exportin domain-containing protein similar to human exportin 1, a nuclear export receptor which is involved in the nuclear translocation of proteins and certain RNAs from the nucleus to the cytoplasm and is thus crucial for the correct localization of cellular components
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins ...
643-961
3.48e-171
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES). CRM1 forms a complex with the NES containing protein and the small GTPase Ran. This region forms an alpha helical structure formed by six helical hairpin motifs that are structurally similar to the HEAT repeat, but share little sequence similarity to the HEAT repeat.
Pssm-ID: 430202 Cd Length: 323 Bit Score: 502.53 E-value: 3.48e-171
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins ...
643-961
1.30e-167
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES). CRM1 forms a complex with the NES containing protein and the small GTPase Ran. This region forms an alpha helical structure formed by six helical hairpin motifs that are structurally similar to the HEAT repeat, but share little sequence similarity to the HEAT repeat.
Pssm-ID: 198170 Cd Length: 321 Bit Score: 493.43 E-value: 1.30e-167
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins ...
643-961
3.48e-171
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES). CRM1 forms a complex with the NES containing protein and the small GTPase Ran. This region forms an alpha helical structure formed by six helical hairpin motifs that are structurally similar to the HEAT repeat, but share little sequence similarity to the HEAT repeat.
Pssm-ID: 430202 Cd Length: 323 Bit Score: 502.53 E-value: 3.48e-171
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins ...
643-961
1.30e-167
CRM1 C terminal; CRM1 (also known as Exportin1) mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES). CRM1 forms a complex with the NES containing protein and the small GTPase Ran. This region forms an alpha helical structure formed by six helical hairpin motifs that are structurally similar to the HEAT repeat, but share little sequence similarity to the HEAT repeat.
Pssm-ID: 198170 Cd Length: 321 Bit Score: 493.43 E-value: 1.30e-167
Exportin 1-like protein; The sequences featured in this family are similar to a region close ...
57-202
9.89e-50
Exportin 1-like protein; The sequences featured in this family are similar to a region close to the N-terminus of yeast exportin 1 (Xpo1, Crm1). This region is found just C-terminal to an importin-beta N-terminal domain (pfam03810) in many members of this family. Exportin 1 is a nuclear export receptor that interacts with leucine-rich nuclear export signal (NES) sequences, and Ran-GTP, and is involved in translocation of proteins out of the nucleus.
Pssm-ID: 462459 Cd Length: 147 Bit Score: 172.41 E-value: 9.89e-50
CRM1 / Exportin repeat 2; Chromosome region maintenance 1 / Exportin 1 mediates the nuclear ...
339-406
2.07e-40
CRM1 / Exportin repeat 2; Chromosome region maintenance 1 / Exportin 1 mediates the nuclear transport of proteins bearing a leucin-rich nuclear export signal (NES). It contains helical repeats that are structurally similar to HEAT repeats, but share little sequence similarity with them. N-, C-terminal and central repeats show slightly different structural arrangements, with N- and C- terminal repeats interacting with each other. This Pfam entry includes some CRM1 repeats that fail to be detected with the pfam18777 model.
Pssm-ID: 436735 Cd Length: 68 Bit Score: 143.01 E-value: 2.07e-40
CRM1 / Exportin repeat 3; Chromosome region maintenance 1 / Exportin 1 mediates the nuclear ...
419-469
7.04e-34
CRM1 / Exportin repeat 3; Chromosome region maintenance 1 / Exportin 1 mediates the nuclear transport of proteins bearing a leucin-rich nuclear export signal (NES). It contains helical repeats that are structurally similar to HEAT repeats, but share little sequence similarity with them. N-, C-terminal and central repeats show slightly different structural arrangements, with N- and C- terminal repeats interacting with each other. This Pfam entry includes some CRM1 repeats that fail to be detected with the PF18777 model.
Pssm-ID: 436736 [Multi-domain] Cd Length: 51 Bit Score: 123.83 E-value: 7.04e-34
Chromosome region maintenance or exportin repeat; Chromosome region maintenance 1 or exportin ...
279-315
2.89e-16
Chromosome region maintenance or exportin repeat; Chromosome region maintenance 1 or exportin 1 mediates the nuclear transport of proteins bearing a leucin-rich nuclear export signal (NES). It contains helical repeats that are structurally similar to HEAT repeats, but share little sequence similarity with them. N-terminal, C-terminal and central repeats show slightly different structural arrangements, with N- and C- termini repeats interacting with each other. This entry represents the central repeats of CRM1.
Pssm-ID: 465864 [Multi-domain] Cd Length: 37 Bit Score: 72.90 E-value: 2.89e-16
Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can ...
10-46
6.17e-05
Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins.. which is important for importin-beta mediated transport.
Pssm-ID: 197981 [Multi-domain] Cd Length: 67 Bit Score: 41.85 E-value: 6.17e-05
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
