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Conserved domains on  [gi|124487081|ref|NP_001074673|]
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beta-1,3-glucosyltransferase precursor [Mus musculus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 229488)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Galactosyl_T super family cl21608
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 255-457 1.05e-76

Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2.


The actual alignment was detected with superfamily member pfam02434:

Pssm-ID: 473923  Cd Length: 248  Bit Score: 240.68  E-value: 1.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081  255 VKKEEIFVAVKTCKKFHADRIPIVKKTWAAQASLIEY-YSDYAETAIPTV---DLGIPNTDRGHCGKTFAIL-----EKF 325
Cdd:pfam02434   1 TELDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYiFTDGEDEGLPTRtggHLINTNCSAGHCRKALSCKmaveyDRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081  326 LNhshNKISWLVIVDDDTLISISRLRHLLSCYDSSDPVFLGER----------YGYGLGTGGYSYVTGGGGMVFSREAIR 395
Cdd:pfam02434  81 LE---SGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpieateRVKGNRKVGFWFATGGAGFCISRGLAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487081  396 RLL--VSSCRCYSNDA----PDDMVLGMCFSG-LGVPVTHSPLFHQARPV--DYPKDYLAHQIPVSFHKHW 457
Cdd:pfam02434 158 KMSpwASGGRFMSTSEkirlPDDCTLGYIIENlLGVPLTHSPLFHSHLENlqDLPPETLHEQVTLSYGKFW 228
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 255-457 1.05e-76

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 240.68  E-value: 1.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081  255 VKKEEIFVAVKTCKKFHADRIPIVKKTWAAQASLIEY-YSDYAETAIPTV---DLGIPNTDRGHCGKTFAIL-----EKF 325
Cdd:pfam02434   1 TELDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYiFTDGEDEGLPTRtggHLINTNCSAGHCRKALSCKmaveyDRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081  326 LNhshNKISWLVIVDDDTLISISRLRHLLSCYDSSDPVFLGER----------YGYGLGTGGYSYVTGGGGMVFSREAIR 395
Cdd:pfam02434  81 LE---SGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpieateRVKGNRKVGFWFATGGAGFCISRGLAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487081  396 RLL--VSSCRCYSNDA----PDDMVLGMCFSG-LGVPVTHSPLFHQARPV--DYPKDYLAHQIPVSFHKHW 457
Cdd:pfam02434 158 KMSpwASGGRFMSTSEkirlPDDCTLGYIIENlLGVPLTHSPLFHSHLENlqDLPPETLHEQVTLSYGKFW 228
PLN03153 PLN03153
hypothetical protein; Provisional
 333-434 1.13e-06

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 51.07  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081 333 ISWLVIVDDDTLISISRLRHLLSCYDSSDPVFLG--ERYGYGLGTGGYSYVTGGGGMVFSR---EAIRRLLVSSCRCYSN 407
Cdd:PLN03153 211 VRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGgpSESHSANSYFSHNMAFGGGGIAISYplaEALSRILDDCLDRYPK 290

                         90       100
                 ....*....|....*....|....*..
gi 124487081 408 DAPDDMVLGMCFSGLGVPVTHSPLFHQ 434
Cdd:PLN03153 291 LYGSDDRLHACITELGVPLSREPGFHQ 317
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 255-457 1.05e-76

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 240.68  E-value: 1.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081  255 VKKEEIFVAVKTCKKFHADRIPIVKKTWAAQASLIEY-YSDYAETAIPTV---DLGIPNTDRGHCGKTFAIL-----EKF 325
Cdd:pfam02434   1 TELDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYiFTDGEDEGLPTRtggHLINTNCSAGHCRKALSCKmaveyDRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081  326 LNhshNKISWLVIVDDDTLISISRLRHLLSCYDSSDPVFLGER----------YGYGLGTGGYSYVTGGGGMVFSREAIR 395
Cdd:pfam02434  81 LE---SGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpieateRVKGNRKVGFWFATGGAGFCISRGLAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487081  396 RLL--VSSCRCYSNDA----PDDMVLGMCFSG-LGVPVTHSPLFHQARPV--DYPKDYLAHQIPVSFHKHW 457
Cdd:pfam02434 158 KMSpwASGGRFMSTSEkirlPDDCTLGYIIENlLGVPLTHSPLFHSHLENlqDLPPETLHEQVTLSYGKFW 228
PLN03153 PLN03153
hypothetical protein; Provisional
 333-434 1.13e-06

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 51.07  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487081 333 ISWLVIVDDDTLISISRLRHLLSCYDSSDPVFLG--ERYGYGLGTGGYSYVTGGGGMVFSR---EAIRRLLVSSCRCYSN 407
Cdd:PLN03153 211 VRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGgpSESHSANSYFSHNMAFGGGGIAISYplaEALSRILDDCLDRYPK 290

                         90       100
                 ....*....|....*....|....*..
gi 124487081 408 DAPDDMVLGMCFSGLGVPVTHSPLFHQ 434
Cdd:PLN03153 291 LYGSDDRLHACITELGVPLSREPGFHQ 317
 
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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