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Conserved domains on  [gi|446523590|ref|WP_000600936|]
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MULTISPECIES: hypothetical protein [Enterobacteriaceae]

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 ...
20-114 1.35e-05

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 cd04181:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 217  Bit Score: 46.42  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446523590  20 VIPPCLLPIGNRTLLEYQAESIRKMSNEKIFLT---LPEdyclsKFEERLLDS----LNIRAIYLSPNLSLGESIYQALD 92
Cdd:cd04181   18 TRPKPLLPIAGKPILEYIIERLARAGIDEIILVvgyLGE-----QIEEYFGDGskfgVNIEYVVQEEPLGTAGAVRNAED 92
                         90       100
                 ....*....|....*....|..
gi 446523590  93 SIGDYTFssdgLkLLHGDTLIN 114
Cdd:cd04181   93 FLGDDDF----L-VVNGDVLTD 109
 
Name Accession Description Interval E-value
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
20-114 1.35e-05

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 46.42  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446523590  20 VIPPCLLPIGNRTLLEYQAESIRKMSNEKIFLT---LPEdyclsKFEERLLDS----LNIRAIYLSPNLSLGESIYQALD 92
Cdd:cd04181   18 TRPKPLLPIAGKPILEYIIERLARAGIDEIILVvgyLGE-----QIEEYFGDGskfgVNIEYVVQEEPLGTAGAVRNAED 92
                         90       100
                 ....*....|....*....|..
gi 446523590  93 SIGDYTFssdgLkLLHGDTLIN 114
Cdd:cd04181   93 FLGDDDF----L-VVNGDVLTD 109
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
21-112 3.85e-03

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 39.07  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446523590  21 IPPCLLPIGNRTLLEYQAESIRKMSNEKIFLTLpeDYCLSKFEERLLD-SLNIRAIYlSPNLSLGESIY---QALDSIGD 96
Cdd:COG1213   20 IPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT--GYKAELIEEALARpGPDVTFVY-NPDYDETNNIYslwLAREALDE 96
                         90
                 ....*....|....*.
gi 446523590  97 YTFssdglkLLHGDTL 112
Cdd:COG1213   97 DFL------LLNGDVV 106
 
Name Accession Description Interval E-value
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
20-114 1.35e-05

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 46.42  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446523590  20 VIPPCLLPIGNRTLLEYQAESIRKMSNEKIFLT---LPEdyclsKFEERLLDS----LNIRAIYLSPNLSLGESIYQALD 92
Cdd:cd04181   18 TRPKPLLPIAGKPILEYIIERLARAGIDEIILVvgyLGE-----QIEEYFGDGskfgVNIEYVVQEEPLGTAGAVRNAED 92
                         90       100
                 ....*....|....*....|..
gi 446523590  93 SIGDYTFssdgLkLLHGDTLIN 114
Cdd:cd04181   93 FLGDDDF----L-VVNGDVLTD 109
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
21-112 3.85e-03

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 39.07  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446523590  21 IPPCLLPIGNRTLLEYQAESIRKMSNEKIFLTLpeDYCLSKFEERLLD-SLNIRAIYlSPNLSLGESIY---QALDSIGD 96
Cdd:COG1213   20 IPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT--GYKAELIEEALARpGPDVTFVY-NPDYDETNNIYslwLAREALDE 96
                         90
                 ....*....|....*.
gi 446523590  97 YTFssdglkLLHGDTL 112
Cdd:COG1213   97 DFL------LLNGDVV 106
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
21-57 7.56e-03

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 38.02  E-value: 7.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446523590  21 IPPCLLPIGNRTLLEYQAESIRKMSNEKIFLTLPEDY 57
Cdd:cd04198   21 IPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
 
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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