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Conserved domains on  [gi|1754759078|ref|NP_001361412|]
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GPI mannosyltransferase 2 isoform b [Homo sapiens]

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 ...
 1-366 7.02e-147

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


The actual alignment was detected with superfamily member pfam04188:

Pssm-ID: 473917  Cd Length: 439  Bit Score: 422.40  E-value: 7.02e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078   1 MLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGL 80
Cdd:pfam04188 123 FLAAKILSQNIRQSLFARTISFKASLLFCLTPAAGFLTSIYSEPLSALFAFVGIWSLECGIDISWVLWFAYSFIMRSNGL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078  81 VSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSVFTLGLPFALFQYYAYTQFCLPGSArpipeplvqlavdkgyri 160
Cdd:pfam04188 203 ASLGRSNCVLLGIYFIDLIELTKNRKFVKAICFPFLSGSLMFLPFLYFQYYLYKTFCPQRSA------------------ 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078 161 aeGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQRSKNNKTL 240
Cdd:pfam04188 265 --GNEPPWCKSQLPLLYSYIQSHYWGVGFLKYWTPKQIPNFLLAVPNIILLIYSSIYYSKTHPWLCLTLGLQYPSYNKKA 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078 241 EKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLgSSTPIMYWFPAHLLQdqepllrSLKTVPWKPLAEDsppgq 320
Cdd:pfam04188 343 EKPDLGFLSPQVFVLVVHTRALVVIVCFFMHVQVLTRFL-SFLPLHYWFLADLLV-------SDKKKMWNPLGDD----- 409

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1754759078 321 kvprnPIMGLLYHWKTCSpvtryilgyflTYWLLGLLLHCNFLPWT 366
Cdd:pfam04188 410 -----KIVKFYIYWLACS-----------FYILLGTLLFANFLPPT 439
 
Name Accession Description Interval E-value
Mannosyl_trans2 pfam04188
Mannosyltransferase (PIG-V); This is a family of eukaryotic ER membrane proteins that are ...
 1-366 7.02e-147

Mannosyltransferase (PIG-V); This is a family of eukaryotic ER membrane proteins that are involved in the synthesis of glycosylphosphatidylinositol (GPI), a glycolipid that anchors many proteins to the eukaryotic cell surface. Proteins in this family are involved in transferring the second mannose in the biosynthetic pathway of GPI.


Pssm-ID: 282094  Cd Length: 439  Bit Score: 422.40  E-value: 7.02e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078   1 MLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGL 80
Cdd:pfam04188 123 FLAAKILSQNIRQSLFARTISFKASLLFCLTPAAGFLTSIYSEPLSALFAFVGIWSLECGIDISWVLWFAYSFIMRSNGL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078  81 VSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSVFTLGLPFALFQYYAYTQFCLPGSArpipeplvqlavdkgyri 160
Cdd:pfam04188 203 ASLGRSNCVLLGIYFIDLIELTKNRKFVKAICFPFLSGSLMFLPFLYFQYYLYKTFCPQRSA------------------ 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078 161 aeGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQRSKNNKTL 240
Cdd:pfam04188 265 --GNEPPWCKSQLPLLYSYIQSHYWGVGFLKYWTPKQIPNFLLAVPNIILLIYSSIYYSKTHPWLCLTLGLQYPSYNKKA 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078 241 EKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLgSSTPIMYWFPAHLLQdqepllrSLKTVPWKPLAEDsppgq 320
Cdd:pfam04188 343 EKPDLGFLSPQVFVLVVHTRALVVIVCFFMHVQVLTRFL-SFLPLHYWFLADLLV-------SDKKKMWNPLGDD----- 409

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1754759078 321 kvprnPIMGLLYHWKTCSpvtryilgyflTYWLLGLLLHCNFLPWT 366
Cdd:pfam04188 410 -----KIVKFYIYWLACS-----------FYILLGTLLFANFLPPT 439
 
Name Accession Description Interval E-value
Mannosyl_trans2 pfam04188
Mannosyltransferase (PIG-V); This is a family of eukaryotic ER membrane proteins that are ...
 1-366 7.02e-147

Mannosyltransferase (PIG-V); This is a family of eukaryotic ER membrane proteins that are involved in the synthesis of glycosylphosphatidylinositol (GPI), a glycolipid that anchors many proteins to the eukaryotic cell surface. Proteins in this family are involved in transferring the second mannose in the biosynthetic pathway of GPI.


Pssm-ID: 282094  Cd Length: 439  Bit Score: 422.40  E-value: 7.02e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078   1 MLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGL 80
Cdd:pfam04188 123 FLAAKILSQNIRQSLFARTISFKASLLFCLTPAAGFLTSIYSEPLSALFAFVGIWSLECGIDISWVLWFAYSFIMRSNGL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078  81 VSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSVFTLGLPFALFQYYAYTQFCLPGSArpipeplvqlavdkgyri 160
Cdd:pfam04188 203 ASLGRSNCVLLGIYFIDLIELTKNRKFVKAICFPFLSGSLMFLPFLYFQYYLYKTFCPQRSA------------------ 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078 161 aeGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQRSKNNKTL 240
Cdd:pfam04188 265 --GNEPPWCKSQLPLLYSYIQSHYWGVGFLKYWTPKQIPNFLLAVPNIILLIYSSIYYSKTHPWLCLTLGLQYPSYNKKA 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759078 241 EKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLgSSTPIMYWFPAHLLQdqepllrSLKTVPWKPLAEDsppgq 320
Cdd:pfam04188 343 EKPDLGFLSPQVFVLVVHTRALVVIVCFFMHVQVLTRFL-SFLPLHYWFLADLLV-------SDKKKMWNPLGDD----- 409

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1754759078 321 kvprnPIMGLLYHWKTCSpvtryilgyflTYWLLGLLLHCNFLPWT 366
Cdd:pfam04188 410 -----KIVKFYIYWLACS-----------FYILLGTLLFANFLPPT 439
 
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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