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Conserved domains on  [gi|399124760|ref|NP_001257695|]
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protein N-terminal asparagine amidohydrolase isoform 2 [Homo sapiens]

Protein Classification

N_Asn_amidohyd domain-containing protein( domain architecture ID 10631637)

N_Asn_amidohyd domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
N_Asn_amidohyd pfam14736
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
1-199 2.16e-115

Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation of N-terminal asparagines in peptides and proteins to aspartic acid.


:

Pssm-ID: 464288  Cd Length: 270  Bit Score: 329.17  E-value: 2.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399124760    1 MNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIK 80
Cdd:pfam14736  71 LSRVQSLSLGSPEGRLELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVK 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399124760   81 TAEIYRASFQDRGPEEQLRAARTLAGG-PMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHF 159
Cdd:pfam14736 151 TGEIFPASFPDKGPDEVLRSARSFTGGdQMLDIYDTSTGQLIIGPFNWDPFRDVDLWLQQDDEFILQNLSTSPDAEPPHF 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 399124760  160 VEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEK 199
Cdd:pfam14736 231 VDHIRSTLRFLQEHPFPDVTLFPDNQPRFYRRDEGGLWER 270
 
Name Accession Description Interval E-value
N_Asn_amidohyd pfam14736
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
1-199 2.16e-115

Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation of N-terminal asparagines in peptides and proteins to aspartic acid.


Pssm-ID: 464288  Cd Length: 270  Bit Score: 329.17  E-value: 2.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399124760    1 MNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIK 80
Cdd:pfam14736  71 LSRVQSLSLGSPEGRLELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVK 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399124760   81 TAEIYRASFQDRGPEEQLRAARTLAGG-PMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHF 159
Cdd:pfam14736 151 TGEIFPASFPDKGPDEVLRSARSFTGGdQMLDIYDTSTGQLIIGPFNWDPFRDVDLWLQQDDEFILQNLSTSPDAEPPHF 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 399124760  160 VEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEK 199
Cdd:pfam14736 231 VDHIRSTLRFLQEHPFPDVTLFPDNQPRFYRRDEGGLWER 270
 
Name Accession Description Interval E-value
N_Asn_amidohyd pfam14736
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
1-199 2.16e-115

Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation of N-terminal asparagines in peptides and proteins to aspartic acid.


Pssm-ID: 464288  Cd Length: 270  Bit Score: 329.17  E-value: 2.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399124760    1 MNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIK 80
Cdd:pfam14736  71 LSRVQSLSLGSPEGRLELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVK 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399124760   81 TAEIYRASFQDRGPEEQLRAARTLAGG-PMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHF 159
Cdd:pfam14736 151 TGEIFPASFPDKGPDEVLRSARSFTGGdQMLDIYDTSTGQLIIGPFNWDPFRDVDLWLQQDDEFILQNLSTSPDAEPPHF 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 399124760  160 VEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEK 199
Cdd:pfam14736 231 VDHIRSTLRFLQEHPFPDVTLFPDNQPRFYRRDEGGLWER 270
 
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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