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Conserved domains on  [gi|255088437|ref|XP_002506141|]
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glycosyltransferase family 13 protein, partial [Micromonas commoda]

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 ...
1-339 1.11e-129

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 cd02514:

Pssm-ID: 472172  Cd Length: 334  Bit Score: 373.59  E-value: 1.11e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437   1 AAVVIMACDRADYLERTVASVraaLGVRPGdVDKFPVFISQDGRHKATRAfaegpKAKDFHW----MQHLEDRPPTTRTR 76
Cdd:cd02514    2 IPVLVIACNRPDYLRRMLDSL---LSYRPS-AEKFPIIVSQDGGYEEVAD-----VAKSFGDgvthIQHPPISIKNVNPP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437  77 FRWdsVAYYRIAAHYKWAMKTLFDDLGYERVIVLEDDMELSPDFFGYFEAAGKVMDADPSVYTVSSWNDNGQKIHVSDE- 155
Cdd:cd02514   73 HKF--QGYYRIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDTp 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437 156 RRLYRSDFFPGLGWMLHKALWRELAPKWPDSYWDDWMRLSDVRRGRESIRPEVCRTFNFGEVGSSKGQFFRAYLREIKPA 235
Cdd:cd02514  151 SLLYRTDFFPGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGVSNGQFFDKYLKKIKLN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437 236 SERIDWASQSLAYISNgDAYEDQVRRTLASATIID---SPTQVRLVPPENaatNVYKVIYASERDFNRLAKRFGVFAEWK 312
Cdd:cd02514  231 TVFVVFTKLDLSYLKK-DNYDKEFHRLVYGAVVLDhekNPCELSFVPDTE---GKVRVVYTGRDDFKTWAKAFGVMDDLK 306
                        330       340
                 ....*....|....*....|....*..
gi 255088437 313 DGVPRAGYRGVVTFkMYKGRaTVMLVP 339
Cdd:cd02514  307 DGVPRTAYKGIVRF-FFKGN-RVFLVP 331
 
Name Accession Description Interval E-value
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
1-339 1.11e-129

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: 373.59  E-value: 1.11e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437   1 AAVVIMACDRADYLERTVASVraaLGVRPGdVDKFPVFISQDGRHKATRAfaegpKAKDFHW----MQHLEDRPPTTRTR 76
Cdd:cd02514    2 IPVLVIACNRPDYLRRMLDSL---LSYRPS-AEKFPIIVSQDGGYEEVAD-----VAKSFGDgvthIQHPPISIKNVNPP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437  77 FRWdsVAYYRIAAHYKWAMKTLFDDLGYERVIVLEDDMELSPDFFGYFEAAGKVMDADPSVYTVSSWNDNGQKIHVSDE- 155
Cdd:cd02514   73 HKF--QGYYRIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDTp 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437 156 RRLYRSDFFPGLGWMLHKALWRELAPKWPDSYWDDWMRLSDVRRGRESIRPEVCRTFNFGEVGSSKGQFFRAYLREIKPA 235
Cdd:cd02514  151 SLLYRTDFFPGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGVSNGQFFDKYLKKIKLN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437 236 SERIDWASQSLAYISNgDAYEDQVRRTLASATIID---SPTQVRLVPPENaatNVYKVIYASERDFNRLAKRFGVFAEWK 312
Cdd:cd02514  231 TVFVVFTKLDLSYLKK-DNYDKEFHRLVYGAVVLDhekNPCELSFVPDTE---GKVRVVYTGRDDFKTWAKAFGVMDDLK 306
                        330       340
                 ....*....|....*....|....*..
gi 255088437 313 DGVPRAGYRGVVTFkMYKGRaTVMLVP 339
Cdd:cd02514  307 DGVPRTAYKGIVRF-FFKGN-RVFLVP 331
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
1-339 2.22e-110

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: 328.40  E-value: 2.22e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437    1 AAVVIMACDRADYLERTVASVraaLGVRPgDVDKFPVFISQDGRHKATRAfaegpKAKDFH----WMQHLEDRPPTTRTR 76
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKL---LTYRP-SAEKFPIIVSQDCSDEAVKS-----KSLSYGnqvtYIQHLDFEPIVTPPG 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437   77 FRwDSVAYYRIAAHYKWAMKTLFDDLGYERVIVLEDDMELSPDFFGYFEAAGKVMDADPSVYTVSSWNDNGQK--IHVSD 154
Cdd:pfam03071 166 HR-QLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKqfVDDTA 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437  155 ERRLYRSDFFPGLGWMLHKALWRELAPKWPDSYWDDWMRLSDVRRGRESIRPEVCRTFNFGEVGSSKGQFFRAYLREIKP 234
Cdd:pfam03071 245 PYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSLGQFFSQHLEPIKL 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437  235 ASERIDWASQSLAYISNGdAYEdqvRRTLAsatiidsptQVRLVPP---ENAATNVYK------VIYASERDFNRLAKRF 305
Cdd:pfam03071 325 NDVTVDFKAKDLGYLTEG-NYT---KYFSG---------LVRQARPlqgSDVVLKAQNikgdvrVRYKGQVEFERIAGEL 391
                         330       340       350
                  ....*....|....*....|....*....|....
gi 255088437  306 GVFAEWKDGVPRAGYRGVVTFKMYKGRatVMLVP 339
Cdd:pfam03071 392 GIMEDWKDGVPRTAYKGIVTFRIQGRR--VFLVP 423
 
