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Conserved domains on  [gi|75161680|sp|Q8VZP6|]
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RecName: Full=Putative glucuronosyltransferase PGSIP8; AltName: Full=Glycogenin-like protein 8; AltName: Full=Plant glycogenin-like starch initiation protein 8

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 10118608)

glycosyltransferase family 8 protein similar to vertebrate glycogenin, which catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached to internal tyrosine residues

CATH:  3.90.550.10
Gene Ontology:  GO:0016757|GO:0005978
PubMed:  10508766|12691742

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
63-315 4.11e-72

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


:

Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 228.68  E-value: 4.11e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  63 NAYATMMYMGtprdyEFYVATRVLIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEdGAKVVRVENVDNPYRRQTNFNSR 142
Cdd:cd02537   1 EAYVTLLTND-----DYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEV-GWIVREVEPIDPPDSANLLKRPR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 143 FKLTLNKLYAWALSDYDRVVMLDADNLFLKKADELFQC-GRFCAVFIN--PCIFHTGLFVLQPSVEVFKDMLHELQVGRK 219
Cdd:cd02537  75 FKDTYTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLpGEFAAAPDCgwPDLFNSGVFVLKPSEETFNDLLDALQDTPS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 220 nPDGADQGFLVSYFSDlldqplfsppsngsvLNGHLRLPLGYQMDASYFYLKLRWNIPCGPNSVITFPGAvwLKPWYWWS 299
Cdd:cd02537 155 -FDGGDQGLLNSYFSD---------------RGIWKRLPFTYNALKPLRYLHPEALWFGDEIKVVHFIGG--DKPWSWWR 216
                       250       260
                ....*....|....*....|...
gi 75161680 300 WP-------VLPLGFSWHEQRRA 315
Cdd:cd02537 217 DPetkekddYNELHQWWWDIYDE 239
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
63-315 4.11e-72

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 228.68  E-value: 4.11e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  63 NAYATMMYMGtprdyEFYVATRVLIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEdGAKVVRVENVDNPYRRQTNFNSR 142
Cdd:cd02537   1 EAYVTLLTND-----DYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEV-GWIVREVEPIDPPDSANLLKRPR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 143 FKLTLNKLYAWALSDYDRVVMLDADNLFLKKADELFQC-GRFCAVFIN--PCIFHTGLFVLQPSVEVFKDMLHELQVGRK 219
Cdd:cd02537  75 FKDTYTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLpGEFAAAPDCgwPDLFNSGVFVLKPSEETFNDLLDALQDTPS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 220 nPDGADQGFLVSYFSDlldqplfsppsngsvLNGHLRLPLGYQMDASYFYLKLRWNIPCGPNSVITFPGAvwLKPWYWWS 299
Cdd:cd02537 155 -FDGGDQGLLNSYFSD---------------RGIWKRLPFTYNALKPLRYLHPEALWFGDEIKVVHFIGG--DKPWSWWR 216
                       250       260
                ....*....|....*....|...
gi 75161680 300 WP-------VLPLGFSWHEQRRA 315
Cdd:cd02537 217 DPetkekddYNELHQWWWDIYDE 239
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
57-242 3.15e-19

N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 87.48  E-value: 3.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  57 RRPEHKNAYATMMymgTPRDYEfyVATRVLIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEdGAKVVRVENVDNpyrrQ 136
Cdd:COG5597   8 GPAGSRRAYVTLV---TNADYA--LGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAAL-GARLVRVDLLPT----S 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 137 TNFNSR-------------------FKLTLN---KLYAWALSDYDRVVMLDADNLFLKKADELFQCGRFCA---VFINPC 191
Cdd:COG5597  78 DAFNARhargrlhgaapftkgrkpaFHTPLDnfcKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAapnVYESLA 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75161680 192 IFH---TGLFVLQPSVEVFKDMLHELQVgrknPDG----ADQGFLVSYFSDLLDQPLF 242
Cdd:COG5597 158 DFHrlnSGVFTARPSQATFEAMLARLDA----PGAfwrrTDQTFLQTFFPDWHGLPVF 211
PLN00176 PLN00176
galactinol synthase
86-235 4.05e-08

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 55.09  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680   86 LIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEdGAKVVRVENVdNPYRRQTNFN-SRFKLTLNKLYAWALSDYDRVVML 164
Cdd:PLN00176  42 LAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQ-GCIVREIEPV-YPPENQTQFAmAYYVINYSKLRIWEFVEYSKMIYL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  165 DADNLFLKKADELF--QCGRFCAVF---------------INPC-------------------IFHTGLFVLQPSVEVFK 208
Cdd:PLN00176 120 DGDIQVFENIDHLFdlPDGYFYAVMdcfcektwshtpqykIGYCqqcpdkvtwpaelgpppplYFNAGMFVFEPSLSTYE 199
                        170       180
                 ....*....|....*....|....*..
gi 75161680  209 DMLHELQVGRKNPdGADQGFLVSYFSD 235
Cdd:PLN00176 200 DLLETLKITPPTP-FAEQDFLNMFFRD 225
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
63-315 4.11e-72

