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Conserved domains on  [gi|258597470|ref|XP_001350517|]
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GPI mannosyltransferase 1 [Plasmodium falciparum 3D7]

Protein Classification

glycosyltransferase family protein( domain architecture ID 229536)

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
PMT_2 super family cl21590
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 39-430 2.56e-89

Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are not captured by pfam02366.


The actual alignment was detected with superfamily member PLN02841:

Pssm-ID: 473917  Cd Length: 440  Bit Score: 278.21  E-value: 2.56e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  39 WQDKNFNVKFTDVDYYVFSDAAKYVLMNKSPYERYTYRYTPLLAYIMIPNFFVHFSFGKILFSFIDILVTILINQIIKIK 118
Cdd:PLN02841  28 WQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLLALLLVPNSLLHRSWGKFLFSAADLLVGLFIHTILRLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 119 YTNCKNYIFYTCLWFLNPLVIIISLRGNADVIPCFLIIVTIFCIYKKHIFLSSIFYGLAVNFKIYTIIYALPFMLYLNKN 198
Cdd:PLN02841 108 GVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIVCAVILWILICLMNGRLLQAAFWYGLVVHFRIYPIIYALPIILVLDKQ 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 199 YLLGENIFQLNEKKKKKKNDFLLNTFFYIFRI-ISNFFVELFklNYEQFLFAICSSSVFLILNCVFYIIYGYEFLYESFI 277
Cdd:PLN02841 188 YFGPGGRPALTKWNSKQNKTPSSNTEATSFLFnLWTFLTSLF--SRERIMFGLISGGVFFALTGVSFYLYGWEFLNEALL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 278 YHIIRRDHRHNFSLFFYLMYLSIEKN-SKIIPLITFVPQIILVALFGFKYARtNLELSMFLQTISFIALNKVCTSQYFIW 356
Cdd:PLN02841 266 YHLTRTDPRHNFSIYFYHIYLHHEQGfSLVERLASFLPQFLVQLALILCFSQ-DLPFCLFLQTVAFVAFNKVITAQYFVW 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258597470 357 CIPFLPIILCAITLSKRNMFLiiSSILFFIVAKLHWLWWAYYLEFRGYNTFLQLFYSSVLFVISEISICWVFMY 430
Cdd:PLN02841 345 FFCLLPLILPWSRMKLKWKGL--LCILVWMGSQLHWLMWAYLLEFKGRNVFLQLWIASLLFLAANTFVLLMIIQ 416
 
Name Accession Description Interval E-value
PLN02841 PLN02841
GPI mannosyltransferase
 39-430 2.56e-89

GPI mannosyltransferase


Pssm-ID: 178434  Cd Length: 440  Bit Score: 278.21  E-value: 2.56e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  39 WQDKNFNVKFTDVDYYVFSDAAKYVLMNKSPYERYTYRYTPLLAYIMIPNFFVHFSFGKILFSFIDILVTILINQIIKIK 118
Cdd:PLN02841  28 WQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLLALLLVPNSLLHRSWGKFLFSAADLLVGLFIHTILRLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 119 YTNCKNYIFYTCLWFLNPLVIIISLRGNADVIPCFLIIVTIFCIYKKHIFLSSIFYGLAVNFKIYTIIYALPFMLYLNKN 198
Cdd:PLN02841 108 GVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIVCAVILWILICLMNGRLLQAAFWYGLVVHFRIYPIIYALPIILVLDKQ 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 199 YLLGENIFQLNEKKKKKKNDFLLNTFFYIFRI-ISNFFVELFklNYEQFLFAICSSSVFLILNCVFYIIYGYEFLYESFI 277
Cdd:PLN02841 188 YFGPGGRPALTKWNSKQNKTPSSNTEATSFLFnLWTFLTSLF--SRERIMFGLISGGVFFALTGVSFYLYGWEFLNEALL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 278 YHIIRRDHRHNFSLFFYLMYLSIEKN-SKIIPLITFVPQIILVALFGFKYARtNLELSMFLQTISFIALNKVCTSQYFIW 356
Cdd:PLN02841 266 YHLTRTDPRHNFSIYFYHIYLHHEQGfSLVERLASFLPQFLVQLALILCFSQ-DLPFCLFLQTVAFVAFNKVITAQYFVW 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258597470 357 CIPFLPIILCAITLSKRNMFLiiSSILFFIVAKLHWLWWAYYLEFRGYNTFLQLFYSSVLFVISEISICWVFMY 430
Cdd:PLN02841 345 FFCLLPLILPWSRMKLKWKGL--LCILVWMGSQLHWLMWAYLLEFKGRNVFLQLWIASLLFLAANTFVLLMIIQ 416
Mannosyl_trans pfam05007
Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many ...
 141-424 6.23e-52

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: 175.29  E-value: 6.23e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  141 ISLRGNADVIPCFLIIVTIFCIYKKHIFLSSIFYGLAVNFKIYTIIYALPFMLYLNKnylLGENIFQlnekkkkkkndfl 220
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLGFAVHFKIYPIIYALPIALSLST---VREQSVA------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  221 lntffyifriisNFFVELfkLNYEQFLFAICSSSVFLILNCVFYIIYGYEFLYESFIYHIIRRDHRHNFSLFFYLMYL-- 298
Cdd:pfam05007  65 ------------AKLNSL--LSIAVLVSILGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLys 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  299 -SIEKNSKIIPLITFVPQIILVALFGFKYaRTNLELSMFLQTISFIALNKVCTSQYFIWCIPFLPIILCAITLSKRNMFL 377
Cdd:pfam05007 131 aSKHAPSQILGLVAFAPQFVLLSFVSLKF-RRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMLSWKKAL 209

