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Conserved domains on  [gi|116007095|ref|NP_001033980|]
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uncharacterized protein Dmel_CG34057, isoform A [Drosophila melanogaster]

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: ...
 93-243 1.79e-09

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: 57.71  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007095   93 HATKAALVNRTWGARCNKLIFMSSQTD---------SNLNILQINKSESRKNLYAKvrtgMAYVHKHYLNEY-DWFLKAD 162
Cdd:pfam02434  17 HKTRLPLLLKTWISRAKHQTYIFTDGEdeglptrtgGHLINTNCSAGHCRKALSCK----MAVEYDRFLESGkKWFCHVD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007095  163 DDTYIVMENLRLFLYPYDPESSVYFGCR-----FKAYFSQG--------YMSGGGGYVLSRDALRRLNLFALNS--TTIC 227
Cdd:pfam02434  93 DDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGGrfMSTS 172

                         170
                  ....*....|....*.
gi 116007095  228 KLNGESEDVQIGHCLQ 243
Cdd:pfam02434 173 EKIRLPDDCTLGYIIE 188
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 93-243 1.79e-09

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: 57.71  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007095   93 HATKAALVNRTWGARCNKLIFMSSQTD---------SNLNILQINKSESRKNLYAKvrtgMAYVHKHYLNEY-DWFLKAD 162
Cdd:pfam02434  17 HKTRLPLLLKTWISRAKHQTYIFTDGEdeglptrtgGHLINTNCSAGHCRKALSCK----MAVEYDRFLESGkKWFCHVD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007095  163 DDTYIVMENLRLFLYPYDPESSVYFGCR-----FKAYFSQG--------YMSGGGGYVLSRDALRRLNLFALNS--TTIC 227
Cdd:pfam02434  93 DDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGGrfMSTS 172

                         170
                  ....*....|....*.
gi 116007095  228 KLNGESEDVQIGHCLQ 243
Cdd:pfam02434 173 EKIRLPDDCTLGYIIE 188
PLN03153 PLN03153
hypothetical protein; Provisional
 152-209 4.85e-04

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 41.82  E-value: 4.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007095 152 LNEYDWFLKADDDTYIVMENLRLFLYPYDPESSVYFGCRFKA-----YFSQGYMSGGGGYVLS 209
Cdd:PLN03153 208 LPDVRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSEShsansYFSHNMAFGGGGIAIS 270
 
Name Accession Description Interval E-value
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 93-243 1.79e-09

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: 57.71  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007095   93 HATKAALVNRTWGARCNKLIFMSSQTD---------SNLNILQINKSESRKNLYAKvrtgMAYVHKHYLNEY-DWFLKAD 162
Cdd:pfam02434  17 HKTRLPLLLKTWISRAKHQTYIFTDGEdeglptrtgGHLINTNCSAGHCRKALSCK----MAVEYDRFLESGkKWFCHVD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007095  163 DDTYIVMENLRLFLYPYDPESSVYFGCR-----FKAYFSQG--------YMSGGGGYVLSRDALRRLNLFALNS--TTIC 227
Cdd:pfam02434  93 DDNYVNVPRLVRLLSCYNHTQDVYLGKPslyrpIEATERVKgnrkvgfwFATGGAGFCISRGLALKMSPWASGGrfMSTS 172

                         170
                  ....*....|....*.
gi 116007095  228 KLNGESEDVQIGHCLQ 243
Cdd:pfam02434 173 EKIRLPDDCTLGYIIE 188
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 124-247 2.26e-07

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.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 50.40  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007095  124 ILQINKSESRKNLYAKVRTGMAYVHKhYLNEYDWFLKADDDTYIVMENLRLFL--YPYDP-ESSVYFGCrFKAY------ 194
Cdd:pfam01762  51 IVVVDFEDTYENLTFKTLTGLLWAVS-KCPSAKYIGKIDDDVYFFPDKLLSLLdnGNIDPsESSFYGYV-MEEGpvirnk 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116007095  195 FSQGYMS-------------GGGGYVLSRDALRRLNLFALNSTTIcklngESEDVQIGHCLQDVGV 247
Cdd:pfam01762 129 KSKWYVSpsdykcsryppyaSGPFYVLSRDAAEKLLKASKHRRFL-----QIEDVYVGILANDLGI 189
PLN03153 PLN03153
hypothetical protein; Provisional
 152-209 4.85e-04

hypothetical protein; Provisional


Pssm-ID: 215605 [Multi-domain]  Cd Length: 537  Bit Score: 41.82  E-value: 4.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007095 152 LNEYDWFLKADDDTYIVMENLRLFLYPYDPESSVYFGCRFKA-----YFSQGYMSGGGGYVLS 209
Cdd:PLN03153 208 LPDVRWFVLGDDDTIFNADNLVAVLSKYDPSEMVYVGGPSEShsansYFSHNMAFGGGGIAIS 270
 
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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