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Conserved domains on  [gi|955689426|ref|NP_001304280|]
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aryl hydrocarbon receptor repressor isoform 2 [Mus musculus]

Protein Classification

PAS domain-containing protein( domain architecture ID 10062837)

PAS domain-containing protein binds ligand(s) and may act as sensors for light and oxygen in signal transduction

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
2-51 3.87e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


:

Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 45.70  E-value: 3.87e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 955689426   2 IFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVV 51
Cdd:cd00130   14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPV 63
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
2-51 3.87e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 45.70  E-value: 3.87e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 955689426   2 IFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVV 51
Cdd:cd00130   14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPV 63
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
2-46 1.32e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 43.16  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 955689426     2 IFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMD 46
Cdd:smart00091  23 ILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
2-45 2.00e-04

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 41.25  E-value: 2.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 955689426    2 IFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAM 45
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQAL 66
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
2-51 3.87e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 45.70  E-value: 3.87e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 955689426   2 IFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVV 51
Cdd:cd00130   14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPV 63
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
2-46 1.32e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 43.16  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 955689426     2 IFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMD 46
Cdd:smart00091  23 ILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
2-45 2.00e-04

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 41.25  E-value: 2.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 955689426    2 IFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAM 45
Cdd:pfam00989  23 ILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQAL 66
 
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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