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Conserved domains on  [gi|1035232642|ref|XP_016886444|]
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alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C isoform X1 [Cynoglossus semilaevis]

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 ...
 87-351 1.95e-94

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: 287.67  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642  87 PSSERYVHTFRDLSNFSGTINvtYRYLAGTPlHRKKYLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLAD 166
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAG-RTGVSLVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 167 FDL*****--*******AHHIIAGRLLVIQAPEEFYPSLDGLKRNYNDPEDRVRFRSKQNVDYAFLLNFCTNLSHFYMML 244
Cdd:pfam04666  78 TDPNYVKQvvKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 245 EDDVRCSKNFLTALKKVVTSRDGSYWVMLEFSKLGYIGKLYHSRDLPRLAHFLLMFYQEMPCDWLLIHFRGLLAQKD--- 321
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1035232642 322 -----------VIRFKPSLFQHMGYYSSYKGAENKLKDDDF 351
Cdd:pfam04666 238 akhckrqkqnrRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
 87-351 1.95e-94

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: 287.67  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642  87 PSSERYVHTFRDLSNFSGTINvtYRYLAGTPlHRKKYLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLAD 166
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAG-RTGVSLVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 167 FDL*****--*******AHHIIAGRLLVIQAPEEFYPSLDGLKRNYNDPEDRVRFRSKQNVDYAFLLNFCTNLSHFYMML 244
Cdd:pfam04666  78 TDPNYVKQvvKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 245 EDDVRCSKNFLTALKKVVTSRDGSYWVMLEFSKLGYIGKLYHSRDLPRLAHFLLMFYQEMPCDWLLIHFRGLLAQKD--- 321
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1035232642 322 -----------VIRFKPSLFQHMGYYSSYKGAENKLKDDDF 351
Cdd:pfam04666 238 akhckrqkqnrRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 81-286 2.69e-11

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: 65.09  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642  81 EASVHTPSSERYVHTFRDLSNFSgtiNVTYRYLAGTPlhRKKYLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVV 160
Cdd:cd21105    33 ELLLRRLEELRLAQALKLLESLK---NSSQALGFRLS--PKPDLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 161 VVHLADFDL************ahhiiagrllviqapEEFYPSLDGLKRNYNDPEDRVRFRS---KQNVDYAFLLNFCTNL 237
Cdd:cd21105   108 SLSICNTESPPATFSEL-------------------ERLSELVPVDSIKRRLEEDKDDSSSwfrKETLDYAYCLRACTES 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035232642 238 -SHFYMMLEDDVRCSKNFLTALKKVVTSRDGS--YWVMLefsklgyigKLYH 286
Cdd:cd21105   169 gSRYTLLLEDDAIATPRFLQRLLSLLEDLESPrrKWLFV---------KLYY 211
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
 87-351 1.95e-94

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: 287.67  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642  87 PSSERYVHTFRDLSNFSGTINvtYRYLAGTPlHRKKYLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLAD 166
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAG-RTGVSLVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 167 FDL*****--*******AHHIIAGRLLVIQAPEEFYPSLDGLKRNYNDPEDRVRFRSKQNVDYAFLLNFCTNLSHFYMML 244
Cdd:pfam04666  78 TDPNYVKQvvKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 245 EDDVRCSKNFLTALKKVVTSRDGSYWVMLEFSKLGYIGKLYHSRDLPRLAHFLLMFYQEMPCDWLLIHFRGLLAQKD--- 321
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1035232642 322 -----------VIRFKPSLFQHMGYYSSYKGAENKLKDDDF 351
Cdd:pfam04666 238 akhckrqkqnrRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 81-286 2.69e-11

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: 65.09  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642  81 EASVHTPSSERYVHTFRDLSNFSgtiNVTYRYLAGTPlhRKKYLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVV 160
Cdd:cd21105    33 ELLLRRLEELRLAQALKLLESLK---NSSQALGFRLS--PKPDLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 161 VVHLADFDL************ahhiiagrllviqapEEFYPSLDGLKRNYNDPEDRVRFRS---KQNVDYAFLLNFCTNL 237
Cdd:cd21105   108 SLSICNTESPPATFSEL-------------------ERLSELVPVDSIKRRLEEDKDDSSSwfrKETLDYAYCLRACTES 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035232642 238 -SHFYMMLEDDVRCSKNFLTALKKVVTSRDGS--YWVMLefsklgyigKLYH 286
Cdd:cd21105   169 gSRYTLLLEDDAIATPRFLQRLLSLLEDLESPrrKWLFV---------KLYY 211
PGAP4-like_fungal cd22189
uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This ...
 126-248 2.06e-07

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: 52.93  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 126 IGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLADFDl************AH--------HIIAGRLLViqape 197
Cdd:cd22189    77 VGIPTVKRPGEQYLDTTVGSLLDGLTPEERADIHLVVLIAHTD-----------PTQHpaygepwlHNLADEVLT----- 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1035232642 198 efYP-SLDGLKRNYNDPEDRVRFRSKQNVDYAFLLNFC--TNLSHFyMMLEDDV 248
Cdd:cd22189   141 --YNvSDEDLEHLRELEEEGGNFREKGLFDYTYLLEACyeTGAPYI-AMFEDDV 191
PGAP4 cd22190
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ...
 207-286 4.90e-03

Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), 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 (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains.


Pssm-ID: 409191  Cd Length: 379  Bit Score: 39.12  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035232642 207 KRNYNDPEDRVRFrSKQNVDYAFLLNFCTNL-SHFYMMLEDDVRCSKNFLTALKKVVTSRdGSYWVMLEFSKLGYIgKLY 285
Cdd:cd22190   151 NEERSDVTSDNRF-EKEKQDYVFCLESSLKLnPKYVLLLEDDALPHPDFFPVLEHLLRYR-LEKKYTPNRRDWAYL-KLY 227


                  .
gi 1035232642 286 H 286
Cdd:cd22190   228 H 228
 
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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