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 228.68  E-value: 4.11e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  63 NAYATMMYMGtprdyEFYVATRVLIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEdGAKVVRVENVDNPYRRQTNFNSR 142
Cdd:cd02537   1 EAYVTLLTND-----DYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEV-GWIVREVEPIDPPDSANLLKRPR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 143 FKLTLNKLYAWALSDYDRVVMLDADNLFLKKADELFQC-GRFCAVFIN--PCIFHTGLFVLQPSVEVFKDMLHELQVGRK 219
Cdd:cd02537  75 FKDTYTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLpGEFAAAPDCgwPDLFNSGVFVLKPSEETFNDLLDALQDTPS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 220 nPDGADQGFLVSYFSDlldqplfsppsngsvLNGHLRLPLGYQMDASYFYLKLRWNIPCGPNSVITFPGAvwLKPWYWWS 299
Cdd:cd02537 155 -FDGGDQGLLNSYFSD---------------RGIWKRLPFTYNALKPLRYLHPEALWFGDEIKVVHFIGG--DKPWSWWR 216
                       250       260
                ....*....|....*....|...
gi 75161680 300 WP-------VLPLGFSWHEQRRA 315
Cdd:cd02537 217 DPetkekddYNELHQWWWDIYDE 239
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
57-242 3.15e-19

N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 87.48  E-value: 3.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  57 RRPEHKNAYATMMymgTPRDYEfyVATRVLIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEdGAKVVRVENVDNpyrrQ 136
Cdd:COG5597   8 GPAGSRRAYVTLV---TNADYA--LGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAAL-GARLVRVDLLPT----S 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 137 TNFNSR-------------------FKLTLN---KLYAWALSDYDRVVMLDADNLFLKKADELFQCGRFCA---VFINPC 191
Cdd:COG5597  78 DAFNARhargrlhgaapftkgrkpaFHTPLDnfcKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAapnVYESLA 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75161680 192 IFH---TGLFVLQPSVEVFKDMLHELQVgrknPDG----ADQGFLVSYFSDLLDQPLF 242
Cdd:COG5597 158 DFHrlnSGVFTARPSQATFEAMLARLDA----PGAfwrrTDQTFLQTFFPDWHGLPVF 211
PLN00176 PLN00176
galactinol synthase
86-235 4.05e-08

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 55.09  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680   86 LIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEdGAKVVRVENVdNPYRRQTNFN-SRFKLTLNKLYAWALSDYDRVVML 164
Cdd:PLN00176  42 LAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQ-GCIVREIEPV-YPPENQTQFAmAYYVINYSKLRIWEFVEYSKMIYL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  165 DADNLFLKKADELF--QCGRFCAVF---------------INPC-------------------IFHTGLFVLQPSVEVFK 208
Cdd:PLN00176 120 DGDIQVFENIDHLFdlPDGYFYAVMdcfcektwshtpqykIGYCqqcpdkvtwpaelgpppplYFNAGMFVFEPSLSTYE 199
                        170       180
                 ....*....|....*....|....*..
gi 75161680  209 DMLHELQVGRKNPdGADQGFLVSYFSD 235
Cdd:PLN00176 200 DLLETLKITPPTP-FAEQDFLNMFFRD 225
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
65-295 1.25e-07

GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases.


Pssm-ID: 133064  Cd Length: 278  Bit Score: 53.20  E-value: 1.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680  65 YATMMYMgtpRDYEFYVATRVLIRSLRSLHVEADLVVIASLDVPLRWVQTLEEEDGAKV---VRVENVDNPYRRQTNFNS 141
Cdd:cd06914   1 YAYVNYA---TNADYLCNALILFEQLRRLGSKAKLVLLVPETLLDRNLDDFVRRDLLLArdkVIVKLIPVIIASGGDAYW 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 142 RFKLTlnKLYAWALSDYDRVVMLDADNLFLKKADELFqcgrfcavFINPCI----------FHTGLFVLQPSVEVFKDML 211
Cdd:cd06914  78 AKSLT--KLRAFNQTEYDRIIYFDSDSIIRHPMDELF--------FLPNYIkfaapraywkFASHLMVIKPSKEAFKELM 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 212 HELQ-VGRKNPDGADQGFLVSYFSDLLDQPLFS----PPSNGSVLNGHLRLPLGYQMDASYFYLKLRWnipcGPNS---- 282
Cdd:cd06914 148 TEILpAYLNKKNEYDMDLINEEFYNSKQLFKPSvlvlPHRQYGLLTGEFREKLHKSFLSNAQHLYEKW----DPDDvfke 223
                       250
                ....*....|....*
gi 75161680 283 --VITFPGAVWLKPW 295
Cdd:cd06914 224 skVIHFSDSPLPKPW 238
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
136-246 1.48e-05

Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.


Pssm-ID: 132996 [Multi-domain]  Cd Length: 246  Bit Score: 46.28  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75161680 136 QTNFNSRFKLTLNKLYAWAL-SDYDRVVMLDADNLFLKKADELFQ----------------------CGRFCAVFINPCI 192
Cdd:cd00505  73 EHLKRPIKIVTLTKLHLPNLvPDYDKILYVDADILVLTDIDELWDtplggqelaaapdpgdrregkyYRQKRSHLAGPDY 152
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75161680 193 FHTGLFVLQPSVEVFKDMLHEL----QVGRKNPDGADQGFLVSYFSDLLDqPLFSPPS 246
Cdd:cd00505 153 FNSGVFVVNLSKERRNQLLKVAlekwLQSLSSLSGGDQDLLNTFFKQVPF-IVKSLPC 209
 
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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