TS

## Overview

TS is a dataset for object detection tasks - it contains Traffic Signs annotations for 1,612 images.

## Getting Started

You can download this dataset for use within your own projects, or fork it into a workspace on Roboflow to create your own model.

  ## License

  This dataset is available under the [Public Domain license](https://creativecommons.org/licenses/Public Domain).

This superfamily describes a β(2)-α(n)-β two layers (α-β) fold domain of EF-Tu (EF1A). In E. coli and mitochondrial Ts there are two subdomains of this fold .

Explore the historical Whois records related to ts-rmq-svc-domain.com (Domain). Get insights into ownership history and changes over time.

This entry includes ADAM-TS and ADAM-TS-like proteins, which are closely related to the ADAM family (A Disintegrin and Metalloproteinase) . ADAM-TS proteases are zinc metalloendopeptidases, most of whose substrates are extracellular matrix (ECM) components, whereas ADAM-TS-like proteins lack a metalloprotease domain, reside in the ECM and have regulatory roles . Examples of ADAM-TS-like proteins are papilin and punctin .

The main entity of this document is a structure with accession number 1tfe

Proteolysis of the extracellular matrix plays a critical role in establishing tissue architecture during development and in tissue degradation in diseases such as cancer, arthritis, Alzheimer's disease and a variety of inflammatory conditions []. The proteolytic enzymes responsible for this process are members of diverse protease families, including the secreted zinc metalloproteases (MPs) []. Recently, a new MP family, ADAM-TS (a disintegrin-like and metalloprotease domain with thrombospondin type I modules) has been identified. The family consists of at least 20 members that share a high degree of sequence similarity and conserved domain organisation [,]. The defining domains of the ADAM-TS family are (from N- to C-termini) a pre-pro metalloprotease domain of the reprolysin type, a snake venom disintegrin-like domain, a thrombospondin type-I (TS) module, a cysteine-rich region, and a cysteine-free (spacer) domain []. Domain organisation following the spacer domain C-terminus shows some variability in certain ADAM-TS members, principally in the number of additional TS domains. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS1, for example, is reported to be involved in inflammation and cancer cachexia [], whilst recessively inherited ADAM-TS2 mutations cause Ehlers-Danlos syndrome type VIIC, a disorder characterised clinically by severe skin fragility []. ADAM-TS4 is an aggrecanase involved in arthritic destruction of cartilage []. ADAM-TS1 was originally cloned in mice []. Human and rat orthologues have also been identified. Expression of ADAMTS-1 is closely associated with acute inflammation [].

This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins . ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organisation among its members [[cite:PUB00017264],[cite:PUB00017277]]. Members of the ADAM-TS family have been implicated in a range of diseases [[cite:PUB00090139],[cite:PUB00098765]]. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles . Examples of ADAM-TS-like proteins are papilin and punctin .

This domain is found C-terminal in Trans-sialidase (TS) from Trypanosoma cruzi and other similar proteins. Members of this group are specific to Trypanosoma. TS is involved in host cell invasion and parasite survival in the bloodstream. The parasite uses TS activity to sialylate its own surface molecules, allowing it to evade lysis by serum factors. This domain follows the catalytic domain and adopts a β-sandwich fold typical for Concanavalin-like lectin/glucanase superfamily. It is likely involved in binding glycan structures present on the surface of the Trypanosomes or host cells and in modulating the activity and biological function of TS .

Explore historical ownership and registration records by performing a reverse Whois lookup for the email address domain@ts.net.sa..

UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway, DNA excision-repair, and cell signalling via protein kinases . HHR23A, the human homologue of yeast Rad23A is a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The fold of the UBA domain consists of a compact three-helical bundle with a right-handed twist, and have a conserved hydrophobic surface patch for protein-protein interactions. UBA-like domains can be found in other proteins as well, such as the TS-N domain in the elongation factor Ts (EF-Ts), which catalyses the recycling of the GTPase EF-Tu required for the binding of aminoacyl-tRNA top the ribosomal A site ; and the C-terminal domain of TAP/NXF1, which functions in nuclear export through the interaction of its UBA-like domain with FG nucleoporins .

