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Conserved domains on  [gi|223718058|ref|NP_001138772|]
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alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4E isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PGAP4-like super family cl04660
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
49-273 7.04e-52

Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4.


The actual alignment was detected with superfamily member pfam04666:

Pssm-ID: 471077  Cd Length: 278  Bit Score: 175.96  E-value: 7.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058   49 LTVGITSESREGPNGLLDTLASLYHTSSTSEQKQMTVLVHLADSDPTWLRRTIIRISSLYRSQILTGQLLLIHAPPDAYP 128
Cdd:pfam04666  35 LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAETDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  129 AV-NDAQNK---VSRGQIYSKQNVDHAFLMSFATKLSTYFLLIEDNVFCAPNFVNHIRSKVGYRKPNTWVLLEFSNMGFL 204
Cdd:pfam04666 115 NLkNLKKTFndsPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQLEDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  205 GKLLHSRDLPLLAHFLLLFHKERPLNWLLLHFRTLL--------------GQQSSILCRPFLFYHRLTHLTFENKtlIGH 270
Cdd:pfam04666 195 GKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKvcnpekdakhckrqKQNRRIRFRPSLFQHVGTYSSLEGK--IQD 272

                  ...
gi 223718058  271 EKD 273
Cdd:pfam04666 273 LKD 275
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
49-273 7.04e-52

N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of oligosaccharides are synthesized through elongation by glycosyltransferases after trimming of the precursor oligosaccharides transferred to proteins in the endoplasmic reticulum. N-Acetylglucosaminyltransferases (GnTs) take part in the formation of branches in the biosynthesis of complex-type sugar chains. In vertebrates, six GnTs, designated as GnT-I to -VI, which catalyze the transfer of GlcNAc to the core mannose residues of Asn-linked sugar chains, have been identified. GnT-IV (EC:2.4.1.145) catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAc1-2Man1-3 arm of core oligosaccharide [Gn2(22)core oligosaccharide] and forms GlcNAc1-4(GlcNAc1-2)Man1-3 structure on the core oligosaccharide (Gn3(2,4,2)core oligosaccharide). In some members the conserved region occupies all but the very for N-terminal, where there is a signal sequence on all members. For other members the conserved region does not occupy the entire protein but is still to the N-terminus of the protein.


Pssm-ID: 461384  Cd Length: 278  Bit Score: 175.96  E-value: 7.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058   49 LTVGITSESREGPNGLLDTLASLYHTSSTSEQKQMTVLVHLADSDPTWLRRTIIRISSLYRSQILTGQLLLIHAPPDAYP 128
Cdd:pfam04666  35 LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAETDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  129 AV-NDAQNK---VSRGQIYSKQNVDHAFLMSFATKLSTYFLLIEDNVFCAPNFVNHIRSKVGYRKPNTWVLLEFSNMGFL 204
Cdd:pfam04666 115 NLkNLKKTFndsPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQLEDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  205 GKLLHSRDLPLLAHFLLLFHKERPLNWLLLHFRTLL--------------GQQSSILCRPFLFYHRLTHLTFENKtlIGH 270
Cdd:pfam04666 195 GKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKvcnpekdakhckrqKQNRRIRFRPSLFQHVGTYSSLEGK--IQD 272

                  ...
gi 223718058  271 EKD 273
Cdd:pfam04666 273 LKD 275
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
45-188 9.05e-06

Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4.


Pssm-ID: 409189  Cd Length: 364  Bit Score: 47.37  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  45 SQAWLTVGITSESREGPNGLLDTLASLYHTSSTSEQKQ--MTVLVHLADSDPTwlrrtiiRISSLYR-SQILtgqlllih 121
Cdd:cd21105   67 PKPDLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYsnVSLSICNTESPPA-------TFSELERlSELV-------- 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223718058 122 aPPDAyPAVNDAQNKVSRGQIYSKQNVDHAFLMSFATKL-STYFLLIEDNVFCAPNFVNHIRSKVGYR 188
Cdd:cd21105  132 -PVDS-IKRRLEEDKDDSSSWFRKETLDYAYCLRACTESgSRYTLLLEDDAIATPRFLQRLLSLLEDL 197
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
49-273 7.04e-52

