Endoribonuclease XendoU; This is a family of endoribonucleases involved in RNA biosynthesis ...
140-405
1.41e-145
Endoribonuclease XendoU; This is a family of endoribonucleases involved in RNA biosynthesis which has been named XendoU in Xenopus laevis. XendoU is a U-specific metal dependent enzyme that produces products with a 2'-3' cyclic phosphate termini.
:
Pssm-ID: 462792 Cd Length: 262 Bit Score: 413.88 E-value: 1.41e-145
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
86-128
3.74e-13
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.
:
Pssm-ID: 197571 Cd Length: 43 Bit Score: 63.16 E-value: 3.74e-13
Endoribonuclease XendoU; This is a family of endoribonucleases involved in RNA biosynthesis ...
140-405
1.41e-145
Endoribonuclease XendoU; This is a family of endoribonucleases involved in RNA biosynthesis which has been named XendoU in Xenopus laevis. XendoU is a U-specific metal dependent enzyme that produces products with a 2'-3' cyclic phosphate termini.
Pssm-ID: 462792 Cd Length: 262 Bit Score: 413.88 E-value: 1.41e-145
Xenopus laevis endoribonuclease XendoU, and related proteins; Xenopus laevis XendoU is a ...
137-405
3.95e-139
Xenopus laevis endoribonuclease XendoU, and related proteins; Xenopus laevis XendoU is a uridylate-specific endoribonuclease, which releases a cleavage product containing a 2',3'-cyclic phosphate at the 3' terminal end. XendoU is a monomer and requires Mn2+. It is involved in the processing of intron-encoded box C/D U16 small, nucleolar RNA. XendoU is distantly related to the Nidovirus uridylate-specific endoribonucleases (NendoUs) which include Nonstructural protein 15 (Nsp15) from coronaviruses, Nsp11 from arteriviruses, and torovirus endoribonuclease.
Pssm-ID: 394910 Cd Length: 264 Bit Score: 397.69 E-value: 3.95e-139
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
86-128
3.74e-13
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.
Pssm-ID: 197571 Cd Length: 43 Bit Score: 63.16 E-value: 3.74e-13
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
21-62
6.69e-09
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.
Pssm-ID: 197571 Cd Length: 43 Bit Score: 51.22 E-value: 6.69e-09
Endoribonuclease XendoU; This is a family of endoribonucleases involved in RNA biosynthesis ...
140-405
1.41e-145
Endoribonuclease XendoU; This is a family of endoribonucleases involved in RNA biosynthesis which has been named XendoU in Xenopus laevis. XendoU is a U-specific metal dependent enzyme that produces products with a 2'-3' cyclic phosphate termini.
Pssm-ID: 462792 Cd Length: 262 Bit Score: 413.88 E-value: 1.41e-145
Xenopus laevis endoribonuclease XendoU, and related proteins; Xenopus laevis XendoU is a ...
137-405
3.95e-139
Xenopus laevis endoribonuclease XendoU, and related proteins; Xenopus laevis XendoU is a uridylate-specific endoribonuclease, which releases a cleavage product containing a 2',3'-cyclic phosphate at the 3' terminal end. XendoU is a monomer and requires Mn2+. It is involved in the processing of intron-encoded box C/D U16 small, nucleolar RNA. XendoU is distantly related to the Nidovirus uridylate-specific endoribonucleases (NendoUs) which include Nonstructural protein 15 (Nsp15) from coronaviruses, Nsp11 from arteriviruses, and torovirus endoribonuclease.
Pssm-ID: 394910 Cd Length: 264 Bit Score: 397.69 E-value: 3.95e-139
Nidoviral uridylate-specific endoribonuclease (NendoU) domain of coronavirus Nonstructural ...
282-405
8.58e-14
Nidoviral uridylate-specific endoribonuclease (NendoU) domain of coronavirus Nonstructural protein 15 (Nsp15), arterivirus Nsp11, torovirus endoribonuclease, Xenopus laevis endoribonuclease XendoU, and related proteins; Nidovirus endoribonucleases (NendoUs) and eukaryotic Xenopus laevis-like endoribonucleases (XendoUs) are uridylate-specific endoribonucleases which release a cleavage product containing a 2',3'-cyclic phosphate at the 3' terminal end. NendoUs include Nsp15 from coronaviruses and Nsp11 from arteriviruses, both of which may participate in the viral replication process and in the evasion of the host immune system. XendoU is involved in the processing of intron-encoded box C/D U16 small, nucleolar RNA. Except for turkey coronavirus (TCoV) Nsp15, Mn2+ is generally essential for the catalytic activity of coronavirus Nsp15. Mn2+ is dispensable, and to some extent inhibits the activity of arterivirus (Porcine Reproductive and Respiratory Syndrome virus) PRRSV Nsp11. XendoU also requires Mn2+. Coronavirus Nsp15 from Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV), human Coronavirus 229E (HCoV229E), and murine hepatitis virus (MHV) forms a functional hexamer while Porcine DeltaCoronavirus (PDCoV) Nsp15 has been shown to exist as a dimer and a monomer in solution. Nsp11 from the arterivirus PRRSV is a dimer.
Pssm-ID: 439156 Cd Length: 113 Bit Score: 67.26 E-value: 8.58e-14
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
86-128
3.74e-13
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.
Pssm-ID: 197571 Cd Length: 43 Bit Score: 63.16 E-value: 3.74e-13
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
21-62
6.69e-09
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.
Pssm-ID: 197571 Cd Length: 43 Bit Score: 51.22 E-value: 6.69e-09
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
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
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
