfam05007 159 F----RRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMlSWKKALGLLLLWFATQALWLLPAYLLEFHGK 234

                         250       260
                  ....*....|....*....|....*.
gi 42742257   361 NVFYPgLFIASVLFFVTNVWLLGQFI 386
Cdd:pfam05007 235 NTFYP-LWLASCLFFLANVYILKQIL 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 ...
 127-386 1.07e-106

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: 315.12  E-value: 1.07e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   127 ISTRGNAESVLCCLIMFTLFFLQKSRYTLAGILYGLSIHFKIYPIIYCIPIAIFIYyNKRNQGPRTQLTSLLNI-----G 201
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLGFAVHFKIYPIIYALPIALSLS-TVREQSVAAKLNSLLSIavlvsI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   202 LSTLTTLLGCGWAMYKIYGYEFLDQAYLYHLYRTDHRHNFSVWNMLLYLDSANKENGESNLSRYAFVPQLLLVLVTgCLE 281
Cdd:pfam05007  80 LGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLYSASKHAPSQILGLVAFAPQFVLLSFV-SLK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   282 WwnptFDNLLRVLFVQTFAFVTYNKVCTSQYFVWYLIFLPFYLSRTHI-GWKKGLLMATLWVGTQGIWLSQGYYLEFEGK 360
Cdd:pfam05007 159 F----RRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMlSWKKALGLLLLWFATQALWLLPAYLLEFHGK 234

                         250       260
                  ....*....|....*....|....*.
gi 42742257   361 NVFYPgLFIASVLFFVTNVWLLGQFI 386
Cdd:pfam05007 235 NTFYP-LWLASCLFFLANVYILKQIL 259
PLN02841 PLN02841
GPI mannosyltransferase
 8-386 5.02e-81

GPI mannosyltransferase


Pssm-ID: 178434  Cd Length: 440  Bit Score: 255.49  E-value: 5.02e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257    8 LTVLSFLVRVGFFLFGIYQDANFKVRYTDIDYFVFHDAAKYVYEGKSPYARDTYRYTPLLSWLLVPNhyfGWFH--LGKV 85
Cdd:PLN02841  11 LLLASALLRVALIVYGEWQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLLALLLVPN---SLLHrsWGKF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   86 IFVIFDLVTGLIIMKLLN-QAISRKRALILESIWLLNPMVITISTRGNAESVLCCLIMFTLFFLQKSRYTLAGILYGLSI 164
Cdd:PLN02841  88 LFSAADLLVGLFIHTILRlRGVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIVCAVILWILICLMNGRLLQAAFWYGLVV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257  165 HFKIYPIIYCIPIAIFIYYNKRNQGPR----------------------------TQLTSLLN-----IGLSTLTTLLGC 211
Cdd:PLN02841 168 HFRIYPIIYALPIILVLDKQYFGPGGRpaltkwnskqnktpssnteatsflfnlwTFLTSLFSrerimFGLISGGVFFAL 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257  212 GWAMYKIYGYEFLDQAYLYHLYRTDHRHNFSVWNMLLYLdsaNKENGESNLSRYA-FVPQLLLVLVTGclewwNPTFDNL 290
Cdd:PLN02841 248 TGVSFYLYGWEFLNEALLYHLTRTDPRHNFSIYFYHIYL---HHEQGFSLVERLAsFLPQFLVQLALI-----LCFSQDL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257  291 LRVLFVQTFAFVTYNKVCTSQYFVWYLIFLPFYLSRTHIGWK-KGLLMATLWVGTQGIWLSQGYYLEFEGKNVFYPgLFI 369
Cdd:PLN02841 320 PFCLFLQTVAFVAFNKVITAQYFVWFFCLLPLILPWSRMKLKwKGLLCILVWMGSQLHWLMWAYLLEFKGRNVFLQ-LWI 398

                        410
                 ....*....|....*..
gi 42742257  370 ASVLFFVTNVWLLGQFI 386
Cdd:PLN02841 399 ASLLFLAANTFVLLMII 415
 
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 ...
 127-386 1.07e-106

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: 315.12  E-value: 1.07e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   127 ISTRGNAESVLCCLIMFTLFFLQKSRYTLAGILYGLSIHFKIYPIIYCIPIAIFIYyNKRNQGPRTQLTSLLNI-----G 201
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLGFAVHFKIYPIIYALPIALSLS-TVREQSVAAKLNSLLSIavlvsI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   202 LSTLTTLLGCGWAMYKIYGYEFLDQAYLYHLYRTDHRHNFSVWNMLLYLDSANKENGESNLSRYAFVPQLLLVLVTgCLE 281
Cdd:pfam05007  80 LGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLYSASKHAPSQILGLVAFAPQFVLLSFV-SLK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   282 WwnptFDNLLRVLFVQTFAFVTYNKVCTSQYFVWYLIFLPFYLSRTHI-GWKKGLLMATLWVGTQGIWLSQGYYLEFEGK 360
Cdd:pfam05007 159 F----RRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMlSWKKALGLLLLWFATQALWLLPAYLLEFHGK 234

