SF3a60/Prp9 C-terminal; This domain corresponds to the C-terminal region of SF3a60 subunit ...
415-536
3.89e-84
SF3a60/Prp9 C-terminal; This domain corresponds to the C-terminal region of SF3a60 subunit (Prp9 in yeast counterpart) from the highly conserved heterotrimeric complex SF3a found in eukaryotes. It is essential for pre-mRNA splicing that functions in spliceosome assembly within the mature U2 snRNP (small ribonucleoprotein particle). This domain has two conserved sequence motifs: PIP and CEICG. It contains a zinc-finger domain of the C2H2-type which might be important for RNA binding and protein-protein interactions with components of the SF3b complex.
Pssm-ID: 432197 Cd Length: 120 Bit Score: 256.28 E-value: 3.89e-84
SF3a60/Prp9 C-terminal; This domain corresponds to the C-terminal region of SF3a60 subunit ...
415-536
3.89e-84
SF3a60/Prp9 C-terminal; This domain corresponds to the C-terminal region of SF3a60 subunit (Prp9 in yeast counterpart) from the highly conserved heterotrimeric complex SF3a found in eukaryotes. It is essential for pre-mRNA splicing that functions in spliceosome assembly within the mature U2 snRNP (small ribonucleoprotein particle). This domain has two conserved sequence motifs: PIP and CEICG. It contains a zinc-finger domain of the C2H2-type which might be important for RNA binding and protein-protein interactions with components of the SF3b complex.
Pssm-ID: 432197 Cd Length: 120 Bit Score: 256.28 E-value: 3.89e-84
Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9; SF3A3 is one of the components of the ...
144-197
7.09e-21
Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9; SF3A3 is one of the components of the SF3a splicing factor complex of the mature U2 snRNP (small nuclear ribonucleoprotein particle). In yeast, SF3a shows a bifurcated assembly structure of three subunits, Prp9 (subunit 3), Prp11 (subunit 2) and Prp21 (subunit 1). Prp9 and Prp21 were not thought to interact with each other but the alpha1 helix of Prp9 does make important contacts with the SURP2 domain of Prp21, thus the two do interact via a bidentate-binding mode. Prp9 harbours a major binding site for stem-loop IIa of U2 snRNA.
Pssm-ID: 465279 Cd Length: 50 Bit Score: 85.65 E-value: 7.09e-21
Splicing factor SF3a60 binding domain; This domain is found in eukaryotes. This domain is ...
90-116
5.51e-09
Splicing factor SF3a60 binding domain; This domain is found in eukaryotes. This domain is about 30 amino acids in length. This domain has a single completely conserved residue Y that may be functionally important. SF3a60 makes up the SF3a complex with SF3a66 and SF3a120. This domain is the binding site of SF3a60 for SF3a120. The SF3a complex is part of the spliceosome, a protein complex involved in splicing mRNA after transcription.
Pssm-ID: 463461 Cd Length: 27 Bit Score: 51.28 E-value: 5.51e-09
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
272-296
3.30e-07
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.
Pssm-ID: 432381 [Multi-domain] Cd Length: 27 Bit Score: 46.39 E-value: 3.30e-07
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ...
272-295
9.76e-06
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.
Pssm-ID: 463736 [Multi-domain] Cd Length: 25 Bit Score: 42.10 E-value: 9.76e-06
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.
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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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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,
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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
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