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Conserved domains on  [gi|17549992|ref|NP_509566|]
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Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase [Caenorhabditis elegans]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
1-441 0e+00

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member pfam03071:

Pssm-ID: 472172  Cd Length: 434  Bit Score: 732.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992     1 MHAVTKIFIIFIFVFILWTLYVEN-DITNRTRNTDNID---DLLESANRLERLLKFEAKKIAALAEDVHKIRANRKGkhV 76
Cdd:pfam03071   1 IPAAFMFIYIQMRLFQTWTQYADRlSSAIESENHDTSQmrgLIDEVAIKQSRIVALEDKMKNRQDEELVQLRDLIQT--F 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992    77 IMEEMVSQDLKQWKDPIPVLVFSCNRAMAVRDHVEKLIRYRPSQEKFPIIVTQDCDNENVKNEVKKFGDKVEYIKHLagD 156
Cdd:pfam03071  79 EKKGIAKLTQGGQMPVIPVLVMACSRADYVRRTVKKLLTYRPSAEKFPIIVSQDCSDEAVKSKSLSYGNQVTYIQHL--D 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   157 KANITIPPSHRQYTAYYRIARHYKLALNHVFVDKGYSSVIITEDDLDISPDFFSYFSSTRYLLENDEKLWCVTAWNDNGK 236
Cdd:pfam03071 157 FEPIVTPPGHRQLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   237 QENIDMTAASTLYRSDFFAGLGWMMSSKTWHELEPIWPVGFWDDWMRDPARRKDRQCIRPEISRTgmMSYGKEGASKGQF 316
Cdd:pfam03071 237 KQFVDDTAPYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRT--MNFGEHGSSLGQF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   317 FSKHLAKIKVNDKYINFGKIDLDYLLPANFAKKTNLEVmKEAVELSIDNVASFVLSseNKGkSVRVMYDGNIDYIRKADK 396
Cdd:pfam03071 315 FSQHLEPIKLNDVTVDFKAKDLGYLTEGNYTKYFSGLV-RQARPLQGSDVVLKAQN--IKG-DVRVRYKGQVEFERIAGE 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 17549992   397 LHIMHDFKAGVPRTAYDGIVTCFINGIRIYLVPDRTkVSAYNPDW 441
Cdd:pfam03071 391 LGIMEDWKDGVPRTAYKGIVTFRIQGRRVFLVPPDT-VMQYGPRW 434
 
Name Accession Description Interval E-value
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
1-441 0e+00

GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus.


Pssm-ID: 397273  Cd Length: 434  Bit Score: 732.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992     1 MHAVTKIFIIFIFVFILWTLYVEN-DITNRTRNTDNID---DLLESANRLERLLKFEAKKIAALAEDVHKIRANRKGkhV 76
Cdd:pfam03071   1 IPAAFMFIYIQMRLFQTWTQYADRlSSAIESENHDTSQmrgLIDEVAIKQSRIVALEDKMKNRQDEELVQLRDLIQT--F 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992    77 IMEEMVSQDLKQWKDPIPVLVFSCNRAMAVRDHVEKLIRYRPSQEKFPIIVTQDCDNENVKNEVKKFGDKVEYIKHLagD 156
Cdd:pfam03071  79 EKKGIAKLTQGGQMPVIPVLVMACSRADYVRRTVKKLLTYRPSAEKFPIIVSQDCSDEAVKSKSLSYGNQVTYIQHL--D 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   157 KANITIPPSHRQYTAYYRIARHYKLALNHVFVDKGYSSVIITEDDLDISPDFFSYFSSTRYLLENDEKLWCVTAWNDNGK 236
Cdd:pfam03071 157 FEPIVTPPGHRQLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   237 QENIDMTAASTLYRSDFFAGLGWMMSSKTWHELEPIWPVGFWDDWMRDPARRKDRQCIRPEISRTgmMSYGKEGASKGQF 316
Cdd:pfam03071 237 KQFVDDTAPYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRT--MNFGEHGSSLGQF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   317 FSKHLAKIKVNDKYINFGKIDLDYLLPANFAKKTNLEVmKEAVELSIDNVASFVLSseNKGkSVRVMYDGNIDYIRKADK 396
Cdd:pfam03071 315 FSQHLEPIKLNDVTVDFKAKDLGYLTEGNYTKYFSGLV-RQARPLQGSDVVLKAQN--IKG-DVRVRYKGQVEFERIAGE 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 17549992   397 LHIMHDFKAGVPRTAYDGIVTCFINGIRIYLVPDRTkVSAYNPDW 441
Cdd:pfam03071 391 LGIMEDWKDGVPRTAYKGIVTFRIQGRRVFLVPPDT-VMQYGPRW 434
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
92-432 0e+00

