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Conserved domains on  [gi|7022103|dbj|BAA91488|]
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unnamed protein product [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
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 ...
23-192 1.41e-111

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: 401639  Cd Length: 172  Bit Score: 315.67  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7022103     23 YSSCYCEENIWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQA-RPGDGPVIWDYHVVLLHVSSGGQ-NFIYDLDT 100
Cdd:pfam09764   1 YTSCYCEENVWKLCEKIKEQNPAPLEDCYVVFISNERKTVPLWKQKAsRDPDGPVIWDYHVILIQRHDGSGeSLVYDLDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7022103    101 VLPFPCLFDTYVEDAFKSDDDIHPQFRRKFRVIRADSYLKNFASDRSHMKDSSGNWREPPPPYPCIETGDSKMNLNDFIS 180
Cdd:pfam09764  81 TLPFPCPFEEYVEETFRPDFQLKPEYQRKFRVVPADQYLKHFASDRSHMKDSDGNWIAPPPPYPPIVTDGSKMNLDDFIS 160
                         170
                  ....*....|..
gi 7022103    181 MDPKVGWGAVYT 192
Cdd:pfam09764 161 MSPSVGYGVVMS 172
 
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 ...
23-192 1.41e-111

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: 401639  Cd Length: 172  Bit Score: 315.67  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7022103     23 YSSCYCEENIWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQA-RPGDGPVIWDYHVVLLHVSSGGQ-NFIYDLDT 100
Cdd:pfam09764   1 YTSCYCEENVWKLCEKIKEQNPAPLEDCYVVFISNERKTVPLWKQKAsRDPDGPVIWDYHVILIQRHDGSGeSLVYDLDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7022103    101 VLPFPCLFDTYVEDAFKSDDDIHPQFRRKFRVIRADSYLKNFASDRSHMKDSSGNWREPPPPYPCIETGDSKMNLNDFIS 180
Cdd:pfam09764  81 TLPFPCPFEEYVEETFRPDFQLKPEYQRKFRVVPADQYLKHFASDRSHMKDSDGNWIAPPPPYPPIVTDGSKMNLDDFIS 160
                         170
                  ....*....|..
gi 7022103    181 MDPKVGWGAVYT 192
Cdd:pfam09764 161 MSPSVGYGVVMS 172
 
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 ...
23-192 1.41e-111

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: 401639  Cd Length: 172  Bit Score: 315.67  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7022103     23 YSSCYCEENIWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQA-RPGDGPVIWDYHVVLLHVSSGGQ-NFIYDLDT 100
Cdd:pfam09764   1 YTSCYCEENVWKLCEKIKEQNPAPLEDCYVVFISNERKTVPLWKQKAsRDPDGPVIWDYHVILIQRHDGSGeSLVYDLDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7022103    101 VLPFPCLFDTYVEDAFKSDDDIHPQFRRKFRVIRADSYLKNFASDRSHMKDSSGNWREPPPPYPCIETGDSKMNLNDFIS 180
Cdd:pfam09764  81 TLPFPCPFEEYVEETFRPDFQLKPEYQRKFRVVPADQYLKHFASDRSHMKDSDGNWIAPPPPYPPIVTDGSKMNLDDFIS 160
                         170
                  ....*....|..
gi 7022103    181 MDPKVGWGAVYT 192
Cdd:pfam09764 161 MSPSVGYGVVMS 172
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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