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Conserved domains on  [gi|258613951|ref|NP_001158225|]
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aspartyl/asparaginyl beta-hydroxylase isoform 9 [Homo sapiens]

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 ...
14-94 1.04e-25

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: 96.06  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951   14 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 93
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65

                  .
gi 258613951   94 G 94
Cdd:pfam05279  66 G 66
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
107-251 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: 42.85  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  107 PEEAEPHTEPEEQVPVEAE-PQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPV 185
Cdd:PTZ00341  948 EEDAEENVEEDAEENVEENvEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENV 1027
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258613951  186 VEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQE 251
Cdd:PTZ00341 1028 EEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVE 1093
 
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 ...
14-94 1.04e-25

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: 96.06  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951   14 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 93
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65

                  .
gi 258613951   94 G 94
Cdd:pfam05279  66 G 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
107-251 1.56e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 42.85  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  107 PEEAEPHTEPEEQVPVEAE-PQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPV 185
Cdd:PTZ00341  948 EEDAEENVEEDAEENVEENvEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENV 1027
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258613951  186 VEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQE 251
Cdd:PTZ00341 1028 EEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVE 1093
 
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 ...
14-94 1.04e-25

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: 96.06  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951   14 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 93
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65

                  .
gi 258613951   94 G 94
Cdd:pfam05279  66 G 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
107-251 1.56e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 42.85  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  107 PEEAEPHTEPEEQVPVEAE-PQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPV 185
Cdd:PTZ00341  948 EEDAEENVEEDAEENVEENvEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENV 1027
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258613951  186 VEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQE 251
Cdd:PTZ00341 1028 EEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVE 1093
ATG27 pfam09451
Autophagy-related protein 27;
4-37 3.36e-03

Autophagy-related protein 27;


Pssm-ID: 430622  Cd Length: 261  Bit Score: 38.08  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 258613951    4 DKETKHGGHKNGRKGGLSGTSFFTWFMVIALLGV 37
Cdd:pfam09451 173 EKDESDPDDGDGGGNGGSGWGWFTWFFIILFLFT 206
rne PRK10811
ribonuclease E; Reviewed
100-239 4.99e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 38.10  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  100 TSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSllhEMVHAEHETEHSYHVEETVSQDcNQDMEEMMSEQENP 179
Cdd:PRK10811  878 AVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHP---EVIAAPVTEQPQVITESDVAVA-QEVAEHAEPVVEPQ 953
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  180 DSSEPVVEDErLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVE 239
Cdd:PRK10811  954 DETADIEEAA-ETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVE 1012
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
128-251 5.68e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 37.84  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  128 NIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVE--DERLHHDTDDvTYQVYEE 205
Cdd:PTZ00341  946 NIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEEnvEENVEENIEE-NVEEYDE 1024
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 258613951  206 QAVYEPLEN----EGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQE 251
Cdd:PTZ00341 1025 ENVEEVEENveeyDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEE 1074
rne PRK10811
ribonuclease E; Reviewed
103-252 9.72e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 37.33  E-value: 9.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  103 PAVPPEEAEPHTEPEEQ------------VPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDME 170
Cdd:PRK10811  846 PVVRPQDVQVEEQREAEevqvqpvvaevpVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVT 925
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613951  171 E---MMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVE 247
Cdd:PRK10811  926 EqpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQ 1005

                  ....*
gi 258613951  248 EQQEV 252
Cdd:PRK10811 1006 VPEAT 1010
 
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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