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Conserved domains on  [gi|193785407|dbj|BAG54560|]
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unnamed protein product [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 ...
 64-330 9.84e-103

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: 308.08  E-value: 9.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407   64 LNSERYVHTFKDLSNFSGAINvtYRYLAATPLQRKRyLTIGLSSVKRKKGNYLLETIKSIFEQSSYEELKEISVVVHLAD 143
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAGRTGVS-LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  144 FNSSWRDAMVQDITQKFAHHIIAGRLMVIHAPEEYYPILDGLKRNYNDPEDRVKFRSKQNVDYAFLLNFCANTSDYYVML 223
Cdd:pfam04666  78 TDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  224 EDDVRCSKNFLTAIKKVIASLEGTYWVTLEFSKLGYIGKLYHSHDLPRLAHFLLMFYQEMPCDWLLTHFRGLLA------ 297
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVcnpekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 193785407  298 --------QKNVIRFKPSLFQHMGYYSSYKGTENKLKDVDF 330
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 ...
 64-330 9.84e-103

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: 308.08  E-value: 9.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407   64 LNSERYVHTFKDLSNFSGAINvtYRYLAATPLQRKRyLTIGLSSVKRKKGNYLLETIKSIFEQSSYEELKEISVVVHLAD 143
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAGRTGVS-LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  144 FNSSWRDAMVQDITQKFAHHIIAGRLMVIHAPEEYYPILDGLKRNYNDPEDRVKFRSKQNVDYAFLLNFCANTSDYYVML 223
Cdd:pfam04666  78 TDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  224 EDDVRCSKNFLTAIKKVIASLEGTYWVTLEFSKLGYIGKLYHSHDLPRLAHFLLMFYQEMPCDWLLTHFRGLLA------ 297
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVcnpekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 193785407  298 --------QKNVIRFKPSLFQHMGYYSSYKGTENKLKDVDF 330
Cdd:pfam04666 238 akhckrqkQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 29-267 9.61e-14

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: 72.41  E-value: 9.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  29 LGVLVIFLLFMNLYI--------EDSYVLEGDKQLIRetsthQLNSERYVHTFKDLSNFSgaiNVTYRYLAATPlqRKRY 100
Cdd:cd21105    1 LIVLAIIFLTLLFLVrlvsprlgHSVFFLASQELLLR-----RLEELRLAQALKLLESLK---NSSQALGFRLS--PKPD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407 101 LTIGLSSVKRKKGNYLLETIKSIFEQSSYEELKEISVVVHLADFNSswrdamvqditqKFAHHIIAGRLmvihapeeyYP 180
Cdd:cd21105   71 LCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNVSLSICNTES------------PPATFSELERL---------SE 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407 181 ILDGLKRNYNDPEDRVKFRS---KQNVDYAFLLNFCANT-SDYYVMLEDDVRCSKNFLTAIKKVIASLEGTYwvtlefSK 256
Cdd:cd21105  130 LVPVDSIKRRLEEDKDDSSSwfrKETLDYAYCLRACTESgSRYTLLLEDDAIATPRFLQRLLSLLEDLESPR------RK 203

                        250
                 ....*....|.
gi 193785407 257 LGYIgKLYHSH 267
Cdd:cd21105  204 WLFV-KLYYPE 213
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
 64-330 9.84e-103

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: 308.08  E-value: 9.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407   64 LNSERYVHTFKDLSNFSGAINvtYRYLAATPLQRKRyLTIGLSSVKRKKGNYLLETIKSIFEQSSYEELKEISVVVHLAD 143
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV--PAVLIGAGRTGVS-LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  144 FNSSWRDAMVQDITQKFAHHIIAGRLMVIHAPEEYYPILDGLKRNYNDPEDRVKFRSKQNVDYAFLLNFCANTSDYYVML 223
Cdd:pfam04666  78 TDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSYYPNLKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  224 EDDVRCSKNFLTAIKKVIASLEGTYWVTLEFSKLGYIGKLYHSHDLPRLAHFLLMFYQEMPCDWLLTHFRGLLA------ 297
Cdd:pfam04666 158 EDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDWLLDHFLALKVcnpekd 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 193785407  298 --------QKNVIRFKPSLFQHMGYYSSYKGTENKLKDVDF 330
Cdd:pfam04666 238 akhckrqkQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
 29-267 9.61e-14

