zinc metalloproteinase family protein contains an HEXXH motif characteristic of metallopeptidases; contains a Jacalin-like lectin domain that may bind mono- or oligosaccharides
Putative peptidase family; This family of proteins is functionally uncharacterized. However, ...
5-430
0e+00
Putative peptidase family; This family of proteins is functionally uncharacterized. However, it does contain an HEXXH motif characteriztic of metallopeptidases. This protein is found mainly in fungi. Proteins in this family are typically between 625 to 773 amino acids in length.
:
Pssm-ID: 432283 Cd Length: 426 Bit Score: 698.73 E-value: 0e+00
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
538-681
4.41e-38
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.
The actual alignment was detected with superfamily member cd09613:
Pssm-ID: 446042 Cd Length: 124 Bit Score: 137.55 E-value: 4.41e-38
Putative peptidase family; This family of proteins is functionally uncharacterized. However, ...
5-430
0e+00
Putative peptidase family; This family of proteins is functionally uncharacterized. However, it does contain an HEXXH motif characteriztic of metallopeptidases. This protein is found mainly in fungi. Proteins in this family are typically between 625 to 773 amino acids in length.
Pssm-ID: 432283 Cd Length: 426 Bit Score: 698.73 E-value: 0e+00
Jacalin-like lectin domain of putative metalloproteases and similar proteins; Members of this ...
538-681
4.41e-38
Jacalin-like lectin domain of putative metalloproteases and similar proteins; Members of this family, which appears restricted to fungi, co-occur with protein domains that contain an HExxH motif characteristic of metallopeptidases. They have not been functionally characterized.
Pssm-ID: 187709 Cd Length: 124 Bit Score: 137.55 E-value: 4.41e-38
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
600-681
2.28e-07
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 50.31 E-value: 2.28e-07
Putative peptidase family; This family of proteins is functionally uncharacterized. However, ...
5-430
0e+00
Putative peptidase family; This family of proteins is functionally uncharacterized. However, it does contain an HEXXH motif characteriztic of metallopeptidases. This protein is found mainly in fungi. Proteins in this family are typically between 625 to 773 amino acids in length.
Pssm-ID: 432283 Cd Length: 426 Bit Score: 698.73 E-value: 0e+00
Jacalin-like lectin domain of putative metalloproteases and similar proteins; Members of this ...
538-681
4.41e-38
Jacalin-like lectin domain of putative metalloproteases and similar proteins; Members of this family, which appears restricted to fungi, co-occur with protein domains that contain an HExxH motif characteristic of metallopeptidases. They have not been functionally characterized.
Pssm-ID: 187709 Cd Length: 124 Bit Score: 137.55 E-value: 4.41e-38
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
604-681
1.32e-13
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.
Pssm-ID: 187706 Cd Length: 128 Bit Score: 67.81 E-value: 1.32e-13
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin ...
604-681
6.55e-09
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin isolated from a red alga, which has shown potential as an inhibitor of viral entry, exhibiting antiviral activity against HIV and SARS. The biological functions of griffithsin and griffithsin-like proteins with respect to their source organisms are not known.
Pssm-ID: 187710 Cd Length: 128 Bit Score: 54.71 E-value: 6.55e-09
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
600-681
2.28e-07
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 50.31 E-value: 2.28e-07
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a ...
597-671
5.11e-04
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a conserved secreted vertebrate protein with tissue-specific expression profiles, which might play a role in glycoprotein secretion, perhaps as a linker protein that participates in the formation and/or transport of the zymogen granule. Its paralog ZG16b (PAUF) has been associated with roles in gene regulation and cancer. This domain family also contains mammalian proteins labelled as prostatic spermine-binding protein (SBP) and salivary-gland specific secreted proteins.
Pssm-ID: 187707 [Multi-domain] Cd Length: 128 Bit Score: 40.38 E-value: 5.11e-04
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
589-634
1.27e-03
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.
Pssm-ID: 187706 Cd Length: 128 Bit Score: 39.31 E-value: 1.27e-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.
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