Dataset

This dataset was created by smitop

Released under CC0: Public Domain

Contents

suppressor APC domain containing 2 Involved in negative regulation of protein localization to cell cortex and positive regulation of cell population proliferation. Located in several cellular components, including apical cortex; apical junction complex; and nuclear lumen. Involved in negative regulation of protein localization to cell cortex and positive regulation of cell population proliferation. Located in several cellular components, including apical cortex; apical junction complex; and nuclear lumen. [provided by Alliance of Genome Resources, Feb 2025]

Explore the historical Whois records related to ts-dent.net (Domain). Get insights into ownership history and changes over time.

UBA/TS-N domain/CUE domain/Domain of unknown function (DUF1771)/Smr domain containing protein

EF-Ts functions as a nucleotide exchange factor in the functional cycle of EF-Tu, another translation elongation factor that facilitates the binding of aminoacylated transfer RNAs (aminoacyl-tRNA) to the ribosomal A site as a ternary complex with guanosine triphosphate during the elongation cycle of protein biosynthesis, and then catalyzes the hydrolysis of GTP and release itself in GDP-bound form. EF-Ts forms complex with EF-Tu and catalyzes the nucleotide exchange reaction promoting the formation of EF-Tu in GTP-bound form from EF-Tu in GDP-bound form. EF-Ts from Thermus thermophiles is shorter than EF-Ts from Escherichia coli, but it has higher thermostability. The mitochondrial translational EF-Ts from chloroplasts and mitochondria display high similarity to the bacterial EF-Ts. The majority of family members contain one ubiquitin-associated (UBA) domain, but some family members from plants harbor two tandem UBA domains.

This entry contains members of the ADAM-TS8 family of metallopeptidases that belong to MEROPS peptidase family M12, subfamily M12B: adamalysin (clan MA).Proteolysis of the extracellular matrix plays a critical role in establishing tissue architecture during development and in tissue degradation in diseases such as cancer, arthritis, Alzheimer's disease and a variety of inflammatory conditions . The proteolytic enzymes responsible for this process are members of diverse protease families, including the secreted zinc metalloproteases (MPs) . Recently, a new MP family, ADAM-TS (a disintegrin-like and metalloprotease domain with thrombospondin type I modules) has been identified. The family consists of at least 20 members that share a high degree of sequence similarity and conserved domain organisation . The defining domains of the ADAM-TS family are (from N- to C-termini) a pre-pro metalloprotease domain of the reprolysin type, a snake venom disintegrin-like domain, a thrombospondin type-I (TS) module, a cysteine-rich region, and a cysteine-free (spacer) domain . Domain organisation following the spacer domain C terminus shows some variability in certain ADAM-TS members, principally in the number of additional TS domains. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS1, for example, is reported to be involved in inflammation and cancer cachexia , whilst recessively inherited ADAM-TS2 mutations cause Ehlers-Danlos syndrome type VIIC, a disorder characterised clinically by severe skin fragility . ADAM-TS4 is an aggrecanase involved in arthritic destruction of cartilage . ADAM-TS8, also termed METH2, was identified by searching expressed sequence tag databases for sequences that contained TS modules . In vitro studies have shown recombinant ADAM-TS8 to be effective in blocking angiogenesis, and to inhibit endothelial cell growth .

Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts [pfam:PF00889] .

Explore the historical Whois records related to ts-marketing.net (Domain). Get insights into ownership history and changes over time.

