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Conserved domains on  [gi|1785372452|ref|XP_031759225|]
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aspartyl/asparaginyl beta-hydroxylase isoform X15 [Xenopus tropicalis]

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 ...
 27-88 1.89e-27

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: 99.15  E-value: 1.89e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785372452  27 EGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDTDGDGDFDVDDAKILLG 88
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
PTZ00121 super family cl31754
MAEBL; Provisional
 93-202 6.34e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372452   93 KIDKKETKAPGEEPGGLAKTKTKVKEEIK--EQLKKVKEKIVVQKKEPKVAERKKpvKETSDKARKPQEGGRPKKEQERD 170
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKkaEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKK 1696

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1785372452  171 EPRQKKD-----EKHKEPVKRTTSGKATERERGKRPE 202
Cdd:PTZ00121  1697 EAEEAKKaeelkKKEAEEKKKAEELKKAEEENKIKAE 1733
 
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 ...
 27-88 1.89e-27

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: 99.15  E-value: 1.89e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785372452  27 EGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDTDGDGDFDVDDAKILLG 88
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
PTZ00121 PTZ00121
MAEBL; Provisional
 93-202 6.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372452   93 KIDKKETKAPGEEPGGLAKTKTKVKEEIK--EQLKKVKEKIVVQKKEPKVAERKKpvKETSDKARKPQEGGRPKKEQERD 170
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKkaEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKK 1696

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1785372452  171 EPRQKKD-----EKHKEPVKRTTSGKATERERGKRPE 202
Cdd:PTZ00121  1697 EAEEAKKaeelkKKEAEEKKKAEELKKAEEENKIKAE 1733
 
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 ...
 27-88 1.89e-27

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: 99.15  E-value: 1.89e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785372452  27 EGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDTDGDGDFDVDDAKILLG 88
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
PTZ00121 PTZ00121
MAEBL; Provisional
 93-202 6.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372452   93 KIDKKETKAPGEEPGGLAKTKTKVKEEIK--EQLKKVKEKIVVQKKEPKVAERKKpvKETSDKARKPQEGGRPKKEQERD 170
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKkaEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKK 1696

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1785372452  171 EPRQKKD-----EKHKEPVKRTTSGKATERERGKRPE 202
Cdd:PTZ00121  1697 EAEEAKKaeelkKKEAEEKKKAEELKKAEEENKIKAE 1733
 
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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