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Conserved domains on  [gi|14250634|gb|AAH08781|]
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WDYHV motif containing 1 [Homo sapiens]

Protein Classification

protein N-terminal glutamine amidohydrolase( domain architecture ID 10561071)

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:0008418|GO:0070773|GO:0036211
PubMed:  19560421

Graphical summary

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List of domain hits

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 ...
23-200 1.02e-117

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: 331.86  E-value: 1.02e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250634    23 YSSCYCEENVWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQA-RPGDGPVIWDYHVVLLHVSSGGQ-SFIYDLDT 100
Cdd:pfam09764   1 YTSCYCEENVYKLCEYIKEQNPAPLEDCYVVFISNERKTVPLWKQKAsRDPDGPVIWDYHVILLHRHDGGGgSLVYDLDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250634   101 VLPFPCLFDTYVEDAIKSDDDIHPQFRRKFRVICADSYLKNFASDRSHMKDSSGNWREPPPPYPCIETGDSKMNLNDFIS 180
Cdd:pfam09764  81 TLPFPCPFEEYVEETFRPDDQLKPEYQRKFRVIPADQYLKHFASDRSHMKDPDGNWIAPPPPYPPIATDGSKMNLDDFIS 160
                         170       180
                  ....*....|....*....|
gi 14250634   181 MDPKVGWGAVYTLSEFTHRF 200
Cdd:pfam09764 161 MSPSVGYGVVMSLDEFVQFF 180
 
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 ...
23-200 1.02e-117

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: 331.86  E-value: 1.02e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250634    23 YSSCYCEENVWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQA-RPGDGPVIWDYHVVLLHVSSGGQ-SFIYDLDT 100
Cdd:pfam09764   1 YTSCYCEENVYKLCEYIKEQNPAPLEDCYVVFISNERKTVPLWKQKAsRDPDGPVIWDYHVILLHRHDGGGgSLVYDLDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250634   101 VLPFPCLFDTYVEDAIKSDDDIHPQFRRKFRVICADSYLKNFASDRSHMKDSSGNWREPPPPYPCIETGDSKMNLNDFIS 180
Cdd:pfam09764  81 TLPFPCPFEEYVEETFRPDDQLKPEYQRKFRVIPADQYLKHFASDRSHMKDPDGNWIAPPPPYPPIATDGSKMNLDDFIS 160
                         170       180
                  ....*....|....*....|
gi 14250634   181 MDPKVGWGAVYTLSEFTHRF 200
Cdd:pfam09764 161 MSPSVGYGVVMSLDEFVQFF 180
 
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 ...
23-200 1.02e-117

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: 331.86  E-value: 1.02e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250634    23 YSSCYCEENVWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQA-RPGDGPVIWDYHVVLLHVSSGGQ-SFIYDLDT 100
Cdd:pfam09764   1 YTSCYCEENVYKLCEYIKEQNPAPLEDCYVVFISNERKTVPLWKQKAsRDPDGPVIWDYHVILLHRHDGGGgSLVYDLDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14250634   101 VLPFPCLFDTYVEDAIKSDDDIHPQFRRKFRVICADSYLKNFASDRSHMKDSSGNWREPPPPYPCIETGDSKMNLNDFIS 180
Cdd:pfam09764  81 TLPFPCPFEEYVEETFRPDDQLKPEYQRKFRVIPADQYLKHFASDRSHMKDPDGNWIAPPPPYPPIATDGSKMNLDDFIS 160
                         170       180
                  ....*....|....*....|
gi 14250634   181 MDPKVGWGAVYTLSEFTHRF 200
Cdd:pfam09764 161 MSPSVGYGVVMSLDEFVQFF 180
 
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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