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Conserved domains on  [gi|295390552|ref|NP_001171322|]
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aspartyl/asparaginyl beta-hydroxylase isoform 5 [Mus musculus]

Protein Classification

Asp-B-Hydro_N domain-containing protein (domain architecture ID 12062539)

Asp-B-Hydro_N domain-containing protein

Graphical summary

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List of domain hits

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 ...
63-291 2.77e-72

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: 191249 [Multi-domain]  Cd Length: 240  Bit Score: 222.50  E-value: 2.77e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552   63 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKERSPSERTFPPeEEAETHAELEE 142
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKEKSTSEPTVPP-EEAEPHAEEEG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552  143 QAPEGADIQNVEDEVKEQIQSLLQESVHTdhDLEADGLAGEPQPEVEDFLTVTDSDDRFEDLEPGTVHEEIEDTYHVEDT 222
Cdd:pfam05279  91 QLAVRKTKQKVEEEVKEQLQSLLEKIVVS--KQEEDGPGKEPQLDEDKFLLAEDSDDRQETLEAGKVHEETEDSYHVEET 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295390552  223 ASQNHPNDMEEMTNEQEN---SEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQQDTP 291
Cdd:pfam05279 169 ASEQYKQDMKEKASEQENedsKEPVEKAERTKAETDDVTEEDYDEEDNPVEDSKAIKEELAKEPVEEQQEVP 240
 
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 ...
63-291 2.77e-72

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: 191249 [Multi-domain]  Cd Length: 240  Bit Score: 222.50  E-value: 2.77e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552   63 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKERSPSERTFPPeEEAETHAELEE 142
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKEKSTSEPTVPP-EEAEPHAEEEG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552  143 QAPEGADIQNVEDEVKEQIQSLLQESVHTdhDLEADGLAGEPQPEVEDFLTVTDSDDRFEDLEPGTVHEEIEDTYHVEDT 222
Cdd:pfam05279  91 QLAVRKTKQKVEEEVKEQLQSLLEKIVVS--KQEEDGPGKEPQLDEDKFLLAEDSDDRQETLEAGKVHEETEDSYHVEET 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295390552  223 ASQNHPNDMEEMTNEQEN---SEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQQDTP 291
Cdd:pfam05279 169 ASEQYKQDMKEKASEQENedsKEPVEKAERTKAETDDVTEEDYDEEDNPVEDSKAIKEELAKEPVEEQQEVP 240
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
131-293 3.56e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 41.70  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552  131 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 208
Cdd:PTZ00341  972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552  209 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 287
Cdd:PTZ00341 1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122

                  ....*.
gi 295390552  288 QDTPPD 293
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 ...
63-291 2.77e-72

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: 191249 [Multi-domain]  Cd Length: 240  Bit Score: 222.50  E-value: 2.77e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552   63 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKERSPSERTFPPeEEAETHAELEE 142
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKEKSTSEPTVPP-EEAEPHAEEEG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552  143 QAPEGADIQNVEDEVKEQIQSLLQESVHTdhDLEADGLAGEPQPEVEDFLTVTDSDDRFEDLEPGTVHEEIEDTYHVEDT 222
Cdd:pfam05279  91 QLAVRKTKQKVEEEVKEQLQSLLEKIVVS--KQEEDGPGKEPQLDEDKFLLAEDSDDRQETLEAGKVHEETEDSYHVEET 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295390552  223 ASQNHPNDMEEMTNEQEN---SEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQQDTP 291
Cdd:pfam05279 169 ASEQYKQDMKEKASEQENedsKEPVEKAERTKAETDDVTEEDYDEEDNPVEDSKAIKEELAKEPVEEQQEVP 240
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
131-293 3.56e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 41.70  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552  131 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 208
Cdd:PTZ00341  972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390552  209 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 287
Cdd:PTZ00341 1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122

                  ....*.
gi 295390552  288 QDTPPD 293
Cdd:PTZ00341 1123 DDENPE 1128
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
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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