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Conserved domains on  [gi|674651080|ref|NP_001288562|]
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ornithine decarboxylase antizyme 3 isoform 1 [Chrysochloris asiatica]

Protein Classification

ornithine decarboxylase antizyme( domain architecture ID 10489290)

ornithine decarboxylase (ODC) antizyme negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ODC_AZ pfam02100
Ornithine decarboxylase antizyme; This family consists of ornithine decarboxylase antizyme ...
 140-223 2.74e-22

Ornithine decarboxylase antizyme; This family consists of ornithine decarboxylase antizyme proteins. The polyamine biosynthetic enzyme ornithine decarboxylase (ODC) is degraded by the 26 S proteasome via a ubiquitin-independent pathway. Its degradation is greatly accelerated by association with the polyamine-induced regulatory protein antizyme 1 (AZ1).


:

Pssm-ID: 460445  Cd Length: 111  Bit Score: 87.71  E-value: 2.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674651080  140 CDHRLFLDIPHRALDQGNRESLTATLEYVEEKTNVDSVFVNFQKNRNDKGA-LLRAFSYMGFEVVRPDHPALP-PWD--- 214
Cdd:pfam02100  22 GERTLFVFFDDGVLGRDLKEGLMALLELAEEPLGCSHVVICFDRSRPDRAKsLVRTLGWVGFELTTLDHWAVGgGEDvts 101

                          90
                  ....*....|
gi 674651080  215 -NVIFMVYPL 223
Cdd:pfam02100 102 dKWLFMGYEI 111
 
Name Accession Description Interval E-value
ODC_AZ pfam02100
Ornithine decarboxylase antizyme; This family consists of ornithine decarboxylase antizyme ...
 140-223 2.74e-22

Ornithine decarboxylase antizyme; This family consists of ornithine decarboxylase antizyme proteins. The polyamine biosynthetic enzyme ornithine decarboxylase (ODC) is degraded by the 26 S proteasome via a ubiquitin-independent pathway. Its degradation is greatly accelerated by association with the polyamine-induced regulatory protein antizyme 1 (AZ1).


Pssm-ID: 460445  Cd Length: 111  Bit Score: 87.71  E-value: 2.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674651080  140 CDHRLFLDIPHRALDQGNRESLTATLEYVEEKTNVDSVFVNFQKNRNDKGA-LLRAFSYMGFEVVRPDHPALP-PWD--- 214
Cdd:pfam02100  22 GERTLFVFFDDGVLGRDLKEGLMALLELAEEPLGCSHVVICFDRSRPDRAKsLVRTLGWVGFELTTLDHWAVGgGEDvts 101

                          90
                  ....*....|
gi 674651080  215 -NVIFMVYPL 223
Cdd:pfam02100 102 dKWLFMGYEI 111
 
Name Accession Description Interval E-value
ODC_AZ pfam02100
Ornithine decarboxylase antizyme; This family consists of ornithine decarboxylase antizyme ...
 140-223 2.74e-22

Ornithine decarboxylase antizyme; This family consists of ornithine decarboxylase antizyme proteins. The polyamine biosynthetic enzyme ornithine decarboxylase (ODC) is degraded by the 26 S proteasome via a ubiquitin-independent pathway. Its degradation is greatly accelerated by association with the polyamine-induced regulatory protein antizyme 1 (AZ1).


Pssm-ID: 460445  Cd Length: 111  Bit Score: 87.71  E-value: 2.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674651080  140 CDHRLFLDIPHRALDQGNRESLTATLEYVEEKTNVDSVFVNFQKNRNDKGA-LLRAFSYMGFEVVRPDHPALP-PWD--- 214
Cdd:pfam02100  22 GERTLFVFFDDGVLGRDLKEGLMALLELAEEPLGCSHVVICFDRSRPDRAKsLVRTLGWVGFELTTLDHWAVGgGEDvts 101

                          90
                  ....*....|
gi 674651080  215 -NVIFMVYPL 223
Cdd:pfam02100 102 dKWLFMGYEI 111
 
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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