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 258597470  378 IIssILFFIVAKLHWLWWAYYLEFRGYNTFLQLFYSSVLFVISEISI 424
Cdd:pfam05007 210 GL--LLLWFATQALWLLPAYLLEFHGKNTFYPLWLASCLFFLANVYI 254
 
Name Accession Description Interval E-value
PLN02841 PLN02841
GPI mannosyltransferase
 39-430 2.56e-89

GPI mannosyltransferase


Pssm-ID: 178434  Cd Length: 440  Bit Score: 278.21  E-value: 2.56e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  39 WQDKNFNVKFTDVDYYVFSDAAKYVLMNKSPYERYTYRYTPLLAYIMIPNFFVHFSFGKILFSFIDILVTILINQIIKIK 118
Cdd:PLN02841  28 WQDAHMEVRYTDVDYLVFSDAAALVASGKSPFARDTYRYSPLLALLLVPNSLLHRSWGKFLFSAADLLVGLFIHTILRLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 119 YTNCKNYIFYTCLWFLNPLVIIISLRGNADVIPCFLIIVTIFCIYKKHIFLSSIFYGLAVNFKIYTIIYALPFMLYLNKN 198
Cdd:PLN02841 108 GVPEKVCTWSVMVWLFNPFTFTIGTRGNCEPIVCAVILWILICLMNGRLLQAAFWYGLVVHFRIYPIIYALPIILVLDKQ 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 199 YLLGENIFQLNEKKKKKKNDFLLNTFFYIFRI-ISNFFVELFklNYEQFLFAICSSSVFLILNCVFYIIYGYEFLYESFI 277
Cdd:PLN02841 188 YFGPGGRPALTKWNSKQNKTPSSNTEATSFLFnLWTFLTSLF--SRERIMFGLISGGVFFALTGVSFYLYGWEFLNEALL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470 278 YHIIRRDHRHNFSLFFYLMYLSIEKN-SKIIPLITFVPQIILVALFGFKYARtNLELSMFLQTISFIALNKVCTSQYFIW 356
Cdd:PLN02841 266 YHLTRTDPRHNFSIYFYHIYLHHEQGfSLVERLASFLPQFLVQLALILCFSQ-DLPFCLFLQTVAFVAFNKVITAQYFVW 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258597470 357 CIPFLPIILCAITLSKRNMFLiiSSILFFIVAKLHWLWWAYYLEFRGYNTFLQLFYSSVLFVISEISICWVFMY 430
Cdd:PLN02841 345 FFCLLPLILPWSRMKLKWKGL--LCILVWMGSQLHWLMWAYLLEFKGRNVFLQLWIASLLFLAANTFVLLMIIQ 416
Mannosyl_trans pfam05007
Mannosyltransferase (PIG-M); PIG-M has a DXD motif. The DXD motif is found in many ...
 141-424 6.23e-52

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: 175.29  E-value: 6.23e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  141 ISLRGNADVIPCFLIIVTIFCIYKKHIFLSSIFYGLAVNFKIYTIIYALPFMLYLNKnylLGENIFQlnekkkkkkndfl 220
Cdd:pfam05007   1 ISTRGNADSIVAFLVLLTLYLLQKRKIYQAALVLGFAVHFKIYPIIYALPIALSLST---VREQSVA------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  221 lntffyifriisNFFVELfkLNYEQFLFAICSSSVFLILNCVFYIIYGYEFLYESFIYHIIRRDHRHNFSLFFYLMYL-- 298
Cdd:pfam05007  65 ------------AKLNSL--LSIAVLVSILGTLISFAACTWLFYYKYGQEFLDEAYLYHVYRTDHRHNFSPYFLLLYLys 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470  299 -SIEKNSKIIPLITFVPQIILVALFGFKYaRTNLELSMFLQTISFIALNKVCTSQYFIWCIPFLPIILCAITLSKRNMFL 377
Cdd:pfam05007 131 aSKHAPSQILGLVAFAPQFVLLSFVSLKF-RRNLPFCCFVQTFAFVTFNKVCTSQYFVWYLVFLPLLLPNFKMLSWKKAL 209

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 258597470  378 IIssILFFIVAKLHWLWWAYYLEFRGYNTFLQLFYSSVLFVISEISI 424
Cdd:pfam05007 210 GL--LLLWFATQALWLLPAYLLEFHGKNTFYPLWLASCLFFLANVYI 254
PIG-U pfam06728
GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via ...
 64-195 1.13e-04

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: 44.14  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597470   64 LMNKSPYERYTYRYTPLL----AYIMIPNFFVHFSFGKILFSFIDILVTILINQIIKIKYTNCKNYI-----------FY 128
Cdd:pfam06728  45 ANGISPYDGGVVHQPPLLlallSLLLSINTKSSPILFSLLFTLIDLLIALLLYAIAKSYQKDISKLFkskrdkslsplLI 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258597470  129 TCLWFLNPLVIIISLRGNADVIPCFLIIVTIFCIYKKHIFLSSIFYGLAVNFKIYTIIYALPFMLYL 195
Cdd:pfam06728 125 AALYLFNPLTILSCIALSTTVFSNLFILLSLYSAVKGNRALSAIALALASYLSLYPILLLAPLLLLL 191
 
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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