The domain within your query sequence starts at position 1072 and ends at position 1114; the E-value for the CXC domain shown below is 1.12e0.
KTIQGCSCKGWCRNKHCGCRKQGVDCCVACGCDPTKCRNRQQE
CXC
Tesmin/TSO1-like CXC domain
SMART accession number:
SM01114
Description:
This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin Q9Y4I5 ((PUBMED:10191092)) and TSO1 Q9LE32 ((PUBMED:10769245)) . This family is called a CXC domain in ((PUBMED:10769245)).
This entry represents a CXC domain found in proteins such as Tesmin Q9Y4I5 [ (PUBMED:10191092) ] and TSO1 Q9LE32 [ (PUBMED:10769245) ]. These proteins have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C.
Family alignment:
There are 8766 CXC domains in 6252 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CXC domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CXC domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CXC domain in the selected taxonomic class.
TSO1 is a novel protein that modulates cytokinesis and cell expansion inArabidopsis.
Development. 2000; 127: 2219-26
Display abstract
Previous analyses of tso1 mutants revealed a loss of control of directionalcellular expansion and coordination of growth of adjacent cells, and defects inkaryokinesis and cytokinesis. We isolated TSO1 using a map-based approach, andshow that it is a member of a family of at least three genes in Arabidopsis.Consistent with the mutant phenotype, TSO1 transcript was most abundant inflowers, where it accumulated to the highest levels in developing ovules andmicrospores. The putative TSO1 protein has two cysteine-rich regions that aresimilar to the CXC domains of a variety of proteins from plants and animals,including a class of kinesins involved in chromosome segregation, and enhancer ofzeste-type proteins. Visualization of TSO1-fusion proteins indicated that TSO1 isa nuclear protein. The tso1 mutant phenotypes and the novelty of the TSO1sequence suggest the existence of previously unknown participants in regulationof directional processes in eukaryotic cells.
A novel testis-specific metallothionein-like protein, tesmin, is an early marker of male germ cell differentiation.
Genomics. 1999; 57: 130-6
Display abstract
We have cloned a novel cDNA encoding testis-specific metallothionein-likeprotein, tesmin, by randomized RT-PCR on RNA from mouse tissues. Twotesmin-related transcripts (2.2 and 1.8 kb) in mouse and one (2.1 kb) in humanwere detected and cloned. These encode a cysteine-rich 32-kDa protein thatcontained a metallothionein-like motif. In situ hybridization analysis in adultmouse testis showed that tesmin is specifically expressed in spermatocytes.Quantitative RT-PCR at different stages of mouse postnatal development (days 4,8, 12, 18, and 42) revealed that tesmin is expressed as early as day 8 andcoincides with the entry of germ cells into meiosis. Furthermore, adult W/Wvsterile mice that harbor the c-kit mutation lacked tesmin expression. The gene isassigned to mouse chromosome 19B, which has been reported to translocate (11;19) in male sterile mice.
Characterization of the cyn operon in Escherichia coli K12.
J Biol Chem. 1988; 263: 14769-75
Display abstract
Escherichia coli can overcome the toxicity of environmental cyanate by hydrolysisof cyanate to ammonia and bicarbonate. This reaction is catalyzed by the enzymecyanase, encoded by the cynS gene. The nucleotide sequence of cynS has beenreported (Sung, Y.-c., Anderson, P. M., and Fuchs, J. A. (1987) J. Bacteriol.169, 5224-5230). The nucleotide sequence of the complete cyn operon has now been determined. The cyn operon is approximately 2600 base pairs and includes cynT,cynS, and cynX, which encode cyanate permease, cyanase, and a protein of unknown function, respectively. Two cyanate-inducible transcripts of 1500 and 2500nucleotides, respectively, were detected by Northern blot analysis. S1 nucleasemapping experiments indicated that two different cyn mRNAs have a common 5'-endand two different 3'-ends. One 3'-end was located within the coding region ofcynX, whereas the other 3'-end includes the entire DNA sequence of cynX. Thelonger transcript contained 98 nucleotides complementary to lac mRNA produced by the predominant lac transcription termination sequence. Termination vectors were used to show that both 3'-ends were generated by sequences that causedtranscriptional termination in vivo. Expression vectors were used to demonstrate that a protein corresponding to the expected size was synthesized from the DNAfragment containing the open reading frame designated cynX. The predicted aminoacid sequence of cynX indicates that it is a very hydrophobic protein. The level of cynX expression was significantly less than that of cynT or cynS expression.