This entry represents members of the ADAM-TS5 family of metallopeptidases that belong to MEROPS peptidase family M12, subfamily M12B: adamalysin (clan MA), M12.225.Proteolysis of the extracellular matrix plays a critical role in establishing tissue architecture during development and in tissue degradation in diseases such as cancer, arthritis, Alzheimer's disease and a variety of inflammatory conditions . The proteolytic enzymes responsible for this process are members of diverse protease families, including the secreted zinc metalloproteases (MPs) . Recently, a new MP family, ADAM-TS (a disintegrin-like and metalloprotease domain with thrombospondin type I modules) has been identified. The family consists of at least 20 members that share a high degree of sequence similarity and conserved domain organisation . The defining domains of the ADAM-TS family are (from N- to C-termini) a pre-pro metalloprotease domain of the reprolysin type, a snake venom disintegrin-like domain, a thrombospondin type-I (TS) module, a cysteine-rich region, and a cysteine-free (spacer) domain . Domain organisation following the spacer domain C terminus shows some variability in certain ADAM-TS members, principally in the number of additional TS domains. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS1, for example, is reported to be involved in inflammation and cancer cachexia , whilst recessively inherited ADAM-TS2 mutations cause Ehlers-Danlos syndrome type VIIC, a disorder characterised clinically by severe skin fragility . ADAM-TS4 is an aggrecanase involved in arthritic destruction of cartilage . ADAM-TS5, also termed aggrecanase 2, was identified through expressed sequence tag database searching, pursuing sequences similar to ADAM-TS1-4 . In vitro studies have shown that ADAM-TS5, like ADAM-TS4, is an aggrecanase able to cleave cartilage aggrecan .

The Sac domain is a region of homology between the N-terminus of synaptojaninand the otherwise unrelated yeast protein Sac1p. The Sac domain isapproximately 400 residues in length, and proteins containing this domain showapproximately 35% identity with other Sac domains throughout this region. TheSac domain exhibits phosphatidylinositol polyphosphate phosphatase activityand can hydrolyse phosphate from any of the three positions of inositol thatmay be phosphorylated (3-, 4- and 5). However, adjacent phosphates areresistant to hydrolysis. Sac domains cannot hydrolyse phosphate fromphosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), or PtdIns(3,4)P2, orPtdIns(3,4,5)P3, but can hydrolyse PtdIns(3,5)P2 .The Sac domain consists of seven highly conserved motifs which appear todefine the catalytic and regulatory regions of the phosphatase. The sixthconserved region contains a highly conserved C-x(5)-R-[TS] motif, thought tobe the catalytic motif of many metal-independent protein and inositidepolyphosphate phosphatases. Interestingly, the Inp51p Sac domain in which thecysteine, arginine and threonine/serine residues within the C-x(5)-R-[TS]motif are absent, does not exhibit any phosphatase activity .Two classes of Sac domain proteins have been identified in mammals as well aslower eukaryotes . The first comprises proteins, which, in addition to anN-terminal phosphatase Sac domain, have all the domains associated with typeII phosphatidylinositol phosphate 5-phosphatases: - Mammalian synaptojanins, type II phosphatidylinositol phosphate 5- phosphatases. - Yeast INP51, a 108 kDa membrane protein. It is involved in endocytosis and regulation of the actin cytoskeleton under conditions of normal vegetative growth. Although the Sac phosphatase domain of INP51 may be catalytically inactive, the domain may retain other functions. - Yeast INP52, a 133 kDa membrane protein. It is involved in endocytosis and regulation of the actin cytoskeleton under conditions of normal vegetative growth. - Yeast INP53, a 124 kDa membrane protein. It appears to have a role in intra-Golgi and Golgi-to-endosomal trafficking.The other class of Sac-containing phosphatases consists of proteins with an N-terminal Sac phosphatase domain and no other recognizable domains: - Yeast Sac1p, a 67 kDa membrane protein found in the endoplasmic reticulum (ER) and Golgi. It regulates the actin cytoskeleton and phospholipid metabolism. - Yeast FIG4, a 101 kDa protein encoded by a pheromone regulated or induced gene. FIG4 might function to regulate effector molecules of the actin cytoskeleton during mating.The profile we developed covers the seven highly conserved motifs found in Sacdomains.