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Conserved domains on  [gi|1907156805|ref|XP_036020191|]
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aspartyl/asparaginyl beta-hydroxylase isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Asp-B-Hydro_N super family cl25755
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 63-132 6.20e-17

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


The actual alignment was detected with superfamily member pfam05279:

Pssm-ID: 428406  Cd Length: 66  Bit Score: 74.49  E-value: 6.20e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  63 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLLG 132
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 206-368 1.56e-04

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 44.01  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  206 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 283
Cdd:PTZ00341   972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  284 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 362
Cdd:PTZ00341  1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122


                   ....*.
gi 1907156805  363 QDTPPD 368
Cdd:PTZ00341  1123 DDENPE 1128
 
Name Accession Description Interval E-value
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 63-132 6.20e-17

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 74.49  E-value: 6.20e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  63 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLLG 132
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 206-368 1.56e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 44.01  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  206 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 283
Cdd:PTZ00341   972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  284 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 362
Cdd:PTZ00341  1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122


                   ....*.
gi 1907156805  363 QDTPPD 368
Cdd:PTZ00341  1123 DDENPE 1128
 
Name Accession Description Interval E-value
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 63-132 6.20e-17

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 74.49  E-value: 6.20e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  63 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLLG 132
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 206-368 1.56e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 44.01  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  206 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 283
Cdd:PTZ00341   972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156805  284 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 362
Cdd:PTZ00341  1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122


                   ....*.
gi 1907156805  363 QDTPPD 368
Cdd:PTZ00341  1123 DDENPE 1128
 
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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