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Conserved domains on  [gi|16915936|ref|NP_463459|]
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alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B isoform 2 [Homo sapiens]

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 ...
 125-402 1.05e-160

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: 459.08  E-value: 1.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   125 LHLPTVFHHLPHLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDS 204
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLVPAVLIGAGRTGVSLVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAETDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   205 QYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVRWRTKQNLDYCFLMMYAQSKGIYYVQLEDD 284
Cdd:pfam04666  81 NYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQLEDD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   285 IVAKPNYLSTMKNFALQQPSEDWMILEFSQLGFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKH 364
Cdd:pfam04666 161 VVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPEKDAKH 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 16915936   365 CDRQKANLRIRFKPSLFQHVGTHSSLAGKIQKLKDKDF 402
Cdd:pfam04666 241 CKRQKQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
 125-402 1.05e-160

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: 459.08  E-value: 1.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   125 LHLPTVFHHLPHLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDS 204
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLVPAVLIGAGRTGVSLVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAETDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   205 QYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVRWRTKQNLDYCFLMMYAQSKGIYYVQLEDD 284
Cdd:pfam04666  81 NYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQLEDD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   285 IVAKPNYLSTMKNFALQQPSEDWMILEFSQLGFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKH 364
Cdd:pfam04666 161 VVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPEKDAKH 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 16915936   365 CDRQKANLRIRFKPSLFQHVGTHSSLAGKIQKLKDKDF 402
Cdd:pfam04666 241 CKRQKQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 158-353 6.12e-09

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: 58.16  E-value: 6.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936 158 SVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDSqyTSAVTENIKALfpteihSGLLEVISPSPHFY 237
Cdd:cd21105  70 DLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNVSLSICNTES--PPATFSELERL------SELVPVDSIKRRLE 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936 238 PDFSRLRESFGdpkervrwrtKQNLDYCFLMMYA-QSKGIYYVQLEDDIVAKPNYLSTMKNFALQQ-------------- 302
Cdd:cd21105 142 EDKDDSSSWFR----------KETLDYAYCLRACtESGSRYTLLLEDDAIATPRFLQRLLSLLEDLesprrkwlfvklyy 211

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16915936 303 -------PSEDWMILEFSQLGFIGKMFKSLdLSLIVEFILMFYRDKPIDWLLDHILWV 353
Cdd:cd21105 212 peywrgfELYFPSILELVSLSVLAGLLTTL-LWLALLRRLRRPFPLRTNLILVFVLFL 268
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
 125-402 1.05e-160

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: 459.08  E-value: 1.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   125 LHLPTVFHHLPHLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDS 204
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLVPAVLIGAGRTGVSLVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAETDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   205 QYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVRWRTKQNLDYCFLMMYAQSKGIYYVQLEDD 284
Cdd:pfam04666  81 NYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQLEDD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936   285 IVAKPNYLSTMKNFALQQPSEDWMILEFSQLGFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKH 364
Cdd:pfam04666 161 VVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVCNPEKDAKH 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 16915936   365 CDRQKANLRIRFKPSLFQHVGTHSSLAGKIQKLKDKDF 402
Cdd:pfam04666 241 CKRQKQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 158-353 6.12e-09

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: 58.16  E-value: 6.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936 158 SVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDSqyTSAVTENIKALfpteihSGLLEVISPSPHFY 237
Cdd:cd21105  70 DLCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNVSLSICNTES--PPATFSELERL------SELVPVDSIKRRLE 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936 238 PDFSRLRESFGdpkervrwrtKQNLDYCFLMMYA-QSKGIYYVQLEDDIVAKPNYLSTMKNFALQQ-------------- 302
Cdd:cd21105 142 EDKDDSSSWFR----------KETLDYAYCLRACtESGSRYTLLLEDDAIATPRFLQRLLSLLEDLesprrkwlfvklyy 211

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16915936 303 -------PSEDWMILEFSQLGFIGKMFKSLdLSLIVEFILMFYRDKPIDWLLDHILWV 353
Cdd:cd21105 212 peywrgfELYFPSILELVSLSVLAGLLTTL-LWLALLRRLRRPFPLRTNLILVFVLFL 268
PGAP4-like_fungal cd22189
uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This ...
 162-310 1.30e-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: 53.71  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936 162 GIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDsqytsavtenikalfpteihsgllevisPSPHfyPDFS 241
Cdd:cd22189  78 GIPTVKRPGEQYLDTTVGSLLDGLTPEERADIHLVVLIAHTD----------------------------PTQH--PAYG 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16915936 242 R-----------LRESFGDPKERVR--------WRTKQNLDYCFLMMYAQSKGI-YYVQLEDDIVAKPN-YLSTMKnfAL 300
Cdd:cd22189 128 EpwlhnladevlTYNVSDEDLEHLReleeeggnFREKGLFDYTYLLEACYETGApYIAMFEDDVVAADGwYHRTLQ--AL 205

                       170
                ....*....|....*...
gi 16915936 301 QQ--------PSEDWMIL 310
Cdd:cd22189 206 RDierktarkGASDWLYL 223
 
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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