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Conserved domains on  [gi|544473480|ref|XP_005572543|]
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PREDICTED: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4 isoform X2 [Macaca fascicularis]

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: ...
132-321 2.25e-45

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: 154.40  E-value: 2.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  132 ERRAAIRSTWGRAGGWAKGRqLKLVFLLGVAGPAPP--AQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACP 209
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGR-IKSLFLVGLSADTDGkvADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  210 QAHFMLKGDDDVFVHIPNVLEFLDG--WDPAQDLLVGDVIRQALPNRNTKVKYFIPLSMYRATHYPPYAGGGGYVMSRAT 287
Cdd:pfam01762  80 SAKYIGKIDDDVYFFPDKLLSLLDNgnIDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDA 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 544473480  288 VRRLQATMEEAELFPIDDVFVGMCLRRLGLSPMH 321
Cdd:pfam01762 160 AEKLLKASKHRRFLQIEDVYVGILANDLGISRVN 193
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
132-321 2.25e-45

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: 154.40  E-value: 2.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  132 ERRAAIRSTWGRAGGWAKGRqLKLVFLLGVAGPAPP--AQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACP 209
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGR-IKSLFLVGLSADTDGkvADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  210 QAHFMLKGDDDVFVHIPNVLEFLDG--WDPAQDLLVGDVIRQALPNRNTKVKYFIPLSMYRATHYPPYAGGGGYVMSRAT 287
Cdd:pfam01762  80 SAKYIGKIDDDVYFFPDKLLSLLDNgnIDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDA 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 544473480  288 VRRLQATMEEAELFPIDDVFVGMCLRRLGLSPMH 321
Cdd:pfam01762 160 AEKLLKASKHRRFLQIEDVYVGILANDLGISRVN 193
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
120-360 4.78e-14

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 73.68  E-value: 4.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480 120 LLLAIKSQPGHVERRAAIRSTWGRAGGWAKGRqLKLVFLLGVAGPAPPAQLLAYESREFDDILQWDFTeDFFNLTLkelh 199
Cdd:PLN03133 387 LFIGVFSTANNFKRRMAVRRTWMQYDAVRSGA-VAVRFFVGLHKNQMVNEELWNEARTYGDIQLMPFV-DYYSLIT---- 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480 200 lqrW-VVAAC------PQAHFMLKGDDDVFVHIPNVLEFLDGWDPAQDLLVGDVIRQALPNRNTKVKYFIPLSMYRATHY 272
Cdd:PLN03133 461 ---WkTLAICifgtevVSAKYVMKTDDDAFVRVDEVLASLKRTNVSHGLLYGLINSDSQPHRNPDSKWYISPEEWPEETY 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480 273 PPYAGGGGYVMSRATVRRLQATMEEAEL--FPIDDVFVGMC---LRRLGL-------SPMHHAGFKTfgirqpldpldpc 340
Cdd:PLN03133 538 PPWAHGPGYVVSRDIAKEVYKRHKEGRLkmFKLEDVAMGIWiaeMKKEGLevkyendGRIYNEGCKD------------- 604
                        250       260
                 ....*....|....*....|
gi 544473480 341 lyrGLLLVHRLSPLEMWTMW 360
Cdd:PLN03133 605 ---GYVVAHYQSPREMLCLW 621
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
132-321 2.25e-45

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: 154.40  E-value: 2.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  132 ERRAAIRSTWGRAGGWAKGRqLKLVFLLGVAGPAPP--AQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACP 209
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGR-IKSLFLVGLSADTDGkvADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  210 QAHFMLKGDDDVFVHIPNVLEFLDG--WDPAQDLLVGDVIRQALPNRNTKVKYFIPLSMYRATHYPPYAGGGGYVMSRAT 287
Cdd:pfam01762  80 SAKYIGKIDDDVYFFPDKLLSLLDNgnIDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDA 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 544473480  288 VRRLQATMEEAELFPIDDVFVGMCLRRLGLSPMH 321
Cdd:pfam01762 160 AEKLLKASKHRRFLQIEDVYVGILANDLGISRVN 193
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
120-360 4.78e-14

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 73.68  E-value: 4.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480 120 LLLAIKSQPGHVERRAAIRSTWGRAGGWAKGRqLKLVFLLGVAGPAPPAQLLAYESREFDDILQWDFTeDFFNLTLkelh 199
Cdd:PLN03133 387 LFIGVFSTANNFKRRMAVRRTWMQYDAVRSGA-VAVRFFVGLHKNQMVNEELWNEARTYGDIQLMPFV-DYYSLIT---- 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480 200 lqrW-VVAAC------PQAHFMLKGDDDVFVHIPNVLEFLDGWDPAQDLLVGDVIRQALPNRNTKVKYFIPLSMYRATHY 272
Cdd:PLN03133 461 ---WkTLAICifgtevVSAKYVMKTDDDAFVRVDEVLASLKRTNVSHGLLYGLINSDSQPHRNPDSKWYISPEEWPEETY 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480 273 PPYAGGGGYVMSRATVRRLQATMEEAEL--FPIDDVFVGMC---LRRLGL-------SPMHHAGFKTfgirqpldpldpc 340
Cdd:PLN03133 538 PPWAHGPGYVVSRDIAKEVYKRHKEGRLkmFKLEDVAMGIWiaeMKKEGLevkyendGRIYNEGCKD------------- 604
                        250       260
                 ....*....|....*....|
gi 544473480 341 lyrGLLLVHRLSPLEMWTMW 360
Cdd:PLN03133 605 ---GYVVAHYQSPREMLCLW 621
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
201-325 1.02e-07

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: 52.32  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  201 QRWVVaacpqaHFmlkgDDDVFVHIPNVLEFLDGWDPAQDLLVGD-----VIR-QALPNRNTKVKYFIplsmyrAThypp 274
Cdd:pfam02434  85 KKWFC------HV----DDDNYVNVPRLVRLLSCYNHTQDVYLGKpslyrPIEaTERVKGNRKVGFWF------AT---- 144
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544473480  275 yaGGGGYVMSRATVRRLQAT------MEEAEL--FPiDDVFVGMCL-RRLGLSPMHHAGF 325
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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