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Conserved domains on  [gi|27735049|ref|NP_775745|]
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protein N-terminal asparagine amidohydrolase isoform 1 [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 ...
36-304 1.28e-161

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: 450.90  E-value: 1.28e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049    36 QSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDH 115
Cdd:pfam14736   1 RPAKAVGPRGLLYVQQREFAVTTPADKSVSIVGSDDATTCHIVVLRHTGSGATCLAHCDGSGTEDGVQLMLSRVQSLSLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049   116 AQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQ 195
Cdd:pfam14736  81 SPEGRLELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVKTGEIFPASFP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049   196 DRGPEEQLRAARTLAGG-PMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMF 274
Cdd:pfam14736 161 DKGPDEVLRSARSFTGGdQMLDIYDTSTGQLIIGPFNWDPFRDVDLWLQQDDEFILQNLSTSPDAEPPHFVDHIRSTLRF 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 27735049   275 LKKHPSPAHTLFSGNKALLYKKNEDGLWEK 304
Cdd:pfam14736 241 LQEHPFPDVTLFPDNQPRFYRRDEGGLWER 270
 
Name Accession Description Interval E-value
N_Asn_amidohyd pfam14736
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
36-304 1.28e-161

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: 450.90  E-value: 1.28e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049    36 QSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDH 115
Cdd:pfam14736   1 RPAKAVGPRGLLYVQQREFAVTTPADKSVSIVGSDDATTCHIVVLRHTGSGATCLAHCDGSGTEDGVQLMLSRVQSLSLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049   116 AQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQ 195
Cdd:pfam14736  81 SPEGRLELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVKTGEIFPASFP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049   196 DRGPEEQLRAARTLAGG-PMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMF 274
Cdd:pfam14736 161 DKGPDEVLRSARSFTGGdQMLDIYDTSTGQLIIGPFNWDPFRDVDLWLQQDDEFILQNLSTSPDAEPPHFVDHIRSTLRF 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 27735049   275 LKKHPSPAHTLFSGNKALLYKKNEDGLWEK 304
Cdd:pfam14736 241 LQEHPFPDVTLFPDNQPRFYRRDEGGLWER 270
 
Name Accession Description Interval E-value
N_Asn_amidohyd pfam14736
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
36-304 1.28e-161

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: 450.90  E-value: 1.28e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049    36 QSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDH 115
Cdd:pfam14736   1 RPAKAVGPRGLLYVQQREFAVTTPADKSVSIVGSDDATTCHIVVLRHTGSGATCLAHCDGSGTEDGVQLMLSRVQSLSLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049   116 AQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQ 195
Cdd:pfam14736  81 SPEGRLELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVKTGEIFPASFP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735049   196 DRGPEEQLRAARTLAGG-PMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMF 274
Cdd:pfam14736 161 DKGPDEVLRSARSFTGGdQMLDIYDTSTGQLIIGPFNWDPFRDVDLWLQQDDEFILQNLSTSPDAEPPHFVDHIRSTLRF 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 27735049   275 LKKHPSPAHTLFSGNKALLYKKNEDGLWEK 304
Cdd:pfam14736 241 LQEHPFPDVTLFPDNQPRFYRRDEGGLWER 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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