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Conserved domains on  [gi|643036788|gb|AIA95023|]
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Anp1, partial [uncultured Lachancea]

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 ...
2-76 1.07e-40

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 pfam03452:

Pssm-ID: 472172  Cd Length: 265  Bit Score: 133.78  E-value: 1.07e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643036788    2 RDIDVETAPATILEDLMHHDKDVIVPNIWRPLPEWLNNEQPYDLNSWQESEGGIELAERLDEDAVIVEGYPEYAT 76
Cdd:pfam03452 145 LDADIVETPPTLIQDLMAHDKDVIVPNVWRRYPDLDGKERPYDLNSWQESDTALELAKKLDEDDIIVEGYAEYPT 219
 
Name Accession Description Interval E-value
Anp1 pfam03452
Anp1; The members of this family (Anp1, Van1 and Mnn9) are membrane proteins required for ...
2-76 1.07e-40

Anp1; The members of this family (Anp1, Van1 and Mnn9) are membrane proteins required for proper Golgi function. These proteins co-localize within the cis Golgi, and that they are physically associated in two distinct complexes.


Pssm-ID: 427303  Cd Length: 265  Bit Score: 133.78  E-value: 1.07e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643036788    2 RDIDVETAPATILEDLMHHDKDVIVPNIWRPLPEWLNNEQPYDLNSWQESEGGIELAERLDEDAVIVEGYPEYAT 76
Cdd:pfam03452 145 LDADIVETPPTLIQDLMAHDKDVIVPNVWRRYPDLDGKERPYDLNSWQESDTALELAKKLDEDDIIVEGYAEYPT 219
 
Name Accession Description Interval E-value
Anp1 pfam03452
Anp1; The members of this family (Anp1, Van1 and Mnn9) are membrane proteins required for ...
2-76 1.07e-40

Anp1; The members of this family (Anp1, Van1 and Mnn9) are membrane proteins required for proper Golgi function. These proteins co-localize within the cis Golgi, and that they are physically associated in two distinct complexes.


Pssm-ID: 427303  Cd Length: 265  Bit Score: 133.78  E-value: 1.07e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643036788    2 RDIDVETAPATILEDLMHHDKDVIVPNIWRPLPEWLNNEQPYDLNSWQESEGGIELAERLDEDAVIVEGYPEYAT 76
Cdd:pfam03452 145 LDADIVETPPTLIQDLMAHDKDVIVPNVWRRYPDLDGKERPYDLNSWQESDTALELAKKLDEDDIIVEGYAEYPT 219
 
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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