N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of oligosaccharides are synthesized through elongation by glycosyltransferases after trimming of the precursor oligosaccharides transferred to proteins in the endoplasmic reticulum. N-Acetylglucosaminyltransferases (GnTs) take part in the formation of branches in the biosynthesis of complex-type sugar chains. In vertebrates, six GnTs, designated as GnT-I to -VI, which catalyze the transfer of GlcNAc to the core mannose residues of Asn-linked sugar chains, have been identified. GnT-IV (EC:2.4.1.145) catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAc1-2Man1-3 arm of core oligosaccharide [Gn2(22)core oligosaccharide] and forms GlcNAc1-4(GlcNAc1-2)Man1-3 structure on the core oligosaccharide (Gn3(2,4,2)core oligosaccharide). In some members the conserved region occupies all but the very for N-terminal, where there is a signal sequence on all members. For other members the conserved region does not occupy the entire protein but is still to the N-terminus of the protein.


Pssm-ID: 461384  Cd Length: 278  Bit Score: 175.96  E-value: 7.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058   49 LTVGITSESREGPNGLLDTLASLYHTSSTSEQKQMTVLVHLADSDPTWLRRTIIRISSLYRSQILTGQLLLIHAPPDAYP 128
Cdd:pfam04666  35 LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAETDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  129 AV-NDAQNK---VSRGQIYSKQNVDHAFLMSFATKLSTYFLLIEDNVFCAPNFVNHIRSKVGYRKPNTWVLLEFSNMGFL 204
Cdd:pfam04666 115 NLkNLKKTFndsPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQLEDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  205 GKLLHSRDLPLLAHFLLLFHKERPLNWLLLHFRTLL--------------GQQSSILCRPFLFYHRLTHLTFENKtlIGH 270
Cdd:pfam04666 195 GKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKvcnpekdakhckrqKQNRRIRFRPSLFQHVGTYSSLEGK--IQD 272

                  ...
gi 223718058  271 EKD 273
Cdd:pfam04666 273 LKD 275
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
45-188 9.05e-06

Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4.


Pssm-ID: 409189  Cd Length: 364  Bit Score: 47.37  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  45 SQAWLTVGITSESREGPNGLLDTLASLYHTSSTSEQKQ--MTVLVHLADSDPTwlrrtiiRISSLYR-SQILtgqlllih 121
Cdd:cd21105   67 PKPDLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYsnVSLSICNTESPPA-------TFSELERlSELV-------- 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223718058 122 aPPDAyPAVNDAQNKVSRGQIYSKQNVDHAFLMSFATKL-STYFLLIEDNVFCAPNFVNHIRSKVGYR 188
Cdd:cd21105  132 -PVDS-IKRRLEEDKDDSSSWFRKETLDYAYCLRACTESgSRYTLLLEDDAIATPRFLQRLLSLLEDL 197
PGAP4-like_fungal cd22189
uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This ...
51-171 7.20e-04

uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This subfamily contains uncharacterized fungal proteins with similarity to animal post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. Proteins from this subfamily contain the putative catalytic site of PGAP4 and may have similar activities.


Pssm-ID: 409190  Cd Length: 375  Bit Score: 41.76  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718058  51 VGITSESREGPNGLLDTLASLYHTSSTSEQKQMTVLVHLADSDPT--------WLRRtiirisslyrsqiLTGQLLLIHA 122
Cdd:cd22189   77 VGIPTVKRPGEQYLDTTVGSLLDGLTPEERADIHLVVLIAHTDPTqhpaygepWLHN-------------LADEVLTYNV 143
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223718058 123 PPDAYPAVNDAQNKvsRGQIYSKQNVDHAFLMS--FATKlSTYFLLIEDNV 171
Cdd:cd22189  144 SDEDLEHLRELEEE--GGNFREKGLFDYTYLLEacYETG-APYIAMFEDDV 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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