                         250       260
                  ....*....|....*....|....*.
gi 42742257   361 NVFYPgLFIASVLFFVTNVWLLGQFI 386
Cdd:pfam05007 235 NTFYP-LWLASCLFFLANVYILKQIL 259
PLN02841 PLN02841
GPI mannosyltransferase
 8-386 5.02e-81

GPI mannosyltransferase


Pssm-ID: 178434  Cd Length: 440  Bit Score: 255.49  E-value: 5.02e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257    8 LTVLSFLVRVGFFLFGIYQDANFKVRYTDIDYFVFHDAAKYVYEGKSPYARDTYRYTPLLSWLLVPNhyfGWFH--LGKV 85
Cdd:PLN02841  11 LLLASALLRVALIVYGEWQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLLALLLVPN---SLLHrsWGKF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   86 IFVIFDLVTGLIIMKLLN-QAISRKRALILESIWLLNPMVITISTRGNAESVLCCLIMFTLFFLQKSRYTLAGILYGLSI 164
Cdd:PLN02841  88 LFSAADLLVGLFIHTILRlRGVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIVCAVILWILICLMNGRLLQAAFWYGLVV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257  165 HFKIYPIIYCIPIAIFIYYNKRNQGPR----------------------------TQLTSLLN-----IGLSTLTTLLGC 211
Cdd:PLN02841 168 HFRIYPIIYALPIILVLDKQYFGPGGRpaltkwnskqnktpssnteatsflfnlwTFLTSLFSrerimFGLISGGVFFAL 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257  212 GWAMYKIYGYEFLDQAYLYHLYRTDHRHNFSVWNMLLYLdsaNKENGESNLSRYA-FVPQLLLVLVTGclewwNPTFDNL 290
Cdd:PLN02841 248 TGVSFYLYGWEFLNEALLYHLTRTDPRHNFSIYFYHIYL---HHEQGFSLVERLAsFLPQFLVQLALI-----LCFSQDL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257  291 LRVLFVQTFAFVTYNKVCTSQYFVWYLIFLPFYLSRTHIGWK-KGLLMATLWVGTQGIWLSQGYYLEFEGKNVFYPgLFI 369
Cdd:PLN02841 320 PFCLFLQTVAFVAFNKVITAQYFVWFFCLLPLILPWSRMKLKwKGLLCILVWMGSQLHWLMWAYLLEFKGRNVFLQ-LWI 398

                        410
                 ....*....|....*..
gi 42742257  370 ASVLFFVTNVWLLGQFI 386
Cdd:PLN02841 399 ASLLFLAANTFVLLMII 415
PIG-U pfam06728
GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via ...
 44-244 6.22e-06

GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via glycosylphosphatidylinositol (GPI), which is posttranslationally attached to the carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a complex of at least four subunits, GPI8, GAA1, PIG-S, and PIG-T. PIG-U is thought to represent a fifth subunit in this complex and may be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.


Pssm-ID: 429085  Cd Length: 375  Bit Score: 47.99  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257    44 DAAKYVYEGK-------SPYARDTYRYTPLL----SWLLVPNHYFGWFHLGkVIFVIFDLVTGLIIMKL---LNQAISRK 109
Cdd:pfam06728  32 TSFKRLQEGLyllangiSPYDGGVVHQPPLLlallSLLLSINTKSSPILFS-LLFTLIDLLIALLLYAIaksYQKDISKL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742257   110 RA---------LILESIWLLNPMVITISTRGNAESVLCCLIMFTLFFLQKSRYTLAGILYGLSIHFKIYPIIYCIPIAIF 180
Cdd:pfam06728 111 FKskrdkslspLLIAALYLFNPLTILSCIALSTTVFSNLFILLSLYSAVKGNRALSAIALALASYLSLYPILLLAPLLLL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42742257   181 IYYNKRNQGPRTQLTSLLNIGLSTLTTLLGCGWAMYKIYG-YEFLDQAYLYHLYRTDHRHNFSVW 244
Cdd:pfam06728 191 LIFKSKNNLSSNSLSKFLSFLLLFLLTLAALLLASFLITGsWDFLDATYGFILTFEDLTPNLGLW 255
 
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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