NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1585744623|ref|XP_028068180|]
View 

alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase-like isoform X3 [Camellia sinensis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
2-357 1.44e-156

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: 446.66  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623   2 DQISIQKGRIVTLEEgNGLEKIIDKVQAPVAAVVVMACNRANYLERALKSILkfsrHQSSVPSKYPLFVSQDAEDPDVKS 81
Cdd:pfam03071  66 EELVQLRDLIQTFEK-KGIAKLTQGGQMPVIPVLVMACSRADYVRRTVKKLL----TYRPSAEKFPIIVSQDCSDEAVKS 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623  82 KALCY-NQLTYMQHLDHEPVHTERPE-EMIVYYKIARHYKWALDQLFYKHNFSRVIILEDDMEISPDFFDYFEAAVALLE 159
Cdd:pfam03071 141 KSLSYgNQVTYIQHLDFEPIVTPPGHrQLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLD 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 160 SDKSIMAVSSWNDNGQKQFVQD--PYMLYRSDFFPGLGWMLAKSTWDELSPKWTKAYWDDWLRLKETHKGRQFIRPEVCR 237
Cdd:pfam03071 221 RDKTLWCVSAWNDNGKKQFVDDtaPYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISR 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 238 TYNFGEHGSSLGQYFKQYLEPIKLNGV-------------QDKYVKHFADMVKNARPVCGTDDVLKECNIDCDVRIQYKD 304
Cdd:pfam03071 301 TMNFGEHGSSLGQFFSQHLEPIKLNDVtvdfkakdlgyltEGNYTKYFSGLVRQARPLQGSDVVLKAQNIKGDVRVRYKG 380
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1585744623 305 KTDFEHIARQFGIFEEWEDGVPRTAYKGVVVFRYQSpKRVFLVGPESLQHLGI 357
Cdd:pfam03071 381 QVEFERIAGELGIMEDWKDGVPRTAYKGIVTFRIQG-RRVFLVPPDTVMQYGP 432
 
Name Accession Description Interval E-value
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
2-357 1.44e-156

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: 446.66  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623   2 DQISIQKGRIVTLEEgNGLEKIIDKVQAPVAAVVVMACNRANYLERALKSILkfsrHQSSVPSKYPLFVSQDAEDPDVKS 81
Cdd:pfam03071  66 EELVQLRDLIQTFEK-KGIAKLTQGGQMPVIPVLVMACSRADYVRRTVKKLL----TYRPSAEKFPIIVSQDCSDEAVKS 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623  82 KALCY-NQLTYMQHLDHEPVHTERPE-EMIVYYKIARHYKWALDQLFYKHNFSRVIILEDDMEISPDFFDYFEAAVALLE 159
Cdd:pfam03071 141 KSLSYgNQVTYIQHLDFEPIVTPPGHrQLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLD 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 160 SDKSIMAVSSWNDNGQKQFVQD--PYMLYRSDFFPGLGWMLAKSTWDELSPKWTKAYWDDWLRLKETHKGRQFIRPEVCR 237
Cdd:pfam03071 221 RDKTLWCVSAWNDNGKKQFVDDtaPYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISR 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 238 TYNFGEHGSSLGQYFKQYLEPIKLNGV-------------QDKYVKHFADMVKNARPVCGTDDVLKECNIDCDVRIQYKD 304
Cdd:pfam03071 301 TMNFGEHGSSLGQFFSQHLEPIKLNDVtvdfkakdlgyltEGNYTKYFSGLVRQARPLQGSDVVLKAQNIKGDVRVRYKG 380
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1585744623 305 KTDFEHIARQFGIFEEWEDGVPRTAYKGVVVFRYQSpKRVFLVGPESLQHLGI 357
Cdd:pfam03071 381 QVEFERIAGELGIMEDWKDGVPRTAYKGIVTFRIQG-RRVFLVPPDTVMQYGP 432
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
39-351 3.87e-152