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: 72.41  E-value: 9.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  29 LGVLVIFLLFMNLYI--------EDSYVLEGDKQLIRetsthQLNSERYVHTFKDLSNFSgaiNVTYRYLAATPlqRKRY 100
Cdd:cd21105    1 LIVLAIIFLTLLFLVrlvsprlgHSVFFLASQELLLR-----RLEELRLAQALKLLESLK---NSSQALGFRLS--PKPD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407 101 LTIGLSSVKRKKGNYLLETIKSIFEQSSYEELKEISVVVHLADFNSswrdamvqditqKFAHHIIAGRLmvihapeeyYP 180
Cdd:cd21105   71 LCIVIIAVNRRPHSYLTQTVASLLRGIQSDLASYSNVSLSICNTES------------PPATFSELERL---------SE 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407 181 ILDGLKRNYNDPEDRVKFRS---KQNVDYAFLLNFCANT-SDYYVMLEDDVRCSKNFLTAIKKVIASLEGTYwvtlefSK 256
Cdd:cd21105  130 LVPVDSIKRRLEEDKDDSSSwfrKETLDYAYCLRACTESgSRYTLLLEDDAIATPRFLQRLLSLLEDLESPR------RK 203

                        250
                 ....*....|.
gi 193785407 257 LGYIgKLYHSH 267
Cdd:cd21105  204 WLFV-KLYYPE 213
PGAP4-like_fungal cd22189
uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This ...
 103-227 9.61e-11

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: 63.33  E-value: 9.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407 103 IGLSSVKRKKGNYLLETIKSIFEQSSYEELKEISVVVHLAD--------FNSSWRDAMVQDITQkfahhiiagrlmviha 174
Cdd:cd22189   77 VGIPTVKRPGEQYLDTTVGSLLDGLTPEERADIHLVVLIAHtdptqhpaYGEPWLHNLADEVLT---------------- 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193785407 175 peeYYPILDGLKRNYNDPEDRVKFRSKQNVDYAFLLNFCANT-SDYYVMLEDDV 227
Cdd:cd22189  141 ---YNVSDEDLEHLRELEEEGGNFREKGLFDYTYLLEACYETgAPYIAMFEDDV 191
PGAP4 cd22190
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ...
 26-265 2.32e-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: 40.28  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407  26 VSFLGVLVIF---LLFMNLYIEDSYVLEGDKQLIREtsthqlNSERY---VHTFKDLSNfsgainvTYRYLAATPLQRKR 99
Cdd:cd22190   11 VTFLVILPLLchrLPFSYYYSRHLSLDDLSDKALQE------NDERGakaLQYFESLDP-------KSSSQFSPLEKQGK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407 100 -YLTIGLSSVKRKKGN----YLLETIKSiFEQSSYEELKEISVVVHLADFNSSWRDamvqditqkfahHIIAGRLmviha 174
Cdd:cd22190   78 pDLAVTIITVSRQSGTksphYLLQVVAR-LLRLLKECGLCNTTRLFICNVDSDPSS------------HEEAVFL----- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785407 175 pEEYYPILD-GLKRNYNDPEDRVKFrSKQNVDYAFLLNFCANT-SDYYVMLEDDVRCSKNFLTAIKKVIAS-LEGTYwvT 251
Cdd:cd22190  140 -SKYVPVVSrYGNEERSDVTSDNRF-EKEKQDYVFCLESSLKLnPKYVLLLEDDALPHPDFFPVLEHLLRYrLEKKY--T 215

                        250
                 ....*....|....
gi 193785407 252 LEFSKLGYIgKLYH 265
Cdd:cd22190  216 PNRRDWAYL-KLYH 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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