Name Accession Description Interval E-value
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
1-339 1.11e-129

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: 373.59  E-value: 1.11e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437   1 AAVVIMACDRADYLERTVASVraaLGVRPGdVDKFPVFISQDGRHKATRAfaegpKAKDFHW----MQHLEDRPPTTRTR 76
Cdd:cd02514    2 IPVLVIACNRPDYLRRMLDSL---LSYRPS-AEKFPIIVSQDGGYEEVAD-----VAKSFGDgvthIQHPPISIKNVNPP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437  77 FRWdsVAYYRIAAHYKWAMKTLFDDLGYERVIVLEDDMELSPDFFGYFEAAGKVMDADPSVYTVSSWNDNGQKIHVSDE- 155
Cdd:cd02514   73 HKF--QGYYRIARHYKWALTQTFNLFGYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDTp 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437 156 RRLYRSDFFPGLGWMLHKALWRELAPKWPDSYWDDWMRLSDVRRGRESIRPEVCRTFNFGEVGSSKGQFFRAYLREIKPA 235
Cdd:cd02514  151 SLLYRTDFFPGLGWMLTRKLWKELEPKWPKAFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGVSNGQFFDKYLKKIKLN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437 236 SERIDWASQSLAYISNgDAYEDQVRRTLASATIID---SPTQVRLVPPENaatNVYKVIYASERDFNRLAKRFGVFAEWK 312
Cdd:cd02514  231 TVFVVFTKLDLSYLKK-DNYDKEFHRLVYGAVVLDhekNPCELSFVPDTE---GKVRVVYTGRDDFKTWAKAFGVMDDLK 306
                        330       340
                 ....*....|....*....|....*..
gi 255088437 313 DGVPRAGYRGVVTFkMYKGRaTVMLVP 339
Cdd:cd02514  307 DGVPRTAYKGIVRF-FFKGN-RVFLVP 331
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
1-339 2.22e-110

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: 328.40  E-value: 2.22e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437    1 AAVVIMACDRADYLERTVASVraaLGVRPgDVDKFPVFISQDGRHKATRAfaegpKAKDFH----WMQHLEDRPPTTRTR 76
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKL---LTYRP-SAEKFPIIVSQDCSDEAVKS-----KSLSYGnqvtYIQHLDFEPIVTPPG 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437   77 FRwDSVAYYRIAAHYKWAMKTLFDDLGYERVIVLEDDMELSPDFFGYFEAAGKVMDADPSVYTVSSWNDNGQK--IHVSD 154
Cdd:pfam03071 166 HR-QLTAYYKIARHYKWALDQVFYKHKFSRVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKqfVDDTA 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437  155 ERRLYRSDFFPGLGWMLHKALWRELAPKWPDSYWDDWMRLSDVRRGRESIRPEVCRTFNFGEVGSSKGQFFRAYLREIKP 234
Cdd:pfam03071 245 PYALYRSDFFPGLGWMLKRSTWDELEPKWPKAFWDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSLGQFFSQHLEPIKL 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437  235 ASERIDWASQSLAYISNGdAYEdqvRRTLAsatiidsptQVRLVPP---ENAATNVYK------VIYASERDFNRLAKRF 305
Cdd:pfam03071 325 NDVTVDFKAKDLGYLTEG-NYT---KYFSG---------LVRQARPlqgSDVVLKAQNikgdvrVRYKGQVEFERIAGEL 391
                         330       340       350
                  ....*....|....*....|....*....|....
gi 255088437  306 GVFAEWKDGVPRAGYRGVVTFKMYKGRatVMLVP 339
Cdd:pfam03071 392 GIMEDWKDGVPRTAYKGIVTFRIQGRR--VFLVP 423
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
3-137 1.51e-03

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.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 38.64  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255088437   3 VVIMACDRADYLERTVASVRAAlgvrpgDVDKFPVFISQDGRHKATRAFAEGPKAKDFHWMQHLEDRPPTTrtrfrwdSV 82
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQ------TYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGL-------AA 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255088437  83 AYYRIAAHykwamktlfddLGYERVIVLEDDMELSPDFfgyFEAAGKVMDADPSV 137
Cdd:cd00761   68 ARNAGLKA-----------ARGEYILFLDADDLLLPDW---LERLVAELLADPEA 108
 
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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