eyes absent (EYA) family protein functions as a transcriptional coactivator and an aspartyl-based protein tyrosine phosphatase; belongs to the HAD (haloacid dehalogenase) superfamily
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
355-626
4.23e-169
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
:
Pssm-ID: 319789 Cd Length: 271 Bit Score: 482.38 E-value: 4.23e-169
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
355-626
4.23e-169
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
Pssm-ID: 319789 Cd Length: 271 Bit Score: 482.38 E-value: 4.23e-169
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
355-626
8.99e-135
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. Metazoan EYA's also contain a variable N-terminal domain consisting largely of low-complexity sequences.
Pssm-ID: 273739 Cd Length: 274 Bit Score: 394.99 E-value: 8.99e-135
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) ...
355-626
4.23e-169
protein tyrosine phosphatase domain of the nuclear transcription factor of Eyes absent (Eya) and related phosphatase domains; Eyes absent (Eya) is a transcriptional coactivator, and an aspartyl-based protein tyrosine phosphatase. Eya and Six operate as a composite transcription factor, within a conserved network of transcription factors called the retinal determination (RD) network. The RD network interacts with a broad variety of signaling pathways to regulate the development and homeostasis of organs and tissues such as eye, muscle, kidney and ear. To date it is not clear what the physiologically relevant substrates of the Eya protein tyrosine phosphatase are, or whether this phosphatase activity plays a role in transcription. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
Pssm-ID: 319789 Cd Length: 271 Bit Score: 482.38 E-value: 4.23e-169
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. ...
355-626
8.99e-135
eyes absent protein conserved domain; This domain is common to all eyes absent (EYA) homologs. Metazoan EYA's also contain a variable N-terminal domain consisting largely of low-complexity sequences.
Pssm-ID: 273739 Cd Length: 274 Bit Score: 394.99 E-value: 8.99e-135
Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the ...
69-252
1.61e-03
Nucleoporin homology of Germinal-centre associated nuclear protein; NupH_GANP is the nucleoporin-homology domain at the N-terminus of human GANP or germinal-centre associated nuclear proteins. GANP is part of the TREX-2 complex that links transcription with nuclear messenger RNA export, and it associates with the mRNP particle through the interaction of the NupH_GANP with NXF1, the export factor. This attachment mediates efficient delivery of mRNPs to nuclear pore complexes.
Pssm-ID: 435572 [Multi-domain] Cd Length: 292 Bit Score: 41.05 E-value: 1.61e-03
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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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.
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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
(illustrated example)
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
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
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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