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Conserved domains on  [gi|1958790386|ref|XP_038935447|]
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protein N-terminal glutamine amidohydrolase isoform X2 [Rattus norvegicus]

Protein Classification

protein N-terminal glutamine amidohydrolase( domain architecture ID 143831)

protein N-terminal glutamine amidohydrolase that mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation

EC:  3.5.1.122
Gene Ontology:  GO:0036211|GO:0005634|GO:0070773|GO:0008418
PubMed:  19560421

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nt_Gln_amidase super family cl20145
N-terminal glutamine amidase; This protein is conserved from plants to humans. It represents a ...
 25-115 4.52e-28

N-terminal glutamine amidase; This protein is conserved from plants to humans. It represents a family of N terminal glutamine amidases. The enzyme removes the NH2 group from a Gln, at the N-terminal, rendering it a Glu.


The actual alignment was detected with superfamily member pfam09764:

Pssm-ID: 462887  Cd Length: 180  Bit Score: 100.74  E-value: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790386  25 YSSCYCEENIWKLCEYIKTHNQYLLEECYAVFISNEKKMnpeegvgflgtratdvcklpcgcweqilgplqeqqVPIWKQ 104
Cdd:pfam09764   1 YTSCYCEENVYKLCEYIKEQNPAPLEDCYVVFISNERKT-----------------------------------VPLWKQ 45

                          90
                  ....*....|..
gi 1958790386 105 QA-RPENGPVIW 115
Cdd:pfam09764  46 KAsRDPDGPVIW 57
 
Name Accession Description Interval E-value
Nt_Gln_amidase pfam09764
N-terminal glutamine amidase; This protein is conserved from plants to humans. It represents a ...
 25-115 4.52e-28

N-terminal glutamine amidase; This protein is conserved from plants to humans. It represents a family of N terminal glutamine amidases. The enzyme removes the NH2 group from a Gln, at the N-terminal, rendering it a Glu.


Pssm-ID: 462887  Cd Length: 180  Bit Score: 100.74  E-value: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790386  25 YSSCYCEENIWKLCEYIKTHNQYLLEECYAVFISNEKKMnpeegvgflgtratdvcklpcgcweqilgplqeqqVPIWKQ 104
Cdd:pfam09764   1 YTSCYCEENVYKLCEYIKEQNPAPLEDCYVVFISNERKT-----------------------------------VPLWKQ 45

                          90
                  ....*....|..
gi 1958790386 105 QA-RPENGPVIW 115
Cdd:pfam09764  46 KAsRDPDGPVIW 57
 
Name Accession Description Interval E-value
Nt_Gln_amidase pfam09764
N-terminal glutamine amidase; This protein is conserved from plants to humans. It represents a ...
 25-115 4.52e-28

N-terminal glutamine amidase; This protein is conserved from plants to humans. It represents a family of N terminal glutamine amidases. The enzyme removes the NH2 group from a Gln, at the N-terminal, rendering it a Glu.


Pssm-ID: 462887  Cd Length: 180  Bit Score: 100.74  E-value: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790386  25 YSSCYCEENIWKLCEYIKTHNQYLLEECYAVFISNEKKMnpeegvgflgtratdvcklpcgcweqilgplqeqqVPIWKQ 104
Cdd:pfam09764   1 YTSCYCEENVYKLCEYIKEQNPAPLEDCYVVFISNERKT-----------------------------------VPLWKQ 45

                          90
                  ....*....|..
gi 1958790386 105 QA-RPENGPVIW 115
Cdd:pfam09764  46 KAsRDPDGPVIW 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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