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Conserved domains on  [gi|237757320|ref|NP_776132|]
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uncharacterized protein LOC240755 [Mus musculus]

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 ...
64-326 1.63e-95

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: 289.59  E-value: 1.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320   64 SKIKNHLKYFTEMQESSHVLQhvtYTVLAGASYQPKRmLTVGIFSVPHSHRTHLLDTMTSLFQASSEQDLEYMLVLVLLS 143
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV---PAVLIGAGRTGVS-LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320  144 DTDPTWLNQTVANISGLFMPHIDSGRLLVVHGRLG-----GSRAKSRNDTSPCGKLYSRQKTSLALLMNFALNLSEYFLL 218
Cdd:pfam04666  77 ETDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSyypnlKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320  219 LGDNVKTAPKFLANVFWALPAWKQLPWVSLDFSSMPLSGKVFHTEDLSRFVSFLLLFPKDIPTH--------------LL 284
Cdd:pfam04666 157 LEDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDwlldhflalkvcnpEK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 237757320  285 LSEFRLLLSQNVPIRLSPSVFYRMDRDSEFEDTCFPAKRDKD 326
Cdd:pfam04666 237 DAKHCKRQKQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
64-326 1.63e-95

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: 289.59  E-value: 1.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320   64 SKIKNHLKYFTEMQESSHVLQhvtYTVLAGASYQPKRmLTVGIFSVPHSHRTHLLDTMTSLFQASSEQDLEYMLVLVLLS 143
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV---PAVLIGAGRTGVS-LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320  144 DTDPTWLNQTVANISGLFMPHIDSGRLLVVHGRLG-----GSRAKSRNDTSPCGKLYSRQKTSLALLMNFALNLSEYFLL 218
Cdd:pfam04666  77 ETDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSyypnlKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320  219 LGDNVKTAPKFLANVFWALPAWKQLPWVSLDFSSMPLSGKVFHTEDLSRFVSFLLLFPKDIPTH--------------LL 284
Cdd:pfam04666 157 LEDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDwlldhflalkvcnpEK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 237757320  285 LSEFRLLLSQNVPIRLSPSVFYRMDRDSEFEDTCFPAKRDKD 326
Cdd:pfam04666 237 DAKHCKRQKQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
 
Name Accession Description Interval E-value
Glyco_transf_54 pfam04666
N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region; The complex-type of ...
64-326 1.63e-95

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: 289.59  E-value: 1.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320   64 SKIKNHLKYFTEMQESSHVLQhvtYTVLAGASYQPKRmLTVGIFSVPHSHRTHLLDTMTSLFQASSEQDLEYMLVLVLLS 143
Cdd:pfam04666   1 SNATNILEHLPHLQKSSLPLV---PAVLIGAGRTGVS-LVLGIPTVKRSKKSYLLDTLLSLFSRMSPSEKKDCVVIVFVA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320  144 DTDPTWLNQTVANISGLFMPHIDSGRLLVVHGRLG-----GSRAKSRNDTSPCGKLYSRQKTSLALLMNFALNLSEYFLL 218
Cdd:pfam04666  77 ETDPNYVKQVVKNISTNFKEHIQSGLLEVISPPLSyypnlKNLKKTFNDSPKRVKWRTKQNLDYAFLMNYAQSKGTYYLQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757320  219 LGDNVKTAPKFLANVFWALPAWKQLPWVSLDFSSMPLSGKVFHTEDLSRFVSFLLLFPKDIPTH--------------LL 284
Cdd:pfam04666 157 LEDDVVAKPGFFTTIKNFARNWESLPWVFLEFSQLGFIGKLFRSPDLPRFVEFFLMFYKDKPIDwlldhflalkvcnpEK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 237757320  285 LSEFRLLLSQNVPIRLSPSVFYRMDRDSEFEDTCFPAKRDKD 326
Cdd:pfam04666 237 DAKHCKRQKQNRRIRFRPSLFQHVGTYSSLEGKIQDLKDKDF 278
 
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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