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Conserved domains on  [gi|1754759099|ref|NP_001361411|]
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GPI mannosyltransferase 2 isoform a [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 10514647)

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
Mannosyl_trans2 pfam04188
Mannosyltransferase (PIG-V); This is a family of eukaryotic ER membrane proteins that are ...
 8-493 0e+00

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: 572.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099   8 RKEVLRFAVSCRILTLMLQALFN-AIIPDHHAEAFSPPRLAPSGFVDQLVEGLLGGLSHWDAEHFLFIAEHGYLYEHNFA 86
Cdd:pfam04188   1 IKELTLYAVLFRSLQLLLVFLTPiRQFPTSTSLALNPPCSASPSEVNSYWNKYLWNLLSWDSVFFLKISENGYQYEHEYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099  87 FFPGFPLALLVGT-ELLRPLRGLLSLRSCLLISVASLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLA 165
Cdd:pfam04188  81 FSPLWPFFVRLFIkSNNDPLYHLLRLRVAIENSLFYLSILLFFLAAKILSQNIRQSLFARTISFKASLLFCLTPAAGFLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 166 AGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSV 245
Cdd:pfam04188 161 SIYSEPLSALFAFVGIWSLECGIDISWVLWFAYSFIMRSNGLASLGRSNCVLLGIYFIDLIELTKNRKFVKAICFPFLSG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 246 FTLGLPFALFQYYAYTQFCLPGSArpipeplvqlavdkgyriaeGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQV 325
Cdd:pfam04188 241 SLMFLPFLYFQYYLYKTFCPQRSA--------------------GNEPPWCKSQLPLLYSYIQSHYWGVGFLKYWTPKQI 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 326 PNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQRSKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRF 405
Cdd:pfam04188 301 PNFLLAVPNIILLIYSSIYYSKTHPWLCLTLGLQYPSYNKKAEKPDLGFLSPQVFVLVVHTRALVVIVCFFMHVQVLTRF 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 406 LgSSTPIMYWFPAHLLQdqepllrSLKTVPWKPLAEDsppgqkvprnPIMGLLYHWKTCSpvtryilgyflTYWLLGLLL 485
Cdd:pfam04188 381 L-SFLPLHYWFLADLLV-------SDKKKMWNPLGDD----------KIVKFYIYWLACS-----------FYILLGTLL 431


                  ....*...
gi 1754759099 486 HCNFLPWT 493
Cdd:pfam04188 432 FANFLPPT 439
 
Name Accession Description Interval E-value
Mannosyl_trans2 pfam04188
Mannosyltransferase (PIG-V); This is a family of eukaryotic ER membrane proteins that are ...
 8-493 0e+00

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: 572.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099   8 RKEVLRFAVSCRILTLMLQALFN-AIIPDHHAEAFSPPRLAPSGFVDQLVEGLLGGLSHWDAEHFLFIAEHGYLYEHNFA 86
Cdd:pfam04188   1 IKELTLYAVLFRSLQLLLVFLTPiRQFPTSTSLALNPPCSASPSEVNSYWNKYLWNLLSWDSVFFLKISENGYQYEHEYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099  87 FFPGFPLALLVGT-ELLRPLRGLLSLRSCLLISVASLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLA 165
Cdd:pfam04188  81 FSPLWPFFVRLFIkSNNDPLYHLLRLRVAIENSLFYLSILLFFLAAKILSQNIRQSLFARTISFKASLLFCLTPAAGFLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 166 AGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSV 245
Cdd:pfam04188 161 SIYSEPLSALFAFVGIWSLECGIDISWVLWFAYSFIMRSNGLASLGRSNCVLLGIYFIDLIELTKNRKFVKAICFPFLSG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 246 FTLGLPFALFQYYAYTQFCLPGSArpipeplvqlavdkgyriaeGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQV 325
Cdd:pfam04188 241 SLMFLPFLYFQYYLYKTFCPQRSA--------------------GNEPPWCKSQLPLLYSYIQSHYWGVGFLKYWTPKQI 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 326 PNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQRSKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRF 405
Cdd:pfam04188 301 PNFLLAVPNIILLIYSSIYYSKTHPWLCLTLGLQYPSYNKKAEKPDLGFLSPQVFVLVVHTRALVVIVCFFMHVQVLTRF 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 406 LgSSTPIMYWFPAHLLQdqepllrSLKTVPWKPLAEDsppgqkvprnPIMGLLYHWKTCSpvtryilgyflTYWLLGLLL 485
Cdd:pfam04188 381 L-SFLPLHYWFLADLLV-------SDKKKMWNPLGDD----------KIVKFYIYWLACS-----------FYILLGTLL 431


