Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is ...
907-1082
4.08e-19
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is typically between 164 to 200 amino acids in length. This domain is found associated with pfam08447.
The actual alignment was detected with superfamily member pfam12114:
Pssm-ID: 463464 Cd Length: 171 Bit Score: 85.92 E-value: 4.08e-19
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
280-368
6.88e-13
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: 65.44 E-value: 6.88e-13
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is ...
907-1082
4.08e-19
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is typically between 164 to 200 amino acids in length. This domain is found associated with pfam08447.
Pssm-ID: 463464 Cd Length: 171 Bit Score: 85.92 E-value: 4.08e-19
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
280-368
6.88e-13
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: 65.44 E-value: 6.88e-13
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
280-372
7.26e-13
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: 65.73 E-value: 7.26e-13
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
280-324
3.23e-08
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: 51.25 E-value: 3.23e-08
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is ...
907-1082
4.08e-19
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is typically between 164 to 200 amino acids in length. This domain is found associated with pfam08447.
Pssm-ID: 463464 Cd Length: 171 Bit Score: 85.92 E-value: 4.08e-19
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
280-368
6.88e-13
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: 65.44 E-value: 6.88e-13
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
280-372
7.26e-13
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: 65.73 E-value: 7.26e-13
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
270-372
2.03e-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: 56.15 E-value: 2.03e-09
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
267-366
1.79e-08
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://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 53.58 E-value: 1.79e-08
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
280-324
3.23e-08
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: 51.25 E-value: 3.23e-08
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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