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Conserved domains on  [gi|930155619|ref|NP_001300956|]
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aryl hydrocarbon receptor isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 174-259 4.57e-14

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.


:

Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 68.13  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619  174 PIGCDAKGQLILGYTEVELCTRG-SGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIY-RNG 251
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdENG 80


                  ....*...
gi 930155619  252 RPDYIIAT 259
Cdd:pfam08447  81 KPVRVIGV 88
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 3-60 1.72e-10

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: 58.41  E-value: 1.72e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 930155619   3 LNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALN 60
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLS 58
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 174-259 4.57e-14

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 68.13  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619  174 PIGCDAKGQLILGYTEVELCTRG-SGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIY-RNG 251
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdENG 80


                  ....*...
gi 930155619  252 RPDYIIAT 259
Cdd:pfam08447  81 KPVRVIGV 88
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 3-60 1.72e-10

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: 58.41  E-value: 1.72e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 930155619   3 LNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALN 60
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLS 58
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 2-60 2.23e-10

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: 58.20  E-value: 2.23e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 930155619    2 ALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALN 60
Cdd:pfam00989   9 SLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALL 67
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 2-60 9.54e-10

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: 55.10  E-value: 9.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 930155619     2 ALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALN 60
Cdd:smart00091   9 SLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 159-263 3.06e-07

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: 49.17  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619 159 TKNFIFRTKHKLDFTpiGCDAKGQLILGYTEVELCTRgSGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWR 238
Cdd:cd00130    1 LPDGVIVLDLDGRIL--YANPAAEQLLGYSPEELIGK-SLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77

                         90       100
                 ....*....|....*....|....*.
gi 930155619 239 WVQSNARLIY-RNGRPDYIIATQRPL 263
Cdd:cd00130   78 WVLVSLTPIRdEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 225-266 4.41e-06

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 44.10  E-value: 4.41e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 930155619   225 MTVFRLLAKHSRWRWVQSNARLIYR-NGRPDYIIATQRPLTDE 266
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDeDGEVEGILGVVRDITER 43
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 184-279 1.30e-04

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 44.97  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619 184 ILGYTEVELCtRGSGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIYRNGRPDYIIATQRPL 263
Cdd:COG5809  173 LLGISIEELI-GKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDI 251

                         90
                 ....*....|....*.
gi 930155619 264 TDEEGREHLQKRSTSL 279
Cdd:COG5809  252 TERKKLEELLRKSEKL 267
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 6-59 1.58e-03

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 41.50  E-value: 1.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 930155619   6 FVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWAL 59
Cdd:COG5809  153 GIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLL 206
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 174-259 4.57e-14

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 68.13  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619  174 PIGCDAKGQLILGYTEVELCTRG-SGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIY-RNG 251
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdENG 80


                  ....*...
gi 930155619  252 RPDYIIAT 259
Cdd:pfam08447  81 KPVRVIGV 88
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 3-60 1.72e-10

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: 58.41  E-value: 1.72e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 930155619   3 LNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALN 60
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLS 58
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 2-60 2.23e-10

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: 58.20  E-value: 2.23e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 930155619    2 ALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALN 60
Cdd:pfam00989   9 SLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALL 67
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 2-60 9.54e-10

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: 55.10  E-value: 9.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 930155619     2 ALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALN 60
Cdd:smart00091   9 SLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 164-268 9.12e-09

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


Pssm-ID: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 53.45  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619  164 FRTKHKLDFTPIGCDAKGQLILGYTEVELcTRGSGYQFIHAADiLHCAESHIR--MIKTGESGMTVFRLLAKHSRWRWVQ 241
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDEL-VGRSIYDLVHPQD-LRTAKSHLReiIQTRGRATSPSYRLRLRDGDFLSVH 81

                          90       100
                  ....*....|....*....|....*....
gi 930155619  242 SNARLIY--RNGRPDYIIATQRPLTDEEG 268
Cdd:pfam14598  82 TKSKLFLnqNSNQQPFIMCTHTILREENA 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 159-263 3.06e-07

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: 49.17  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619 159 TKNFIFRTKHKLDFTpiGCDAKGQLILGYTEVELCTRgSGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWR 238
Cdd:cd00130    1 LPDGVIVLDLDGRIL--YANPAAEQLLGYSPEELIGK-SLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77

                         90       100
                 ....*....|....*....|....*.
gi 930155619 239 WVQSNARLIY-RNGRPDYIIATQRPL 263
Cdd:cd00130   78 WVLVSLTPIRdEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 225-266 4.41e-06

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 44.10  E-value: 4.41e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 930155619   225 MTVFRLLAKHSRWRWVQSNARLIYR-NGRPDYIIATQRPLTDE 266
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDeDGEVEGILGVVRDITER 43
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 184-279 1.30e-04

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 44.97  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619 184 ILGYTEVELCtRGSGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIYRNGRPDYIIATQRPL 263
Cdd:COG5809  173 LLGISIEELI-GKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDI 251

                         90
                 ....*....|....*.
gi 930155619 264 TDEEGREHLQKRSTSL 279
Cdd:COG5809  252 TERKKLEELLRKSEKL 267
PAS COG2202
PAS domain [Signal transduction mechanisms];
184-265 2.08e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 43.47  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619 184 ILGYTEVELCTRgSGYQFIHAADILHCAESHIRMIKTG-ESGMTVFRLLAKHSRWRWVQSNARLIYRNGRPDYIIATQRP 262
Cdd:COG2202  169 LLGYSPEELLGK-SLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRD 247


                 ...
gi 930155619 263 LTD 265
Cdd:COG2202  248 ITE 250
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 6-59 1.58e-03

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 41.50  E-value: 1.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 930155619   6 FVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWAL 59
Cdd:COG5809  153 GIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLL 206
PAS COG2202
PAS domain [Signal transduction mechanisms];
184-265 3.56e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930155619 184 ILGYTEVELCTRgSGYQFIHAADILHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIY-RNGRPDYIIATQRP 262
Cdd:COG2202   43 LTGYSAEELLGK-TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRdEDGEITGFVGIARD 121


                 ...
gi 930155619 263 LTD 265
Cdd:COG2202  122 ITE 124
 
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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