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Conserved domains on  [gi|973215673|ref|XP_015194399|]
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PREDICTED: protein N-terminal asparagine amidohydrolase-like isoform X1 [Lepisosteus oculatus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
N_Asn_amidohyd super family cl20664
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
44-300 1.49e-66

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


The actual alignment was detected with superfamily member pfam14736:

Pssm-ID: 464288  Cd Length: 270  Bit Score: 209.76  E-value: 1.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673   44 PDYLLYVSQREYATIDLCKGPVTRIGSDEATTCHIIVLHCPGTGKVSLAHIDGSKVGVGVKFMVeemkKQCKDFSQHWPw 123
Cdd:pfam14736   8 PRGLLYVQQREFAVTTPADKSVSIVGSDDATTCHIVVLRHTGSGATCLAHCDGSGTEDGVQLML----SRVQSLSLGSP- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673  124 AGFpqtdhlyvicnsLDLYMAGGFIDERGISHDNTMKLLREFMKQDCQIELQLACVSEMNDVVREGNHWPVVSGVGVKMD 203
Cdd:pfam14736  83 EGR------------LELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673  204 GNSfhIYRATFPEKVPDITLRGARLTV--DMMMrRVYDTETDRLIVGPYNFyeHMLKTDDDSRDLTDGEIRRGFSTSPLV 281
Cdd:pfam14736 151 TGE--IFPASFPDKGPDEVLRSARSFTggDQML-DIYDTSTGQLIIGPFNW--DPFRDVDLWLQQDDEFILQNLSTSPDA 225
                         250
                  ....*....|....*....
gi 973215673  282 ERPEFVQMIKDHYKYLADH 300
Cdd:pfam14736 226 EPPHFVDHIRSTLRFLQEH 244
 
Name Accession Description Interval E-value
N_Asn_amidohyd pfam14736
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
44-300 1.49e-66

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: 209.76  E-value: 1.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673   44 PDYLLYVSQREYATIDLCKGPVTRIGSDEATTCHIIVLHCPGTGKVSLAHIDGSKVGVGVKFMVeemkKQCKDFSQHWPw 123
Cdd:pfam14736   8 PRGLLYVQQREFAVTTPADKSVSIVGSDDATTCHIVVLRHTGSGATCLAHCDGSGTEDGVQLML----SRVQSLSLGSP- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673  124 AGFpqtdhlyvicnsLDLYMAGGFIDERGISHDNTMKLLREFMKQDCQIELQLACVSEMNDVVREGNHWPVVSGVGVKMD 203
Cdd:pfam14736  83 EGR------------LELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673  204 GNSfhIYRATFPEKVPDITLRGARLTV--DMMMrRVYDTETDRLIVGPYNFyeHMLKTDDDSRDLTDGEIRRGFSTSPLV 281
Cdd:pfam14736 151 TGE--IFPASFPDKGPDEVLRSARSFTggDQML-DIYDTSTGQLIIGPFNW--DPFRDVDLWLQQDDEFILQNLSTSPDA 225
                         250
                  ....*....|....*....
gi 973215673  282 ERPEFVQMIKDHYKYLADH 300
Cdd:pfam14736 226 EPPHFVDHIRSTLRFLQEH 244
 
Name Accession Description Interval E-value
N_Asn_amidohyd pfam14736
Protein N-terminal asparagine amidohydrolase; This family of enzymes catalyze the deamindation ...
44-300 1.49e-66

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: 209.76  E-value: 1.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673   44 PDYLLYVSQREYATIDLCKGPVTRIGSDEATTCHIIVLHCPGTGKVSLAHIDGSKVGVGVKFMVeemkKQCKDFSQHWPw 123
Cdd:pfam14736   8 PRGLLYVQQREFAVTTPADKSVSIVGSDDATTCHIVVLRHTGSGATCLAHCDGSGTEDGVQLML----SRVQSLSLGSP- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673  124 AGFpqtdhlyvicnsLDLYMAGGFIDERGISHDNTMKLLREFMKQDCQIELQLACVSEMNDVVREGNHWPVVSGVGVKMD 203
Cdd:pfam14736  83 EGR------------LELHLVGGFDDDRGYSEKLCLQLLVAFHKQQEEIHLTTCCVGELNTTVRGGIHWPIIYGIGVNVK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973215673  204 GNSfhIYRATFPEKVPDITLRGARLTV--DMMMrRVYDTETDRLIVGPYNFyeHMLKTDDDSRDLTDGEIRRGFSTSPLV 281
Cdd:pfam14736 151 TGE--IFPASFPDKGPDEVLRSARSFTggDQML-DIYDTSTGQLIIGPFNW--DPFRDVDLWLQQDDEFILQNLSTSPDA 225
                         250
                  ....*....|....*....
gi 973215673  282 ERPEFVQMIKDHYKYLADH 300
Cdd:pfam14736 226 EPPHFVDHIRSTLRFLQEH 244
 
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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