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Conserved domains on  [gi|961931715|ref|XP_014864108|]
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PREDICTED: alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C [Poecilia mexicana]

Protein Classification

glycosyltransferase family 54 protein( domain architecture ID 10519914)

glycosyltransferase family 54 protein similar to alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
 58-324 1.24e-100

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: 302.69  E-value: 1.24e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715   58 PSSERYAHTFRDLSNFSGTINvtYRYLAGTPLNRKKFlTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLAD 137
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAGRTGVSL-VLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  138 FDLVWCENVVQEITRKFAHHIIAGRLLVIQAPEEFYPSLDGLKRNYNDPEDRVRFRSKQNVDYAFLLNFCTNLSHFYMML 217
Cdd:pfam04666  78 TDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  218 EDDVRCSRNFLTALKKVITSREGSYWVMMEFSKLGYIGKLYHSRDLPRLAHFLLMFYQEMPCDWLLIHFRGLLAQKD--- 294
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 961931715  295 -----------VIRFKPSLFQHMGYYSSYKGVENKLKDDDF 324
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 ...
 58-324 1.24e-100

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: 302.69  E-value: 1.24e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715   58 PSSERYAHTFRDLSNFSGTINvtYRYLAGTPLNRKKFlTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLAD 137
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAGRTGVSL-VLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  138 FDLVWCENVVQEITRKFAHHIIAGRLLVIQAPEEFYPSLDGLKRNYNDPEDRVRFRSKQNVDYAFLLNFCTNLSHFYMML 217
Cdd:pfam04666  78 TDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  218 EDDVRCSRNFLTALKKVITSREGSYWVMMEFSKLGYIGKLYHSRDLPRLAHFLLMFYQEMPCDWLLIHFRGLLAQKD--- 294
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 961931715  295 -----------VIRFKPSLFQHMGYYSSYKGVENKLKDDDF 324
Cdd:pfam04666 238 akhckrqkqnrRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 52-259 3.58e-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: 64.71  E-value: 3.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  52 EASVHPPSSERYAHTFRDLSNFSgtiNVTYRYLAGTPlnRKKFLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVV 131
Cdd:cd21105   33 ELLLRRLEELRLAQALKLLESLK---NSSQALGFRLS--PKPDLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715 132 VVHLADFDLvwCENVVQEItrkfahhiiagrllviqapEEFYPSLDGLKRNYNDPEDRVRFRS---KQNVDYAFLLNFCT 208
Cdd:cd21105  108 SLSICNTES--PPATFSEL-------------------ERLSELVPVDSIKRRLEEDKDDSSSwfrKETLDYAYCLRACT 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961931715 209 NL-SHFYMMLEDDVRCSRNFLTALKKVITSREGSYwvmmefSKLGYIgKLYH 259
Cdd:cd21105  167 ESgSRYTLLLEDDAIATPRFLQRLLSLLEDLESPR------RKWLFV-KLYY 211
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
 58-324 1.24e-100

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: 302.69  E-value: 1.24e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715   58 PSSERYAHTFRDLSNFSGTINvtYRYLAGTPLNRKKFlTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLAD 137
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAGRTGVSL-VLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  138 FDLVWCENVVQEITRKFAHHIIAGRLLVIQAPEEFYPSLDGLKRNYNDPEDRVRFRSKQNVDYAFLLNFCTNLSHFYMML 217
Cdd:pfam04666  78 TDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  218 EDDVRCSRNFLTALKKVITSREGSYWVMMEFSKLGYIGKLYHSRDLPRLAHFLLMFYQEMPCDWLLIHFRGLLAQKD--- 294
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 961931715  295 -----------VIRFKPSLFQHMGYYSSYKGVENKLKDDDF 324
Cdd:pfam04666 238 akhckrqkqnrRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 52-259 3.58e-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: 64.71  E-value: 3.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  52 EASVHPPSSERYAHTFRDLSNFSgtiNVTYRYLAGTPlnRKKFLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVV 131
Cdd:cd21105   33 ELLLRRLEELRLAQALKLLESLK---NSSQALGFRLS--PKPDLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715 132 VVHLADFDLvwCENVVQEItrkfahhiiagrllviqapEEFYPSLDGLKRNYNDPEDRVRFRS---KQNVDYAFLLNFCT 208
Cdd:cd21105  108 SLSICNTES--PPATFSEL-------------------ERLSELVPVDSIKRRLEEDKDDSSSwfrKETLDYAYCLRACT 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961931715 209 NL-SHFYMMLEDDVRCSRNFLTALKKVITSREGSYwvmmefSKLGYIgKLYH 259
Cdd:cd21105  167 ESgSRYTLLLEDDAIATPRFLQRLLSLLEDLESPR------RKWLFV-KLYY 211
PGAP4-like_fungal cd22189
uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This ...
 64-221 7.19e-09

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: 57.56  E-value: 7.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715  64 AHTFrdLSNFSGTINVTYRYLAGTPlnrkKFLTIGLSSVKRKRGNYLLETIKSIFDQSSYEELKEIVVVVHLAD------ 137
Cdd:cd22189   50 ADAF--IDSANATPPPPNSTKAGSN----PSLCVGIPTVKRPGEQYLDTTVGSLLDGLTPEERADIHLVVLIAHtdptqh 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715 138 --FDLVWCENVVQEI-TRKfahhiiagrllVIQAPEEFYPSLDGLKRNYNDpedrvrfrsKQNVDYAFLLNFC--TNLSH 212
Cdd:cd22189  124 paYGEPWLHNLADEVlTYN-----------VSDEDLEHLRELEEEGGNFRE---------KGLFDYTYLLEACyeTGAPY 183


                 ....*....
gi 961931715 213 FyMMLEDDV 221
Cdd:cd22189  184 I-AMFEDDV 191
PGAP4 cd22190
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ...
 180-259 1.10e-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: 41.05  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961931715 180 KRNYNDPEDRVRFrSKQNVDYAFLLNFCTNL-SHFYMMLEDDVRCSRNFLTALKKVITSReGSYWVMMEFSKLGYIgKLY 258
Cdd:cd22190  151 NEERSDVTSDNRF-EKEKQDYVFCLESSLKLnPKYVLLLEDDALPHPDFFPVLEHLLRYR-LEKKYTPNRRDWAYL-KLY 227


                 .
gi 961931715 259 H 259
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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