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: 431.37  E-value: 3.87e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623  39 CNRANYLERALKSILKfsrHQSSVpSKYPLFVSQDAEDPDVKSKALCYN-QLTYMQHLDHEPVHTERPEEMIVYYKIARH 117
Cdd:cd02514     9 CNRPDYLRRMLDSLLS---YRPSA-EKFPIIVSQDGGYEEVADVAKSFGdGVTHIQHPPISIKNVNPPHKFQGYYRIARH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 118 YKWALDQLFYKHNFSRVIILEDDMEISPDFFDYFEAAVALLESDKSIMAVSSWNDNGQKQFVQD-PYMLYRSDFFPGLGW 196
Cdd:cd02514    85 YKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFFPGLGW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 197 MLAKSTWDELSPKWTKAYWDDWLRLKETHKGRQFIRPEVCRTYNFGEHGSSLGQYFKQYLEPIKLNGV------------ 264
Cdd:cd02514   165 MLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGVSNGQFFDKYLKKIKLNTVfvvftkldlsyl 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 265 -QDKYVKHFADMVKNARPVCGTD---DVLKECNIDCDVRIQYKDKTDFEHIARQFGIFEEWEDGVPRTAYKGVVVFRYQS 340
Cdd:cd02514   245 kKDNYDKEFHRLVYGAVVLDHEKnpcELSFVPDTEGKVRVVYTGRDDFKTWAKAFGVMDDLKDGVPRTAYKGIVRFFFKG 324
                         330
                  ....*....|.
gi 1585744623 341 pKRVFLVGPES 351
Cdd:cd02514   325 -NRVFLVPPPT 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, ...
2-357 1.44e-156

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: 446.66  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623   2 DQISIQKGRIVTLEEgNGLEKIIDKVQAPVAAVVVMACNRANYLERALKSILkfsrHQSSVPSKYPLFVSQDAEDPDVKS 81
Cdd:pfam03071  66 EELVQLRDLIQTFEK-KGIAKLTQGGQMPVIPVLVMACSRADYVRRTVKKLL----TYRPSAEKFPIIVSQDCSDEAVKS 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623  82 KALCY-NQLTYMQHLDHEPVHTERPE-EMIVYYKIARHYKWALDQLFYKHNFSRVIILEDDMEISPDFFDYFEAAVALLE 159
Cdd:pfam03071 141 KSLSYgNQVTYIQHLDFEPIVTPPGHrQLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLD 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 160 SDKSIMAVSSWNDNGQKQFVQD--PYMLYRSDFFPGLGWMLAKSTWDELSPKWTKAYWDDWLRLKETHKGRQFIRPEVCR 237
Cdd:pfam03071 221 RDKTLWCVSAWNDNGKKQFVDDtaPYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISR 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 238 TYNFGEHGSSLGQYFKQYLEPIKLNGV-------------QDKYVKHFADMVKNARPVCGTDDVLKECNIDCDVRIQYKD 304
Cdd:pfam03071 301 TMNFGEHGSSLGQFFSQHLEPIKLNDVtvdfkakdlgyltEGNYTKYFSGLVRQARPLQGSDVVLKAQNIKGDVRVRYKG 380
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1585744623 305 KTDFEHIARQFGIFEEWEDGVPRTAYKGVVVFRYQSpKRVFLVGPESLQHLGI 357
Cdd:pfam03071 381 QVEFERIAGELGIMEDWKDGVPRTAYKGIVTFRIQG-RRVFLVPPDTVMQYGP 432
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
39-351 3.87e-152

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: 431.37  E-value: 3.87e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623  39 CNRANYLERALKSILKfsrHQSSVpSKYPLFVSQDAEDPDVKSKALCYN-QLTYMQHLDHEPVHTERPEEMIVYYKIARH 117
Cdd:cd02514     9 CNRPDYLRRMLDSLLS---YRPSA-EKFPIIVSQDGGYEEVADVAKSFGdGVTHIQHPPISIKNVNPPHKFQGYYRIARH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 118 YKWALDQLFYKHNFSRVIILEDDMEISPDFFDYFEAAVALLESDKSIMAVSSWNDNGQKQFVQD-PYMLYRSDFFPGLGW 196
Cdd:cd02514    85 YKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFFPGLGW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 197 MLAKSTWDELSPKWTKAYWDDWLRLKETHKGRQFIRPEVCRTYNFGEHGSSLGQYFKQYLEPIKLNGV------------ 264
Cdd:cd02514   165 MLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGVSNGQFFDKYLKKIKLNTVfvvftkldlsyl 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744623 265 -QDKYVKHFADMVKNARPVCGTD---DVLKECNIDCDVRIQYKDKTDFEHIARQFGIFEEWEDGVPRTAYKGVVVFRYQS 340
Cdd:cd02514   245 kKDNYDKEFHRLVYGAVVLDHEKnpcELSFVPDTEGKVRVVYTGRDDFKTWAKAFGVMDDLKDGVPRTAYKGIVRFFFKG 324
                         330
                  ....*....|.
gi 1585744623 341 pKRVFLVGPES 351
Cdd:cd02514   325 -NRVFLVPPPT 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH