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Conserved domains on  [gi|21755075|dbj|BAC04622|]
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unnamed protein product [Homo sapiens]

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: ...
107-296 9.27e-46

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 pfam01762:

Pssm-ID: 473923 [Multi-domain]  Cd Length: 195  Bit Score: 154.79  E-value: 9.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   107 ERRAAIRSTWGRVGGWaRGQQLKLVFLLGVAGSAPP--AQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACP 184
Cdd:pfam01762   1 ARRNAIRKTWMNQGNS-EGGRIKSLFLVGLSADTDGkvADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   185 QAHFMLKGDDDVFVHVPNVLEFLDG--WDPAQDLLVGDVIRQALPNRNTKVKYFIPPSMYRATHYPPYAGGGGYVMSRAT 262
Cdd:pfam01762  80 SAKYIGKIDDDVYFFPDKLLSLLDNgnIDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDA 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 21755075   263 VRRLQAIMEDAELFPIDDVFVGMCLRRLGLSPMH 296
Cdd:pfam01762 160 AEKLLKASKHRRFLQIEDVYVGILANDLGISRVN 193
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
107-296 9.27e-46

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: 154.79  E-value: 9.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   107 ERRAAIRSTWGRVGGWaRGQQLKLVFLLGVAGSAPP--AQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACP 184
Cdd:pfam01762   1 ARRNAIRKTWMNQGNS-EGGRIKSLFLVGLSADTDGkvADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   185 QAHFMLKGDDDVFVHVPNVLEFLDG--WDPAQDLLVGDVIRQALPNRNTKVKYFIPPSMYRATHYPPYAGGGGYVMSRAT 262
Cdd:pfam01762  80 SAKYIGKIDDDVYFFPDKLLSLLDNgnIDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDA 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 21755075   263 VRRLQAIMEDAELFPIDDVFVGMCLRRLGLSPMH 296
Cdd:pfam01762 160 AEKLLKASKHRRFLQIEDVYVGILANDLGISRVN 193
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
95-349 2.33e-15

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 77.15  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   95 LLLAIKSQPGHVERRAAIRSTWGRVGGwARGQQLKLVFLLGVAGSAPPAQLLAYESREFDDILQWDFTeDFFNLTLkelh 174
Cdd:PLN03133 387 LFIGVFSTANNFKRRMAVRRTWMQYDA-VRSGAVAVRFFVGLHKNQMVNEELWNEARTYGDIQLMPFV-DYYSLIT---- 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075  175 lqrW-VVAAC------PQAHFMLKGDDDVFVHVPNVLEFLDGWDPAQDLLVGDVIRQALPNRNTKVKYFIPPSMYRATHY 247
Cdd:PLN03133 461 ---WkTLAICifgtevVSAKYVMKTDDDAFVRVDEVLASLKRTNVSHGLLYGLINSDSQPHRNPDSKWYISPEEWPEETY 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075  248 PPYAGGGGYVMSRATVRRLQAIMEDAEL--FPIDDVFVGMC---LRRLGL-------SPMHHAGFKTfgirrpldpldpc 315
Cdd:PLN03133 538 PPWAHGPGYVVSRDIAKEVYKRHKEGRLkmFKLEDVAMGIWiaeMKKEGLevkyendGRIYNEGCKD------------- 604
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 21755075  316 lyrGLLLVHRLSPLEMWTMW-ALVTDEGLKCAAGP 349
Cdd:PLN03133 605 ---GYVVAHYQSPREMLCLWqKLQEGKRATCCGEW 636
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
107-296 9.27e-46

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: 154.79  E-value: 9.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   107 ERRAAIRSTWGRVGGWaRGQQLKLVFLLGVAGSAPP--AQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACP 184
Cdd:pfam01762   1 ARRNAIRKTWMNQGNS-EGGRIKSLFLVGLSADTDGkvADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   185 QAHFMLKGDDDVFVHVPNVLEFLDG--WDPAQDLLVGDVIRQALPNRNTKVKYFIPPSMYRATHYPPYAGGGGYVMSRAT 262
Cdd:pfam01762  80 SAKYIGKIDDDVYFFPDKLLSLLDNgnIDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDA 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 21755075   263 VRRLQAIMEDAELFPIDDVFVGMCLRRLGLSPMH 296
Cdd:pfam01762 160 AEKLLKASKHRRFLQIEDVYVGILANDLGISRVN 193
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
95-349 2.33e-15

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 77.15  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   95 LLLAIKSQPGHVERRAAIRSTWGRVGGwARGQQLKLVFLLGVAGSAPPAQLLAYESREFDDILQWDFTeDFFNLTLkelh 174
Cdd:PLN03133 387 LFIGVFSTANNFKRRMAVRRTWMQYDA-VRSGAVAVRFFVGLHKNQMVNEELWNEARTYGDIQLMPFV-DYYSLIT---- 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075  175 lqrW-VVAAC------PQAHFMLKGDDDVFVHVPNVLEFLDGWDPAQDLLVGDVIRQALPNRNTKVKYFIPPSMYRATHY 247
Cdd:PLN03133 461 ---WkTLAICifgtevVSAKYVMKTDDDAFVRVDEVLASLKRTNVSHGLLYGLINSDSQPHRNPDSKWYISPEEWPEETY 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075  248 PPYAGGGGYVMSRATVRRLQAIMEDAEL--FPIDDVFVGMC---LRRLGL-------SPMHHAGFKTfgirrpldpldpc 315
Cdd:PLN03133 538 PPWAHGPGYVVSRDIAKEVYKRHKEGRLkmFKLEDVAMGIWiaeMKKEGLevkyendGRIYNEGCKD------------- 604
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 21755075  316 lyrGLLLVHRLSPLEMWTMW-ALVTDEGLKCAAGP 349
Cdd:PLN03133 605 ---GYVVAHYQSPREMLCLWqKLQEGKRATCCGEW 636
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
176-300 7.73e-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: 55.79  E-value: 7.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   176 QRWVVaacpqaHFmlkgDDDVFVHVPNVLEFLDGWDPAQDLLVGD-----VIR-QALPNRNTKVKYFIppsmyrAThypp 249
Cdd:pfam02434  85 KKWFC------HV----DDDNYVNVPRLVRLLSCYNHTQDVYLGKpslyrPIEaTERVKGNRKVGFWF------AT---- 144
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755075   250 yaGGGGYVMSRATVRRLQAI------MEDAEL--FPiDDVFVGMCL-RRLGLSPMHHAGF 300
Cdd:pfam02434 145 --GGAGFCISRGLALKMSPWasggrfMSTSEKirLP-DDCTLGYIIeNLLGVPLTHSPLF 201
 
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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