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Conserved domains on  [gi|111160385|ref|NP_171608|]
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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9 [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: ...
130-334 1.55e-39

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: 139.77  E-value: 1.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  130 ERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGAGSGGADEVGEGARThwrallraeslaYADILLWAFDDTFFNLTLKEI 209
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGRIKSLFLVGLSADTDGKVADLVMEEAKL------------YGDIVVVDFEDTYENLTFKTL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  210 HFLAWASAFCPDVRFVFKGDADVFVNVGNLLEFLAPR--DPAQDLLAGDVIVHARPIRTRASKYYIPEAVYGLPAYPAYA 287
Cdd:pfam01762  69 TGLLWAVSKCPSAKYIGKIDDDVYFFPDKLLSLLDNGniDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYA 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 111160385  288 GGGGFVLSGATLHRLAGACAQVELFPIDDVFLGMCLQRLRLTPEPHP 334
Cdd:pfam01762 149 SGPFYVLSRDAAEKLLKASKHRRFLQIEDVYVGILANDLGISRVNLP 195
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
130-334 1.55e-39

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: 139.77  E-value: 1.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  130 ERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGAGSGGADEVGEGARThwrallraeslaYADILLWAFDDTFFNLTLKEI 209
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGRIKSLFLVGLSADTDGKVADLVMEEAKL------------YGDIVVVDFEDTYENLTFKTL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  210 HFLAWASAFCPDVRFVFKGDADVFVNVGNLLEFLAPR--DPAQDLLAGDVIVHARPIRTRASKYYIPEAVYGLPAYPAYA 287
Cdd:pfam01762  69 TGLLWAVSKCPSAKYIGKIDDDVYFFPDKLLSLLDNGniDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYA 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 111160385  288 GGGGFVLSGATLHRLAGACAQVELFPIDDVFLGMCLQRLRLTPEPHP 334
Cdd:pfam01762 149 SGPFYVLSRDAAEKLLKASKHRRFLQIEDVYVGILANDLGISRVNLP 195
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
112-321 2.39e-14

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 74.84  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385 112 PGGRPDLLIAVKSVAEDFERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGagsggaDEVGEGarthwralLRAESLAYAD 191
Cdd:PLN03133 381 PKKPLDLFIGVFSTANNFKRRMAVRRTWMQYDAVRSGAVAVRFFVGLHKN------QMVNEE--------LWNEARTYGD 446
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385 192 ILLWAFDDTFFNLTLKEIHFLAW----ASAfcpdvRFVFKGDADVFVNVGNLLEFLAPRDPAQDLLAGDVIVHARPIRTR 267
Cdd:PLN03133 447 IQLMPFVDYYSLITWKTLAICIFgtevVSA-----KYVMKTDDDAFVRVDEVLASLKRTNVSHGLLYGLINSDSQPHRNP 521
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385 268 ASKYYIPEAVYGLPAYPAYAGGGGFVLSgatlHRLAGAC------AQVELFPIDDVFLGM 321
Cdd:PLN03133 522 DSKWYISPEEWPEETYPPWAHGPGYVVS----RDIAKEVykrhkeGRLKMFKLEDVAMGI 577
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
130-334 1.55e-39

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: 139.77  E-value: 1.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  130 ERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGAGSGGADEVGEGARThwrallraeslaYADILLWAFDDTFFNLTLKEI 209
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGRIKSLFLVGLSADTDGKVADLVMEEAKL------------YGDIVVVDFEDTYENLTFKTL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  210 HFLAWASAFCPDVRFVFKGDADVFVNVGNLLEFLAPR--DPAQDLLAGDVIVHARPIRTRASKYYIPEAVYGLPAYPAYA 287
Cdd:pfam01762  69 TGLLWAVSKCPSAKYIGKIDDDVYFFPDKLLSLLDNGniDPSESSFYGYVMEEGPVIRNKKSKWYVSPSDYKCSRYPPYA 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 111160385  288 GGGGFVLSGATLHRLAGACAQVELFPIDDVFLGMCLQRLRLTPEPHP 334
Cdd:pfam01762 149 SGPFYVLSRDAAEKLLKASKHRRFLQIEDVYVGILANDLGISRVNLP 195
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
112-321 2.39e-14

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 74.84  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385 112 PGGRPDLLIAVKSVAEDFERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGagsggaDEVGEGarthwralLRAESLAYAD 191
Cdd:PLN03133 381 PKKPLDLFIGVFSTANNFKRRMAVRRTWMQYDAVRSGAVAVRFFVGLHKN------QMVNEE--------LWNEARTYGD 446
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385 192 ILLWAFDDTFFNLTLKEIHFLAW----ASAfcpdvRFVFKGDADVFVNVGNLLEFLAPRDPAQDLLAGDVIVHARPIRTR 267
Cdd:PLN03133 447 IQLMPFVDYYSLITWKTLAICIFgtevVSA-----KYVMKTDDDAFVRVDEVLASLKRTNVSHGLLYGLINSDSQPHRNP 521
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385 268 ASKYYIPEAVYGLPAYPAYAGGGGFVLSgatlHRLAGAC------AQVELFPIDDVFLGM 321
Cdd:PLN03133 522 DSKWYISPEEWPEETYPPWAHGPGYVVS----RDIAKEVykrhkeGRLKMFKLEDVAMGI 577
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
116-332 1.86e-04

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: 42.69  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  116 PDLLIAVKSVAEdF--ERRQAVRQTWGAEGRVQgalvRRVFLLGVPRGAGSGGADEVG--EGARTHWRALLraeslayaD 191
Cdd:pfam02434   4 DDIFIAVKTTKK-FhkTRLPLLLKTWISRAKHQ----TYIFTDGEDEGLPTRTGGHLIntNCSAGHCRKAL--------S 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111160385  192 ILLWAFDDTFFNLTLKeihflaWasaFCpdvRFvfkgDADVFVNVGNLLEFLAPRDPAQDLLAGdvivharpirtRASKY 271
Cdd:pfam02434  71 CKMAVEYDRFLESGKK------W---FC---HV----DDDNYVNVPRLVRLLSCYNHTQDVYLG-----------KPSLY 123
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111160385  272 YIPEAVYGLPAYPA----YA-GGGGFVLSGATLHRLAG---------ACAQVELfPiDDVFLGMCLQRL---RLTPEP 332
Cdd:pfam02434 124 RPIEATERVKGNRKvgfwFAtGGAGFCISRGLALKMSPwasggrfmsTSEKIRL-P-DDCTLGYIIENLlgvPLTHSP 199
 
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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