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 528.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992  92 PIPVLVFSCNRAMAVRDHVEKLIRYRPSQEKFPIIVTQDCDNENVKNEVKKFGDKVEYIKHLAGDKANITIPPshrQYTA 171
Cdd:cd02514   1 VIPVLVIACNRPDYLRRMLDSLLSYRPSAEKFPIIVSQDGGYEEVADVAKSFGDGVTHIQHPPISIKNVNPPH---KFQG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992 172 YYRIARHYKLALNHVFVDKGYSSVIITEDDLDISPDFFSYFSSTRYLLENDEKLWCVTAWNDNGKQENIDMTaASTLYRS 251
Cdd:cd02514  78 YYRIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDT-PSLLYRT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992 252 DFFAGLGWMMSSKTWHELEPIWPVGFWDDWMRDPARRKDRQCIRPEISRTGMMsyGKEGASKGQFFSKHLAKIKVNDKYI 331
Cdd:cd02514 157 DFFPGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHF--GKKGVSNGQFFDKYLKKIKLNTVFV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992 332 NFGKIDLDYLLPANFAKKTNLEVMKEAVELSIDNVaSFVLSSENKGKSVRVMYDGNIDYIRKADKLHIMHDFKAGVPRTA 411
Cdd:cd02514 235 VFTKLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNP-CELSFVPDTEGKVRVVYTGRDDFKTWAKAFGVMDDLKDGVPRTA 313
                       330       340
                ....*....|....*....|.
gi 17549992 412 YDGIVTCFINGIRIYLVPDRT 432
Cdd:cd02514 314 YKGIVRFFFKGNRVFLVPPPT 334
 
Name Accession Description Interval E-value
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
1-441 0e+00

GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus.


Pssm-ID: 397273  Cd Length: 434  Bit Score: 732.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992     1 MHAVTKIFIIFIFVFILWTLYVEN-DITNRTRNTDNID---DLLESANRLERLLKFEAKKIAALAEDVHKIRANRKGkhV 76
Cdd:pfam03071   1 IPAAFMFIYIQMRLFQTWTQYADRlSSAIESENHDTSQmrgLIDEVAIKQSRIVALEDKMKNRQDEELVQLRDLIQT--F 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992    77 IMEEMVSQDLKQWKDPIPVLVFSCNRAMAVRDHVEKLIRYRPSQEKFPIIVTQDCDNENVKNEVKKFGDKVEYIKHLagD 156
Cdd:pfam03071  79 EKKGIAKLTQGGQMPVIPVLVMACSRADYVRRTVKKLLTYRPSAEKFPIIVSQDCSDEAVKSKSLSYGNQVTYIQHL--D 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   157 KANITIPPSHRQYTAYYRIARHYKLALNHVFVDKGYSSVIITEDDLDISPDFFSYFSSTRYLLENDEKLWCVTAWNDNGK 236
Cdd:pfam03071 157 FEPIVTPPGHRQLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   237 QENIDMTAASTLYRSDFFAGLGWMMSSKTWHELEPIWPVGFWDDWMRDPARRKDRQCIRPEISRTgmMSYGKEGASKGQF 316
Cdd:pfam03071 237 KQFVDDTAPYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRT--MNFGEHGSSLGQF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992   317 FSKHLAKIKVNDKYINFGKIDLDYLLPANFAKKTNLEVmKEAVELSIDNVASFVLSseNKGkSVRVMYDGNIDYIRKADK 396
Cdd:pfam03071 315 FSQHLEPIKLNDVTVDFKAKDLGYLTEGNYTKYFSGLV-RQARPLQGSDVVLKAQN--IKG-DVRVRYKGQVEFERIAGE 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 17549992   397 LHIMHDFKAGVPRTAYDGIVTCFINGIRIYLVPDRTkVSAYNPDW 441
Cdd:pfam03071 391 LGIMEDWKDGVPRTAYKGIVTFRIQGRRVFLVPPDT-VMQYGPRW 434
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
92-432 0e+00

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 528.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992  92 PIPVLVFSCNRAMAVRDHVEKLIRYRPSQEKFPIIVTQDCDNENVKNEVKKFGDKVEYIKHLAGDKANITIPPshrQYTA 171
Cdd:cd02514   1 VIPVLVIACNRPDYLRRMLDSLLSYRPSAEKFPIIVSQDGGYEEVADVAKSFGDGVTHIQHPPISIKNVNPPH---KFQG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992 172 YYRIARHYKLALNHVFVDKGYSSVIITEDDLDISPDFFSYFSSTRYLLENDEKLWCVTAWNDNGKQENIDMTaASTLYRS 251
Cdd:cd02514  78 YYRIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDT-PSLLYRT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992 252 DFFAGLGWMMSSKTWHELEPIWPVGFWDDWMRDPARRKDRQCIRPEISRTGMMsyGKEGASKGQFFSKHLAKIKVNDKYI 331
Cdd:cd02514 157 DFFPGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHF--GKKGVSNGQFFDKYLKKIKLNTVFV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549992 332 NFGKIDLDYLLPANFAKKTNLEVMKEAVELSIDNVaSFVLSSENKGKSVRVMYDGNIDYIRKADKLHIMHDFKAGVPRTA 411
Cdd:cd02514 235 VFTKLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNP-CELSFVPDTEGKVRVVYTGRDDFKTWAKAFGVMDDLKDGVPRTA 313
                       330       340
                ....*....|....*....|.
gi 17549992 412 YDGIVTCFINGIRIYLVPDRT 432
Cdd:cd02514 314 YKGIVRFFFKGNRVFLVPPPT 334
 
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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