                  ....*...
gi 1754759099 486 HCNFLPWT 493
Cdd:pfam04188 432 FANFLPPT 439
COG5542 COG5542
Mannosyltransferase related to Gpi18 [Carbohydrate transport and metabolism];
64-203 1.10e-07

Mannosyltransferase related to Gpi18 [Carbohydrate transport and metabolism];


Pssm-ID: 444286 [Multi-domain]  Cd Length: 208  Bit Score: 52.26  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099  64 SHWDAEHFLFIAEHGYLY----EHNfAFFPGFPLALLVGTELlrplrGLLSLRSCLLISVaslnfLFFMLAAVALHDLgC 139
Cdd:COG5542     2 TAFLSPWYRAIATSGYFAalgkQFG-DYFPLYPYLLRLVMYL-----GLPFLLAGKLVSI-----LADLVAAYLLYRW-V 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1754759099 140 LVLHCPHQSFYAALLFCLSPANVFLAAGY--SEALFALLTFSAMGQLERGRVWTSVLLFAFATGVR 203
Cdd:COG5542    70 KKYYGGNAALLAAAVLAFLPTVLLNSAIWgqTDSLYTLFSLAALYALLRGRYGWAALFFALATAFK 135
 
Name Accession Description Interval E-value
Mannosyl_trans2 pfam04188
Mannosyltransferase (PIG-V); This is a family of eukaryotic ER membrane proteins that are ...
 8-493 0e+00

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: 572.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099   8 RKEVLRFAVSCRILTLMLQALFN-AIIPDHHAEAFSPPRLAPSGFVDQLVEGLLGGLSHWDAEHFLFIAEHGYLYEHNFA 86
Cdd:pfam04188   1 IKELTLYAVLFRSLQLLLVFLTPiRQFPTSTSLALNPPCSASPSEVNSYWNKYLWNLLSWDSVFFLKISENGYQYEHEYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099  87 FFPGFPLALLVGT-ELLRPLRGLLSLRSCLLISVASLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLA 165
Cdd:pfam04188  81 FSPLWPFFVRLFIkSNNDPLYHLLRLRVAIENSLFYLSILLFFLAAKILSQNIRQSLFARTISFKASLLFCLTPAAGFLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 166 AGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSV 245
Cdd:pfam04188 161 SIYSEPLSALFAFVGIWSLECGIDISWVLWFAYSFIMRSNGLASLGRSNCVLLGIYFIDLIELTKNRKFVKAICFPFLSG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 246 FTLGLPFALFQYYAYTQFCLPGSArpipeplvqlavdkgyriaeGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQV 325
Cdd:pfam04188 241 SLMFLPFLYFQYYLYKTFCPQRSA--------------------GNEPPWCKSQLPLLYSYIQSHYWGVGFLKYWTPKQI 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 326 PNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQRSKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRF 405
Cdd:pfam04188 301 PNFLLAVPNIILLIYSSIYYSKTHPWLCLTLGLQYPSYNKKAEKPDLGFLSPQVFVLVVHTRALVVIVCFFMHVQVLTRF 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099 406 LgSSTPIMYWFPAHLLQdqepllrSLKTVPWKPLAEDsppgqkvprnPIMGLLYHWKTCSpvtryilgyflTYWLLGLLL 485
Cdd:pfam04188 381 L-SFLPLHYWFLADLLV-------SDKKKMWNPLGDD----------KIVKFYIYWLACS-----------FYILLGTLL 431


                  ....*...
gi 1754759099 486 HCNFLPWT 493
Cdd:pfam04188 432 FANFLPPT 439
COG5542 COG5542
Mannosyltransferase related to Gpi18 [Carbohydrate transport and metabolism];
64-203 1.10e-07

Mannosyltransferase related to Gpi18 [Carbohydrate transport and metabolism];


Pssm-ID: 444286 [Multi-domain]  Cd Length: 208  Bit Score: 52.26  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754759099  64 SHWDAEHFLFIAEHGYLY----EHNfAFFPGFPLALLVGTELlrplrGLLSLRSCLLISVaslnfLFFMLAAVALHDLgC 139
Cdd:COG5542     2 TAFLSPWYRAIATSGYFAalgkQFG-DYFPLYPYLLRLVMYL-----GLPFLLAGKLVSI-----LADLVAAYLLYRW-V 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1754759099 140 LVLHCPHQSFYAALLFCLSPANVFLAAGY--SEALFALLTFSAMGQLERGRVWTSVLLFAFATGVR 203
Cdd:COG5542    70 KKYYGGNAALLAAAVLAFLPTVLLNSAIWgqTDSLYTLFSLAALYALLRGRYGWAALFFALATAFK 135
 
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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