NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|221044698|dbj|BAH14026|]
View 

unnamed protein product [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

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
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 20-198 1.72e-129

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03793:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 590  Bit Score: 377.87  E-value: 1.72e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698  20 RVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHF 99
Cdd:cd03793   75 KVHFGRWLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEFAAQFDPQPAVVAHF 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698 100 HEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVS 179
Cdd:cd03793  155 HEWQAGVGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVS 234

                        170
                 ....*....|....*....
gi 221044698 180 QITAIEAQHLLKRKPGIWT 198
Cdd:cd03793  235 EITAYEAEHLLKRKPDIVT 253
 
Name Accession Description Interval E-value
GT3_GSY2-like cd03793
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ...
 20-198 1.72e-129

glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related to the GT3 family of glycosyltransferases, catalyzes the transfer of a glucose molecule from UDP-glucose to a terminal branch of a glycogen molecule, a rate-limit step of glycogen biosynthesis. GSY2, the member of this family in S. cerevisiae, has been shown to possess glycogen synthase activity.


Pssm-ID: 340824 [Multi-domain]  Cd Length: 590  Bit Score: 377.87  E-value: 1.72e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698  20 RVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHF 99
Cdd:cd03793   75 KVHFGRWLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEFAAQFDPQPAVVAHF 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698 100 HEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVS 179
Cdd:cd03793  155 HEWQAGVGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVS 234

                        170
                 ....*....|....*....
gi 221044698 180 QITAIEAQHLLKRKPGIWT 198
Cdd:cd03793  235 EITAYEAEHLLKRKPDIVT 253
Glycogen_syn pfam05693
Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, ...
 20-198 4.04e-125

Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, GYS2 and GYS3. Glycogen synthase (GS) is the enzyme responsible for the synthesis of -1,4-linked glucose chains in glycogen. It is the rate limiting enzyme in the synthesis of the polysaccharide, and its activity is highly regulated through phosphorylation at multiple sites and also by allosteric effectors, mainly glucose 6-phosphate (G6P).


Pssm-ID: 399009 [Multi-domain]  Cd Length: 639  Bit Score: 368.33  E-value: 4.04e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698   20 RVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHF 99
Cdd:pfam05693  70 KIHYGRWLIEGAPRVILFDLGSAAWKLNEWKGELWEQCGIGIPHHDIETNDAIILGFLVAWFLGEFREHATSTPAVVAHF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698  100 HEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVS 179
Cdd:pfam05693 150 HEWQAGVGLPLTRKRKLDIATVFTTHATLLGRYLCAGGVDFYNNLDKFDVDAEAGKRQIYHRYCLERAAAHTAHVFTTVS 229

                         170
                  ....*....|....*....
gi 221044698  180 QITAIEAQHLLKRKPGIWT 198
Cdd:pfam05693 230 EITALEAEHLLKRKPDVVT 248
 
Name Accession Description Interval E-value
GT3_GSY2-like cd03793
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ...
 20-198 1.72e-129

glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related to the GT3 family of glycosyltransferases, catalyzes the transfer of a glucose molecule from UDP-glucose to a terminal branch of a glycogen molecule, a rate-limit step of glycogen biosynthesis. GSY2, the member of this family in S. cerevisiae, has been shown to possess glycogen synthase activity.


Pssm-ID: 340824 [Multi-domain]  Cd Length: 590  Bit Score: 377.87  E-value: 1.72e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698  20 RVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHF 99
Cdd:cd03793   75 KVHFGRWLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEFAAQFDPQPAVVAHF 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698 100 HEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVS 179
Cdd:cd03793  155 HEWQAGVGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVS 234

                        170
                 ....*....|....*....
gi 221044698 180 QITAIEAQHLLKRKPGIWT 198
Cdd:cd03793  235 EITAYEAEHLLKRKPDIVT 253
Glycogen_syn pfam05693
Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, ...
 20-198 4.04e-125

Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, GYS2 and GYS3. Glycogen synthase (GS) is the enzyme responsible for the synthesis of -1,4-linked glucose chains in glycogen. It is the rate limiting enzyme in the synthesis of the polysaccharide, and its activity is highly regulated through phosphorylation at multiple sites and also by allosteric effectors, mainly glucose 6-phosphate (G6P).


Pssm-ID: 399009 [Multi-domain]  Cd Length: 639  Bit Score: 368.33  E-value: 4.04e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698   20 RVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHF 99
Cdd:pfam05693  70 KIHYGRWLIEGAPRVILFDLGSAAWKLNEWKGELWEQCGIGIPHHDIETNDAIILGFLVAWFLGEFREHATSTPAVVAHF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221044698  100 HEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVS 179
Cdd:pfam05693 150 HEWQAGVGLPLTRKRKLDIATVFTTHATLLGRYLCAGGVDFYNNLDKFDVDAEAGKRQIYHRYCLERAAAHTAHVFTTVS 229

                         170
                  ....*....|....*....
gi 221044698  180 QITAIEAQHLLKRKPGIWT 198
Cdd:pfam05693 230 EITALEAEHLLKRKPDVVT 248
 
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